Researcher basic information

• Doctor of Engineering, The University of Tokyo

• https://researchmap.jp/read0212540?lang=en

• https://jglobal.jst.go.jp/detail?JGLOBAL_ID=200901070791806654
• http://convallaria.pharm.hokudai.ac.jp/bunshi/

• 200901070791806654

• X線結晶構造解析
• 蛋白質間相互作用
• 免疫制御
• 蛋白質
• 細胞表面受容体
• 表面プラズモン共鳴
• NMR解析
• ペア型レセプター
• 分子認識
• 主要組織適合性抗原
• ファージディスプレイ
• LILR受容体
• NMR
• 免疫系レセプター
• 翻訳
• MILL
• ペア型受容体
• 相互作用解析
• CD160
• NK細胞
• 巻き戻し
• Ig-like receptor
• T細胞レセプター
• 強直性脊椎炎
• HIV
• MHC様分子
• セレノシステイン
• KIR
• リボソーム
• 伸長因子
• 蛋白工学
• 分子免疫学
• 構造生物学
• Protein Engineering
• Molecular Immunology
• Structural Biology

• Life Science, Immunology
• Life Science, Biophysics
• Life Science, Structural biochemistry

• Bachelor's degree program, School of Pharmaceutical Sciences and Pharmacy
• Master's degree program, Graduate School of Life Science
• Doctoral (PhD) degree program, Graduate School of Life Science

Research activity information

• Jun. 2015, 北海道大学, 北海道大学総長賞研究奨励賞
  前仲 勝実
• Jun. 2014, 北海道大学, 北海道大学総長賞教育奨励賞
  前仲 勝実
• Dec. 2008, 日本免疫学会, 日本免疫学会研究奨励賞
  生体防御に関わる細胞表面受容体の分子認識機構
  前仲 勝実

• Molecular basis of fibrinogen recognition by the innate immune receptor LILRA2
  Jiaqi Wang; Atsushi Furukawa; Liuan Chen; Ryo Suzuki; Hisashi Arase; Kouyuki Hirayasu; Katsumi Maenaka
  Journal of Biological Chemistry, Apr. 2026
  Scientific journal
• Exploring potential targets of Chlamydia trachomatis required for cellular adaptation through screening approved-drug libraries
  Ruiyu Li; Saicheng Zhang; Satoko Otsuguro; Akira Matsuda; Sora Kuroiwa; Tsubasa Tatsumiya; Jeewan Thapa; Torahiko Okubo; Katsumi Maenaka; Yuichi Takizawa; Hideaki Higashi; Hiroyuki Yamaguchi
  Next Research, Mar. 2026
  Scientific journal
• Structural basis of lenacapavir-induced HIV-1 capsid disruption during virion maturation
  Hiroki Tanaka; Reina Morita; Tomomasa Oka; Shunsuke Kita; Mina Sasaki; Katsumi Maenaka; Shinichi Machida
  16 Feb. 2026
• Exploratory transcriptomics and in vivo analyses of suramin in tongue squamous cell carcinoma
  Wataru Kakuguchi; Masahiro Morimoto; Kenta Takahashi; Nako Maishi; Kyoko Hida; Takao Nomura; Satoko Otsuguro; Katsumi Maenaka; Yoichi Ohiro
  Biomedical Reports, 24, 3, 1, 10, Spandidos Publications, 23 Jan. 2026
  Scientific journal
• The effect of guide RNA thermal denaturation on the quality of Cas9 ribonucleoprotein-loaded lipid nanoparticle formulations
  Rina Shimizu; Yuji Kashiwakura; Morisada Hayakawa; Shunsuke Kita; Mina Sato; Masatoshi Maeki; Manabu Tokeshi; Katsumi Maenaka; Tsukasa Ohmori; Yuma Yamada; Hideyoshi Harashima; Yusuke Sato
  RSC Pharmaceutics, 2026
  Scientific journal
• Enhanced Sampling Reveals Metastable Conformations Driving K417N-Mediated Class I Antibody Escape.
  Xu Pan; Takashi Tadokoro; Taishi Onodera; Shunsuke Kita; Yoshimasa Takahashi; Katsumi Maenaka; Hisham M Dokainish
  Journal of chemical information and modeling, 65, 21, 11925, 11936, 10 Nov. 2025, [International Magazine]
  English, Scientific journal, The continuous emergence of SARS-CoV-2 variants compromises the effectiveness of neutralizing antibodies (nAbs), contributing to immune evasion. Several single-point mutations in the receptor-binding domain (RBD) have been shown to drastically affect the recognition of Class I antibodies. Understanding the molecular mechanisms behind such single-point mutations remains challenging, especially as weak binding affinity prevents the characterization of complex structures through conventional experimental methods. Here, we employ enhanced sampling molecular dynamics (MD) simulations, the generalized replica exchange with solute tempering (gREST), to investigate the structural and dynamic impacts of the K417N mutation on NT-193 (Class I) binding to RBD. Although stable conformations of wild-type and mutants show similar binding interactions, the mutation profoundly reshapes the transient metastable states. At the key interface between the heavy and light chains, the substitution of lysine with asparagine disrupts key interactions with the heavy chain in metastable states, facilitating antibody dissociation. Consistent with simulation results, surface plasmon resonance (SPR) experiments confirm that K417N significantly increases the dissociation rate, reducing the overall binding affinity to RBD. These findings illustrate the importance of capturing metastable conformations to fully understand mutation-driven immune evasion mechanisms. Moreover, this study demonstrates the power of applying gREST to unravel essential insights into transient and weakly interacting antibody-antigen complexes, facilitating the rational design and optimization of next-generation antibody therapeutics capable of overcoming viral immune escape.
• Molecular basis for selection and inhibition of HIV-1 escape virus by T cells and KIR2DL2+NK cells.
  Takayuki Chikata; Kimiko Kuroki; Nozomi Kuse; Anna E Kliszczak; Wayne Paes; Nanami Tomioka; Robert Parker; Aure Aflalo; Tomohiro Akahoshi; Yu Zhang; Ryoya Yamashita; Ryuma Sakata; Hiroki Kusaka; Yosuke Watanabe; Annalisa Nicastri; Haruki Matsubara; Toyoyuki Ose; Shunsuke Kita; Shinichi Oka; Hiroyuki Gatanaga; Zhansong Lin; Nicola Ternette; Persephone Borrow; Katsumi Maenaka; Masafumi Takiguchi
  Nature communications, 16, 1, 9796, 9796, 06 Nov. 2025, [International Magazine]
  English, Scientific journal, NK cells and CD8+ T cells both contribute to HIV-1 control. These cells not only suppress HIV-1 replication, but also select HIV-1 escape mutant viruses. Most viruses bearing T cell escape mutations are expected to remain susceptible to NK cell suppression, but their inhibition by NK cells is unclear. We investigated the role of HIV-1-specific CD8+ T cells and NK cells recognizing superimposed Pol peptides in selection and control of HIV-1 mutant virus. KIR2DL2+NK cells have an enhanced ability to recognize HIV-1-infected cells after selection of Pol mutant virus by PolIY11-specific HLA-C*12:02-restricted T cells. Mass spectrometry-based immunopeptidome profiling of HIV-1-infected cells and analysis of crystal structures of TCR- and KIR2DL2-HLA-C*12:02-peptide complexes demonstrate the molecular basis for selection and recognition of the escape mutant epitope by TCR and KIR2DL2. The present study elucidates the mechanism for selection and inhibition of an HIV-1 escape virus by T cells and NK cells.
• Thermoresponsive hydrogelation of N-acetyl chitohexaose: Gelation mechanism and application in controlled protein release.
  Hiroyuki Kono; Yuya Nagaoka; Ayumu Izutsu; Shunsuke Kita; Katsumi Maenaka; Shunsuke Nishio; Takeshi Hattori; Yuka Yoshikawa; Kousuke Michishita; Taichi Usui; Takuya Isono; Makoto Ogata
  Carbohydrate polymers, 366, 123897, 123897, 15 Oct. 2025, [International Magazine]
  English, Scientific journal, Chitin is a polysaccharide composed of N-acetylglucosamine units that form highly crystalline structures in biological systems; however, the precise mechanism underlying its self-assembly in aqueous environments remains unclear. In this study, we demonstrated that N-acetyl chitohexaose (GN6), a chitin oligosaccharide with a degree of polymerization of six, uniquely undergoes thermally induced self-assembly into crystalline nanofibers and forms reversible hydrogels in water. Among chitin oligosaccharides ranging from monomer to hexamer, only GN6 exhibited gelation upon heating, which is attributed to its optimal molecular length and balanced hydrophilic-hydrophobic characteristics. Comprehensive structural analyses using solid-state nuclear magnetic resonance spectroscopy, small- and wide-angle X-ray scattering, transmission electron microscopy, atomic force microscopy, and microcrystal electron diffraction revealed that GN6 molecules align along the crystallographic β-axis and assemble into nanofibers with highly ordered α-chitin-type molecular packing. This directional organization is driven by cooperative hydrogen bonding and hydrophobic interactions. Furthermore, the hydrogels exhibited a sustained release of encapsulated proteins, including insulin, albumin, and immunoglobulin G, for more than four weeks under physiological conditions, without using chemical crosslinking agents. These findings highlight the potential of this oligosaccharide as a biocompatible, drug delivery material and as a minimalistic model system for studying polysaccharide self-assembly in aqueous environments.
• Examining the Impact of Storage Conditions on the Stability of a Liquid Formulation of mRNA-Loaded Lipid Nanoparticles.
  Mina Sato; Eleni Samaridou; Moritz Beck-Broichsitter; Masatoshi Maeki; Shunsuke Kita; Manabu Tokeshi; Katsumi Maenaka; Hideyoshi Harashima; Yusuke Sato
  Pharmaceutics, 17, 9, 14 Sep. 2025, [International Magazine]
  English, Scientific journal, Background/Objectives: This study investigated the effect of storage conditions on mRNA-LNPs in situ via identification of the formulation traits necessary for improving storage stability. Methods: We synthesized an ionizable lipid, namely TOT-28, which has a hydrolysis-susceptible ester bond in its hydrophilic head group that allows it to act as an indicator of the hydrophilic environment within the mRNA-LNPs. LNPs were stored either at 4 or 25 °C for up to 8 weeks to investigate the effect of pH and temperature on ester hydrolysis, internal mRNA integrity, physicochemical properties of the LNPs, and mRNA gene expression. Results: The results indicate that, at 25 °C, a lower buffer pH increases ester hydrolysis, whereas an opposite trend slightly occurs in ester hydrolysis with storage at 4 °C. We also found that TOT-28-based LNPs were less hydrated and microviscosity was higher at 4 °C compared with storage temperature at 25 °C. Therefore, TOT-28-based LNPs seem less sensitive to external buffer solutions because of a higher-order structure when stored at lower temperatures. In addition, we found that LNPs with different ionizable lipid structures exhibit distinct responses to pH changes at specific storage temperatures. Conclusions: Our findings provide novel insights into the appropriate conditions for long-term storage of the mRNA-LNPs as a liquid formulation.
• Understanding the structure of measles virus and its implications for novel drug discovery.
  Liuan Chen; Shunsuke Kita; Hideo Fukuhara; Katsumi Maenaka
  Expert opinion on drug discovery, 20, 9, 1131, 1140, Sep. 2025, [International Magazine]
  English, Scientific journal, INTRODUCTION: Despite having a stably effectively vaccine for decades, the Measles virus (MV) still causes periodic outbreaks given its highly contagious nature and a consistent decline in immunization coverage, which was further exacerbated during the COVID-19 pandemic, leading to reduced immunization rates. Equally concerning, there are also no approved treatments for measles. AREAS COVERED: Herein, the authors explore the current challenges of MV therapy discovery. Firstly, the article will provide an overview of the potential drug-targeted steps in the MV infection process, followed by discussion on the characteristics of existing drugs as well as the feasibility of structure-based drug discovery. Finally, the authors highlight the current progress in the field and the future opportunities for antiviral development. This article is based on a literature review including original publications, standard sources, the Protein Data Bank and clinical trials. EXPERT OPINION: First and foremost, a comprehensive structural analysis of neutralizing antibodies and RdRp inhibitors is required for efficient antiviral development. Moreover, the therapeutic prospects and current limitations for acute MV and subacute sclerosing panencephalitis (SSPE) treatments should be considered. Due to various factors including mutations, the development of broad-spectrum antivirals may minimize many of the existing barriers.
• An FDA-approved drug library screening identifies proteasome inhibitors as selective cytotoxic agents for angiosarcoma cells.
  Che-Yuan Hsu; Teruki Yanagi; Kodai Miyamoto; Satoko Otsuguro; Katsumi Maenaka; Hiroshi Nishihara; Hideki Nakamura; Kenzo Takahashi; Hideyuki Ujiie
  British journal of cancer, 133, 1, 3, 13, Jul. 2025, [International Magazine]
  English, Scientific journal, Cutaneous angiosarcoma (CAS) is a life-threatening neoplasm with a 5-year survival rate of under 40% in advanced cases. As available treatments for CAS are limited, novel therapeutics must be explored. To identify potential therapeutic candidates, we conducted a drug screening analysis using an angiosarcoma cell line, HAMON. Cancer-related gene analysis revealed alterations in FGFR4, MYCN, CDKN2A, NF1, TP53, KDM6A, ATRX, MSH6, ATM, and NOTCH1 in HAMON cells. Screening of 4681 FDA-approved drugs identified four candidate compounds, with the proteasome inhibitor bortezomib selected for further study. ATP and MTT assays revealed bortezomib to be the most effective candidate against HAMON cells. Clonogenic assays revealed fewer HAMON cell colonies in the range of 1-10 nM bortezomib. DNA-content fluorescence-activated cell sorting analysis revealed a notable increase in the sub-G0/G1 phases, suggesting cell death without cell cycle arrest. Annexin V-propidium iodide staining revealed a significant increase in the percentage of early and late apoptotic cells in the bortezomib group. Mechanistically, bortezomib induced activation of NF-κB and endoplasmic reticulum stress signaling. The administration of bortezomib to immunocompromised mice implanted with HAMON cells induced apoptosis of tumor cells. This study identified the proteasome inhibitor bortezomib as a potential candidate for angiosarcoma in vitro and in vivo.
• Structural basis of the hepatitis B virus X protein in complex with DDB1.
  Hiroki Tanaka; Joao Diogo Dias; Basile Jay; Shunsuke Kita; Mina Sasaki; Hiroyuki Takeda; Naoki Kishimoto; Shunsuke Sasaki; Shogo Misumi; Masashi Mizokami; Christine Neuveut; Takashi Sumikama; Mikihiro Shibata; Katsumi Maenaka; Shinichi Machida
  Proceedings of the National Academy of Sciences of the United States of America, 122, 24, e2421325122, 17 Jun. 2025, [International Magazine]
  English, Scientific journal, A cure for chronic hepatitis B requires eliminating or permanently silencing covalently closed circular DNA (cccDNA). A pivotal target of this approach is the hepatitis B virus (HBV) X protein (HBx), which is a key factor that promotes transcription from cccDNA. However, the HBx structure remains unsolved. Here, we present the cryoelectron microscopy structure of HBx in complex with DDB1, which is an essential complex for cccDNA transcription. In this structure, hydrophobic interactions within HBx were identified, and mutational analysis highlighted their importance in the HBV life cycle. Our biochemical analysis revealed that the HBx-DDB1 complex directly interacts simultaneously with NSE3, which is a component of the SMC5/6 complex, and Spindlin1. Additionally, HBx-DDB1 complex dynamics were explored via high-speed atomic force microscopy. These findings provide comprehensive insights into the structure and function of HBx in HBV replication.
• Evolutionary and structural basis of SLAMF1 utilization in morbilliviruses-Implications for host range and cross-species transmission.
  Ayumu Hyodo; Fumio Seki; Kento Fukuda; Kaede Tashiro; Yuki Kitai; Yukiko Akahori; Hideko Watabe; Hiroshi Katoh; Rikuto Osaki; Daisuke Takaya; Norihito Kawashita; Hideo Fukuhara; Satoshi Ikegame; Tomoki Yoshikawa; Park Eunsil; Shigeru Morikawa; Ryoji Yamaguchi; Benhur Lee; Katsumi Maenaka; Tsuyoshi Shirai; Kaori Fukuzawa; Shigenori Tanaka; Makoto Takeda
  PLoS pathogens, 21, 6, e1012990, Jun. 2025, [International Magazine]
  English, Scientific journal, Morbilliviruses, including measles virus (MV), canine distemper virus (CDV), peste des petits ruminants virus, and cetacean morbillivirus pose a significant threat to humans and animals. While the host range of morbilliviruses is generally well-defined, cross-species transmission events with significant mortality have also been reported. Their entry into immune cells, the primary targets of morbilliviruses, relies on the signaling lymphocytic activation molecule (SLAM), also known as SLAMF1 or CD150. In this study, we hypothesize that the ability of morbilliviruses to utilize heterologous SLAM receptors stems from evolutionarily conserved structural determinants within the SLAM protein and that minimal genetic changes in the viral receptor-binding H protein can enable adaptation to novel hosts. To test this, we systematically assessed SLAM utilization and adaptation by diverse morbilliviruses. We found that most morbilliviruses efficiently utilize SLAM from multiple host species, including Myotis bat SLAM, but not human SLAM. Only MV could efficiently utilize human SLAM. Additionally, unlike other morbilliviruses, MV utilized Myotis bat SLAM inefficiently. As an example of morbillivirus adaptation to non-host animal SLAM, we conducted an MV adaptation experiment with Myotis bat SLAM. We demonstrated that MV readily adapted to utilize Myotis bat SLAM by acquiring a single N187Y mutation in its hemagglutinin protein. Notably, hypothetical ancestral SLAMs acted as universal receptors for all morbilliviruses. These results reinforced that morbillivirus receptor usage is primarily supported by evolutionarily conserved structural features of SLAM, highlighting a molecular basis that enables morbilliviruses to rapidly adapt to diverse animal SLAMs.
• Regulatory mimicry of cyclin-dependent kinases by a conserved herpesvirus protein kinase.
  Naoto Koyanagi; Kowit Hengphasatporn; Akihisa Kato; Moeka Nobe; Kosuke Takeshima; Yuhei Maruzuru; Katsumi Maenaka; Yasuteru Shigeta; Yasushi Kawaguchi
  Proceedings of the National Academy of Sciences of the United States of America, 122, 16, e2500264122, 22 Apr. 2025, [International Magazine]
  English, Scientific journal, Herpesviruses encode conserved protein kinases (CHPKs) that target cellular cyclin-dependent kinase (CDK) phosphorylation sites; thus, they are termed viral CDK-like kinases. Tyrosine 15 in the GxGxxG motifs of CDK1 and CDK2, whose phosphorylation down-regulates their catalytic activities, is conserved in the corresponding motifs of CHPKs. We found that CHPK UL13, the corresponding Tyr-162 in herpes simplex virus 2 (HSV-2), was phosphorylated in HSV-2-infected cells. Mutational analyses of HSV-2 UL13 Tyr-162 suggested that phosphorylation of UL13 Tyr-162 reduced the phosphorylation of all UL13 substrates tested in HSV-2-infected cells. These findings suggested that HSV-2 UL13 mimicked the regulatory mechanism of CDKs and that this CHPK has regulatory and functional mimicry with CDKs. Furthermore, phosphorylation of HSV-2 UL13 Tyr-162 was suggested to be required for the downregulation of viral replication and pathogenicity, specifically in the brains of mice, and for efficient viral recurrence in guinea pigs. These findings highlight the dual impact of the regulatory mimicry of CDKs by CHPK on the fine-tuned regulation of lytic and latent HSV-2 infections in vivo.
• ARNAX is an ideal adjuvant for COVID-19 vaccines to enhance antigen-specific CD4+ and CD8+ T-cell responses and neutralizing antibody induction.
  Tomomi Kawakita; Toshiki Sekiya; Yayoi Kameda; Naoki Nomura; Marumi Ohno; Chimuka Handabile; Akari Yamaya; Hideo Fukuhara; Yuki Anraku; Shunsuke Kita; Shinsuke Toba; Hirotake Tsukamoto; Tomohiro Sawa; Hiroyuki Oshiumi; Yasushi Itoh; Katsumi Maenaka; Akihiko Sato; Hirofumi Sawa; Yasuhiko Suzuki; Lorena E Brown; David C Jackson; Hiroshi Kida; Misako Matsumoto; Tsukasa Seya; Masashi Shingai
  Journal of virology, e0229024, 15 Apr. 2025, [International Magazine]
  English, Scientific journal, UNLABELLED: ARNAX is a synthetic nucleotide-based Toll-like receptor 3 (TLR3) ligand that specifically stimulates the TLR3/TIR domain-containing adaptor molecule 1 (TICAM-1) pathway without activating inflammatory responses. ARNAX activates cellular immunity via cross-presentation; hence, its practical application has been demonstrated in cancer immunotherapy. Given the importance of cellular immunity in virus infections, ARNAX is expected to be a more effective vaccine adjuvant for virus infections than alum, an adjuvant approved for human use that mainly enhances humoral immunity. In the present study, the trimeric recombinant spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was prepared as a vaccine antigen and formulated with ARNAX. When T-cell and neutralizing antibody responses were evaluated in immunized mice, antigen formulated with ARNAX generated significantly larger numbers of antigenspecific CD4+ and CD8+ T cells, as well as higher titers of neutralizing antibodies, compared to antigen alone or antigen formulated with alum. In experiments where immunized mice were challenged with a SARS-CoV-2 mouse-adapted virus derived from the ancestral strain, immunization with antigen formulated with ARNAX reduced virus titers in the lungs at 3 days post-infection to a much greater extent than did immunization with either antigen alone or that formulated with alum. These results show that ARNAX potently enhances the levels of both cellular and humoral immunity above those seen with alum, providing significantly greater viral clearing responses. Thus, ARNAX may act as a useful adjuvant for prophylactic vaccines, particularly for viral infectious diseases. IMPORTANCE: Cellular immunity is a critical immunological defense system against virus infections. However, aluminum salts, the most widely used adjuvant for vaccines for human use, do not promote strong cellular immunity. To prepare for the next pandemic of viral origin, the development of Th1-type adjuvants with low adverse reactions that induce cellular immunity is necessary. ARNAX is a TLR3 agonist consisting of DNA-RNA hybrid nucleic acid, which is expected to be an adjuvant that induces cellular immunity. The present study using a coronavirus disease 2019 mouse model demonstrated that ARNAX potently induces cellular immunity in addition to humoral immunity with minimal induction of inflammatory cytokines. Therefore, ARNAX has the potential to be used as a potent and welltolerated adjuvant for vaccines against pandemic viruses emerging in the future.
• Structural analysis shows the mode of inhibition for Staphylococcus aureus lipase by antipsychotic penfluridol.
  Julia Kitadokoro; Takatsugu Hirokawa; Masayuki Kamo; Naoki Furubayashi; Yukiko Okuno; Takaaki Hikima; Masaki Yamamoto; Koji Inaka; Katsumi Maenaka; Shigeki Kamitani; Kengo Kitadokoro
  Scientific reports, 15, 1, 11876, 11876, 14 Apr. 2025, [International Magazine]
  English, Scientific journal, It is now well-established that Staphylococcus aureus can produce a range of toxin proteins, resulting in a spectrum of pathological conditions when it infects individuals with pre-existing medical conditions or immunocompromised. Among these, MRSA is one of the most prominent antimicrobial-resistant organisms and a significant cause of mortality in many patients. It has been demonstrated that Staphylococcus aureus lipase (SAL) is a vital factor in the proliferation of this bacterium. A combination of in silico screening and X-ray crystallography was employed to analyze inhibitors of SAL, and the results were highly significant. In silico screening identified a number of compounds, and the enzyme activity assay demonstrated that the antipsychotic drug penfluridol exhibited potent inhibitory activity against SAL. We have conducted co-crystallization of penfluridol and SAL on the ground and in space. The resulting co-crystals were subjected to data measurement using the synchrotron radiation facility at SPring-8, and the complex structure was determined. The crystal structure of the penfluridol-SAL complex was determined at 2.2 Å resolution, thereby providing the structural basis for developing new anti-infective agents that inhibit the growth of Staphylococcus aureus. These findings are anticipated to facilitate the development of compounds with potent inhibitory activity.
• Structural and virological identification of neutralizing antibody footprint provides insights into therapeutic antibody design against SARS-CoV-2 variants.
  Yuki Anraku; Shunsuke Kita; Taishi Onodera; Akihiko Sato; Takashi Tadokoro; Shiori Ito; Yu Adachi; Ryutaro Kotaki; Tateki Suzuki; Jiei Sasaki; Nozomi Shiwa-Sudo; Naoko Iwata-Yoshikawa; Noriyo Nagata; Souta Kobayashi; Yasuhiro Kazuki; Mitsuo Oshimura; Takao Nomura; Michihito Sasaki; Yasuko Orba; Tadaki Suzuki; Hirofumi Sawa; Takao Hashiguchi; Hideo Fukuhara; Yoshimasa Takahashi; Katsumi Maenaka
  Communications biology, 8, 1, 483, 483, 22 Mar. 2025, [International Magazine]
  English, Scientific journal, Medical treatments using potent neutralizing SARS-CoV-2 antibodies have achieved remarkable improvements in clinical symptoms, changing the situation for the severity of COVID-19 patients. We previously reported an antibody, NT-108 with potent neutralizing activity. However, the structural and functional basis for the neutralizing activity of NT-108 has not yet been understood. Here, we demonstrated the therapeutic effects of NT-108 in a hamster model and its protective effects at low doses. Furthermore, we determined the cryo-EM structure of NT-108 in complex with SARS-CoV-2 spike. The single-chain Fv construction of NT-108 improved the cryo-EM maps because of the prevention of preferred orientations induced by Fab orientation. The footprints of NT-108 illuminated how escape mutations such as E484K evade from class 2 antibody recognition without ACE2 affinity attenuation. The functional and structural basis for the potent neutralizing activity of NT-108 provides insights into the rational design of therapeutic antibodies.
• Structural analysis reveals how tetrameric tyrosine-phosphorylated STAT1 is targeted by the rabies virus P-protein
  Aoi Sugiyama; Miku Minami; Kaito Ugajin; Satomi Inaba-Inoue; Nana Yabuno; Yuichiro Takekawa; Sun Xiaomei; Shiho Takei; Mina Sasaki; Tomo Nomai; Xinxin Jiang; Shunsuke Kita; Katsumi Maenaka; Mika Hirose; Min Yao; Paul R. Gooley; Gregory W. Moseley; Yukihiko Sugita; Toyoyuki Ose
  Science Signaling, 18, 878, American Association for the Advancement of Science (AAAS), 18 Mar. 2025
  Scientific journal, Signal transducer and activator of transcription (STAT) family members mediate signaling in the Janus kinase (JAK)–STAT pathway and are activated by phosphorylation at a conserved tyrosine residue, resulting in dimerization through reciprocal interactions between the phosphotyrosine and a Src homology 2 (SH2) domain. Tyrosine-phosphorylated STAT (pY-STAT) then translocates to the nucleus to induce the expression of genes encoding antiviral proteins. Although the active and functional forms of STATs are conventionally considered to be dimers, STATs can undergo higher-order oligomerization, which is implicated in regulating transcriptional activity. We present the cryo–electron microscopy (cryo-EM) structure of the tetrameric form of intact pY-STAT1 in complex with DNA, which indicates that interactions between the amino-terminal domains (NTDs) of STAT1 induce oligomerization. The tetrameric structure revealed a compact conformation with a previously uncharacterized binding interface: Two DNA-bound dimers are twofold symmetrically aligned to transform into a tandem DNA-binding model without NTD dimer separation. Moreover, biochemical analyses indicated that the rabies virus P-protein selectively targeted tetrameric pY-STAT1. Combined with data showing which regions contribute to the interaction between pY-STAT1 and the P-protein, we constructed a binding model explaining how P recognizes the pY-STAT1 tetramer. These data provide insight into how pathogenic viruses target signaling pathways that mediate the host immune response.
• The strategy used by naïve anti-PEG antibodies to capture flexible and featureless PEG chains.
  Yiwei Liu; Takahiro Mori; Yusei Ito; Kimiko Kuroki; Seiichiro Hayashi; Daisuke Kohda; Taro Shimizu; Tatsuhiro Ishida; Steve R Roffler; Mika K Kaneko; Yukinari Kato; Takao Arimori; Takamasa Teramoto; Kazuhiro Takemura; Kenta Ishibashi; Yoshiki Katayama; Katsumi Maenaka; Yoshimitsu Kakuta; Akio Kitao; Takeshi Mori
  Journal of controlled release : official journal of the Controlled Release Society, 380, 396, 403, 10 Feb. 2025, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Polyethylene glycol (PEG) is widely used as a standard stealth polymer, although the induction of anti-PEG antibodies and consequent effects have drawn attention in recent years. To date, several anti-PEG antibodies induced by PEG-modified proteins via the T cell-dependent (TD) pathway, in which affinity maturation occurs, have been reported. In contrast, structures of the naïve anti-PEG antibodies before affinity maturation have not been described in the literature. Here, to understand the details of the naïve anti-PEG antibodies capturing PEG, we studied a naïve anti-PEG antibody induced by a PEG-modified liposome in the absence of affinity maturation via the T cell-independent (TI) pathway. The mutation levels, structures as well as in vitro and in silico binding properties of TI and TD anti-PEG antibodies were compared. The TI anti-PEG antibody showed no mutation and a low binding affinity toward PEG, meanwhile, it allowed PEG chain sliding and weak interaction with the terminal group. Furthermore, the naïve anti-PEG antibodies may obtain high affinities by forming tunnel structures via minimal mutations. This research provides new insights into polymer-antibody interactions, which can facilitate the development of novel stealth polymers that can avoid antibody induction.
• Enhanced effect of the immunosuppressive soluble HLA-G2 homodimer by site-specific PEGylation.
  Chisato Yamada; Kimiko Kuroki; Naoyoshi Maeda; Hiroshi Watanabe; Ami Takahashi; Katsumi Maenaka
  Scientific reports, 15, 1, 2509, 2509, 20 Jan. 2025, [International Magazine]
  English, Scientific journal, Human leukocyte antigen (HLA)-G is a nonclassical HLA class I molecule that has an immunosuppressive effect mediated by binding to immune inhibitory leukocyte immunoglobulin-like receptors (LILR) B1 and LILRB2. A conventional HLA-G isoform, HLA-G1, forms a heterotrimeric complex composed of a heavy chain (α1-α3 domains), β2-microglobulin (β2m) and a cognate peptide. One of the other isoforms, HLA-G2, lacks a α2 domain or β2m to form a nondisulfide-linked homodimer, and its ectodomain specifically binds to LILRB2 expressed in human monocytes, macrophages, and dendritic cells. The administration of the ectodomain of HLA-G2, designated the soluble HLA-G2 homodimer, showed significant immunosuppressive effects in mouse models of rheumatoid arthritis and systemic lupus erythematosus, presumably by binding to a mouse ortholog of LILRB2, paired immunoglobulin-like receptor B. However, the refolded soluble HLA-G2 homodimer used in these studies tends to aggregate and degrade; thus, its stability for clinical use has been a concern. In the present study, we improved the stability of the refolded soluble HLA-G2 homodimer via a site-directed PEGylation method. PEGylation at an original free cysteine residue, Cys42, resulted in increased lyophilization and thermal and serum stability. Furthermore, the PEGylated soluble HLA-G2 homodimer could better suppress atopic symptoms in mice than the non-PEGylated homodimer. These results suggest that PEGylated soluble HLA-G2 homodimers could be candidates for immunosuppressive biologics that specifically target LILRB2-positive myelomonocytic antigen-presenting cells.
• Japan–Korea collaboration on biophysical techniques for drug discovery in infectious diseases: Toward future pandemic preparedness
  Katsumi Maenaka
  Biophysics and Physicobiology, 2025
  Scientific journal
• X-206 exhibits broad-spectrum anti-β-coronavirus activity, covering SARS-CoV-2 variants and drug-resistant isolates.
  Jiei Sasaki; Akihiko Sato; Michihito Sasaki; Iori Okabe; Kota Kodama; Satoko Otsuguro; Kosuke Yasuda; Hirotatsu Kojima; Yasuko Orba; Hirofumi Sawa; Katsumi Maenaka; Yusuke Yanagi; Takao Hashiguchi
  Antiviral research, 106039, 106039, 19 Nov. 2024, [International Magazine]
  English, Scientific journal, Coronaviruses such as the Middle East respiratory syndrome coronavirus (MERS-CoV), severe acute respiratory syndrome coronavirus (SARS-CoV), and SARS-CoV-2, causing MERS, SARS, and Coronavirus disease-19, respectively, are highly pathogenic to humans. Notably, several antiviral drugs against SARS-CoV-2, such as nirmatrelvir and remdesivir, have been approved. However, no approved vaccines or antiviral agents are available for other highly pathogenic β-coronaviruses. In this study, we identified two compounds, thapsigargin and X-206, that exhibit antiviral activities against SARS-CoV, MERS-CoV, and SARS-CoV-2. Notably, both compounds effectively inhibited the cell-to-cell fusion mediated by the Spike proteins of all three β-coronaviruses. X-206 exhibited antiviral activity against nirmatrelvir- and remdesivir-resistant SARS-CoV-2 isolates and SARS-CoV-2 variants, including Delta, BA.5, and XBB.1. Consequently, the mechanism of action of these compounds with anti-β-coronavirus activities may differ from that of the approved direct-acting drugs for SARS-CoV-2, thereby offering potential use as a cocktail with other antivirals, and serving as a chemical basis for developing therapeutic agents against β-coronaviruses in preparation for the next spillover and pandemic.
• Structural basis for receptor-binding domain mobility of the spike in SARS-CoV-2 BA.2.86 and JN.1
  Hisano Yajima; Yuki Anraku; Yu Kaku; Kanako Terakado Kimura; Arnon Plianchaisuk; Kaho Okumura; Yoshiko Nakada-Nakura; Yusuke Atarashi; Takuya Hemmi; Daisuke Kuroda; Yoshimasa Takahashi; Shunsuke Kita; Jiei Sasaki; Hiromi Sumita; Keita Matsuno; Naganori Nao; Hirofumi Sawa; Keita Mizuma; Jingshu Li; Izumi Kida; Yume Mimura; Yuma Ohari; Shinya Tanaka; Masumi Tsuda; Lei Wang; Yoshikata Oda; Zannatul Ferdous; Kenji Shishido; Hiromi Mohri; Miki Iida; Takasuke Fukuhara; Tomokazu Tamura; Rigel Suzuki; Saori Suzuki; Shuhei Tsujino; Hayato Ito; Naoko Misawa; Ziyi Guo; Alfredo A. Hinay; Kaoru Usui; Wilaiporn Saikruang; Spyridon Lytras; Keiya Uriu; Ryo Yoshimura; Shusuke Kawakubo; Luca Nishumura; Yusuke Kosugi; Shigeru Fujita; Jarel Elgin M.Tolentino; Luo Chen; Lin Pan; Wenye Li; Maximilian Stanley Yo; Kio Horinaka; Mai Suganami; Mika Chiba; Kyoko Yasuda; Keiko Iida; Adam Patrick Strange; Naomi Ohsumi; Shiho Tanaka; Eiko Ogawa; Tsuki Fukuda; Rina Osujo; Kazuhisa Yoshimura; Kenji Sadamas; Mami Nagashima; Hiroyuki Asakura; Isao Yoshida; So Nakagawa; Kazuo Takayama; Rina Hashimoto; Sayaka Deguchi; Yukio Watanabe; Yoshitaka Nakata; Hiroki Futatsusako; Ayaka Sakamoto; Naoko Yasuhara; Tateki Suzuki; Yukari Nakajima; Takashi Irie; Ryoko Kawabata; Kaori Sasaki-Tabata; Terumasa Ikeda; Hesham Nasser; Ryo Shimizu; M. S. T. Monira Begum; Michael Jonathan; Yuka Mugita; Sharee Leong; Otowa Takahashi; Takamasa Ueno; Chihiro Motozono; Mako Toyoda; Akatsuki Saito; Anon Kosaka; Miki Kawano; Natsumi Matsubara; Tomoko Nishiuchi; Jiri Zahradnik; Prokopios Andrikopoulos; Miguel Padilla-Blanco; Aditi Konar; Jumpei Ito; Katsumi Maenaka; Kei Sato; Takao Hashiguchi
  Nature Communications, 15, 1, Springer Science and Business Media LLC, 07 Oct. 2024
  English, Scientific journal, Since 2019, SARS-CoV-2 has undergone mutations, resulting in pandemic and epidemic waves. The SARS-CoV-2 spike protein, crucial for cellular entry, binds to the ACE2 receptor exclusively when its receptor-binding domain (RBD) adopts the up-conformation. However, whether ACE2 also interacts with the RBD in the down-conformation to facilitate the conformational shift to RBD-up remains unclear. Herein, we present the structures of the BA.2.86 and the JN.1 spike proteins bound to ACE2. Notably, we successfully observed the ACE2-bound down-RBD, indicating an intermediate structure before the RBD-up conformation. The wider and mobile angle of RBDs in the up-state provides space for ACE2 to interact with the down-RBD, facilitating the transition to the RBD-up state. The K356T, but not N354-linked glycan, contributes to both of infectivity and neutralizing-antibody evasion in BA.2.86. These structural insights the spike-protein dynamics would help understand the mechanisms underlying SARS-CoV-2 infection and its neutralization.
• Identification of BAY61-3606 Derivatives With Improved Activity in Splicing Modulation That Induces Inclusion of Cassette Exons Similar to the Splicing Factor 3B Subunit 1 Mutation.
  Takanori Matsumaru; Toshiki Iwamatsu; Kana Ishigami; Makoto Inai; Wataru Kanto; Ayumi Ishigaki; Atsushi Toyoda; Satoshi Shuto; Katsumi Maenaka; Shinichi Nakagawa; Hiroshi Maita
  Chemical biology & drug design, 104, 4, e70002, Oct. 2024, [International Magazine]
  English, Scientific journal, Splicing modulation by a small compound offers therapeutic potential for diseases caused by splicing abnormality. However, only a few classes of compounds that can modulate splicing have been identified. We previously identified BAY61-3606, a multiple kinase inhibitor, as a compound that relaxes the splicing fidelity at the 3' splice site recognition. We have also reported the synthesis of derivatives of BAY61-3606. In this study, we tested those compounds for their splicing modulation capabilities and identified two contrasting compounds. These compounds were further investigated for their effects on the whole transcriptome, and analysis of changes in transcription and splicing revealed that the highly active derivative in the splicing reporter assay also showed significantly higher activity in modulating the splicing of endogenously expressed genes. Particularly, cassette exon inclusion was highly upregulated by this compound, and clustering analysis revealed that these effects resembled those in splicing factor 3b subunit 1 (SF3B1) K700E mutant cells but contrasted with those of the splicing inhibitor H3B-8800. Additionally, a group of serine/arginine-rich (SR) protein genes was identified as representatively affected, likely via modulation of poison exon inclusion. This finding could guide further analysis of the mode of action of these compounds on splicing, which could be valuable for developing drugs for diseases associated with splicing abnormalities.
• Molecular and structural insights into SARS-CoV-2 evolution: from BA.2 to XBB subvariants.
  Hisano Yajima; Tomo Nomai; Kaho Okumura; Katsumi Maenaka; Jumpei Ito; Takao Hashiguchi; Kei Sato
  mBio, e0322023, 16 Sep. 2024, [International Magazine]
  English, Scientific journal, Due to the incessant emergence of various SARS-CoV-2 variants with enhanced fitness in the human population, controlling the COVID-19 pandemic has been challenging. Understanding how the virus enhances its fitness during a pandemic could offer valuable insights for more effective control of viral epidemics. In this manuscript, we review the evolution of SARS-CoV-2 from early 2022 to the end of 2023-from Omicron BA.2 to XBB descendants. Focusing on viral evolution during this period, we provide concrete examples that SARS-CoV-2 has increased its fitness by enhancing several functions of the spike (S) protein, including its binding affinity to the ACE2 receptor and its ability to evade humoral immunity. Furthermore, we explore how specific mutations modify these functions of the S protein through structural alterations. This review provides evolutionary, molecular, and structural insights into how SARS-CoV-2 has increased its fitness and repeatedly caused epidemic surges during the pandemic.
• Chlamydia trachomatis L2 434/Bu readily activates glycolysis under hypoxia for efficient metabolism.
  Ruiyu Li; Saicheng Zhang; Satoko Otsuguro; Manabu Nagao; Akira Matsuda; Jeewan Thapa; Torahiko Okubo; Katsumi Maenaka; Hideaki Higashi; Hiroyuki Yamaguchi
  Biochemical and biophysical research communications, 736, 150461, 150461, 06 Aug. 2024, [International Magazine]
  English, Scientific journal, To understand why Chlamydia trachomatis (Ct) (L2/434/Bu) favors hypoxia, we examined the dynamics of infected cells using a glycolysis-related PCR array and metabolomic analysis, along with the perturbation of nucleotide synthesis. Our findings revealed that, compared to normoxia, hypoxia with infection significantly and selectively upregulates the expression of genes related to glycolysis, glycogen degradation, and the pentose phosphate pathway. Furthermore, hypoxia induced a significant decrease in metabolite levels, particularly methionine-related metabolites, independent of infection, indicating efficient metabolism under hypoxia. Additionally, the perturbation of nucleotide synthesis with adenosine derivatives impaired Ct growth. Collectively, our results suggest that Ct favors a hypoxic environment with efficient metabolism, in which Ct readily activates glycolysis responsible for stable nucleotide synthesis as well as ATP supply.
• Glycan-shielded homodimer structure and dynamical features of the canine distemper virus hemagglutinin relevant for viral entry and efficient vaccination.
  Hideo Fukuhara; Kohei Yumoto; Miyuki Sako; Mizuho Kajikawa; Toyoyuki Ose; Mihiro Kawamura; Mei Yoda; Surui Chen; Yuri Ito; Shin Takeda; Mwila Mwaba; Jiaqi Wang; Takao Hashiguchi; Jun Kamishikiryo; Nobuo Maita; Chihiro Kitatsuji; Makoto Takeda; Kimiko Kuroki; Katsumi Maenaka
  eLife, 12, 24 Jul. 2024, [International Magazine]
  English, Scientific journal, Canine distemper virus (CDV) belongs to morbillivirus, including measles virus (MeV) and rinderpest virus, which causes serious immunological and neurological disorders in carnivores, including dogs and rhesus monkeys, as recently reported, but their vaccines are highly effective. The attachment glycoprotein hemagglutinin (CDV-H) at the CDV surface utilizes signaling lymphocyte activation molecule (SLAM) and Nectin-4 (also called poliovirus-receptor-like-4; PVRL4) as entry receptors. Although fusion models have been proposed, the molecular mechanism of morbillivirus fusion entry is poorly understood. Here, we determined the crystal structure of the globular head domain of CDV-H vaccine strain at 3.2 Å resolution, revealing that CDV-H exhibits a highly tilted homodimeric form with a six-bladed β-propeller fold. While the predicted Nectin-4-binding site is well conserved with that of MeV-H, that of SLAM is similar but partially different, which is expected to contribute to host specificity. Five N-linked sugars covered a broad area of the CDV-H surface to expose receptor-binding sites only, supporting the effective production of neutralizing antibodies. These features are common to MeV-H, although the glycosylation sites are completely different. Furthermore, real-time observation using high-speed atomic force microscopy revealed highly mobile features of the CDV-H dimeric head via the connector region. These results suggest that sugar-shielded tilted homodimeric structure and dynamic conformational changes are common characteristics of morbilliviruses and ensure effective fusion entry and vaccination.
• Thermostability and binding properties of single-chained Fv fragments derived from therapeutic antibodies.
  Takashi Tadokoro; Harumi Tsuboi; Kota Nakamura; Tetsushi Hayakawa; Reo Ohmura; Izumi Kato; Masaki Inoue; Shin-Ichi Tsunoda; Sayaka Niizuma; Yukari Okada; Satoko Otsuguro; Katsumi Maenaka
  Protein science : a publication of the Protein Society, 33, 7, e5084, Jul. 2024, [International Magazine]
  English, Scientific journal, Small antibody fragments have recently been used as alternatives to full-length monoclonal antibodies in therapeutic applications. One of the most popular fragment antibodies is single-chain fragment variables (scFvs), consisting of variable heavy (VH) and variable light (VL) domains linked by a flexible peptide linker. scFvs have small molecular sizes, which enables good tissue penetration and low immunogenicity. Despite these advantages, the use of scFvs, especially for therapeutic purpose, is still limited because of the difficulty to regulate the binding activity and conformational stability. In this study, we constructed and analyzed 10 scFv fragments derived from 10 representatives of FDA-approved mAbs to evaluate their physicochemical properties. Differential scanning calorimetry analysis showed that scFvs exhibited relatively high but varied thermostability, from 50 to 70°C of melting temperatures, and different unfolding cooperativity. Surface plasmon resonance analysis revealed that scFvs fragments that exhibit high stability and cooperative unfolding likely tend to maintain antigen binding. This study demonstrated the comprehensive physicochemical properties of scFvs derived from FDA-approved antibodies, providing insights into antibody design and development.
• Protocol to identify the ligand binding site of Mincle using NMR spectroscopy.
  Atsushi Furukawa; Hiroyuki Kumeta; Takashi Saitoh; Katsumi Maenaka
  STAR protocols, 5, 2, 102996, 102996, 03 Apr. 2024, [International Magazine]
  English, Scientific journal, Mincle (macrophage-inducible C-type lectin, CLEC4E) is a C-type lectin immune-stimulatory receptor that can be targeted for inducing potent adjuvant effects. Mincle can recognize trehalose dimycolate and related glycolipids. Here, we present a protocol to identify the ligand binding mode of Mincle. We describe steps for preparing labeled Mincle ectodomain, data acquisition, and analysis of nuclear magnetic resonance experiments using non-detergent sulfobetaine-195. This protocol can be applied to other protein-ligand interactions that have aggregation problems for complex formation. For complete details on the use and execution of this protocol, please refer to Furukawa et al.1.
• A triggering structure of SARS-CoV-2 BA.2.86 spike upon ACE2 binding for receptor-binding domain up
  Takao Hashiguchi; Hisano Yajima; Yuki Anraku; Yu Kaku; Kanako Kimura; Arnon Plianchaisuk; Kaho Okumura; Yoshiko Nakada-Nakura; Shunsuke Kita; Jiei Sasaki; Hiromi Sumita; Jumpei Ito; Katsumi Maenaka; Kei Sato
  22 Mar. 2024
• Rational in silico design identifies two mutations that restore UT28K SARS-CoV-2 monoclonal antibody activity against Omicron BA.1.
  Tatsuhiko Ozawa; Yoshiki Ikeda; Liuan Chen; Rigel Suzuki; Atsushi Hoshino; Akira Noguchi; Shunsuke Kita; Yuki Anraku; Emiko Igarashi; Yumiko Saga; Noriko Inasaki; Shunta Taminishi; Jiei Sasaki; Yuhei Kirita; Hideo Fukuhara; Katsumi Maenaka; Takao Hashiguchi; Takasuke Fukuhara; Kenichi Hirabayashi; Hideki Tani; Hiroyuki Kishi; Hideki Niimi
  Structure (London, England : 1993), 32, 3, 263, 272, Elsevier BV, 07 Mar. 2024, [International Magazine]
  English, Scientific journal, SARS-CoV-2 rapidly mutates and acquires resistance to neutralizing antibodies. We report an in-silico-designed antibody that restores the neutralizing activity of a neutralizing antibody. Our previously generated antibody, UT28K, exhibited broad neutralizing activity against mutant variants; however, its efficacy against Omicron BA.1 was compromised by the mutation. Using previously determined structural information, we designed a modified-UT28K (VH T28R/N57D), UT28K-RD targeting the mutation site. In vitro and in vivo experiments demonstrated the efficacy of UT28K-RD in neutralizing Omicron BA.1. Although the experimentally determined structure partially differed from the predicted model, our study serves as a successful case of antibody design, wherein the predicted amino acid substitution enhanced the recognition of the previously elusive Omicron BA.1. We anticipate that numerous similar cases will be reported, showcasing the potential of this approach for improving protein-protein interactions. Our findings will contribute to the development of novel therapeutic strategies for highly mutable viruses, such as SARS-CoV-2.
• Virological characteristics of the SARS-CoV-2 Omicron XBB.1.5 variant.
  Tomokazu Tamura; Takashi Irie; Sayaka Deguchi; Hisano Yajima; Masumi Tsuda; Hesham Nasser; Keita Mizuma; Arnon Plianchaisuk; Saori Suzuki; Keiya Uriu; Mst Monira Begum; Ryo Shimizu; Michael Jonathan; Rigel Suzuki; Takashi Kondo; Hayato Ito; Akifumi Kamiyama; Kumiko Yoshimatsu; Maya Shofa; Rina Hashimoto; Yuki Anraku; Kanako Terakado Kimura; Shunsuke Kita; Jiei Sasaki; Kaori Sasaki-Tabata; Katsumi Maenaka; Naganori Nao; Lei Wang; Yoshitaka Oda; Terumasa Ikeda; Akatsuki Saito; Keita Matsuno; Jumpei Ito; Shinya Tanaka; Kei Sato; Takao Hashiguchi; Kazuo Takayama; Takasuke Fukuhara
  Nature communications, 15, 1, 1176, 1176, 08 Feb. 2024, [International Magazine]
  English, Scientific journal, Circulation of SARS-CoV-2 Omicron XBB has resulted in the emergence of XBB.1.5, a new Variant of Interest. Our phylogenetic analysis suggests that XBB.1.5 evolved from XBB.1 by acquiring the S486P spike (S) mutation, subsequent to the acquisition of a nonsense mutation in ORF8. Neutralization assays showed similar abilities of immune escape between XBB.1.5 and XBB.1. We determine the structural basis for the interaction between human ACE2 and the S protein of XBB.1.5, showing similar overall structures between the S proteins of XBB.1 and XBB.1.5. We provide the intrinsic pathogenicity of XBB.1 and XBB.1.5 in hamsters. Importantly, we find that the ORF8 nonsense mutation of XBB.1.5 resulted in impairment of MHC suppression. In vivo experiments using recombinant viruses reveal that the XBB.1.5 mutations are involved with reduced virulence of XBB.1.5. Together, our study identifies the two viral functions defined the difference between XBB.1 and XBB.1.5.
• [Challenges Facing Middle Molecule Drug Discovery and How to Overcome Them].
  Hiroyuki Miyachi; Katsumi Maenaka
  Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan, 144, 5, 527, 528, The Pharmaceutical Society of Japan, 2024, [Domestic magazines]
  Japanese, Scientific journal
• [Development of Integrated Database for Experiments and Simulations].
  Issaku Yamada; Naoki Kimura; Takao Nomura; Satoko Otsuguro; Hiroyuki Miyachi; Yasuteru Shigeta; Katsumi Maenaka
  Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan, 144, 5, 539, 543, The Pharmaceutical Society of Japan, 2024, [Domestic magazines]
  Japanese, Scientific journal, Researchers collect data and use various methods to organize it. Ensuring the reliability and reproducibility of data is crucial, and collaboration across different research fields is on the rise. However, when there is geographical distance, sharing data becomes a challenging task. Therefore, there is a need for the development of a mechanism for sharing data on the web. We have developed an integrated database to facilitate the sharing and management of research data, particularly focusing on small molecules. The integrated database serves as a platform for centralizing data related to small molecules, including their chemical structures, wet lab experimental data, simulation data, and more. It has been constructed as a web application, offering features such as library management for small molecules, registration and viewing of wet lab experiment results, generation of initial conformations for simulations, and data visualization. This enables researchers to efficiently share their research data and collaborate seamlessly, whether within their research group or via cloud-based access that allows project and team members to connect from anywhere. This integrated database plays a critical role in connecting wet lab experiments and simulations, enabling researchers to cross-reference and analyze experimental data comprehensively. It serves as an essential tool to advance research and foster idea generation.
• The human immune checkpoint molecule, HLA-G2, induces tolerance in monocytes and dendritic cells via upregulation of PD-L1
  Ami Takahashi; Kimiko Kuroki; Naoyoshi Maeda; Mie Nieda; Katsumi Maenaka
  18 Oct. 2023
• 2-thiouridine is a broad-spectrum antiviral nucleoside analogue against positive-strand RNA viruses.
  Kentaro Uemura; Haruaki Nobori; Akihiko Sato; Shinsuke Toba; Shinji Kusakabe; Michihito Sasaki; Koshiro Tabata; Keita Matsuno; Naoyoshi Maeda; Shiori Ito; Mayu Tanaka; Yuki Anraku; Shunsuke Kita; Mayumi Ishii; Kayoko Kanamitsu; Yasuko Orba; Yoshiharu Matsuura; William W Hall; Hirofumi Sawa; Hiroshi Kida; Akira Matsuda; Katsumi Maenaka
  Proceedings of the National Academy of Sciences of the United States of America, 120, 42, e2304139120, 17 Oct. 2023, [International Magazine]
  English, Scientific journal, Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infections are causing significant morbidity and mortality worldwide. Furthermore, over 1 million cases of newly emerging or re-emerging viral infections, specifically dengue virus (DENV), are known to occur annually. Because no virus-specific and fully effective treatments against these or many other viruses have been approved, there is an urgent need for novel, effective therapeutic agents. Here, we identified 2-thiouridine (s2U) as a broad-spectrum antiviral ribonucleoside analogue that exhibited antiviral activity against several positive-sense single-stranded RNA (ssRNA+) viruses, such as DENV, SARS-CoV-2, and its variants of concern, including the currently circulating Omicron subvariants. s2U inhibits RNA synthesis catalyzed by viral RNA-dependent RNA polymerase, thereby reducing viral RNA replication, which improved the survival rate of mice infected with DENV2 or SARS-CoV-2 in our animal models. Our findings demonstrate that s2U is a potential broad-spectrum antiviral agent not only against DENV and SARS-CoV-2 but other ssRNA+ viruses.
• Unprecedented spike flexibility revealed by BSL3 Cryo-ET of active SARS-CoV-2 virions
  Hideo Fukuhara; Hisham M. Dokainish; Shunsuke Kita; Koshiro Tabata; Akira Takasu; Juha T. Huiskonen; Yuki Anraku; Toshiya Senda; David I. Stuart; Michihito Sasaki; Yasuko Orba; Yasuhiko Suzuki; Hirofumi Sawa; Katsumi Maenaka
  11 Oct. 2023
• Beneficial effects of a new neuroprotective compound in neuronal cells and MPTP-administered mouse model of Parkinson's disease.
  Izumi Kato; Yudai Ogawa; Fumika Yakushiji; Jiro Ogura; Masaki Kobayashi; Naoya Shindo; Satoshi Ichikawa; Katsumi Maenaka; Masahiro Sakaitani
  Chemical communications (Cambridge, England), 59, 82, 12306, 12309, 27 Sep. 2023, [International Magazine]
  English, Scientific journal, A new compound, a derivative of 3,4,5-trimethoxy-N-phenyl benzamide bearing an 8''-methylimidazopyridine moiety, is found to demonstrate neuroprotective effects by preventing cell death caused by oxidative stress. The compound possesses high solubility and metabolic stability, and inhibits MPTP-induced effects in vivo, indicating high potential as a therapeutic drug for Parkinson's disease.
• Protein kinase Cβ is involved in cigarette smoke gas phase-induced ferroptosis in J774 macrophages.
  Tsunehito Higashi; Haruka Handa; Yosuke Mai; Katsumi Maenaka; Takashi Tadokoro
  Journal of pharmacological sciences, 153, 1, 22, 25, Sep. 2023, [Domestic magazines]
  English, Scientific journal, Cigarette smoking is a risk factor for respiratory infection caused by immune cell dysfunction. Cigarette smoke is divided into tar and gas phases. Although the gas phase induces cell death in various cell types, the mechanism for gas phase-induced cell death remains to be clarified. In this study, we have examined the effects of cigarette smoke gas phase on J774 macrophages. Cigarette smoke gas phase and cytotoxic factors in the gas phase induced protein kinase C (PKC)-dependent ferroptosis. Pharmacological studies using isoform-specific PKC inhibitors have revealed that PKCβ is involved in cigarette smoke gas phase-induced ferroptosis in J774 macrophages.
• Structural delineation and computational design of SARS-CoV-2-neutralizing antibodies against Omicron subvariants.
  Saya Moriyama; Yuki Anraku; Shunta Taminishi; Yu Adachi; Daisuke Kuroda; Shunsuke Kita; Yusuke Higuchi; Yuhei Kirita; Ryutaro Kotaki; Keisuke Tonouchi; Kohei Yumoto; Tateki Suzuki; Taiyou Someya; Hideo Fukuhara; Yudai Kuroda; Tsukasa Yamamoto; Taishi Onodera; Shuetsu Fukushi; Ken Maeda; Fukumi Nakamura-Uchiyama; Takao Hashiguchi; Atsushi Hoshino; Katsumi Maenaka; Yoshimasa Takahashi
  Nature communications, 14, 1, 4198, 4198, 14 Jul. 2023, [Peer-reviewed], [International Magazine]
  English, Scientific journal, SARS-CoV-2 Omicron subvariants have evolved to evade receptor-binding site (RBS) antibodies that exist in diverse individuals as public antibody clones. We rationally selected RBS antibodies resilient to mutations in emerging Omicron subvariants. Y489 was identified as a site of virus vulnerability and a common footprint of broadly neutralizing antibodies against the subvariants. Multiple Y489-binding antibodies were encoded by public clonotypes and additionally recognized F486, potentially accounting for the emergence of Omicron subvariants harboring the F486V mutation. However, a subclass of antibodies broadly neutralized BA.4/BA.5 variants via hydrophobic binding sites of rare clonotypes along with high mutation-resilience under escape mutation screening. A computationally designed antibody based on one of the Y489-binding antibodies, NIV-10/FD03, was able to bind XBB with any 486 mutation and neutralized XBB.1.5. The structural basis for the mutation-resilience of this Y489-binding antibody group may provide important insights into the design of therapeutics resistant to viral escape.
• Structural basis for plastic glycolipid recognition of the C-type lectin Mincle
  Atsushi Furukawa; Yusuke Shuchi; Jiaqi Wang; Pablo Adrian Guillen-Poza; Shigenari Ishizuka; Misuzu Kagoshima; Risa Ikeno; Hiroyuki Kumeta; Sho Yamasaki; Takanori Matsumaru; Takashi Saitoh; Katsumi Maenaka
  Structure, 31, 9, 1077, 1085, Elsevier BV, Jun. 2023, [International Magazine]
  English, Scientific journal, Mincle (macrophage-inducible C-type lectin, CLEC4E) is a C-type lectin immune-stimulatory receptor for cord factor, trehalose dimycolate (TDM), which serves as a potent component of adjuvants. The recognition of glycolipids by Mincle, especially their lipid parts, is poorly understood. Here, we performed nuclear magnetic resonance analysis, revealing that titration of trehalose harboring a linear short acyl chain showed a chemical shift perturbation of hydrophobic residues next to the Ca-binding site. Notably, there were split signals for Tyr201 upon complex formation, indicating two binding modes for the acyl chain. In addition, most Mincle residues close to the Ca-binding site showed no observable signals, suggesting their mobility on an ∼ ms scale even after complex formation. Mutagenesis study supported two putative lipid-binding modes for branched acyl-chain TDM binding. These results provide novel insights into the plastic-binding modes of Mincle toward a wide range of glycol- and glycerol-lipids, important for rational adjuvant development.
• Virological characteristics of the SARS-CoV-2 XBB variant derived from recombination of two Omicron subvariants.
  Tomokazu Tamura; Jumpei Ito; Keiya Uriu; Jiri Zahradnik; Izumi Kida; Yuki Anraku; Hesham Nasser; Maya Shofa; Yoshitaka Oda; Spyros Lytras; Naganori Nao; Yukari Itakura; Sayaka Deguchi; Rigel Suzuki; Lei Wang; Mst Monira Begum; Shunsuke Kita; Hisano Yajima; Jiei Sasaki; Kaori Sasaki-Tabata; Ryo Shimizu; Masumi Tsuda; Yusuke Kosugi; Shigeru Fujita; Lin Pan; Daniel Sauter; Kumiko Yoshimatsu; Saori Suzuki; Hiroyuki Asakura; Mami Nagashima; Kenji Sadamasu; Kazuhisa Yoshimura; Yuki Yamamoto; Tetsuharu Nagamoto; Gideon Schreiber; Katsumi Maenaka; Takao Hashiguchi; Terumasa Ikeda; Takasuke Fukuhara; Akatsuki Saito; Shinya Tanaka; Keita Matsuno; Kazuo Takayama; Kei Sato
  Nature communications, 14, 1, 2800, 2800, 16 May 2023, [International Magazine]
  English, Scientific journal, In late 2022, SARS-CoV-2 Omicron subvariants have become highly diversified, and XBB is spreading rapidly around the world. Our phylogenetic analyses suggested that XBB emerged through the recombination of two cocirculating BA.2 lineages, BJ.1 and BM.1.1.1 (a progeny of BA.2.75), during the summer of 2022. XBB.1 is the variant most profoundly resistant to BA.2/5 breakthrough infection sera to date and is more fusogenic than BA.2.75. The recombination breakpoint is located in the receptor-binding domain of spike, and each region of the recombinant spike confers immune evasion and increases fusogenicity. We further provide the structural basis for the interaction between XBB.1 spike and human ACE2. Finally, the intrinsic pathogenicity of XBB.1 in male hamsters is comparable to or even lower than that of BA.2.75. Our multiscale investigation provides evidence suggesting that XBB is the first observed SARS-CoV-2 variant to increase its fitness through recombination rather than substitutions.
• An Electron-Deficient CpE Iridium(III) Catalyst: Synthesis, Characterization, and Application to Ether-Directed C-H Amidation.
  Eiki Tomita; Masahiro Kojima; Yuki Nagashima; Ken Tanaka; Haruki Sugiyama; Yasutomo Segawa; Atsushi Furukawa; Katsumi Maenaka; Satoshi Maeda; Tatsuhiko Yoshino; Shigeki Matsunaga
  Angewandte Chemie (International ed. in English), 62, 21, e202301259, 14 Mar. 2023, [International Magazine]
  English, Scientific journal, The synthesis, characterization, and catalytic performance of an iridium(III) catalyst with an electron-deficient cyclopentadienyl ligand ([CpEIrI2]2) are reported. The [CpEIrI2]2 catalyst was synthesized by complexation of a precursor of the CpE ligand with [Ir(cod)OAc]2, followed by oxidation, desilylation, and removal of the COD ligand. The electron-deficient [CpEIrI2]2 catalyst enabled C-H amidation reactions assisted by a weakly coordinating ether directing group. Experimental mechanistic studies and DFT calculations suggested that the high catalytic performance of [CpEIrI2]2 is due to its electron-deficient nature, which accelerates both C-H activation and Ir(V)-nitrenoid formation.
• Ready-to-Use-Type Lyophilized Lipid Nanoparticle Formulation for the Postencapsulation of Messenger RNA.
  Hiroki Tanaka; Shinya Hagiwara; Daiki Shirane; Takuma Yamakawa; Yuka Sato; Chika Matsumoto; Kota Ishizaki; Miho Hishinuma; Katsuyuki Chida; Kasumi Sasaki; Etsuo Yonemochi; Keisuke Ueda; Kenjirou Higashi; Kunikazu Moribe; Takashi Tadokoro; Katsumi Maenaka; Sakura Taneichi; Yuta Nakai; Kota Tange; Yu Sakurai; Hidetaka Akita
  ACS nano, 17, 3, 2588, 2601, 31 Jan. 2023, [International Magazine]
  English, Scientific journal, Based on the clinical success of an in vitro transcribed mRNA (IVT-mRNA) that is encapsulated in lipid nanoparticles (mRNA-LNPs), there is a growing demand by researchers to test whether their own biological findings might be applicable for use in mRNA-based therapeutics. However, the equipment and/or know-how required for manufacturing such nanoparticles is often inaccessible. To encourage more innovation in mRNA therapeutics, a simple method for preparing mRNA-LNPs is prerequisite. In this study, we report on a method for encapsulating IVT-mRNA into LNPs by rehydrating a Ready-to-Use empty freeze-dried LNP (LNPs(RtoU)) formulation with IVT-mRNA solution followed by heating. The resulting mRNA-LNPs(RtoU) had a similar intraparticle structure compared to the mRNA-LNPs prepared by conventional microfluidic mixing. In vivo genome editing, a promising application of these types of mRNA-LNPs, was accomplished using the LNPs(RtoU) containing co-encapsulated Cas9-mRNA and a small guide RNA.
• Corrigendum: Intraocular human cytomegaloviruses of ocular diseases are distinct from those of viremia and are capable of escaping from innate and adaptive immunity by exploiting HLA-E-mediated peripheral and central tolerance(Front. Immunol., (2022), 13, (1008220), 10.3389/fimmu.2022.1008220)
  Mariko Shirane; Nobuyo Yawata; Daisuke Motooka; Kensuke Shibata; Seik Soon Khor; Yosuke Omae; Toshikatsu Kaburaki; Ryoji Yanai; Hisashi Mashimo; Satoshi Yamana; Takako Ito; Akira Hayashida; Yasuo Mori; Akihiko Numata; Yusuke Murakami; Kohta Fujiwara; Nobuyuki Ohguro; Mayumi Hosogai; Masato Akiyama; Eiichi Hasegawa; Michael Paley; Atsunobu Takeda; Katsumi Maenaka; Koichi Akashi; Wayne M. Yokoyama; Katsushi Tokunaga; Makoto Yawata; Koh Hei Sonoda
  Frontiers in Immunology, 13, 1124440, 1124440, 05 Jan. 2023, [International Magazine]
  English, Scientific journal
• Structural delineation of SARS-CoV-2 broadly neutralizing antibody to Omicron subvariants including BA.4/BA.5 and BA.2.75
  Saya Moriyama; Yuki Anraku; Shunta Taminishi; Yu Adachi; Daisuke Kuroda; Shunsuke Kita; Yusuke Higuchi; Ryutaro Kotaki; Keisuke Tonouchi; Kohei Yumoto; Tateki Suzuki; Taiyou Someya; Hideo Fukuhara; Yudai Kuroda; Tsukasa Yamamoto; Taishi Onodera; Shuetsu Fukushi; Ken Maeda; Fukumi Nakamura-Uchiyama; Takao Hashiguchi; Atsushi Hoshino; Katsumi Maenaka; Yoshimasa Takahashi
  Research Square Platform LLC, 21 Dec. 2022
  Abstract
  
  SARS-CoV-2 Omicron subvariants have evolved to evade receptor-binding site (RBS) antibodies that exist in diverse individuals as public antibody clones. We rationally selected RBS antibodies resilient to mutations in emerging Omicron subvariants. Y489 was identified as a site of virus vulnerability and a common footprint of broadly neutralizing antibodies against the subvariants. Multiple Y489-binding antibodies were encoded by public clonotypes and additionally recognized F486, potentially accounting for the emergence of Omicron subvariants harboring the F486V mutation. However, a subclass of antibodies broadly neutralized BA.4/BA.5 variants via hydrophobic binding sites of rare clonotypes along with extremely high mutation-resilience under escape mutation screening. The structural basis for mutation-resilience of this antibody group may inform the design of therapeutics resistant to viral escape.
• Dihydromaniwamycin E, a Heat-Shock Metabolite from Thermotolerant Streptomyces sp. JA74, Exhibiting Antiviral Activity against Influenza and SARS-CoV-2 Viruses.
  Shun Saito; Kayo Funayama; Wataru Kato; Mayu Okuda; Meiko Kawamoto; Teruhiko Matsubara; Toshinori Sato; Akihiko Sato; Satoko Otsuguro; Michihito Sasaki; Yasuko Orba; Hirofumi Sawa; Katsumi Maenaka; Kazutoshi Shindo; Masaya Imoto; Midori A Arai
  Journal of natural products, 85, 11, 2583, 2591, 25 Nov. 2022, [International Magazine]
  English, Scientific journal, Dihydromaniwamycin E (1), a new maniwamycin derivative featuring an azoxy moiety, has been isolated from the culture extract of thermotolerant Streptomyces sp. JA74 along with the known analogue maniwamycin E (2). Compound 1 is produced only by cultivation of strain JA74 at 45 °C, and this type of compound has been previously designated a "heat shock metabolite (HSM)" by our research group. Compound 2 is detected as a production-enhanced metabolite at high temperature. Structures of 1 and 2 are elucidated by NMR and MS spectroscopic analyses. The absolute structure of 1 is determined after the total synthesis of four stereoisomers. Though the absolute structure of 2 has been proposed to be the same as the structure of maniwamycin D, the NMR and the optical rotation value of 2 are in agreement with those of maniwamycin E. Therefore, this study proposes a structural revision of maniwamycins D and E. Compounds 1 and 2 show inhibitory activity against the influenza (H1N1) virus infection of MDCK cells, demonstrating IC50 values of 25.7 and 63.2 μM, respectively. Notably, 1 and 2 display antiviral activity against SARS-CoV-2, the causative agent of COVID-19, when used to infect 293TA and VeroE6T cells, with 1 and 2 showing IC50 values (for infection of 293TA cells) of 19.7 and 9.7 μM, respectively. The two compounds do not exhibit cytotoxicity in these cell lines at those IC50 concentrations.
• Virological characteristics of the SARS-CoV-2 Omicron BA.2.75 variant.
  Akatsuki Saito; Tomokazu Tamura; Jiri Zahradnik; Sayaka Deguchi; Koshiro Tabata; Yuki Anraku; Izumi Kimura; Jumpei Ito; Daichi Yamasoba; Hesham Nasser; Mako Toyoda; Kayoko Nagata; Keiya Uriu; Yusuke Kosugi; Shigeru Fujita; Maya Shofa; Mst Monira Begum; Ryo Shimizu; Yoshitaka Oda; Rigel Suzuki; Hayato Ito; Naganori Nao; Lei Wang; Masumi Tsuda; Kumiko Yoshimatsu; Jin Kuramochi; Shunsuke Kita; Kaori Sasaki-Tabata; Hideo Fukuhara; Katsumi Maenaka; Yuki Yamamoto; Tetsuharu Nagamoto; Hiroyuki Asakura; Mami Nagashima; Kenji Sadamasu; Kazuhisa Yoshimura; Takamasa Ueno; Gideon Schreiber; Akifumi Takaori-Kondo; Kotaro Shirakawa; Hirofumi Sawa; Takashi Irie; Takao Hashiguchi; Kazuo Takayama; Keita Matsuno; Shinya Tanaka; Terumasa Ikeda; Takasuke Fukuhara; Kei Sato
  Cell host & microbe, 30, 11, 1540, 1555, 09 Nov. 2022, [International Magazine]
  English, Scientific journal, The SARS-CoV-2 Omicron BA.2.75 variant emerged in May 2022. BA.2.75 is a BA.2 descendant but is phylogenetically distinct from BA.5, the currently predominant BA.2 descendant. Here, we show that BA.2.75 has a greater effective reproduction number and different immunogenicity profile than BA.5. We determined the sensitivity of BA.2.75 to vaccinee and convalescent sera as well as a panel of clinically available antiviral drugs and antibodies. Antiviral drugs largely retained potency, but antibody sensitivity varied depending on several key BA.2.75-specific substitutions. The BA.2.75 spike exhibited a profoundly higher affinity for its human receptor, ACE2. Additionally, the fusogenicity, growth efficiency in human alveolar epithelial cells, and intrinsic pathogenicity in hamsters of BA.2.75 were greater than those of BA.2. Our multilevel investigations suggest that BA.2.75 acquired virological properties independent of BA.5, and the potential risk of BA.2.75 to global health is greater than that of BA.5.
• Genome-wide CRISPR screens identify CD48 defining susceptibility to NK cytotoxicity in peripheral T-cell lymphomas.
  Masahiro Chiba; Joji Shimono; Takashi Ishio; Norio Takei; Kohei Kasahara; Reiki Ogasawara; Takahide Ara; Hideki Goto; Koh Izumiyama; Satoko Otsuguro; Liyanage P Perera; Hiroo Hasegawa; Michiyuki Maeda; Satoshi Hashino; Katsumi Maenaka; Takanori Teshima; Thomas A Waldmann; Yibin Yang; Masao Nakagawa
  Blood, 140, 18, 1951, 1963, 03 Nov. 2022, [International Magazine]
  English, Scientific journal, Adult T-cell leukemia/lymphoma (ATLL) is one of the aggressive peripheral T-cell neoplasms with a poor prognosis. Accumulating evidence demonstrates that escape from adaptive immunity is a hallmark of ATLL pathogenesis. However, the mechanisms by which ATLL cells evade natural killer (NK)-cell-mediated immunity have been poorly understood. Here we show that CD48 expression in ATLL cells determines the sensitivity for NK-cell-mediated cytotoxicity against ATLL cells. We performed unbiased genome-wide clustered regularly interspaced short palindromic repeat (CRISPR) screening using 2 ATLL-derived cell lines and discovered CD48 as one of the best-enriched genes whose knockout conferred resistance to YT1-NK cell line-mediated cytotoxicity. The ability of CD48-knockout ATLL cells to evade NK-cell effector function was confirmed using human primary NK cells with reduced interferon-γ (IFNγ) induction and degranulation. We found that primary ATLL cells had reduced CD48 expression along with disease progression. Furthermore, other subgroups among aggressive peripheral T-cell lymphomas (PTCLs) also expressed lower concentrations of CD48 than normal T cells, suggesting that CD48 is a key molecule in malignant T-cell evasion of NK-cell surveillance. Thus, this study demonstrates that CD48 expression is likely critical for malignant T-cell lymphoma cell regulation of NK-cell-mediated immunity and provides a rationale for future evaluation of CD48 as a molecular biomarker in NK-cell-associated immunotherapies.
• High-Throughput Screening Assay Identifies Berberine and Mubritinib as Neuroprotection Drugs for Spinal Cord Injury via Blood-Spinal Cord Barrier Protection.
  Yuki Suzuki; Shinsuke Nakagawa; Takeshi Endo; Akihito Sotome; Rufei Yuan; Tsuyoshi Asano; Satoko Otsuguro; Katsumi Maenaka; Norimasa Iwasaki; Ken Kadoya
  Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics, 19, 6, 1976, 1991, Oct. 2022, [International Magazine]
  English, Scientific journal, Because the breakdown of the blood-brain spinal cord barrier (BBSCB) worsens many central nervous system (CNS) diseases, prevention of BBSCB breakdown has been a major therapeutic target, especially for spinal cord injury (SCI). However, effective drugs that protect BBSCB function have yet to be developed. The purpose of the current study was 1) to develop a high-throughput screening assay (HTSA) to identify candidate drugs to protect BBSCB function, 2) to identify candidate drugs from existing drugs with newly developed HTSA, and 3) to examine the therapeutic effects of candidate drugs on SCI. Our HTSA included a culture of immortalized human brain endothelial cells primed with candidate drugs, stress with H2O2, and evaluation of their viability. A combination of the resazurin-based assay with 0.45 mM H2O2 qualified as a reliable HTSA. Screening of 1,570 existing drugs identified 90 drugs as hit drugs. Through a combination of reproducibility tests, exclusion of drugs inappropriate for clinical translation, and dose dependency tests, berberine, mubritinib, and pioglitazone were identified as a candidate. An in vitro BBSCB functional test revealed that berberine and mubritinib, but not pioglitazone, protected BBSCB from oxygen-glucose deprivation and reoxygenation stress. Additionally, these two drugs minimized BBSCB breakdown 1 day after cervical SCI in mice. Furthermore, berberine and mubritinib reduced neuronal loss and improved gait performance 8 weeks after SCI. Collectively, the current study established a useful HTSA to identify potential neuroprotective drugs by maintaining BBSCB function and demonstrated the neuroprotective effect of berberine and mubritinib after SCI.
• Hydrophobic Alpha-Helical Short Peptides in Overlapping Reading Frames of the Coronavirus Genome
  Takashi Okura; Kazuya Shirato; Masatoshi Kakizaki; Satoko Sugimoto; Shutoku Matsuyama; Tomohisa Tanaka; Yohei Kume; Mina Chishiki; Takashi Ono; Kohji Moriishi; Masashi Sonoyama; Mitsuaki Hosoya; Koichi Hashimoto; Katsumi Maenaka; Makoto Takeda
  Pathogens, 11, 8, 877, 877, MDPI AG, 03 Aug. 2022, [International Magazine]
  English, Scientific journal, In this study, we show that the coronavirus (CoV) genome may encode many functional hydrophobic alpha-helical peptides (HAHPs) in overlapping reading frames of major coronaviral proteins throughout the entire viral genome. These HAHPs can theoretically be expressed from non-canonical sub-genomic (sg)RNAs that are synthesized in substantial amounts in infected cells. We selected and analyzed five and six HAHPs encoded in the S gene regions of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and Middle East respiratory syndrome coronavirus (MERS-CoV), respectively. Two and three HAHPs derived from SARS-CoV-2 and MERS-CoV, respectively, specifically interacted with both the SARS-CoV-2 and MERS-CoV S proteins and inhibited their membrane fusion activity. Furthermore, one of the SARS-CoV-2 HAHPs specifically inhibited viral RNA synthesis by accumulating at the site of viral RNA synthesis. Our data show that a group of HAHPs in the coronaviral genome potentially has a regulatory role in viral propagation.
• 免疫受容体LILRA2のANGPTL6認識機構(Molecular mechanism of ANGPTL6 recognition by immune activation receptor LILRA2)
  Wang Jiaqi; Furukawa Atsushi; Yamazaki Rika; Hirayasu Kouyuki; Kadomatsu Tsuyoshi; Oike Yuichi; Arase Hisashi; Maenaka Katsumi
  生物物理, 62, Suppl.1-2, S269, S269, (一社)日本生物物理学会, Aug. 2022
  English
• 構造解析に向けたヒト免疫不全ウイルス2(HIV-2)エンベロープ糖タンパク質の調製(Preparation of human immunodeficiency virus type-2(HIV-2) envelope glycoprotein for structure analysis)
  Anraku Yuki; Kita Shunsuke; Fukuhara Hideo; Kawabata Haruka; Akiyama Takaki; Davis Simon; Furukawa Atsushi; de Silva Thushan I.; Robinson James E.; Zhao Yuguang; Jones E. Yvonne; Stuart David; Huiskonen Juha T.; Rowland-Jones Sarah; Maenaka Katsumi
  生物物理, 62, Suppl.1-2, S350, S350, (一社)日本生物物理学会, Aug. 2022
  English
• Structure of the human galanin receptor 2 bound to galanin and Gq reveals the basis of ligand specificity and how binding affects the G-protein interface.
  Yunseok Heo; Naito Ishimoto; Ye-Eun Jeon; Ji-Hye Yun; Mio Ohki; Yuki Anraku; Mina Sasaki; Shunsuke Kita; Hideo Fukuhara; Tatsuya Ikuta; Kouki Kawakami; Asuka Inoue; Katsumi Maenaka; Jeremy R H Tame; Weontae Lee; Sam-Yong Park
  PLoS biology, 20, 8, e3001714, Aug. 2022, [International Magazine]
  English, Scientific journal, Galanin is a neuropeptide expressed in the central and peripheral nervous systems, where it regulates various processes including neuroendocrine release, cognition, and nerve regeneration. Three G-protein coupled receptors (GPCRs) for galanin have been discovered, which is the focus of efforts to treat diseases including Alzheimer's disease, anxiety, and addiction. To understand the basis of the ligand preferences of the receptors and to assist structure-based drug design, we used cryo-electron microscopy (cryo-EM) to solve the molecular structure of GALR2 bound to galanin and a cognate heterotrimeric G-protein, providing a molecular view of the neuropeptide binding site. Mutant proteins were assayed to help reveal the basis of ligand specificity, and structural comparison between the activated GALR2 and inactive hβ2AR was used to relate galanin binding to the movements of transmembrane (TM) helices and the G-protein interface.
• Intraocular human cytomegaloviruses of ocular diseases are distinct from those of viremia and are capable of escaping from innate and adaptive immunity by exploiting HLA-E-mediated peripheral and central tolerance.
  Mariko Shirane; Nobuyo Yawata; Daisuke Motooka; Kensuke Shibata; Seik-Soon Khor; Yosuke Omae; Toshikatsu Kaburaki; Ryoji Yanai; Hisashi Mashimo; Satoshi Yamana; Takako Ito; Akira Hayashida; Yasuo Mori; Akihiko Numata; Yusuke Murakami; Kohta Fujiwara; Nobuyuki Ohguro; Mayumi Hosogai; Masato Akiyama; Eiichi Hasegawa; Michael Paley; Atsunobu Takeda; Katsumi Maenaka; Koichi Akashi; Wayne M Yokoyama; Katsushi Tokunaga; Makoto Yawata; Koh-Hei Sonoda
  Frontiers in immunology, 13, 1008220, 1008220, Jul. 2022, [International Magazine]
  English, Scientific journal, Human cytomegalovirus (HCMV) infections develop into CMV diseases that result in various forms of manifestations in local organs. CMV-retinitis is a form of CMV disease that develops in immunocompromised hosts with CMV-viremia after viruses in the peripheral circulation have entered the eye. In the HCMV genome, extensive diversification of the UL40 gene has produced peptide sequences that modulate NK cell effector functions when loaded onto HLA-E and are subsequently recognized by the NKG2A and NKG2C receptors. Notably, some HCMV strains carry UL40 genes that encode peptide sequences identical to the signal peptide sequences of specific HLA-A and HLA-C allotypes, which enables these CMV strains to escape HLA-E-restricted CD8⁺T cell responses. Variations in UL40 sequences have been studied mainly in the peripheral blood of CMV-viremia cases. In this study, we sought to investigate how ocular CMV disease develops from CMV infections. CMV gene sequences were compared between the intraocular fluids and peripheral blood of 77 clinical cases. UL40 signal peptide sequences were more diverse, and multiple sequences were typically present in CMV-viremia blood compared to intraocular fluid. Significantly stronger NK cell suppression was induced by UL40-derived peptides from intraocular HCMV compared to those identified only in peripheral blood. HCMV present in intraocular fluids were limited to those carrying a UL40 peptide sequence corresponding to the leader peptide sequence of the host's HLA class I, while UL40-derived peptides from HCMV found only in the peripheral blood were disparate from any HLA class I allotype. Overall, our analyses of CMV-retinitis inferred that specific HCMV strains with UL40 signal sequences matching the host's HLA signal peptide sequences were those that crossed the blood-ocular barrier to enter the intraocular space. UL40 peptide repertoires were the same in the intraocular fluids of all ocular CMV diseases, regardless of host immune status, implying that virus type is likely to be a common determinant in ocular CMV disease development. We thus propose a mechanism for ocular CMV disease development, in which particular HCMV types in the blood exploit peripheral and central HLA-E-mediated tolerance mechanisms and, thus, escape the antivirus responses of both innate and adaptive immunity.
• Identification of RPL15 60S Ribosomal Protein as a Novel Topotecan Target Protein That Correlates with DAMP Secretion and Antitumor Immune Activation.
  Shunsuke Yamada; Yuichi Kitai; Takashi Tadokoro; Runa Takahashi; Haruka Shoji; Taiga Maemoto; Marie Ishiura; Ryuta Muromoto; Jun-Ichi Kashiwakura; Ken J Ishii; Katsumi Maenaka; Taro Kawai; Tadashi Matsuda
  Journal of immunology (Baltimore, Md. : 1950), 209, 1, 171, 179, 20 Jun. 2022, [International Magazine]
  English, Scientific journal, Damage-associated molecular patterns (DAMPs) contribute to antitumor immunity during cancer chemotherapy. We previously demonstrated that topotecan (TPT), a topoisomerase I inhibitor, induces DAMP secretion from cancer cells, which activates STING-mediated antitumor immune responses. However, how TPT induces DAMP secretion in cancer cells is yet to be elucidated. Here, we identified RPL15, a 60S ribosomal protein, as a novel TPT target and showed that TPT inhibited preribosomal subunit formation via its binding to RPL15, resulting in the induction of DAMP-mediated antitumor immune activation independent of TOP1. TPT inhibits RPL15-RPL4 interactions and decreases RPL4 stability, which is recovered by CDK12 activity. RPL15 knockdown induced DAMP secretion and increased the CTL population but decreased the regulatory T cell population in a B16-F10 murine melanoma model, which sensitized B16-F10 tumors against PD-1 blockade. Our study identified a novel TPT target protein and showed that ribosomal stress is a trigger of DAMP secretion, which contributes to antitumor immunotherapy.
• Novel super-neutralizing antibody UT28K is capable of protecting against infection from a wide variety of SARS-CoV-2 variants.
  Tatsuhiko Ozawa; Hideki Tani; Yuki Anraku; Shunsuke Kita; Emiko Igarashi; Yumiko Saga; Noriko Inasaki; Hitoshi Kawasuji; Hiroshi Yamada; So-Ichiro Sasaki; Mayu Somekawa; Jiei Sasaki; Yoshihiro Hayakawa; Yoshihiro Yamamoto; Yoshitomo Morinaga; Nobuyuki Kurosawa; Masaharu Isobe; Hideo Fukuhara; Katsumi Maenaka; Takao Hashiguchi; Hiroyuki Kishi; Isao Kitajima; Shigeru Saito; Hideki Niimi
  mAbs, 14, 1, 2072455, 2072455, Jun. 2022, [International Magazine]
  English, Scientific journal, Many potent neutralizing SARS-CoV-2 antibodies have been developed and used for therapies. However, the effectiveness of many antibodies has been reduced against recently emerging SARS-CoV-2 variants, especially the Omicron variant. We identified a highly potent SARS-CoV-2 neutralizing antibody, UT28K, in COVID-19 convalescent individuals who recovered from a severe condition. UT28K showed efficacy in neutralizing SARS-CoV-2 in an in vitro assay and in vivo prophylactic treatment, and the reactivity to the Omicron strain was reduced. The structural analyses revealed that antibody UT28K Fab and SARS-CoV-2 RBD protein interactions were mainly chain-dominated antigen-antibody interactions. In addition, a mutation analysis suggested that the emergence of a UT28K neutralization-resistant SARS-CoV-2 variant was unlikely, as this variant would likely lose its competitive advantage over circulating SARS-CoV-2. Our data suggest that UT28K offers potent protection against SARS-CoV-2, including newly emerging variants.
• Low-Cost Cell-Surface-Mimic Analysis of Ligand Interactions of Biotinylated Immune Receptors Using Surface Plasmon Resonance.
  Kimiko Kuroki; Hideo Fukuhara; Takashi Tadokoro; Katsumi Maenaka
  Methods in molecular biology (Clifton, N.J.), 2421, 21, 35, Jun. 2022, [International Magazine]
  English, Scientific journal, On the immune cell surface, many immune receptors are expressed and modulate the inhibitory or activating signals to control the immune responses. Recently, some of these receptors have been categorized as immune checkpoint receptors and targeted for cancer immunity or autoimmune diseases. To analyze the weak and fast binding typical for immune receptor-ligand interactions, a real-time surface plasmon resonance (SPR) technique is useful. However, it sometimes becomes difficult to optimize the immobilization conditions and appropriate controls. Considering that receptor orientation is relevant for achieving function on the cell surface, it is important to immobilize ligand proteins using specific tags at the membrane proximal end to avoid steric hindrance and structural changes in specific binding regions. Here we introduce a sensor chip, Sensor Chip CAP (Cytiva), which enables reversible and orientation-controlled immobilization of biotinylated ligands, resulting in a significant cost-effective method. We further show preparation methods of several biotinylated immune receptor proteins for SPR analysis, which are also useful for structural and other functional analyses.
• Impact of Micropolymorphism Outside the Peptide Binding Groove in the Clinically Relevant Allele HLA-C*14 on T Cell Responses in HIV-1 Infection.
  Takayuki Chikata; Wayne Paes; Nozomi Kuse; Thomas Partridge; Hiroyuki Gatanaga; Yu Zhang; Kimiko Kuroki; Katsumi Maenaka; Nicola Ternette; Shinichi Oka; Persephone Borrow; Masafumi Takiguchi
  Journal of virology, 96, 10, e0043222, 25 May 2022, [International Magazine]
  English, Scientific journal, There is increasing evidence for the importance of human leukocyte antigen C (HLA-C)-restricted CD8+ T cells in HIV-1 control, but these responses are relatively poorly investigated. The number of HLA-C-restricted HIV-1 epitopes identified is much smaller than those of HLA-A-restricted or HLA-B-restricted ones. Here, we utilized a mass spectrometry-based approach to identify HIV-1 peptides presented by HLA-C*14:03 protective and HLA-C*14:02 nonprotective alleles. We identified 25 8- to 11-mer HLA-I-bound HIV-1 peptides from HIV-1-infected HLA-C*14:02+/14:03+ cells. Analysis of T cell responses to these peptides identified novel 6 T cell epitopes targeted in HIV-1-infected HLA-C*14:02+/14:03+ subjects. Analyses using HLA stabilization assays demonstrated that all 6 epitope peptides exhibited higher binding to and greater cell surface stabilization of HLA-C*14:02 than HLA-C*14:03. T cell response magnitudes were typically higher in HLA-C*14:02+ than HLA-C*14:03+ individuals, with responses to the Pol KM9 and Nef epitopes being significantly higher. The results show that HLA-C*14:02 can elicit stronger T cell responses to HIV-1 than HLA-C*14:03 and suggest that the single amino acid difference between these HLA-C14 subtypes at position 21, outside the peptide-binding groove, indirectly influences the stability of peptide-HLA-C*14 complexes and induction/expansion of HIV-specific T cells. Taken together with a previous finding that KIR2DL2+ NK cells recognized HLA-C*14:03+ HIV-1-infected cells more than HLA-C*14:02+ ones, the present study indicates that these HLA-C*14 subtypes differentially impact HIV-1 control by T cells and NK cells. IMPORTANCE Some human leukocyte antigen (HLA) class I alleles are associated with good clinical outcomes in HIV-1 infection and are called protective HLA alleles. Identification of T cell epitopes restricted by protective HLA alleles can give important insight into virus-immune system interactions and inform design of immune-based prophylactic/therapeutic strategies. Although epitopes restricted by many protective HLA-A/B alleles have been identified, protective HLA-C alleles are relatively understudied. Here, we identified 6 novel T cell epitopes presented by both HLA-C*14:02 (no association with protection) and HLA-C*14:03 (protective) using a mass spectrometry-based immunopeptidome profiling approach. We found that these peptides bound to and stabilized HLA-C*14:02 better than HLA-C*14:03 and observed differences in induction/expansion of epitope-specific T cell responses in HIV-infected HLA-C*14:02+ versus HLA-C*14:03+ individuals. These results enhance understanding of how the microstructural difference at position 21 between these HLA-C*14 subtypes may influence cellular immune responses involved in viral control in HIV-1 infection.
• Binding of LAG-3 to stable peptide-MHC class II limits T cell function and suppresses autoimmunity and anti-cancer immunity.
  Takumi Maruhashi; Daisuke Sugiura; Il-Mi Okazaki; Kenji Shimizu; Takeo K Maeda; Jun Ikubo; Harunori Yoshikawa; Katsumi Maenaka; Naozumi Ishimaru; Hidetaka Kosako; Tatsuya Takemoto; Taku Okazaki
  Immunity, 55, 5, 912, 924, 05 Apr. 2022, [International Magazine]
  English, Scientific journal, Lymphocyte activation gene-3 (LAG-3) is a potent inhibitory co-receptor; yet, its functional ligand remains elusive, with distinct potential ligands identified. Here, we investigated the relative contribution of potential ligands, stable peptide-MHC class II complexes (pMHCII) and fibrinogen-like protein 1 (FGL1), to LAG-3 activity in vitro and in vivo. Binding of LAG-3 to stable pMHCII but not to FGL1 induced T cell suppression in vitro. Consistently, LAG-3 mutants lacking FGL1-binding capacity but not those lacking stable pMHCII-binding capacity retained suppressive activity in vitro. Accordingly, targeted disruption of stable pMHCII- but not FGL1-binding capacity of LAG-3 in NOD mice recapitulated diabetes exacerbation by LAG-3 deficiency. Additionally, the loss of stable pMHCII-binding capacity of LAG-3 augmented anti-cancer immunity comparably with LAG-3 deficiency in C57BL/6 mice. These results identify stable pMHCII as a functional ligand of LAG-3 both in autoimmunity and anti-cancer immunity. Thus, stable pMHCII-LAG-3 interaction is a potential therapeutic target in human diseases.
• Application of Acoustic Ejection MS System to High-Throughput Screening for SARS-CoV-2 3CL Protease Inhibitors.
  Tsukasa Hasegawa; Riyo M Imamura; Tateki Suzuki; Takao Hashiguchi; Takao Nomura; Satoko Otsuguro; Katsumi Maenaka; Michihito Sasaki; Yasuko Orba; Hirofumi Sawa; Akihiko Sato; Takayoshi Okabe; Tetsuo Nagano; Hirotatsu Kojima
  Chemical & pharmaceutical bulletin, 70, 3, 199, 201, 01 Mar. 2022, [Domestic magazines]
  English, Scientific journal, MS is a powerful methodology for chemical screening to directly quantify substrates and products of enzymes, but its low throughput has been an issue. Recently, an acoustic liquid-handling apparatus (Echo®) used for rapid nano-dispensing has been coupled to a high-sensitivity mass spectrometer to create the Echo® MS system, and we applied this system to screening of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) 3CL protease inhibitors. Primary screening of 32033 chemical samples was completed in 12 h. Among the hits showing selective, dose-dependent 3CL-inhibitory activity, 8 compounds showed antiviral activity in cell-based assay.
• Synthesis and Anti-dengue Virus Activity of 5-Ethynylimidazole-4-carboxamide (EICA) Nucleotide Prodrugs.
  Motoki Nakamura; Kentaro Uemura; Noriko Saito-Tarashima; Akihiko Sato; Yasuko Orba; Hirofumi Sawa; Akira Matsuda; Katsumi Maenaka; Noriaki Minakawa
  Chemical & pharmaceutical bulletin, 70, 3, 220, 225, 01 Mar. 2022, [Domestic magazines]
  English, Scientific journal, We previously showed that 5-ethynyl-(1-β-D-ribofuranosyl)imidazole-4-carboxamide (1; EICAR) is a potent anti-dengue virus (DENV) compound but is cytotoxic to some cell lines, while its 4-thio derivative, 5-ethynyl-(4-thio-1-β-D-ribofuranosyl)imidazole-4-carboxamide (2; 4'-thioEICAR), has less cytotoxicity but also less anti-DENV activity. Based on the hypothesis that the lower anti-DENV activity of 2 is due to reduced susceptibility to phosphorylation by cellular kinase(s), we investigated whether a monophosphate prodrug of 2 can improve its activity. Here, we first prepared two types of prodrug of 1, which revealed that the S-acyl-2-thioethyl (SATE) prodrug had stronger anti-DENV activity than the aryloxyphosphoramidate (so-called ProTide) prodrug. Based on these findings, we next prepared the SATE prodrug of 4'-thioEICAR 18. As expected, the resulting 18 showed potent anti-DENV activity, which was comparable to that of 1; however, its cytotoxicity was also increased relative to 2. Our findings suggest that prodrugs of 4'-thioribonucleoside derivatives such as EICAR (1) represent an effective approach to developing potent biologically active compounds; however, the balance between antiviral activity and cytotoxicity remains to be addressed.
• Correction: Synthesis of glycerolipids containing simple linear acyl chains or aromatic rings and evaluation of their Mincle signaling activity.
  Takanori Matsumaru; Risa Ikeno; Yusuke Shuchi; Toshiki Iwamatsu; Takashi Tadokoro; Sho Yamasaki; Yukari Fujimoto; Atsushi Furukawa; Katsumi Maenaka
  Chemical communications (Cambridge, England), 58, 15, 2580, 2580, 17 Feb. 2022, [International Magazine]
  English, Correction for 'Synthesis of glycerolipids containing simple linear acyl chains or aromatic rings and evaluation of their Mincle signaling activity' by Takanori Matsumaru et al., Chem. Commun., 2019, 55, 711-714, DOI: 10.1039/C8CC07322H.
• Characterization of Single-Chain Fv Fragments of Neutralizing Antibodies to Rabies Virus Glycoprotein.
  Kohei Yumoto; Tomoaki Arisaka; Kazuma Okada; Kyosuke Aoki; Toyoyuki Ose; Tatsunori Masatani; Makoto Sugiyama; Naoto Ito; Hideo Fukuhara; Katsumi Maenaka
  Viruses, 13, 11, 19 Nov. 2021, [International Magazine]
  English, Scientific journal, Rabies has almost a 100% case-fatality rate and kills more than 59,000 people annually around the world. There is no established treatment for rabies. The rabies virus (RABV) expresses only the glycoprotein (RABVG) at the viral surface, and it is the target for the neutralizing antibodies. We previously established mouse monoclonal antibodies, 15-13 and 12-22, which showed neutralizing activity against the RABV, targeting the sequential and conformational epitopes on the RABVG, respectively. However, the molecular basis for the neutralizing activity of these antibodies is not yet fully understood. In this study, we evaluated the binding characteristics of the Fab fragments of the 15-13 and 12-22 antibodies. The recombinant RABVG protein, in prefusion form for the binding analysis, was prepared by the silkworm-baculovirus expression system. Biolayer interferometry (BLI) analysis indicated that the 15-13 Fab interacts with the RABVG, with a KD value at the nM level, and that the 12-22 Fab has a weaker binding affinity (KD ~ μM) with the RABVG compared to the 15-13 Fab. Furthermore, we determined the amino acid sequences of both the antibodies and the designed single-chain Fv fragments (scFvs) of the 15-13 and 12-22 antibodies as another potential biopharmaceutical for targeting rabies. The 15-13 and 12-22 scFvs were successfully prepared by the refolding method and were shown to interact with the RABVG at the nM level and the μM level of the KD, respectively. These binding characteristics were similar to that of each Fab. On the other hand, differential scanning fluorometry (DSF) revealed that the thermal stability of these scFvs decreases compared to their Fabs. While the improvement of the stability of scFvs will still be required, these results provide insights into the neutralizing activity and the potential therapeutic use of antibody fragments for RABV infection.
• 5-Hydroxymethyltubercidin exhibits potent antiviral activity against flaviviruses and coronaviruses, including SARS-CoV-2.
  Kentaro Uemura; Haruaki Nobori; Akihiko Sato; Takao Sanaki; Shinsuke Toba; Michihito Sasaki; Akiho Murai; Noriko Saito-Tarashima; Noriaki Minakawa; Yasuko Orba; Hiroaki Kariwa; William W Hall; Hirofumi Sawa; Akira Matsuda; Katsumi Maenaka
  iScience, 24, 10, 103120, 103120, 22 Oct. 2021, [International Magazine]
  English, Scientific journal, Newly emerging or re-emerging viral infections continue to cause significant morbidity and mortality every year worldwide, resulting in serious effects on both health and the global economy. Despite significant drug discovery research against dengue viruses (DENVs) and severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), no fully effective and specific drugs directed against these viruses have been discovered. Here, we examined the anti-DENV activity of tubercidin derivatives from a compound library from Hokkaido University and demonstrated that 5-hydroxymethyltubercidin (HMTU, HUP1108) possessed both potent anti-flavivirus and anti-coronavirus activities at submicromolar levels without significant cytotoxicity. Furthermore, HMTU inhibited viral RNA replication and specifically inhibited replication at the late stages of the SARS-CoV-2 infection process. Finally, we demonstrated that HMTU 5'-triphosphate inhibited RNA extension catalyzed by the viral RNA-dependent RNA polymerase. Our findings suggest that HMTU has the potential of serving as a lead compound for the development of a broad spectrum of antiviral agents, including SARS-CoV-2.
• A SARS-CoV-2 Antibody Broadly Neutralizes SARS-related Coronaviruses and Variants by Coordinated Recognition of a Virus Vulnerable Site
  Taishi Onodera; Shunsuke Kita; Yu Adachi; Saya Moriyama; Akihiko Sato; Takao Nomura; Shuhei Sakakibara; Takeshi Inoue; Takashi Tadokoro; Yuki Anraku; Kohei Yumoto; Cong Tian; Hideo Fukuhara; Michihito Sasaki; Yasuko Orba; Nozomi Shiwa; Naoko Iwata; Noriyo Nagata; Tateki Suzuki; Jiei Sasaki; Tsuyoshi Sekizuka; Keisuke Tonouchi; Lin Sun; Shuetsu Fukushi; Hiroyuki Satofuka; Yasuhiro Kazuki; Mitsuo Oshimura; Tomohiro Kurosaki; Makoto Kuroda; Yoshiharu Matsuura; Tadaki Suzuki; Hirofumi Sawa; Takao Hashiguchi; Katsumi Maenaka; Yoshimasa Takahashi
  Immunity, 54, 10, 2385, 2398.e10, Elsevier BV, Aug. 2021, [International Magazine]
  English, Scientific journal, Potent neutralizing SARS-CoV-2 antibodies often target the spike protein receptor-binding site (RBS), but the variability of RBS epitopes hampers broad neutralization of multiple sarbecoviruses and drifted viruses. Here, using humanized mice, we identified an RBS antibody with a germline VH gene that potently neutralized SARS-related coronaviruses, including SARS-CoV and SARS-CoV-2 variants. X-ray crystallography revealed coordinated recognition by the heavy chain of non-RBS conserved sites and the light chain of RBS with a binding angle mimicking the angiotensin-converting enzyme 2 (ACE2) receptor. The minimum footprints in the hypervariable region of RBS contributed to the breadth of neutralization, which was enhanced by immunoglobulin G3 (IgG3) class switching. The coordinated binding resulted in broad neutralization of SARS-CoV and emerging SARS-CoV-2 variants of concern. Low-dose therapeutic antibody treatment in hamsters reduced the virus titers and morbidity during SARS-CoV-2 challenge. The structural basis for broad neutralizing activity may inform the design of a broad spectrum of therapeutics and vaccines.
• Potential anti-COVID-19 agents, cepharanthine and nelfinavir, and their usage for combination treatment.
  Hirofumi Ohashi; Koichi Watashi; Wakana Saso; Kaho Shionoya; Shoya Iwanami; Takatsugu Hirokawa; Tsuyoshi Shirai; Shigehiko Kanaya; Yusuke Ito; Kwang Su Kim; Takao Nomura; Tateki Suzuki; Kazane Nishioka; Shuji Ando; Keisuke Ejima; Yoshiki Koizumi; Tomohiro Tanaka; Shin Aoki; Kouji Kuramochi; Tadaki Suzuki; Takao Hashiguchi; Katsumi Maenaka; Tetsuro Matano; Masamichi Muramatsu; Masayuki Saijo; Kazuyuki Aihara; Shingo Iwami; Makoto Takeda; Jane A McKeating; Takaji Wakita
  iScience, 24, 4, 102367, 102367, 23 Apr. 2021, [International Magazine]
  English, Scientific journal, Antiviral treatments targeting the coronavirus disease 2019 are urgently required. We screened a panel of already approved drugs in a cell culture model of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and identified two new agents having higher antiviral potentials than the drug candidates such as remdesivir and chroloquine in VeroE6/TMPRSS2 cells: the anti-inflammatory drug cepharanthine and human immunodeficiency virus protease inhibitor nelfinavir. Cepharanthine inhibited SARS-CoV-2 entry through the blocking of viral binding to target cells, while nelfinavir suppressed viral replication partly by protease inhibition. Consistent with their different modes of action, synergistic effect of this combined treatment to limit SARS-CoV-2 proliferation was highlighted. Mathematical modeling in vitro antiviral activity coupled with the calculated total drug concentrations in the lung predicts that nelfinavir will shorten the period until viral clearance by 4.9 days and the combining cepharanthine/nelfinavir enhanced their predicted efficacy. These results warrant further evaluation of the potential anti-SARS-CoV-2 activity of cepharanthine and nelfinavir.
• Nickel‐Catalyzed Acyl Group Transfer of o‐ Alkynylphenol Esters Accompanied by C−O Bond Fission for Synthesis of Benzo[ b ]furan
  Ryohei Doi; Koji Shimizu; Yuma Ikemoto; Masashi Uchiyama; Mikiko Koshiba; Atsushi Furukawa; Katsumi Maenaka; Satoshi Watanabe; Yoshihiro Sato
  ChemCatChem, 13, 8, 2086, 2092, Wiley, 21 Apr. 2021
  Scientific journal
• Structure, solubility, and permeability relationships in a diverse middle molecule library.
  Hiroyuki Miyachi; Kayoko Kanamitsu; Mayumi Ishii; Eri Watanabe; Akira Katsuyama; Satoko Otsuguro; Fumika Yakushiji; Mizuki Watanabe; Kouhei Matsui; Yukina Sato; Satoshi Shuto; Takashi Tadokoro; Shunsuke Kita; Takanori Matsumaru; Akira Matsuda; Tomoyasu Hirose; Masato Iwatsuki; Yasuteru Shigeta; Tetsuo Nagano; Hirotatsu Kojima; Satoshi Ichikawa; Toshiaki Sunazuka; Katsumi Maenaka
  Bioorganic & medicinal chemistry letters, 37, 127847, 127847, 01 Apr. 2021, [International Magazine]
  English, Scientific journal, To develop methodology to predict the potential druggability of middle molecules, we examined the structure, solubility, and permeability relationships of a diverse library (HKDL ver.1) consisting of 510 molecules (359 natural product derivatives, 76 non-natural products, 46 natural products, and 29 non-natural product derivatives). The library included peptides, depsipeptides, macrolides, and lignans, and 476 of the 510 compounds had a molecular weight in the range of 500-2000 Da. The solubility and passive diffusion velocity of the middle molecules were assessed using the parallel artificial membrane permeability assay (PAMPA). Quantitative values of solubility of 471 molecules and passive diffusion velocity of 287 molecules were obtained, and their correlations with the structural features of the molecules were examined. Based on the results, we propose a method to predict the passive diffusion characteristics of middle molecules from their three-dimensional structural features.
• The physiological TMPRSS2 inhibitor HAI-2 alleviates SARS-CoV-2 infection.
  Yuriko Tomita; Shutoku Matsuyama; Hideo Fukuhara; Katsumi Maenaka; Hiroaki Kataoka; Takao Hashiguchi; Makoto Takeda
  Journal of virology, 95, 12, 31 Mar. 2021, [International Magazine]
  English, The largest disease pandemic in modern human history caused by severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) is still ongoing.….
• Canonical versus non-canonical transsynaptic signaling of neuroligin 3 tunes development of sociality in mice.
  Tomoyuki Yoshida; Atsushi Yamagata; Ayako Imai; Juhyon Kim; Hironori Izumi; Shogo Nakashima; Tomoko Shiroshima; Asami Maeda; Shiho Iwasawa-Okamoto; Kenji Azechi; Fumina Osaka; Takashi Saitoh; Katsumi Maenaka; Takashi Shimada; Yuko Fukata; Masaki Fukata; Jumpei Matsumoto; Hisao Nishijo; Keizo Takao; Shinji Tanaka; Shigeo Okabe; Katsuhiko Tabuchi; Takeshi Uemura; Masayoshi Mishina; Hisashi Mori; Shuya Fukai
  Nature communications, 12, 1, 1848, 1848, 23 Mar. 2021, [International Magazine]
  English, Scientific journal, Neuroligin 3 (NLGN3) and neurexins (NRXNs) constitute a canonical transsynaptic cell-adhesion pair, which has been implicated in autism. In autism spectrum disorder (ASD) development of sociality can be impaired. However, the molecular mechanism underlying NLGN3-mediated social development is unclear. Here, we identify non-canonical interactions between NLGN3 and protein tyrosine phosphatase δ (PTPδ) splice variants, competing with NRXN binding. NLGN3-PTPδ complex structure revealed a splicing-dependent interaction mode and competition mechanism between PTPδ and NRXNs. Mice carrying a NLGN3 mutation that selectively impairs NLGN3-NRXN interaction show increased sociability, whereas mice where the NLGN3-PTPδ interaction is impaired exhibit impaired social behavior and enhanced motor learning, with imbalance in excitatory/inhibitory synaptic protein expressions, as reported in the Nlgn3 R451C autism model. At neuronal level, the autism-related Nlgn3 R451C mutation causes selective impairment in the non-canonical pathway. Our findings suggest that canonical and non-canonical NLGN3 pathways compete and regulate the development of sociality.
• MRC5 cells engineered to express ACE2 serve as a model system for the discovery of antivirals targeting SARS-CoV-2.
  Kentaro Uemura; Michihito Sasaki; Takao Sanaki; Shinsuke Toba; Yoshimasa Takahashi; Yasuko Orba; William W Hall; Katsumi Maenaka; Hirofumi Sawa; Akihiko Sato
  Scientific reports, 11, 1, 5376, 5376, 08 Mar. 2021, [International Magazine]
  English, Scientific journal, Although the spread of Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2) has resulted in a worldwide pandemic, there are currently no virus-specific drugs that are fully effective against SARS-CoV-2. Only a limited number of human-derived cells are capable of supporting SARS-CoV-2 replication and the infectivity of SARS-CoV-2 in these cells remains poor. In contrast, monkey-derived Vero cells are highly susceptibility to infection with SARS-CoV-2, although they are not suitable for the study of antiviral effects by small molecules due to their limited capacity to metabolize drugs compared to human-derived cells. In this study, our goal was to generate a virus-susceptible human cell line that would be useful for the identification and testing of candidate drugs. Towards this end, we stably transfected human lung-derived MRC5 cells with a lentiviral vector encoding angiotensin-converting enzyme 2 (ACE2), the cellular receptor for SARS-CoV-2. Our results revealed that SARS-CoV-2 replicates efficiently in MRC5/ACE2 cells. Furthermore, viral RNA replication and progeny virus production were significantly reduced in response to administration of the replication inhibitor, remdesivir, in MRC5/ACE2 cells compared with Vero cells. We conclude that the MRC5/ACE2 cells will be important in developing specific anti-viral therapeutics and will assist in vaccine development to combat SARS-CoV-2 infections.
• Evaluation of immunosuppressive effects of HLA-G2 in systemic lupus erythematosus model mice
  渡邊紘士; 黒木喜美子; 山田千聖; 佐分利由香里; 高橋愛実; 前田直良; 前仲勝実
  日本薬学会年会要旨集(Web), 141年会, 27V08, am09S, (公社)日本薬学会, Mar. 2021
  Japanese
• Development of novel monoclonal antibodies against immunosuppressive HLA-G2 protein
  赤岩愛記; 黒木喜美子; 引地和馬; 古川敦; 前田直良; 前仲勝実
  日本薬学会年会要旨集(Web), 141年会, 29P01, 105S, (公社)日本薬学会, Mar. 2021
  Japanese
• Enzootic nasal tumor virus type 2 envelope of goats acts as a retroviral oncogene in cell transformation.
  Naoyoshi Maeda; Yasuo Inoshima; Marcelo De Las Heras; Katsumi Maenaka
  Virus genes, 57, 1, 50, 59, Feb. 2021, [International Magazine]
  English, Scientific journal, Enzootic nasal tumor virus type 1 (ENTV-1) (ovine nasal tumor virus) and ENTV-2 (caprine nasal tumor virus) are known to be causative agents of enzootic nasal adenocarcinoma (ENA) in sheep and goats, respectively. Although the nucleotide and amino acid sequences of ENTV-1 and ENTV-2 are quite similar, they are recognized as phylogenetically distinct viruses. The envelope protein of ENTV-1 functions as an oncoprotein in the in vitro transformation of epithelial cells and fibroblasts. Thus, it is the primary determinant of in vivo tumorigenesis in ENA. As per our knowledge, no previous studies have reported in detail the role of ENTV-2 in ENA tumorigenesis. Here, in order to investigate the molecular mechanism of caprine ENA oncogenesis by ENTV-2, we have attempted to identify the transforming potential of ENTV-2 envelope, and investigated the activation of cell signaling pathways in oncogenic transformation. Our findings confirmed that ENTV-2 envelope was capable of inducing oncogenic transformation of rat cell lines in vitro. Further, we found that MAPK, Akt, and p38 were constitutively activated in ENTV-2 envelope-transformed clone cells. In addition, inhibitor experiments revealed that MEK-MAPK and PI3K-Akt signaling pathways are involved in the ENTV-2 envelope-induced cell transformation. These data indicate that ENTV-2 envelope could induce oncogenic transformation by signaling pathways that are also utilized by ENTV-1 envelope.
• SARS-CoV-2 variants with mutations at the S1/S2 cleavage site are generated in vitro during propagation in TMPRSS2-deficient cells.
  Michihito Sasaki; Kentaro Uemura; Akihiko Sato; Shinsuke Toba; Takao Sanaki; Katsumi Maenaka; William W Hall; Yasuko Orba; Hirofumi Sawa
  PLoS pathogens, 17, 1, e1009233, Jan. 2021, [International Magazine]
  English, Scientific journal, The spike (S) protein of Severe Acute Respiratory Syndrome-Coronavirus-2 (SARS-CoV-2) binds to a host cell receptor which facilitates viral entry. A polybasic motif detected at the cleavage site of the S protein has been shown to broaden the cell tropism and transmissibility of the virus. Here we examine the properties of SARS-CoV-2 variants with mutations at the S protein cleavage site that undergo inefficient proteolytic cleavage. Virus variants with S gene mutations generated smaller plaques and exhibited a more limited range of cell tropism compared to the wild-type strain. These alterations were shown to result from their inability to utilize the entry pathway involving direct fusion mediated by the host type II transmembrane serine protease, TMPRSS2. Notably, viruses with S gene mutations emerged rapidly and became the dominant SARS-CoV-2 variants in TMPRSS2-deficient cells including Vero cells. Our study demonstrated that the S protein polybasic cleavage motif is a critical factor underlying SARS-CoV-2 entry and cell tropism. As such, researchers should be alert to the possibility of de novo S gene mutations emerging in tissue-culture propagated virus strains.
• Antitumor Effect of Sugar-Modified Cytosine Nucleosides on Growth of Adult T-Cell Leukemia Cells in Mice.
  Naoyoshi Maeda; Akira Matsuda; Satoko Otsuguro; Masahiko Takahashi; Masahiro Fujii; Katsumi Maenaka
  Vaccines, 8, 4, 05 Nov. 2020, [International Magazine]
  English, Scientific journal, Adult T-cell leukemia (ATL) is a CD4+ T-cell neoplasm caused by human T-cell leukemia virus type I. As the prognosis for patients with ATL remains extremely poor due to resistance to conventional chemotherapy regimens, introduction of novel therapeutic agents is needed. Previous studies have reported that nucleosides 2'-deoxy-2'-methylidenecytidine (DMDC) and its derivative 2'-deoxy-2'-methylidene-5-fluorocytidine (FDMDC) exhibit antitumor activities in T-cell acute lymphoblastic leukemia (T-ALL) and solid tumor cell lines. Another nucleoside, 1-(2-azido-2-deoxy-β-D-arabinofuranosyl)cytosine (cytarazid), is considered a therapeutic drug with antitumor activity in human solid tumors. In this study, we investigated the effects of these nucleosides on cell growth in vitro and in vivo using relevant leukemia cell lines and NOD/Shi-scid, IL-2Rgnull (NOG) mice, respectively. The nucleosides demonstrated significant cytotoxic effects in ATL and T-ALL cell lines. Intraperitoneal administration of FDMDC and DMDC into tumor-bearing NOG mice resulted in significant suppression of tumor growth without lethal side effects. Our findings support a therapeutic application of these nucleosides against tumor progression by targeting DNA polymerase-dependent DNA synthesis in patients with ATL.
• Structural comparison of the C-terminal domain of functionally divergent lyssavirus P proteins.
  Aoi Sugiyama; Tomo Nomai; Xinxin Jiang; Miku Minami; Min Yao; Katsumi Maenaka; Naoto Ito; Paul R Gooley; Gregory W Moseley; Toyoyuki Ose
  Biochemical and biophysical research communications, 529, 2, 507, 512, 20 Aug. 2020, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Lyssavirus P protein is a multifunctional protein that interacts with numerous host-cell proteins. The C-terminal domain (CTD) of P is important for inhibition of JAK-STAT signaling enabling the virus to evade host immunity. Several regions on the surface of rabies virus P are reported to interact with host factors. Among them, an extended, discrete hydrophobic patch of P CTD is notable. Although structures of P CTD of two strains of rabies virus, and of mokola virus have been solved, the structure of P CTD for Duvenhage virus, which is functionally divergent from these species for immune evasion function, is not known. Here, we analyze the structures of P CTD of Duvenhage and of a distinct rabies virus strain to gain further insight on the nature and potential function of the hydrophobic surface. Molecular contacts in crystals suggest that the hydrophobic patch is important to intermolecular interactions with other proteins, which differ between the lyssavirus species.
• The Measles Virus V Protein Binding Site to STAT2 Overlaps That of IRF9.
  Yuma Nagano; Aoi Sugiyama; Madoka Kimoto; Takuya Wakahara; Yasuyo Noguchi; Xinxin Jiang; Shinya Saijo; Nobutaka Shimizu; Nana Yabuno; Min Yao; Paul R Gooley; Gregory W Moseley; Takashi Tadokoro; Katsumi Maenaka; Toyoyuki Ose
  Journal of virology, 94, 17, American Society for Microbiology, 17 Aug. 2020, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Measles virus (MeV) is a highly immunotropic and contagious pathogen that can even diminish preexisting antibodies and remains a major cause of childhood morbidity and mortality worldwide despite the availability of effective vaccines. MeV is one of the most extensively studied viruses with respect to the mechanisms of JAK-STAT antagonism. Of the three proteins translated from the MeV P gene, P and V are essential for inactivation of this pathway. However, the lack of data from direct analyses of the underlying interactions means that the detailed molecular mechanism of antagonism remains unresolved. Here, we prepared recombinant MeV V protein, which is responsible for human JAK-STAT antagonism, and a panel of variants, enabling the biophysical characterization of V protein, including direct V/STAT1 and V/STAT2 interaction assays. Unambiguous direct interactions between the host and viral factors, in the absence of other factors such as Jak1 or Tyk2, were observed, and the dissociation constants were quantified for the first time. Our data indicate that interactions between the C-terminal region of V and STAT2 is 1 order of magnitude stronger than that of the N-terminal region of V and STAT1. We also clarified that these interactions are completely independent of each other. Moreover, results of size exclusion chromatography demonstrated that addition of MeV-V displaces STAT2-core, a rigid region of STAT2 lacking the N- and C-terminal domains, from preformed complexes of STAT2-core/IRF-associated domain (IRF9). These results provide a novel model whereby MeV-V can not only inhibit the STAT2/IRF9 interaction but also disrupt preassembled interferon-stimulated gene factor 3.IMPORTANCE To evade host immunity, many pathogenic viruses inactivate host Janus kinase signal transducer and activator of transcription (STAT) signaling pathways using diverse strategies. Measles virus utilizes P and V proteins to counteract this signaling pathway. Data derived largely from cell-based assays have indicated several amino acid residues of P and V proteins as important. However, biophysical properties of V protein or its direct interaction with STAT molecules using purified proteins have not been studied. We have developed novel molecular tools enabling us to identify a novel molecular mechanism for immune evasion whereby V protein disrupts critical immune complexes, providing a clear strategy by which measles virus can suppress interferon-mediated antiviral gene expression.
• Efficient preparation of human and mouse CD1d proteins using silkworm baculovirus expression system.
  Hiroki Kusaka; Shunsuke Kita; Takashi Tadokoro; Kouki Yoshida; Yoshiyuki Kasai; Harumi Niiyama; Yukari Fujimoto; Shinya Hanashima; Michio Murata; Shigeru Sugiyama; Toyoyuki Ose; Kimiko Kuroki; Katsumi Maenaka
  Protein expression and purification, 172, 105631, 105631, Aug. 2020, [Peer-reviewed], [International Magazine]
  English, Scientific journal, CD1d is a major histocompatibility complex (MHC) class I-like glycoprotein and binds to glycolipid antigens that are recognized by natural killer T (NKT) cells. To date, our understanding of the structural basis for glycolipid binding and receptor recognition of CD1d is still limited. Here, we established a preparation method for the ectodomain of human and mouse CD1d using a silkworm-baculovirus expression system. The co-expression of human and mouse CD1d and β2-microglobulin (β2m) in the silkworm-baculovirus system was successful, but the yield of human CD1d was low. A construct of human CD1d fused with β2m via a flexible GS linker as a single polypeptide was prepared to improve protein yield. The production of this single-chained complex was higher (50 μg/larva) than that of the co-expression complex. Furthermore, differential scanning calorimetry revealed that the linker made the CD1d complex more stable and homogenous. These results suggest that the silkworm-baculovirus expression system is useful for structural and biophysical studies of CD1d in several aspects including low cost, easy handling, biohazard-free, rapid, and high yielding.
• Molecular mechanism of the recognition of bacterially cleaved immunoglobulin by the immune regulatory receptor LILRA2.
  Rika Yamazaki; Atsushi Furukawa; Kouyuki Hirayasu; Kohei Yumoto; Hideo Fukuhara; Hisashi Arase; Katsumi Maenaka
  The Journal of biological chemistry, 295, 28, 9531, 9541, 10 Jul. 2020, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Human leukocyte immunoglobulin-like receptors (LILRs) typically regulate immune activation by binding to the human leukocyte antigen class I molecules. LILRA2, a member of the LILR family, was recently reported to bind to other unique ligands, the bacterially degraded Igs (N-truncated Igs), for the activation of immune cells. Therefore, LILRA2 is currently attracting significant attention as a novel innate immune receptor. However, the detailed recognition mechanisms required for this interaction remain unclear. In this study, using several biophysical techniques, we uncovered the molecular mechanism of N-truncated Ig recognition by LILRA2. Surface plasmon resonance analysis disclosed that LILRA2 specifically binds to N-truncated Ig with weak affinity (Kd = 4.8 μm) and fast kinetics. However, immobilized LILRA2 exhibited a significantly enhanced interaction with N-truncated Ig due to avidity effects. This suggests that cell surface-bound LILRA2 rapidly monitors and identifies bi- or multivalent abnormal N-truncated Igs through specific cross-linking to induce immune activation. Van't Hoff analysis revealed that this interaction is enthalpy-driven, with a small entropy loss, and results from differential scanning calorimetry indicated the instability of the putative LILRA2-binding site, the Fab region of the N-truncated Ig. Atomic force microscopy revealed that N truncation does not cause significant structural changes in Ig. Furthermore, mutagenesis analysis identified the hydrophobic region of LILRA2 domain 2 as the N-truncated Ig-binding site, representing a novel ligand-binding site for the LILR family. These results provide detailed insights into the molecular regulation of LILR-mediated immune responses targeting ligands that have been modified by bacteria.
• Structural characteristics of measles virus entry.
  Hideo Fukuhara; Mwila Hilton Mwaba; Katsumi Maenaka
  Current opinion in virology, 41, 52, 58, Apr. 2020, [International Magazine]
  English, Scientific journal, Measles virus, a member of the genus Morbillivirus, is highly contagious and still shows considerable mortality with over 100000 deaths annually, although efficient attenuated vaccines exist. Recent studies of measles virus haemagglutinin (MeV-H) and its receptor, including crystallographic and electron microscopic structural analyses combined with functional assays, have revealed how the MeV-H protein recognizes its cognate receptors, SLAM and Nectin-4, and how the glycan shield ensures effective vaccination. In addition, the crystal structure of the MeV-F protein indicated its similarity to those of other paramyxoviruses. Taking into account these data, several models of viral entry/membrane fusion of measles viruses and related paramyxoviruses have been proposed. Furthermore, anti-MeV-F inhibitors targeted to specific regions to inhibit MeV-F protein activation were reported, with potency for preventing MeV infection. The inhibitors targeted for entry events may potentially be applied to treatment of MeV-derived diseases, although escape mutations and drug profiles should be considered.
• Biophysical research in Hokkaido University, Japan.
  Tomoyasu Aizawa; Makoto Demura; Kazutoshi Gohara; Hisashi Haga; Koichiro Ishimori; Masataka Kinjo; Tamiki Komatsuzaki; Katsumi Maenaka; Min Yao
  Biophysical reviews, 12, 2, 233, 236, Apr. 2020, [Peer-reviewed], [International Magazine]
  English
• Therapeutic effects of soluble human leukocyte antigen G2 isoform in lupus-prone MRL/lpr mice.
  Hiroshi Watanabe; Kimiko Kuroki; Chisato Yamada; Yukari Saburi; Naoyoshi Maeda; Katsumi Maenaka
  Human immunology, 81, 4, 186, 190, Apr. 2020, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Human leukocyte antigen (HLA)-G, a non-classical HLA class I molecule, has one of the splicing isoforms, HLA-G2, which lacks one domain (α2) and forms a non-covalent homodimer. HLA-G2 is expressed on placental cells, regulatory T cells, tumor cells, and virus-infected cells, and is involved in immunosuppression. The major isoform of HLA-G, HLA-G1, binds to leukocyte immunoglobulin (Ig)-like receptor (LILR) B1 and LILRB2, on the contrary, HLA-G2 binds to only LILRB2. We previously reported that HLA-G2 bound LILRB2 more strongly than HLA-G1 and also to paired Ig-like receptor (PIR)-B, a mouse homolog of LILRBs. Furthermore, HLA-G2 showed immunosuppressive effects in both collagen-induced arthritis (CIA) and atopic dermatitis-like model mice. In this study, we examine in vivo effects of HLA-G2 in systemic lupus erythematosus (SLE) model mice. HLA-G2 showed the suppression of the typical SLE symptoms such as serum anti-dsDNA antibody level and urinary albumin index. Furthermore, HLA-G2 tended to downregulate B-lymphocyte stimulator (BLyS) production. This is the first observation of the immunosuppressive effects of HLA-G2 isoform in SLE model mice, suggesting that HLA-G2 could be a useful therapeutic agent for SLE.
• Cysteine-Rich Secretory Proteins (CRISPs) From Venomous Snakes: An Overview of the Functional Diversity in A Large and Underappreciated Superfamily.
  Takashi Tadokoro; Cassandra M Modahl; Katsumi Maenaka; Narumi Aoki-Shioi
  Toxins, 12, 3, 12 Mar. 2020, [Peer-reviewed], [International Magazine]
  English, Scientific journal, The CAP protein superfamily (Cysteine-rich secretory proteins (CRISPs), Antigen 5 (Ag5), and Pathogenesis-related 1 (PR-1) proteins) is widely distributed, but for toxinologists, snake venom CRISPs are the most familiar members. Although CRISPs are found in the majority of venoms, very few of these proteins have been functionally characterized, but those that have been exhibit diverse activities. Snake venom CRISPs (svCRISPs) inhibit ion channels and the growth of new blood vessels (angiogenesis). They also increase vascular permeability and promote inflammatory responses (leukocyte and neutrophil infiltration). Interestingly, CRISPs in lamprey buccal gland secretions also manifest some of these activities, suggesting an evolutionarily conserved function. As we strive to better understand the functions that CRISPs serve in venoms, it is worth considering the broad range of CRISP physiological activities throughout the animal kingdom. In this review, we summarize those activities, known crystal structures and sequence alignments, and we discuss predicted functional sites. CRISPs may not be lethal or major components of venoms, but given their almost ubiquitous occurrence in venoms and the accelerated evolution of svCRISP genes, these venom proteins are likely to have functions worth investigating.
• The mitochondrial inner membrane protein LETM1 modulates cristae organization through its LETM domain.
  Seiko Nakamura; Aiko Matsui; Shiori Akabane; Yasushi Tamura; Azumi Hatano; Yuriko Miyano; Hiroshi Omote; Mizuho Kajikawa; Katsumi Maenaka; Yoshinori Moriyama; Toshiya Endo; Toshihiko Oka
  Communications biology, 3, 1, 99, 99, 05 Mar. 2020, [Peer-reviewed], [International Magazine]
  English, Scientific journal, LETM1 is a mitochondrial inner membrane protein that is required for maintaining the mitochondrial morphology and cristae structures, and regulates mitochondrial ion homeostasis. Here we report a role of LETM1 in the organization of cristae structures. We identified four amino acid residues of human LETM1 that are crucial for complementation of the growth deficiency caused by gene deletion of a yeast LETM1 orthologue. Substituting amino acid residues with alanine disrupts the correct assembly of a protein complex containing LETM1 and prevents changes in the mitochondrial morphology induced by exogenous LETM1 expression. Moreover, the LETM1 protein changes the shapes of the membranes of in vitro-reconstituted proteoliposomes, leading to the formation of invaginated membrane structures on artificial liposomes. LETM1 mutant proteins with alanine substitutions fail to facilitate the formation of invaginated membrane structures, suggesting that LETM1 plays a fundamental role in the organization of mitochondrial membrane morphology.
• Structure of HIV-2 Nef Reveals Features Distinct from HIV-1 Involved in Immune Regulation.
  Kengo Hirao; Sophie Andrews; Kimiko Kuroki; Hiroki Kusaka; Takashi Tadokoro; Shunsuke Kita; Toyoyuki Ose; Sarah L Rowland-Jones; Katsumi Maenaka
  iScience, 23, 1, 100758, 100758, 24 Jan. 2020, [Peer-reviewed], [International Magazine]
  English, Scientific journal, The human immunodeficiency virus (HIV) accessory protein Nef plays a major role in establishing and maintaining infection, particularly through immune evasion. Many HIV-2-infected people experience long-term viral control and survival, resembling HIV-1 elite control. HIV-2 Nef has overlapping but also distinct functions from HIV-1 Nef. Here we report the crystal structure of HIV-2 Nef core. The di-leucine sorting motif forms a helix bound to neighboring molecules, and moreover, isothermal titration calorimetry demonstrated that the CD3 endocytosis motif can directly bind to HIV-2 Nef, ensuring AP-2-mediated endocytosis for CD3. The highly conserved C-terminal region forms a α-helix, absent from HIV-1. We further determined the structure of simian immunodeficiency virus (SIV) Nef harboring this region, demonstrating similar C-terminal α-helix, which may contribute to AP-1 binding for MHC-I downregulation. These results provide insights into the distinct pathogenesis of HIV-2 infection.
• Measles Virus Hemagglutinin Protein Establishes a Specific Interaction With the Extreme N-Terminal Region of Human Signaling Lymphocytic Activation Molecule to Enhance Infection.
  Fumio Seki; Yuta Yamamoto; Hideo Fukuhara; Kazue Ohishi; Tadashi Maruyama; Katsumi Maenaka; Hiroaki Tokiwa; Makoto Takeda
  Frontiers in microbiology, 11, 1830, 1830, 2020, [International Magazine]
  English, Scientific journal, Measles virus (MV) is a human pathogen that is classified in the genus Morbillivirus in the family Paramyxoviridae together with several non-human animal morbilliviruses. They cause severe systemic infections by using signaling lymphocytic activation molecule (SLAM) and poliovirus receptor-like 4 expressed on immune and epithelial cells, respectively, as receptors. The viral hemagglutinin (H) protein is responsible for the receptor-binding. Previously determined structures of MV-H and SLAM complexes revealed a major binding interface between the SLAM V domain and MV-H with four binding components (sites 1-4) in the interface. We studied the MV-H and human SLAM (hSLAM) complex structure in further detail by in silico analyses and determined missing regions or residues in the previously determined complex structures. These analyses showed that, in addition to sites 1-4, MV-H establishes a unique interaction with the extreme N-terminal region (ExNTR) of hSLAM. The first principles calculation-based fragment molecular orbital computation method revealed that methionine at position 29 (hSLAM-Met29) is the key residue for the interaction. hSLAM-Met29 was predicted to establish a CH-π interaction with phenylalanine at position 549 of MV-H (MVH-Phe549). A cell-cell fusion assay showed that the hSLAM-Met29 and MVH-Phe549 interaction is important for hSLAM-dependent MV membrane fusion. Furthermore, Jurkat cell lines expressing hSLAM with or without Met29 and recombinant MV possessing the H protein with or without Phe549 showed that the hSLAM-Met29 and MVH-Phe549 interaction enhanced hSLAM-dependent MV infection by ~10-fold. We speculate that in the evolutionary history of morbilliviruses, this interaction may have contributed to MV adaptation to humans because this interaction is unique for MV and only MV uses hSLAM efficiently among morbilliviruses.
• Biophysical characterization and single-chain Fv construction of a neutralizing antibody to measles virus.
  Takashi Tadokoro; Mst Lubna Jahan; Yuri Ito; Maino Tahara; Surui Chen; Atsutoshi Imai; Natsumi Sugimura; Koki Yoshida; Mizuki Saito; Toyoyuki Ose; Takao Hashiguchi; Makoto Takeda; Hideo Fukuhara; Katsumi Maenaka
  The FEBS journal, 287, 1, 145, 159, Jan. 2020, [Peer-reviewed], [International Magazine]
  English, Scientific journal, The measles virus (MV) is a major cause of childhood morbidity and mortality worldwide. We previously established a mouse monoclonal antibody, 2F4, which shows high neutralizing titers against eight different genotypes of MV. However, the molecular basis for the neutralizing activity of the 2F4 antibody remains incompletely understood. Here, we have evaluated the binding characteristics of a Fab fragment of the 2F4 antibody. Using the MV infectious assay, we demonstrated that 2F4 Fab inhibits viral entry via either of two cellular receptors, SLAM and Nectin4. Surface plasmon resonance (SPR) analysis of recombinant proteins indicated that 2F4 Fab interacts with MV hemagglutinin (MV-H) with a KD value at the nm level. Furthermore, we designed a single-chain Fv fragment of 2F4 antibody as another potential biopharmaceutical to target measles. The stable 2F4 scFv was successfully prepared by the refolding method and shown to interact with MV-H at the μm level. Like 2F4 Fab, scFv inhibited receptor binding and viral entry. This indicates that 2F4 mAb uses the receptor-binding site and/or a neighboring region as an epitope with high affinity. These results provide insight into the neutralizing activity and potential therapeutic use of antibody fragments for MV infection.
• Relation of Colloidal and Conformational Stabilities to Aggregate Formation in a Monoclonal Antibody.
  Hiroaki Oyama; Hiroki Koga; Takashi Tadokoro; Katsumi Maenaka; Akira Shiota; Masami Yokoyama; Masanori Noda; Tetsuo Torisu; Susumu Uchiyama
  Journal of pharmaceutical sciences, 109, 1, 308, 315, Jan. 2020, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Aggregation of therapeutic monoclonal antibodies has a potential risk of immunogenicity, requiring minimization of aggregate formation. We have developed a fitting formula for antibody aggregation at 40°C based on physicochemical parameters, including colloidal and conformational stabilities. An IgG1 monoclonal antibody, MAb-T, was formulated in 24 combinations of different buffer types and pH with or without sodium chloride. The fitting formula for monomer loss was successfully established by nonlinear regression analysis of the results from accelerated stability testing. Calculated monomer fraction values by the fitting formula were strongly correlated with experimental values (R2 = 0.92). The model includes secondary virial coefficient, B22, as the representative parameter of colloidal stability, and aggregation temperature, Tagg, representing conformational stability. Then, we examined charge state, conformational flexibility, and thermal unfolding profile of MAb-T to clarify the molecular basis for the different aggregation propensities in sodium acetate buffer and in sodium citrate buffer at the same pH and buffer concentration. We concluded that the accumulation of citrate anions on the surface of MAb-T is the primary source of the less colloidal and conformational stabilities, resulting in the higher aggregation propensity in sodium citrate buffer.
• Structural and Functional Basis for LILRB Immune Checkpoint Receptor Recognition of HLA-G Isoforms.
  Kimiko Kuroki; Haruki Matsubara; Ryo Kanda; Naoyuki Miyashita; Mitsunori Shiroishi; Yuko Fukunaga; Jun Kamishikiryo; Atsushi Fukunaga; Hideo Fukuhara; Kaoru Hirose; Joan S Hunt; Yuji Sugita; Shunsuke Kita; Toyoyuki Ose; Katsumi Maenaka
  Journal of immunology (Baltimore, Md. : 1950), 203, 12, 3386, 3394, 15 Dec. 2019, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Human leukocyte Ig-like receptors (LILR) LILRB1 and LILRB2 are immune checkpoint receptors that regulate a wide range of physiological responses by binding to diverse ligands, including HLA-G. HLA-G is exclusively expressed in the placenta, some immunoregulatory cells, and tumors and has several unique isoforms. However, the recognition of HLA-G isoforms by LILRs is poorly understood. In this study, we characterized LILR binding to the β2-microglobulin (β2m)-free HLA-G1 isoform, which is synthesized by placental trophoblast cells and tends to dimerize and multimerize. The multimerized β2m-free HLA-G1 dimer lacked detectable affinity for LILRB1, but bound strongly to LILRB2. We also determined the crystal structure of the LILRB1 and HLA-G1 complex, which adopted the typical structure of a classical HLA class I complex. LILRB1 exhibits flexible binding modes with the α3 domain, but maintains tight contacts with β2m, thus accounting for β2m-dependent binding. Notably, both LILRB1 and B2 are oriented at suitable angles to permit efficient signaling upon complex formation with HLA-G1 dimers. These structural and functional features of ligand recognition by LILRs provide novel insights into their important roles in the biological regulations.
• Repurposing existing drugs: identification of irreversible IMPDH inhibitors by high-throughput screening.
  Albertus Eka Yudistira Sarwono; Shinya Mitsuhashi; Mohammad Hazzaz Bin Kabir; Kengo Shigetomi; Tadashi Okada; Fumina Ohsaka; Satoko Otsuguro; Katsumi Maenaka; Makoto Igarashi; Kentaro Kato; Makoto Ubukata
  Journal of enzyme inhibition and medicinal chemistry, 34, 1, 171, 178, Dec. 2019, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Inosine 5'-monophosphate dehydrogenase (IMPDH) is an essential enzyme for the production of guanine nucleotides. Disruption of IMPDH activity has been explored as a therapeutic strategy for numerous purposes, such as for anticancer, immunosuppression, antiviral, and antimicrobial therapy. In the present study, we established a luciferase-based high-throughput screening system to identify IMPDH inhibitors from our chemical library of known bioactive small molecules. The screening of 1400 compounds resulted in the discovery of three irreversible inhibitors: disulfiram, bronopol, and ebselen. Each compound has a distinct chemical moiety that differs from other reported IMPDH inhibitors. Further evaluation revealed that these compounds are potent inhibitors of IMPDHs with kon values of 0.7 × 104 to 9.3 × 104 M-1·s-1. Both disulfiram and bronopol exerted similar degree of inhibition to protozoan and mammalian IMPDHs. Ebselen showed an intriguing difference in mode of inhibition for different IMPDHs, with reversible and irreversible inhibition to each Cryptosporidium parvum IMPDH and human IMPDH type II, respectively. In the preliminary efficacy experiment against cryptosporidiosis in severe combined immunodeficiency (SCID) mouse, a decrease in the number of oocyst shed was observed upon the oral administration of disulfiram and bronopol, providing an early clinical proof-of-concept for further utilization of these compounds as IMPDH inhibitors.
• Evaluation of the Reactivity and Receptor Competition of HLA-G Isoforms toward Available Antibodies: Implications of Structural Characteristics of HLA-G Isoforms.
  Atsushi Furukawa; Manami Meguro; Rika Yamazaki; Hiroshi Watanabe; Ami Takahashi; Kimiko Kuroki; Katsumi Maenaka
  International journal of molecular sciences, 20, 23, 26 Nov. 2019, [Peer-reviewed], [International Magazine]
  English, Scientific journal, The human leucocyte antigen (HLA)-G, which consists of seven splice variants, is a tolerogenic immune checkpoint molecule. It plays an important role in the protection of the fetus from the maternal immune response by binding to inhibitory receptors, including leukocyte Ig-like receptors (LILRs). Recent studies have also revealed that HLA-G is involved in the progression of cancer cells and the protection from autoimmune diseases. In contrast to its well characterized isoform, HLA-G1, the binding activities of other major HLA-G isoforms, such as HLA-G2, toward available anti-HLA-G antibodies are only partially understood. Here, we investigate the binding specificities of anti-HLA-G antibodies by using surface plasmon resonance. MEM-G9 and G233 showed strong affinities to HLA-G1, with a nM range for their dissociation constants, but did not show affinities to HLA-G2. The disulfide-linker HLA-G1 dimer further exhibited significant avidity effects. On the other hand, 4H84 and MEM-G1, which can be used for the Western blotting of HLA-G isoforms, can bind to native HLA-G2, while MEM-G9 and G233 cannot. These results reveal that HLA-G2 has a partially intrinsically disordered structure. Furthermore, MEM-G1, but not 4H84, competes with the LILRB2 binding of HLA-G2. These results provide novel insight into the functional characterization of HLA-G isoforms and their detection systems.
• Novel Notch signaling inhibitor NSI‑1 suppresses nuclear translocation of the Notch intracellular domain.
  Takaya Shiraishi; Masahiro Sakaitani; Satoko Otsuguro; Katsumi Maenaka; Toshiharu Suzuki; Tadashi Nakaya
  International journal of molecular medicine, 44, 4, 1574, 1584, Oct. 2019, [Peer-reviewed], [International Magazine]
  English, Scientific journal, The Notch receptor serves a fundamental role in the regulation of cell fate determination through intracellular signal transmission. Mutation of the Notch receptor results in abnormal active signaling, leading to the development of diseases involving abnormal cell growth, including malignant tumors. Therefore, the Notch signaling pathway is a useful pharmacological target for the treatment of cancer. In the present study, a compound screening system was designed to identify inhibitors of the Notch signaling targeting Notch intracellular domain (NICD). A total of 9,600 compounds were analyzed using the Michigan Cancer Foundation‑7 (MCF7) human breast adenocarcinoma cell line and the SH‑SY5Y human neuroblastoma cell line with the reporter assay system using an artificial protein encoding a partial Notch carboxyl‑terminal fragment fused to the Gal4 DNA‑binding domain. The molecular mechanism underlying the inhibition of Notch signaling by a hit compound was further validated using biochemical and cell biological approaches. Using the screening system, a potential candidate, Notch signaling inhibitor‑1 (NSI‑1), was isolated which showed 50% inhibition at 6.1 µM in an exogenous Notch signaling system. In addition, NSI‑1 suppressed the nuclear translocation of NICD and endogenous gene expression of hairy and enhancer of split‑1, indicating that NSI‑1 specifically targets Notch. Notably, NSI‑1 suppressed the cell viability of MCF7 cells and another human breast adenocarcinoma cell line, MDA‑MB‑231 exhibiting constitutive and high Notch signaling activity, whereas no significant effect was observed in the SH‑SY5Y cells bearing a lower Notch signaling activity. NSI‑1 significantly suppressed the viability of SH‑SY5Y cells expressing exogenous human Notch1. These results indicate that NSI‑1 is a novel Notch signaling inhibitor and suggest its potential as a useful drug for the treatment of diseases induced by constitutively active Notch signaling.
• Specificity of Morbillivirus Hemagglutinins to Recognize SLAM of Different Species.
  Hideo Fukuhara; Yuri Ito; Miyuki Sako; Mizuho Kajikawa; Koki Yoshida; Fumio Seki; Mwila Hilton Mwaba; Takao Hashiguchi; Masa-Aki Higashibata; Toyoyuki Ose; Kimiko Kuroki; Makoto Takeda; Katsumi Maenaka
  Viruses, 11, 8, 19 Aug. 2019, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Measles virus (MV) and canine distemper virus (CDV) are highly contagious and deadly, forming part of the morbillivirus genus. The receptor recognition by morbillivirus hemagglutinin (H) is important for determining tissue tropism and host range. Recent reports largely urge caution as regards to the potential expansion of host specificities of morbilliviruses. Nonetheless, the receptor-binding potential in different species of morbillivirus H proteins is largely unknown. Herein, we show that the CDV-H protein binds to the dog signaling lymphocyte activation molecule (SLAM), but not to the human, tamarin, or mouse SLAM. In contrast, MV-H can bind to human, tamarin and dog SLAM, but not to that of mice. Notably, MV binding to dog SLAM showed a lower affinity and faster kinetics than that of human SLAM, and MV exhibits a similar entry activity in dog SLAM- and human SLAM-expressing Vero cells. The mutagenesis study using a fusion assay, based on the MV-H-SLAM complex structure, revealed differences in tolerance for the receptor specificity between MV-H and CDV-H. These results provide insights into H-SLAM specificity related to potential host expansion.
• Identification of IgG1 Aggregation Initiation Region by Hydrogen Deuterium Mass Spectrometry.
  Masanori Noda; Kentaro Ishii; Mika Yamauchi; Hiroaki Oyama; Takashi Tadokoro; Katsumi Maenaka; Tetsuo Torisu; Susumu Uchiyama
  Journal of pharmaceutical sciences, 108, 7, 2323, 2333, Jul. 2019, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Antibody aggregates are a potential risk for immunogenicity; therefore, rational approaches to improve associated aggregation properties need to be developed. Here, we report the amino acid region responsible for aggregation initiation. Two types of therapeutic IgG1 antibody monomer samples were prepared: IgG1 mAb40-3M stored at 40°C for 3 months, which existed in monodisperse state, and the monomer mAb65-5m, which was dissociated from small soluble aggregates by heating at 65°C for 5 min. Hydrogen deuterium exchange mass spectrometry of mAb40-3M identified 2 sites in the Fc region (site 1, F239-M256; site 2, S428-G450) with increased exchange rates. Site 1 includes a region reported as being susceptible to structural change induced by stress. Exposure of site 1 was undetected after 2 months of storage at 40°C but was subsequently detectable after 3 months. As site 2 is spatially close to site 1, the structural change of site 1 could propagate site 2. Besides these 2 regions, hydrogen deuterium exchange mass spectrometry of mAb65-5m identified an exposure of I257-W281 in Fc (site 3), within which a peptide sequence with high aggregation tendency was discovered. We thus concluded that exposure of site 3 is a trigger for the association of a partially denatured antibody.
• HLA-G dimer targets Granzyme B pathway to prolong human renal allograft survival.
  Ashwin Ajith; Vera Portik-Dobos; Anh Thu Nguyen-Lefebvre; Christine Callaway; Daniel D Horuzsko; Rajan Kapoor; Carlos Zayas; Katsumi Maenaka; Laura L Mulloy; Anatolij Horuzsko
  FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 33, 4, 5220, 5236, Apr. 2019, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Human leukocyte antigen G (HLA-G), a nonclassic HLA class Ib molecule involved in the maintenance of maternal tolerance to semiallogeneic fetal tissues during pregnancy, has emerged as a potential therapeutic target to control allograft rejection. We demonstrate here that the level of soluble HLA-G dimer was higher in a group of 90 patients with a functioning renal allograft compared with 40 patients who rejected (RJ) their transplants. The HLA-G dimer level was not affected by demographic status. One of the potential mechanisms in tissue-organ allograft rejection involves the induction of granzymes and perforin, which are the main effector molecules expressed by CD8+ cytotoxic T lymphocytes and function to destroy allogeneic transplants. Using genomics and molecular and cellular analyses of cells from T-cell-mediated RJ and nonrejected kidney transplant patients, cells from leukocyte Ig-like receptor B1 (LILRB1) transgenic mice, humanized mice, and genetically engineered HLA-G dimer, we demonstrated a novel mechanism by which HLA-G dimer inhibits activation and cytotoxic capabilities of human CD8+ T cells. This mechanism implicated the down-regulation of Granzyme B expression and the essential involvement of LILRB1. Thus, HLA-G dimer has the potential to be a specific and effective therapy for prevention of allograft rejection and prolongation of graft survival.-Ajith, A., Portik-Dobos, V., Nguyen-Lefebvre, A. T., Callaway, C., Horuzsko, D. D., Kapoor, R., Zayas, C., Maenaka, K., Mulloy, L. L., Horuzsko, A. HLA-G dimer targets Granzyme B pathway to prolong human renal allograft survival.
• Crystal structure of the complex between venom toxin and serum inhibitor from Viperidae snake.
  Narumi Shioi; Takashi Tadokoro; Seijiro Shioi; Yuki Okabe; Haruki Matsubara; Shunsuke Kita; Toyoyuki Ose; Kimiko Kuroki; Shigeyuki Terada; Katsumi Maenaka
  The Journal of biological chemistry, 294, 4, 1250, 1256, 25 Jan. 2019, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Venomous snakes have endogenous proteins that neutralize the toxicity of their venom components. We previously identified five small serum proteins (SSP-1-SSP-5) from a highly venomous snake belonging to the family Viperidae as inhibitors of various toxins from snake venom. The endogenous inhibitors belong to the prostate secretory protein of 94 amino acids (PSP94) family. SSP-2 interacts with triflin, which is a member of the cysteine-rich secretory protein (CRISP) family that blocks smooth muscle contraction. However, the structural basis for the interaction and the biological roles of these inhibitors are largely unknown. Here, we determined the crystal structure of the SSP-2-triflin complex at 2.3 Å resolution. A concave region centrally located in the N-terminal domain of triflin is fully occupied by the terminal β-strands of SSP-2. SSP-2 does not bind tightly to the C-terminal cysteine-rich domain of triflin; this domain is thought to be responsible for its channel-blocker function. Instead, the cysteine-rich domain is tilted 7.7° upon binding to SSP-2, and the inhibitor appears to sterically hinder triflin binding to calcium channels. These results help explain how an endogenous inhibitor prevents the venomous protein from maintaining homeostasis in the host. Furthermore, this interaction also sheds light on the binding interface between the human homologues PSP94 and CRISP-3, which are up-regulated in prostate and ovarian cancers.
• Synthesis of glycerolipids containing simple linear acyl chains or aromatic rings and evaluation of their Mincle signaling activity.
  Takanori Matsumaru; Risa Ikeno; Yusuke Shuchi; Toshiki Iwamatsu; Takashi Tadokoro; Sho Yamasaki; Yukari Fujimoto; Atsushi Furukawa; Katsumi Maenaka
  Chemical communications (Cambridge, England), 55, 5, 711, 714, 10 Jan. 2019, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Mincle, expressed in activated phagocytes, recognizes the lipid ligand to activate the innate immune system. We have synthesized glycerol derivatives possessing simple alkyl chains or aromatic rings and elucidated their structure-activity relationships using a Mincle-mediated signaling assay. The activity depends on the length of the simple acyl chains of the glycerol derivatives.
• Suramin, screened from an approved drug library, inhibits HuR functions and attenuates malignant phenotype of oral cancer cells.
  Wataru Kakuguchi; Takao Nomura; Tetsuya Kitamura; Satoko Otsuguro; Kazuhiro Matsushita; Masahiro Sakaitani; Katsumi Maenaka; Kanchu Tei
  Cancer medicine, 7, 12, 6269, 6280, Dec. 2018, [Peer-reviewed], [International Magazine]
  English, Scientific journal, AU-rich elements (ARE) exist in the 3'-untranslated regions of the mRNA transcribed from cell growth-related genes such as proto-oncogenes, cyclin-related genes, and growth factors. HuR binds and stabilizes ARE-mRNA. HuR is expressed abundantly in cancer cells and related malignant phenotypes. HuR knockdown attenuates the malignant phenotype of oral cancer cells. In this study, we screened 1570 compounds in the approved drug library by differential scanning fluorimetry (DSF) to discover a HuR-targeted compound. Firstly, 55 compounds were selected by DSF. Then, 8 compounds that showed a shift in the melting temperature value in a concentration-dependent manner were selected by DSF. Of them, suramin, an anti-trypanosomal drug, binds to HuR, exhibiting fast-on and fast-off kinetic behavior on surface plasmon resonance (SPR). We confirmed that suramin significantly decreased mRNA and protein expression of cyclin A2 and cyclin B1. The cyclin A2 and cyclin B1 mRNAs were destabilized by suramin. Furthermore, the motile and invasive activities of a tongue carcinoma cell line treated with suramin were markedly lower than those of control cells. The above findings suggest that suramin binds to HuR and inhibits its function. We also showed that the anticancer effects of suramin were caused by the inhibition of HuR function, indicating its potential as a novel therapeutic agent in the treatment of oral cancer. Our results suggest that suramin, via its different mechanism, may effectively suppress progressive oral cancer that cannot be controlled using other anticancer agents.
• Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility.
  Mizuho Kajikawa; Toyoyuki Ose; Yuko Fukunaga; Yuki Okabe; Naoki Matsumoto; Kento Yonezawa; Nobutaka Shimizu; Simon Kollnberger; Masanori Kasahara; Katsumi Maenaka
  Nature communications, 9, 1, 4330, 4330, 18 Oct. 2018, [Peer-reviewed], [International Magazine]
  English, Scientific journal, The MILL family, composed of MILL1 and MILL2, is a group of nonclassical MHC class I molecules that occur in some orders of mammals. It has been reported that mouse MILL2 is involved in wound healing; however, the molecular mechanisms remain unknown. Here, we determine the crystal structure of MILL2 at 2.15 Å resolution, revealing an organization similar to classical MHC class I. However, the α1-α2 domains are not tightly fixed on the α3-β2m domains, indicating unusual interdomain flexibility. The groove between the two helices in the α1-α2 domains is too narrow to permit ligand binding. Notably, an unusual basic patch on the α3 domain is involved in the binding to heparan sulfate which is essential for MILL2 interactions with fibroblasts. These findings suggest that MILL2 has a unique structural architecture and physiological role, with binding to heparan sulfate proteoglycans on fibroblasts possibly regulating cellular recruitment in biological events.
• Structural insights into modulation and selectivity of transsynaptic neurexin-LRRTM interaction.
  Atsushi Yamagata; Sakurako Goto-Ito; Yusuke Sato; Tomoko Shiroshima; Asami Maeda; Masahiko Watanabe; Takashi Saitoh; Katsumi Maenaka; Tohru Terada; Tomoyuki Yoshida; Takeshi Uemura; Shuya Fukai
  Nature communications, 9, 1, 3964, 3964, 27 Sep. 2018, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Leucine-rich repeat transmembrane neuronal proteins (LRRTMs) function as postsynaptic organizers that induce excitatory synapses. Neurexins (Nrxns) and heparan sulfate proteoglycans have been identified as presynaptic ligands for LRRTMs. Specifically, LRRTM1 and LRRTM2 bind to the Nrxn splice variant lacking an insert at the splice site 4 (S4). Here, we report the crystal structure of the Nrxn1β-LRRTM2 complex at 3.4 Å resolution. The Nrxn1β-LRRTM2 interface involves Ca2+-mediated interactions and overlaps with the Nrxn-neuroligin interface. Together with structure-based mutational analyses at the molecular and cellular levels, the present structural analysis unveils the mechanism of selective binding between Nrxn and LRRTM1/2 and its modulation by the S4 insertion of Nrxn.
• A Sialylated Voltage-Dependent Ca2+ Channel Binds Hemagglutinin and Mediates Influenza A Virus Entry into Mammalian Cells.
  Yoichiro Fujioka; Shinya Nishide; Toyoyuki Ose; Tadaki Suzuki; Izumi Kato; Hideo Fukuhara; Mari Fujioka; Kosui Horiuchi; Aya O Satoh; Prabha Nepal; Sayaka Kashiwagi; Jing Wang; Mika Horiguchi; Yuko Sato; Sarad Paudel; Asuka Nanbo; Tadaaki Miyazaki; Hideki Hasegawa; Katsumi Maenaka; Yusuke Ohba
  Cell host & microbe, 23, 6, 809, 818, 13 Jun. 2018, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Influenza A virus (IAV) infection is initiated by the attachment of the viral glycoprotein hemagglutinin (HA) to sialic acid on the host cell surface. However, the sialic acid-containing receptor crucial for IAV infection has remained unidentified. Here, we show that HA binds to the voltage-dependent Ca2+ channel Cav1.2 to trigger intracellular Ca2+ oscillations and subsequent IAV entry and replication. IAV entry was inhibited by Ca2+ channel blockers (CCBs) or by knockdown of Cav1.2. The CCB diltiazem also inhibited virus replication in vivo. Reintroduction of wild-type but not the glycosylation-deficient mutants of Cav1.2 restored Ca2+ oscillations and virus infection in Cav1.2-depleted cells, demonstrating the significance of Cav1.2 sialylation. Taken together, we identify Cav1.2 as a sialylated host cell surface receptor that binds HA and is critical for IAV entry.
• Ribavirin-related compounds exert in vitro inhibitory effects toward rabies virus.
  Anindita PD; Sasaki M; Okada K; Ito N; Sugiyama M; Saito-Tarashima N; Minakawa N; Shuto S; Otsuguro S; Ichikawa S; Matsuda A; Maenaka K; Orba Y; Sawa H
  Antiviral research, 154, 1, 9, Mar. 2018, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Rabies remains an invariably fatal neurological disease despite the availability of a preventive vaccination and post-exposure prophylaxis that must be immediately administered to the exposed individual before symptom onset. There is no effective medication for treatment during the symptomatic phase. Ribavirin, a guanine nucleoside analog, is a potent inhibitor of rabies virus (RABV) replication in vitro but lacks clinical efficacy. Therefore, we attempted to identify potential ribavirin analogs with comparable or superior anti-RABV activity. Antiviral activity and cytotoxicity of the compounds were initially examined in human neuroblastoma cells. Among the tested compounds, two exhibited a 5- to 27-fold higher anti-RABV activity than ribavirin. Examination of the anti-RABV mechanisms of action of the compounds using time-of-addition and minigenome assays revealed that they inhibited viral genome replication and transcription. Addition of exogenous guanosine to RABV-infected cells diminished the antiviral activity of the compounds, suggesting that they are involved in guanosine triphosphate (GTP) pool depletion by inhibiting inosine monophosphate dehydrogenase (IMPDH). Taken together, our findings underline the potency of nucleoside analogs as a class of antiviral compounds for the development of novel agents against RABV.
• Heparan sulfate proteoglycans serve as an attachment factor for rabies virus entry and infection.
  Sasaki M; Anindita PD; Ito N; Sugiyama M; Carr M; Fukuhara H; Ose T; Maenaka K; Takada A; Hall WW; Orba Y; Sawa H
  The Journal of infectious diseases, 217, 11, 1740, 1749, Feb. 2018, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Rabies virus (RABV) is the causative agent of fatal neurological disease. Cellular attachment is the initial and essential step for viral infections. Although extensive studies have demonstrated that RABV uses various target cell molecules to mediate infection, no specific molecule has been identified as an attachment factor for RABV infection. Here we demonstrate that cellular heparan sulfate (HS) supports RABV adhesion and subsequent entry into target cells. Enzymatic removal of HS reduced cellular susceptibility to RABV infection, and heparin, a highly sulfated form of HS, blocked viral adhesion and infection. The direct binding between RABV glycoprotein and heparin was demonstrated, and this interaction was shown to require HS N- and 6-O-sulfation. We also revealed that basic amino acids in the ectodomain of RABV glycoprotein serve as major determinants for the RABV-HS interaction. Collectively, our study highlights a previously undescribed role of HS as an attachment factor for RABV infection.
• Structural and thermodynamic analyses reveal critical features of glycopeptide recognition by the human PILR alpha immune cell receptor
  Atsushi Furukawa; Kosuke Kakita; Tomoki Yamada; Mikihiro Ishizuka; Jiro Sakamoto; Nanao Hatori; Naoyoshi Maeda; Fumina Ohsaka; Takashi Saitoh; Takao Nomura; Kimiko Kuroki; Hisanori Nambu; Hisashi Arase; Shigeki Matsunaga; Masahiro Anada; Toyoyuki Ose; Shunichi Hashimoto; Katsumi Maenaka
  JOURNAL OF BIOLOGICAL CHEMISTRY, 292, 51, 21128, 21136, Dec. 2017, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• X-ray crystal structure of Escherichia coli HspQ, a protein involved in the retardation of replication initiation
  Yoshito Abe; Seijiro Shioi; Shunsuke Kita; Hikaru Nakata; Katsumi Maenaka; Daisuke Kohda; Tsutomu Katayama; Tadashi Ueda
  FEBS LETTERS, 591, 22, 3805, 3816, Nov. 2017, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• X-ray crystal structure of Escherichia coli HspQ, a protein involved in the retardation of replication initiation
  Yoshito Abe; Seijiro Shioi; Shunsuke Kita; Hikaru Nakata; Katsumi Maenaka; Daisuke Kohda; Tsutomu Katayama; Tadashi Ueda
  FEBS Letters, 591, 22, 3805, 3816, Wiley Blackwell, 01 Nov. 2017, [Peer-reviewed]
  English
• Production of Single-Chain Fv Antibodies Specific for GA-Pyridine, an Advanced Glycation End-Product (AGE), with Reduced Inter-Domain Motion
  Natsuki Fukuda; Kentaro Noi; Lidong Weng; Yoshihiro Kobashigawa; Hiromi Miyazaki; Yukari Wakeyama; Michiyo Takaki; Yusuke Nakahara; Yuka Tatsuno; Makiyo Uchida-Kamekura; Yoshiaki Suwa; Takashi Sato; Naoki Ichikawa-Tomikawa; Motoyoshi Nomizu; Yukio Fujiwara; Fumina Ohsaka; Takashi Saito; Katsumi Maenaka; Hiroyuki Kumeta; Shoko Shinya; Chojiro Kojima; Teru Ogura; Hiroshi Morioka
  MOLECULES, 22, 10, Oct. 2017, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• The Roles of Matricellular Proteins in Oncogenic Virus-Induced Cancers and Their Potential Utilities as Therapeutic Targets
  Naoyoshi Maeda; Katsumi Maenaka
  INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 18, 10, Oct. 2017, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Therapeutic application of human leukocyte antigen-G1 improves atopic dermatitis-like skin lesions in mice
  Naoyoshi Maeda; Chisato Yamada; Ami Takahashi; Kimiko Kuroki; Katsumi Maenaka
  INTERNATIONAL IMMUNOPHARMACOLOGY, 50, 202, 207, Sep. 2017, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Molecular basis of selective mitochondrial fusion by heterotypic action between OPA1 and cardiolipin.
  Tadato Ban; Takaya Ishihara; Hiroto Kohno; Shotaro Saita; Ayaka Ichimura; Katsumi Maenaka; Toshihiko Oka; Katsuyoshi Mihara; Naotada Ishihara
  Nature cell biology, 19, 7, 856, 863, Jul. 2017, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Mitochondria are highly dynamic organelles that undergo frequent fusion and fission. Optic atrophy 1 (OPA1) is an essential GTPase protein for both mitochondrial inner membrane (IM) fusion and cristae morphology. Under mitochondria-stress conditions, membrane-anchored L-OPA1 is proteolytically cleaved to form peripheral S-OPA1, leading to the selection of damaged mitochondria for mitophagy. However, molecular details of the selective mitochondrial fusion are less well understood. Here, we showed that L-OPA1 and cardiolipin (CL) cooperate in heterotypic mitochondrial IM fusion. We reconstituted an in vitro membrane fusion reaction using purified human L-OPA1 protein expressed in silkworm, and found that L-OPA1 on one side of the membrane and CL on the other side are sufficient for fusion. GTP-independent membrane tethering through L-OPA1 and CL primes the subsequent GTP-hydrolysis-dependent fusion, which can be modulated by the presence of S-OPA1. These results unveil the most minimal intracellular membrane fusion machinery. In contrast, independent of CL, a homotypic trans-OPA1 interaction mediates membrane tethering, thereby supporting the cristae structure. Thus, multiple OPA1 functions are modulated by local CL conditions for regulation of mitochondrial morphology and quality control.
• Cutting Edge: Class II-like Structural Features and Strong Receptor Binding of the Nonclassical HLA-G2 Isoform Homodimer
  Kimiko Kuroki; Kazuhiro Mio; Ami Takahashi; Haruki Matsubara; Yoshiyuki Kasai; Sachie Manaka; Masahide Kikkawa; Daizo Hamada; Chikara Sato; Katsumi Maenaka
  JOURNAL OF IMMUNOLOGY, 198, 9, 3399, 3403, May 2017, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Divergent synthesis of kinase inhibitor derivatives, leading to discovery of selective Gck inhibitors
  Takanori Matsumaru; Makoto Inai; Kana Ishigami; Toshiki Iwamatsu; Hiroshi Maita; Satoko Otsuguro; Takao Nomura; Akira Matsuda; Satoshi Ichikawa; Masahiro Sakaitani; Satoshi Shuto; Katsumi Maenaka; Toshiyuki Kan
  BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, 27, 10, 2144, 2147, May 2017, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• A trimeric structural fusion of an antagonistic tumor necrosis factor-alpha mutant enhances molecular stability and enables facile modification
  Masaki Inoue; Daisuke Ando; Haruhiko Kamada; Shintaro Taki; Mayumi Niiyama; Yohei Mukai; Takashi Tadokoro; Katsumi Maenaka; Taisuke Nakayama; Yuji Kado; Tsuyoshi Inoue; Yasuo Tsutsumi; Shin-ichi Tsunoda
  JOURNAL OF BIOLOGICAL CHEMISTRY, 292, 16, 6438, 6451, Apr. 2017, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Isolated Polar Amino Acid Residues Modulate Lipid Binding in the Large Hydrophobic Cavity of CD1d
  Shinsuke Inuki; Toshihiko Aiba; Natsumi Hirata; Osamu Ichihara; Daisuke Yoshidome; Shunsuke Kita; Katsumi Maenaka; Koichi Fukase; Yukari Fujimoto
  ACS CHEMICAL BIOLOGY, 11, 11, 3132, 3139, Nov. 2016, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Rapid Screening by Cell-Based Fusion Assay for Identifying Novel Antivirals of Glycoprotein B-Mediated Herpes Simplex Virus Type 1 Infection
  Naoyoshi Maeda; Atsushi Furukawa; Kosuke Kakita; Masahiro Anada; Shunichi Hashimoto; Shigeki Matsunaga; Kimiko Kuroki; Toyoyuki Ose; Akihisa Kato; Jun Arii; Yasushi Kawaguchi; Hisashi Arase; Katsumi Maenaka
  BIOLOGICAL & PHARMACEUTICAL BULLETIN, 39, 11, 1897, 1902, Nov. 2016, [Peer-reviewed], [Domestic magazines]
  English, Scientific journal
• Measles Virus Hemagglutinin Protein Epitopes: The Basis of Antigenic Stability (vol 8, 216, 2016)
  Maino Tahara; Jean-Philippe Buerckert; Kazuhiko Kanou; Katsumi Maenaka; Claude P. Muller; Makoto Takeda
  VIRUSES-BASEL, 8, 11, Nov. 2016, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• HIV-1 Control by NK Cells via Reduced Interaction between KIR2DL2 and HLA-C*12:02/C*14:03
  Zhansong Lin; Kimiko Kuroki; Nozomi Kuse; Xiaoming Sun; Tomohiro Akahoshi; Ying Qi; Takayuki Chikata; Takuya Naruto; Madoka Koyanagi; Hayato Murakoshi; Hiroyuki Gatanaga; Shinichi Oka; Mary Carrington; Katsumi Maenaka; Masafumi Takiguchi
  CELL REPORTS, 17, 9, 2210, 2220, Nov. 2016, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• The immunosuppressive effect of domain-deleted dimer of HLA-G2 isoform in collagen-induced arthritis mice
  Ami Takahashi; Kimiko Kuroki; Yuki Okabe; Yoshiyuki Kasai; Naoki Matsumoto; Chisato Yamada; Toshiyuki Takai; Toyoyuki Ose; Shigeyuki Kon; Tadashi Matsuda; Katsumi Maenaka
  HUMAN IMMUNOLOGY, 77, 9, 754, 759, Sep. 2016, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Establishment of the BacMam system using silkworm baculovirus
  Atsutoshi Imai; Takashi Tadokoro; Shunsuke Kita; Masataka Horiuchi; Hideo Fukuhara; Katsumi Maenaka
  BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 478, 2, 580, 585, Sep. 2016, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Chemical Screening Identifies EUrd as a Novel Inhibitor Against Temozolomide-Resistant Glioblastoma-Initiating Cells
  Yoshihiro Tsukamoto; Naoki Ohtsu; Smile Echizenya; Satoko Otsuguro; Ryosuke Ogura; Manabu Natsumeda; Mizuho Isogawa; Hiroshi Aoki; Satoshi Ichikawa; Masahiro Sakaitani; Akira Matsuda; Katsumi Maenaka; Yukihiko Fujii; Toru Kondo
  STEM CELLS, 34, 8, 2016, 2025, Aug. 2016, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Synthesis and Th1-immunostimulatory activity of alpha-galactosylceramide analogues bearing a halogen-containing or selenium-containing acyl chain
  Md. Imran Hossain; Shinya Hanashima; Takuto Nomura; Sebastien Lethu; Hiroshi Tsuchikawa; Michio Murata; Hiroki Kusaka; Shunsuke Kita; Katsumi Maenaka
  BIOORGANIC & MEDICINAL CHEMISTRY, 24, 16, 3687, 3695, Aug. 2016, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Measles Virus Hemagglutinin Protein Epitopes: The Basis of Antigenic Stability
  Maino Tahara; Jean-Philippe Burckert; Kazuhiko Kanou; Katsumi Maenaka; Claude P. Muller; Makoto Takeda
  VIRUSES-BASEL, 8, 8, Aug. 2016, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Ribophorin II is involved in the tissue factor expression mediated by phosphatidylserine-dependent antiprothrombin antibody on monocytes
  Yuichiro Fujieda; Olga Amengual; Masaki Matsumoto; Kimiko Kuroki; Hidehisa Takahashi; Michihito Kono; Takashi Kurita; Kotaro Otomo; Masaru Kato; Kenji Oku; Toshiyuki Bohgaki; Tetsuya Horita; Shinsuke Yasuda; Katsumi Maenaka; Shigetsugu Hatakeyama; Keiichi I. Nakayama; Tatsuya Atsumi
  RHEUMATOLOGY, 55, 6, 1117, 1126, Jun. 2016, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Structures and Functions of MHC-like Proteins
  Shunsuke Kita; Katsumi Maenaka
  Encyclopedia of Immunobiology, 2, 271, 278, Elsevier Inc., 27 Apr. 2016, [Peer-reviewed]
  English, In book
• Binding affinity and biological activity evaluation of novel C-type lectin Mincle ligands
  Matsumaru Takanori; Furukawa Atsushi; Ikeno Risa; Shuchi Yusuke; Maenaka Katsumi
  ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 251, 13 Mar. 2016, [Peer-reviewed]
• Antibody-mediated molecular-targeted therapy for adult T-cell leukemia: recent progress and future challenges in the treatment of cancers.
  Maeda N; Matsuda A; Maenaka K
  Cancer Cell & Microenvironment, 3, 2, e1201, Mar. 2016, [Peer-reviewed]
  English, Scientific journal
• Structural aspects of C-type lectin receptors
  Atsushi Furukawa; Shunsuke Kita; Takashi Tadokoro; Hideo Fukuhara; Katsumi Maenaka
  C-Type Lectin Receptors in Immunity, 179, 190, Springer Japan, 01 Jan. 2016, [Peer-reviewed]
  English, In book
• Osteopontin-integrin interaction as a novel molecular target for antibody-mediated immunotherapy in adult T-cell leukemia
  Naoyoshi Maeda; Takashi Ohashi; Haorile Chagan-Yasutan; Toshio Hattori; Yayoi Takahashi; Hideo Harigae; Hiroo Hasegawa; Yasuaki Yamada; Masahiro Fujii; Katsumi Maenaka; Toshimitsu Uede
  RETROVIROLOGY, 12, 99, 99, Nov. 2015, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Solution structure of an avirulence protein, AVR-Pia, from Magnaporthe oryzae
  Toyoyuki Ose; Azusa Oikawa; Yukiko Nakamura; Katsumi Maenaka; Yuya Higuchi; Yuki Satoh; Shiho Fujiwara; Makoto Demura; Teruo Sone; Masakatsu Kamiya
  JOURNAL OF BIOMOLECULAR NMR, 63, 2, 229, 235, Oct. 2015, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• The cell competition-based high-throughput screening identifies small compounds that promote the elimination of RasV12-transformed cells from epithelia
  Hajime Yamauchi; Takanori Matsumaru; Tomoko Morita; Susumu Ishikawa; Katsumi Maenaka; Ichigaku Takigawa; Kentaro Semba; Shunsuke Kon; Yasuyuki Fujita
  SCIENTIFIC REPORTS, 5, 15336, 15336, Oct. 2015, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Effect of hydrophobic scaffold on the cellular uptake and gene transfection activities of DNA-encapsulating liposomal nanoparticles via intracerebroventricular administration
  Hidetaka Akita; Taichi Nakatani; Kimiko Kuroki; Katsumi Maenaka; Kota Tange; Yuta Nakai; Hideyoshi Harashima
  INTERNATIONAL JOURNAL OF PHARMACEUTICS, 490, 1-2, 142, 145, Jul. 2015, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Screening for FtsZ Dimerization Inhibitors Using Fluorescence Cross-Correlation Spectroscopy and Surface Resonance Plasmon Analysis
  Shintaro Mikuni; Kota Kodama; Akira Sasaki; Naoki Kohira; Hideki Maki; Masaharu Munetomo; Katsumi Maenaka; Masataka Kinjo
  PLOS ONE, 10, 7, e0130933, Jul. 2015, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Crystal structure of extracellular domain of human lectin-like transcript 1 (LLT1), the ligand for natural killer receptor-P1A
  Shunsuke Kita; Haruki Matsubara; Yoshiyuki Kasai; Takaharu Tamaoki; Yuki Okabe; Hideo Fukuhara; Jun Kamishikiryo; Elena Krayukhina; Susumu Uchiyama; Toyoyuki Ose; Kimiko Kuroki; Katsumi Maenaka
  EUROPEAN JOURNAL OF IMMUNOLOGY, 45, 6, 1605, 1613, Jun. 2015, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Heat Shock Protein 70 Regulates Degradation of the Mumps Virus Phosphoprotein via the Ubiquitin-Proteasome Pathway
  Hiroshi Katoh; Toru Kubota; Shunsuke Kita; Yuichiro Nakatsu; Natsuko Aoki; Yoshio Mori; Katsumi Maenaka; Makoto Takeda; Minoru Kidokoro
  JOURNAL OF VIROLOGY, 89, 6, 3188, 3199, Mar. 2015, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• New Binding Face of C-type Lectin-like Domains
  Hideo Fukuhara; Atsushi Furukawa; Katsumi Maenaka
  STRUCTURE, 22, 12, 1694, 1696, Dec. 2014, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• The structural basis for receptor recognition of human interleukin-18
  Naotaka Tsutsumi; Takeshi Kimura; Kyohei Arita; Mariko Ariyoshi; Hidenori Ohnishi; Takahiro Yamamoto; Xiaobing Zuo; Katsumi Maenaka; Enoch Y. Park; Naomi Kondo; Masahiro Shirakawa; Hidehito Tochio; Zenichiro Kato
  NATURE COMMUNICATIONS, 5, 5340, 5340, Dec. 2014, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• The N-terminal Arg Residue Is Essential for Autocatalytic Activation of a Lipopolysaccharide-responsive Protease Zymogen
  Yuki Kobayashi; Takafumi Shiga; Toshio Shibata; Miyuki Sako; Katsumi Maenaka; Takumi Koshiba; Hikaru Mizumura; Toshio Oda; Shun-ichiro Kawabata
  JOURNAL OF BIOLOGICAL CHEMISTRY, 289, 37, 25987, 25995, Sep. 2014, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Efficient and cost effective production of active-form human PKB using silkworm larvae
  Ryoko Maesaki; Ryosuke Satoh; Masato Taoka; Teppei Kanaba; Tsunaki Asano; Chiharu Fujita; Toshinobu Fujiwara; Yutaka Ito; Toshiaki Isobe; Toshio Hakoshima; Katsumi Maenaka; Masaki Mishima
  SCIENTIFIC REPORTS, 4, 6016, 6016, Aug. 2014, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILR alpha
  Kimiko Kuroki; Jing Wang; Toyoyuki Ose; Munechika Yamaguchi; Shigekazu Tabata; Nobuo Maita; Seiko Nakamura; Mizuho Kajikawa; Amane Kogure; Takeshi Satoh; Hisashi Arase; Katsumi Maenaka
  PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 111, 24, 8877, 8882, Jun. 2014, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• The Host Protease TMPRSS2 Plays a Major Role in In Vivo Replication of Emerging H7N9 and Seasonal Influenza Viruses
  Kouji Sakai; Yasushi Ami; Maino Tahara; Toru Kubota; Masaki Anraku; Masako Abe; Noriko Nakajima; Tsuyoshi Sekizuka; Kazuya Shirato; Yuriko Suzaki; Akira Ainai; Yuichiro Nakatsu; Kazuhiko Kanou; Kazuya Nakamura; Tadaki Suzuki; Katsuhiro Komase; Eri Nobusawa; Katsumi Maenaka; Makoto Kuroda; Hideki Hasegawa; Yoshihiro Kawaoka; Masato Tashiro; Makoto Takeda
  JOURNAL OF VIROLOGY, 88, 10, 5608, 5616, May 2014, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Heterologous production, purification, and immunodetection of Magnaporthe oryzae avirulence protein AVR-Pia
  Yuki Satoh; Shinsuke Miki; Toyoyuki Ose; Azusa Oikawa; Katsumi Maenaka; Ryouhei Terauchi; Kozo Asano; Teruo Sone
  BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, 78, 4, 680, 686, Apr. 2014, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• NKG2D Triggers Cytotoxicity in Murine Epidermal gamma delta T Cells via PI3K-Dependent, Syk/ZAP70-Independent Signaling Pathway
  Atsuko Ibusuki; Kazuhiro Kawai; Shigeru Yoshida; Youhei Uchida; Ayano Nitahara-Takeuchi; Kimiko Kuroki; Mizuho Kajikawa; Toyoyuki Ose; Katsumi Maenaka; Masanori Kasahara; Takuro Kanekura
  JOURNAL OF INVESTIGATIVE DERMATOLOGY, 134, 2, 396, 404, Feb. 2014, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Allosteric Regulation of Epoxide Opening Cascades by a Pair of Epoxide Hydrolases in Monensin Biosynthesis
  Atsushi Minami; Toyoyuki Ose; Kyohei Sato; Azusa Oikawa; Kimiko Kuroki; Katsumi Maenaka; Hiroki Oguri; Hideaki Oikawa
  ACS CHEMICAL BIOLOGY, 9, 2, 562, 569, Feb. 2014, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• 1P005 Structure analysis of lectin-like transcript 1 (LLT1) and model building of LLT1-CD161 complex(Protein: Structure,Poster,The 52th Annual Meeting of the Biophysical Society of Japan(BSJ2014))
  Shunsuke Kita; Haruki Matsubara; Jun Kamishikiryo; Yuki Okabe; Hideo Fukuhara; Kimiko Kuroki; Katsumi Maenaka
  Seibutsu Butsuri, 54, 1, S141, The Biophysical Society of Japan General Incorporated Association, 2014
  English
• Crystal Structure of the Lamprey Variable Lymphocyte Receptor C Reveals an Unusual Feature in Its N-Terminal Capping Module
  Ryo Kanda; Yoichi Sutoh; Jun Kasamatsu; Katsumi Maenaka; Masanori Kasahara; Toyoyuki Ose
  PLOS ONE, 9, 1, e85875, Jan. 2014, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• TMPRSS2 Is an Activating Protease for Respiratory Parainfluenza Viruses
  Masako Abe; Maino Tahara; Kouji Sakai; Hiromi Yamaguchi; Kazuhiko Kanou; Kazuya Shirato; Miyuki Kawase; Masahiro Noda; Hirokazu Kimura; Shutoku Matsuyama; Hideo Fukuhara; Katsumi Mizuta; Katsumi Maenaka; Yasushi Ami; Mariko Esumi; Atsushi Kato; Makoto Takeda
  JOURNAL OF VIROLOGY, 87, 21, 11930, 11935, Nov. 2013, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Structural and functional mosaic nature of MHC class I molecules in their peptide-free form
  Eiji Kurimoto; Kimiko Kuroki; Yoshiki Yamaguchi; Maho Yagi-Utsumi; Takahiro Igaki; Takeshi Iguchi; Katsumi Maenaka; Koichi Kato
  Molecular Immunology, 55, 3-4, 393, 399, Oct. 2013, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Structural analysis for glycolipid recognition by the C-type lectins Mincle and MCL
  Atsushi Furukawa; Jun Kamishikiryo; Daiki Mori; Kenji Toyonaga; Yuki Okabe; Aya Toji; Ryo Kanda; Yasunobu Miyake; Toyoyuki Ose; Sho Yamasaki; Katsumi Maenaka
  PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 110, 43, 17438, 17443, Oct. 2013, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Functional Characterization of a Juvenile Hormone Esterase Related Gene in the Moth Sesamia nonagrioides through RNA Interference
  Dimitrios Kontogiannatos; Luc Swevers; Katsumi Maenaka; Enoch Y. Park; Kostas Iatrou; Anna Kourti
  PLOS ONE, 8, 9, e73834, Sep. 2013, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Entry Mechanism of Morbillivirus Family
  Hideo Fukuhara; Surui Chen; Shin Takeda; Katsumi Maenaka
  YAKUGAKU ZASSHI-JOURNAL OF THE PHARMACEUTICAL SOCIETY OF JAPAN, 133, 5, 549, 559, May 2013, [Peer-reviewed], [Domestic magazines]
  Japanese, Scientific journal
• The long-term immunosuppressive effects of disulfide-linked HLA-G dimer in mice with collagen-induced arthritis
  Kimiko Kuroki; Kaoru Hirose; Yuki Okabe; Yuko Fukunaga; Ami Takahashi; Mitsunori Shiroishi; Mizuho Kajikawa; Shigekazu Tabata; Seiko Nakamura; Toshiyuki Takai; Satoru Koyanagi; Shigehiro Ohdo; Katsumi Maenaka
  HUMAN IMMUNOLOGY, 74, 4, 433, 438, Apr. 2013, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• The Receptor-Binding Site of the Measles Virus Hemagglutinin Protein Itself Constitutes a Conserved Neutralizing Epitope
  Maino Tahara; Shinji Ohno; Kouji Sakai; Yuri Ito; Hideo Fukuhara; Katsuhiro Komase; Melinda A. Brindley; Paul A. Rota; Richard K. Plemper; Katsumi Maenaka; Makoto Takeda
  JOURNAL OF VIROLOGY, 87, 6, 3583, 3586, Mar. 2013, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Distinct HIV-1 Escape Patterns Selected by Cytotoxic T Cells with Identical Epitope Specificity
  Yuichi Yagita; Nozomi Kuse; Kimiko Kuroki; Hiroyuki Gatanaga; Jonathan M. Carlson; Takayuki Chikata; Zabrina L. Brumme; Hayato Murakoshi; Tomohiro Akahoshi; Nico Pfeifer; Simon Mallal; Mina John; Toyoyuki Ose; Haruki Matsubara; Ryo Kanda; Yuko Fukunaga; Kazutaka Honda; Yuka Kawashima; Yasuo Ariumi; Shinichi Oka; Katsumi Maenaka; Masafumi Takiguchi
  JOURNAL OF VIROLOGY, 87, 4, 2253, 2263, Feb. 2013, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Functional and Structural Characterization of Neutralizing Epitopes of Measles Virus Hemagglutinin Protein
  Maino Tahara; Yuri Ito; Melinda A. Brindley; Xuemin Ma; Jilan He; Songtao Xu; Hideo Fukuhara; Kouji Sakai; Katsuhiro Komase; Paul A. Rota; Richard K. Plemper; Katsumi Maenaka; Makoto Takeda
  JOURNAL OF VIROLOGY, 87, 1, 666, 675, Jan. 2013, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Canine distemper virus with the intact C protein has the potential to replicate in human epithelial cells by using human nectin4 as a receptor
  Noriyuki Otsuki; Tsuyoshi Sekizuka; Fumio Seki; Kouji Sakai; Toru Kubota; Yuichiro Nakatsu; Surui Chen; Hideo Fukuhara; Katsumi Maenaka; Ryoji Yamaguchi; Makoto Kuroda; Makoto Takeda
  VIROLOGY, 435, 2, 485, 492, Jan. 2013, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• 3P006 Three dimensional reconstruction of HLA-G2/G6 isoform(01A. Protein: Structure,Poster)
  Mio Kazuhiro; Kuroki Kimiko; Matsubara Haruki; Kasai Yoshiyuki; Sato Chikara; Maenaka Katsumi
  Seibutsu Butsuri, 53, 1, S212, The Biophysical Society of Japan General Incorporated Association, 2013
  English
• Fabrication of growth factor- and extracellular matrix-loaded, gelatin-based scaffolds and their biocompatibility with Schwann cells and dorsal root ganglia
  Rodolfo E. Gamez Sazo; Katsumi Maenaka; Weiyong Gu; Patrick M. Wood; Mary Bartlett Bunge
  BIOMATERIALS, 33, 33, 8529, 8539, Nov. 2012, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Inhibiting HLA-B27 homodimer-driven immune cell inflammation in spondylarthritis
  Sravan K. Payeli; Simon Kollnberger; Osiris Marroquin Belaunzaran; Markus Thiel; Kirsty McHugh; Joanna Giles; Jacqueline Shaw; Sascha Kleber; Anna Ridley; Isabel Wong-Baeza; Sarah Keidel; Kimiko Kuroki; Katsumi Maenaka; Andreas Wadle; Christoph Renner; Paul Bowness
  ARTHRITIS AND RHEUMATISM, 64, 10, 3139, 3149, Oct. 2012, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Establishment of a Bombyx mori nucleopolyhedrovirus (BmNPV) hyper-sensitive cell line from the silkworm e21 strain
  Jae Man Lee; Naoya Kawakami; Hiroaki Mon; Hitoshi Mitsunobu; Kazuhiro Iiyama; Satoshi Ninaki; Katsumi Maenaka; Enoch Y. Park; Takahiro Kusakabe
  BIOTECHNOLOGY LETTERS, 34, 10, 1773, 1779, Oct. 2012, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Ribophorin II Is Involved in the Tissue Factor Expression Mediated by Phosphatidylserine-Dependent Antiprothrombin Antibody On Monocytes.
  Yuichiro Fujieda; Olga Amengual; Yusaku Kanetsuka; Toshio Odani; Kotaro Otomo; Kenji Oku; Toshiyuki Bohgaki; Tetsuya Horita; Shinsuke Yasuda; Kimiko Kuroki; Katsumi Maenaka; Masaki Matsumoto; Shigetsugu Hatakeyama; Tatsuya Atsumi
  ARTHRITIS AND RHEUMATISM, 64, 10, S741, S741, Oct. 2012, [Peer-reviewed]
  English
• Simultaneous inhibition of Src and Aurora kinases by SU6656 induces therapeutic synergy in human synovial sarcoma growth, invasion and angiogenesis in vivo
  Ryuta Arai; Masumi Tsuda; Takuya Watanabe; Toyoyuki Ose; Chikashi Obuse; Katsumi Maenaka; Akio Minami; Yusuke Ohba
  EUROPEAN JOURNAL OF CANCER, 48, 15, 2417, 2430, Oct. 2012, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Nectin4 Is an Epithelial Cell Receptor for Canine Distemper Virus and Involved in Neurovirulence
  Watanyoo Pratakpiriya; Fumio Seki; Noriyuki Otsuki; Kouji Sakai; Hideo Fukuhara; Hiromu Katamoto; Takuya Hirai; Katsumi Maenaka; Somporn Techangamsuwan; Nguyen Thi Lan; Makoto Takeda; Ryoji Yamaguchi
  JOURNAL OF VIROLOGY, 86, 18, 10207, 10210, Sep. 2012, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• HLA-B27 Homodimers and Free H Chains Are Stronger Ligands for Leukocyte Ig-like Receptor B2 than Classical HLA Class I
  Joanna Giles; Jackie Shaw; Christopher Piper; Isabel Wong-Baeza; Kirsty McHugh; Anna Ridley; Demin Li; Izabela Lenart; Antony N. Antoniou; Katilin DiGleria; Kimiko Kuroki; Katsumi Maenaka; Paul Bowness; Simon Kollnberger
  JOURNAL OF IMMUNOLOGY, 188, 12, 6184, 6193, Jun. 2012, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Involvement of an NKG2D ligand H60c in epidermal dendritic T cell-mediated wound repair
  Shigeru Yoshida; Rania Hassan Mohamed; Mizuho Kajikawa; Jun Koizumi; Minami Tanaka; Kazunori Fugo; Noriyuki Otsuka; Katsumi Maenaka; Hideo Yagita; Hitoshi Chiba; Masanori Kasahara
  Journal of Immunology, 188, 8, 3972, 3979, 15 Apr. 2012, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Blockade of interaction between NKG2D and an NKG2D ligand H60c delays wound repair
  Yoshida S; Mohamed RH; Kajikawa M; Koizumi J; Tanaka M; Fugo K; Otsuka N; Maenaka K; Yagita H; Chiba H; Kasahara M
  Journal of Immunology, 188, 8, 3972, 3979, Apr. 2012, [Peer-reviewed]
  English, Scientific journal
• Crystallization Strategy for the Glycoprotein-Receptor Complex Between Measles Virus Hemagglutinin and Its Cellular Receptor SLAM
  Takao Hashiguchi; Toyoyuki Ose; Marie Kubota; Nobuo Maita; Jun Kamishikiryo; Katsumi Maenaka; Yusuke Yanagi
  PROTEIN AND PEPTIDE LETTERS, 19, 4, 468, 473, Apr. 2012, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• [Structural basis for measles virus-receptor recognition and its functional implications for viral entry and vaccination].
  Maenaka K; Hashiguchi T; Yanagi Y
  Nihon rinsho. Japanese journal of clinical medicine, 70, 4, 695, 703, Apr. 2012, [Peer-reviewed], [Domestic magazines]
  Japanese, Scientific journal, Measles is one of the most contagious and devastating viral diseases. However, highly effective live vaccines have been successfully used for more than five decades. Recent structural studies of measles virus hemagglutinin and its complexes with receptors (the signaling lymphocyte activation molecule (SLAM, CD150) and CD46) have provided many insights into measles virus entry mechanism. Furthermore, the sugar shields that cover the large surface areas of the hemagglutinin have implications for effective measles virus vaccination. These studies should help strengthen current global efforts to control and eliminate measles worldwide.
• Molecular recognition of paired receptors in the immune system
  Kimiko Kuroki; Atsushi Furukawa; Katsumi Maenaka
  FRONTIERS IN MICROBIOLOGY, 3, 429, 429, 2012, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Molecular Basis for Herpesvirus Entry Mediator Recognition by the Human Immune Inhibitory Receptor CD160 and Its Relationship to the Cosignaling Molecules BTLA and LIGHT
  Rieko Kojima; Mizuho Kajikawa; Mitsunori Shiroishi; Kimiko Kuroki; Katsumi Maenaka
  JOURNAL OF MOLECULAR BIOLOGY, 413, 4, 762, 772, Nov. 2011, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Construction, Expression, and Characterization of a Single-Chain Variable Fragment Antibody Against 2,4-Dichlorophenoxyacetic Acid in the Hemolymph of Silkworm Larvae
  Seiichi Sakamoto; Benyakan Pongkitwitoon; Seiko Nakamura; Kaori Sasaki-Tabata; Yusuke Tanizaki; Katsumi Maenaka; Hiroyuki Tanaka; Satoshi Morimoto
  APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 164, 6, 715, 728, Jul. 2011, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Molecular Basis for LLT1 Protein Recognition by Human CD161 Protein (NKRP1A/KLRB1)
  Jun Kamishikiryo; Hideo Fukuhara; Yuki Okabe; Kimiko Kuroki; Katsumi Maenaka
  JOURNAL OF BIOLOGICAL CHEMISTRY, 286, 27, 23823, 23830, Jul. 2011, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Differential but Competitive Binding of Nogo Protein and Class I Major Histocompatibility Complex (MHCI) to the PIR-B Ectodomain Provides an Inhibition of Cells
  Haruka Matsushita; Shota Endo; Eiji Kobayashi; Yuzuru Sakamoto; Keisuke Kobayashi; Kohji Kitaguchi; Kimiko Kuroki; Arvid Soderhall; Katsumi Maenaka; Akira Nakamura; Stephen M. Strittmatter; Toshiyuki Takai
  JOURNAL OF BIOLOGICAL CHEMISTRY, 286, 29, 25739, 25747, Jul. 2011, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM
  Takao Hashiguchi; Toyoyuki Ose; Marie Kubota; Nobuo Maita; Jun Kamishikiryo; Katsumi Maenaka; Yusuke Yanagi
  NATURE STRUCTURAL & MOLECULAR BIOLOGY, 18, 2, 135, U191, Feb. 2011, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• A fluorescent single domain antibody against plumbagin expressed in silkworm larvae for fluorescence-linked immunosorbent assay (FLISA)
  Seiichi Sakamoto; Benyakan Pongkitwitoon; Kaori Sasaki-Tabata; Waraporn Putalun; Katsumi Maenaka; Hiroyuki Tanaka; Satoshi Morimoto
  ANALYST, 136, 10, 2056, 2063, 2011, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Analysis of receptor-ligand interactions by surface plasmon resonance.
  Kuroki K; Maenaka K
  Methods in molecular biology (Clifton, N.J.), 748, 83, 106, 2011, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Many immunological responses are often regulated by cell surface receptors in cell-cell recognition events. Such immune receptors on the cell surface typically exhibit low-affinity and fast-kinetic ligand interactions (e.g., K (d) in the μM range, k (off)  =  10(-2) to 20 s(-1)). Real-time surface plasmon resonance (SPR) detection systems are generally useful for determining these binding parameters. However, several technical points should be considered because the determination of low-affinity binding and fast kinetics is often rather difficult. Here, we introduce a general procedure for SPR experiments and, moreover, show typical examples for ligand binding of immune cell surface receptors, including experimentally useful tips. We also show how to determine the thermodynamic characteristics using the nonlinear van't Hoff and Arrhenius analyses. These affinity, kinetic, and thermodynamic parameters of immune-receptor binding are important for understanding immunological events as well as developing drugs and vaccines.
• Structures and molecular recognition for leukocyte immunoglobulin-like receptor family
  Kimiko Kuroki; Katsumi Maenaka
  Seikagaku, 83, 8, 715, 726, 東京 : 日本生化学会, 2011, [Peer-reviewed], [Domestic magazines]
  Japanese
• Measles virus hemagglutinin: structural insights into cell entry and measles vaccine
  Takao Hashiguchi; Katsumi Maenaka; Yusuke Yanagi
  FRONTIERS IN MICROBIOLOGY, 2, 247, 247, 2011, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Efficient silkworm expression of single-chain variable fragment antibody against ginsenoside Re using Bombyx mori nucleopolyhedrovirus bacmid DNA system and its application in enzyme-linked immunosorbent assay for quality control of total ginsenosides
  Seiichi Sakamoto; Benyakan Pongkitwitoon; Seiko Nakamura; Katsumi Maenaka; Hiroyuki Tanaka; Satoshi Morimoto
  JOURNAL OF BIOCHEMISTRY, 148, 3, 335, 340, Sep. 2010, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Long-Term Control of HIV-1 in Hemophiliacs Carrying Slow-Progressing Allele HLA-B*5101
  Yuka Kawashima; Nozomi Kuse; Hiroyuki Gatanaga; Takuya Naruto; Mamoru Fujiwara; Sachi Dohki; Tomohiro Akahoshi; Katsumi Maenaka; Philip Goulder; Shinichi Oka; Masafumi Takiguchi
  JOURNAL OF VIROLOGY, 84, 14, 7151, 7160, Jul. 2010, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Dictyostelium Differentiation-Inducing Factor-1 Binds to Mitochondrial Malate Dehydrogenase and Inhibits Its Activity
  Tomoko Matsuda; Fumi Takahashi-Yanaga; Tatsuya Yoshihara; Katsumi Maenaka; Yutaka Watanabe; Yoshikazu Miwa; Sachio Morimoto; Yuzuru Kubohara; Masato Hirata; Toshiyuki Sasaguri
  JOURNAL OF PHARMACOLOGICAL SCIENCES, 112, 3, 320, 326, Mar. 2010, [Peer-reviewed], [Domestic magazines]
  English, Scientific journal
• Silkworm expression system as a platform technology in life science
  Tatsuya Kato; Mizuho Kajikawa; Katsumi Maenaka; Enoch Y. Park
  APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 85, 3, 459, 470, Jan. 2010, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Importance of the Hydrogen Bonding Network Including Asp52 for Catalysis, as Revealed by Asn59 Mutant Hen Egg-white Lysozymes
  Toyoyuki Ose; Kimiko Kuroki; Masaaki Matsushima; Katsumi Maenaka; Izumi Kumagai
  JOURNAL OF BIOCHEMISTRY, 146, 5, 651, 657, Nov. 2009, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Molecular Basis for E-cadherin Recognition by Killer Cell Lectin-like Receptor G1 (KLRG1)
  Seiko Nakamura; Kimiko Kuroki; Izuru Ohki; Kaori Sasaki; Mizuho Kajikawa; Takuma Maruyama; Masayuki Ito; Yosuke Kameda; Mitsuhiko Ikura; Kazuo Yamamoto; Naoki Matsumoto; Katsumi Maenaka
  JOURNAL OF BIOLOGICAL CHEMISTRY, 284, 40, 27327, 27335, Oct. 2009, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Silkworm expression and sugar profiling of human immune cell surface receptor, KIR2DL1.
  Kaori Sasaki; Mizuho Kajikawa; Kimiko Kuroki; Tomoko Motohashi; Tsukasa Shimojima; Enoch Y Park; Sachiko Kondo; Hirokazu Yagi; Koichi Kato; Katsumi Maenaka
  Biochemical and biophysical research communications, 387, 3, 575, 80, 25 Sep. 2009, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Immune cell surface receptors are directly involved in human diseases, and thus represent major drug targets. However, it is generally difficult to obtain sufficient amounts of these receptors for biochemical and structural studies because they often require posttranslational modifications, especially sugar modification. Recently, we have established a bacmid expression system for the baculovirus BmNPV, which directly infects silkworms, an attractive host for the large-scale production of recombinant sugar-modified proteins. Here we produced the human immune cell surface receptor, killer cell Ig-like receptor 2DL1 (KIR2DL1), by using the BmNPV bacmid expression system, in silkworms. By the direct injection of the bacmid DNA, the recombinant KIR2DL1 protein was efficiently expressed, secreted into body fluids, and purified by Ni(2+) affinity column chromatography. We further optimized the expression conditions, and the final yield was 0.2mg/larva. The sugar profiling revealed that the N-linked sugars of the purified protein comprised very few components, two paucimannose-type oligosaccharides, Manalpha1-6Manbeta1-4GlcNAcbeta1-4GlcNAc and Manalpha1-6Manbeta1-4GlcNAcbeta1-4(Fucalpha1-6)GlcNAc. This revealed that the protein product was much more homogeneous than the complex-sugar type product obtained by mammalian cell expression. The surface plasmon resonance analysis demonstrated that the purified KIR2DL1 protein exhibited specific binding to the HLA-Cw4 ligand. Moreover, the CD spectrum showed the proper secondary structure. These results clearly suggested that the silkworm expression system is quite useful for the expression of cell surface receptors that require posttranslational modifications, as well as for their structural and binding studies, due to the relatively homogeneous N-linked sugar modifications.
• HLA-G Molecule
  Jun Kamishikiryo; Katsumi Maenaka
  CURRENT PHARMACEUTICAL DESIGN, 15, 28, 3318, 3324, Sep. 2009, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Efficient silkworm expression of human GPCR (nociceptin receptor) by a Bombyx mori bacmid DNA system
  Mizuho Kajikawa; Kaori Sasaki; Yoshitaro Wakimoto; Masaru Toyooka; Tomoko Motohashi; Tsukasa Shimojima; Shigeki Takeda; Enoch Y. Park; Katsumi Maenaka
  BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 385, 3, 375, 379, Jul. 2009, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Crystallization and Preliminary X-Ray Analysis of the Low-Affinity Complex Between Human Leukocyte Antigen-G (HLA-G) and Leukocyte Ig-Like Receptor B2 (LILRB2)
  Mitsunori Shiroishi; Katsumi Maenaka
  PROTEIN AND PEPTIDE LETTERS, 16, 4, 447, 449, Apr. 2009, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Reciprocal recognition of an HLA-Cw4-restricted HIV-1 gp120 epitope by CD8(+) T cells and NK cells
  Hathairat Thananchai; Tariro Makadzange; Katsumi Maenaka; Kimiko Kuroki; Yanchun Peng; Chris Conlon; Sarah Rowland-Jones; Tao Dong
  AIDS, 23, 2, 189, 193, Jan. 2009, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Enzyme-mediated protein refolding
  Jun Okada; Tatsuo Maruyama; Konomi Motomura; Kimiko Kuroki; Katsumi Maenaka; Masafumi Sakono; Masahiro Goto
  CHEMICAL COMMUNICATIONS, 46, 7197, 7199, 2009, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Efficient protein expression in Bombyx mori larvae of the strain d17 highly sensitive to B-Mori nucleopolyhedrovirus
  Naoya Kawakami; Jae Man Lee; Hiroaki Mon; Yuji Kubo; Yutaka Banno; Yutaka Kawaguchi; Katsumi Maenaka; Enoch Y. Park; Katsumi Koga; Takahiro Kusakabe
  MOLECULAR BIOTECHNOLOGY, 40, 2, 180, 185, Oct. 2008, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Serotriflin, a CRISP family protein with binding affinity for small serum protein-2 in snake serum
  Narumi Aoki; Akie Sakiyama; Kimiko Kuroki; Katsumi Maenaka; Daisuke Kohda; Masanobu Deshimaru; Shigeyuki Terada
  BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1784, 4, 621, 628, Apr. 2008, [Peer-reviewed]
  English, Scientific journal
• Association of LILRA2 (ILT1, LIR7) splice site polymorphism with systemic lupus erythematosus and microscopic polyangiitis
  K. Mamegano; K. Kuroki; R. Miyashita; M. Kusaoi; S. Kobayashi; K. Matsuta; K. Maenaka; M. Colonna; S. Ozaki; H. Hashimoto; Y. Takasaki; K. Tokunaga; N. Tsuchiya
  GENES AND IMMUNITY, 9, 3, 214, 223, Apr. 2008, [Peer-reviewed]
  English, Scientific journal
• Serotriflin, a CRISP family protein with binding affinity for small serum protein-2 in snake serum.
  Aoki N; Sakiyama A; Kuroki K; Maenaka K; Kohda D; Deshimaru M; Terada S
  Biochimica et biophysica acta, 1784, 4, 621, 628, Apr. 2008, [Peer-reviewed], [International Magazine]
  English, Scientific journal, Habu (Trimeresurus flavoviridis) serum contains 3 small serum proteins (SSP-1, SSP-2, and SSP-3) with molecular masses of 6.5 to 10 kDa. Gel filtration analysis showed that all the SSPs exist in high molecular mass forms of approximately 60 kDa in the serum. Ultrafiltration of Habu serum showed that SSPs dissociated from the complex below a pH of 4. An SSP-binding protein was purified from Habu serum by gel filtration, ion exchange, and reverse-phase HPLC. N-terminal sequencing yielded a 39-amino acid sequence, similar to the N-terminal region of triflin, which is a snake venom-derived Ca2+ channel blocker that suppresses smooth muscle contraction. The amino acid sequence of this protein, termed serotriflin, was established by peptide analysis and cDNA cloning. Serotriflin is a glycosylated protein and consists of 221 amino acids. Among the 3 SSPs, only SSP-2 formed a noncovalent complex with serotriflin. It was bound to triflin and serotriflin with high affinity, as evidenced by surface plasmon resonance. SSP-2 is considered to be a protein that prevents self injury by accidental leaking of venom into the blood.
• Biophysical characterization of O-glycosylated CD99 recognition by paired ig-like type 2 receptors
  Shigekazu Tabata; Kimiko Kuroki; Jing Wang; Mizuho Kajikawa; Ikuo Shiratori; Daisuke Kohda; Hisashi Arase; Katsumi Maenaka
  JOURNAL OF BIOLOGICAL CHEMISTRY, 283, 14, 8893, 8901, Apr. 2008, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Dynamic interaction of the measles virus hemagglutinin with its receptor signaling lymphocytic activation molecule (SLAM, CD150)
  Chanakha K. Navaratnarajah; Sompong Vongpunsawad; Numan Oezguen; Thilo Stehle; Werner Braun; Takao Hashiguchi; Katsumi Maenaka; Yusuke Yanagi; Roberto Cattaneo
  JOURNAL OF BIOLOGICAL CHEMISTRY, 283, 17, 11763, 11771, Apr. 2008, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Homogeneous sugar modification improves crystallization of measles virus hemagglutinin
  Takao Hashiguchi; Mizuho Kajikawa; Maita Nobuo; Makoto Takeda; Kimiko Kuroki; Kaori Sasaki; Daisuke Kohda; Yusuke Yanagi; Katsumi Maenaka
  JOURNAL OF VIROLOGICAL METHODS, 149, 1, 171, 174, Apr. 2008, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• CENP-O class proteins form a stable complex and are required for proper kinetochore function
  Tetsuya Hori; Masahiro Okada; Katsumi Maenaka; Tatsuo Fukagawa
  MOLECULAR BIOLOGY OF THE CELL, 19, 3, 843, 854, Mar. 2008, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Two novel NKG2D ligands of the mouse H60 family with differential expression patterns and binding affinities to NKG2D
  Akio Takada; Shigeru Yoshida; Mizuho Kajikawa; Yukiko Miyatake; Utano Tomaru; Masaharu Sakai; Hitoshi Chiba; Katsumi Maenaka; Daisuke Kohda; Kazunori Fugo; Masanori Kasahara
  JOURNAL OF IMMUNOLOGY, 180, 3, 1678, 1685, Feb. 2008, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• 3P-015 Structural analyses of β2 microglobulin in MHC complex by NMR spectroscopy(The 46th Annual Meeting of the Biophysical Society of Japan)
  Kurimoto Eiji; Yamaguchi Yoshiki; Kuroki Kimiko; Maenaka Katsumi; Kohda Daisuke; Kato Koichi
  Seibutsu Butsuri, 48, S130, The Biophysical Society of Japan General Incorporated Association, 2008
  English
• Structure-guided identification of a new catalytic motif of oligosaccharyltransferase
  Mayumi Igura; Nobuo Maita; Jun Kamishikiryo; Masaki Yamada; Takayuki Obita; Katsumi Maenaka; Daisuke Kohda
  EMBO JOURNAL, 27, 1, 234, 243, Jan. 2008, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Expression, crystallization and preliminary X-ray diffraction analysis of human paired Ig-like type 2 receptor alpha (PILR alpha)
  Shigekazu Tabata; Kimiko Kuroki; Nobuo Maita; Jing Wang; Ikuo Shiratori; Hisashi Arase; Daisuke Kohda; Katsumi Maenaka
  ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, 64, Pt 1, 44, 46, Jan. 2008, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Crystal structure of measles virus hemagglutinin provides insight into effective vaccines
  Takao Hashiguchi; Mizuho Kajikawa; Nobuo Maita; Makoto Takeda; Kimiko Kuroki; Kaori Sasaki; Daisuke Kohda; Yusuke Yanagi; Katsumi Maenaka
  PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 104, 49, 19535, 19540, Dec. 2007, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• New oligosaccharyltransferase assay method
  Daisuke Kohda; Masaki Yamada; Mayumi Igura; Jun Kamishikiryo; Katsumi Maenaka
  GLYCOBIOLOGY, 17, 11, 1175, 1182, Nov. 2007, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Tom20 recognizes mitochondrial presequences through dynamic equilibrium among multiple bound states
  Takashi Saitoh; Mayumi Igura; Takayuki Obita; Toyoyuki Ose; Rieko Kojima; Katsumi Maenaka; Toshiya Endo; Daisuke Kohda
  EMBO JOURNAL, 26, 22, 4777, 4787, Nov. 2007, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Purification, crystallization and preliminary X-ray diffraction studies of the soluble domain of the oligosaccharyltransferase STT3 subunit from the thermophilic archaeon Pyrococcus furiosus
  Mayumi Igura; Nobuo Maita; Takayuki Obita; Jun Kamishikiryo; Katsumi Maenaka; Daisuke Kohda
  ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, 63, Pt 9, 798, 801, Sep. 2007, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Immune modulation of HLA-G dimer in maternal-fetal interface
  Kirniko Kuroki; Katsurni Maenaka
  EUROPEAN JOURNAL OF IMMUNOLOGY, 37, 7, 1727, 1729, Jul. 2007, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Structural basis of the 3'-end recognition of a leading strand in stalled replication forks by PriA
  Kaori Sasaki; Toyoyuki Ose; Naoaki Okamoto; Katsumi Maenaka; Taku Tanaka; Hisao Masai; Mihoko Saito; Tsuyoshi Shirai; Daisuke Kohda
  EMBO JOURNAL, 26, 10, 2584, 2593, May 2007, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Structural basis for dynamic interdomain movement and RNA recognition of the selenocysteine-specific elongation factor SelB
  Toyoyuki Ose; Nicolas Soler; Linda Rasubala; Kimiko Kuroki; Daisuke Kohda; Dominique Fourmy; Satoko Yoshizawa; Katsumi Maenaka
  STRUCTURE, 15, 5, 577, 586, May 2007, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Detection of weak ligand interactions of leukocyte Ig-like receptor B1 by fluorescence correlation spectroscopy
  Kimiko Kuroki; Sayoko Kobayashi; Mitsunori Shiroishi; Mizuho Kajikawa; Naoaki Okamoto; Daisuke Kohda; Katsumi Maenaka
  JOURNAL OF IMMUNOLOGICAL METHODS, 320, 1-2, 172, 176, Mar. 2007, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Cutting edge: Allele-specific and peptide-dependent interactions between KIR3DL1 and HLA-A and HLA-B
  Hathairat Thananchai; Geraldine Gillespie; Maureen P. Martin; Arman Bashirova; Nobuyo Yawata; Makoto Yawata; Philippa Easterbrook; Daniel W. McVicar; Katsumi Maenaka; Peter Parham; Mary Carrington; Tao Dong; Sarah Rowland-Jones
  JOURNAL OF IMMUNOLOGY, 178, 1, 33, 37, Jan. 2007, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Structural basis for recognition of the nonclassical MHC molecule HLA-G by the leukocyte Ig-like receptor B2 (LILRB2/LIR2/ILT4/CD85d)
  Mitsunori Shiroishi; Kimiko Kuroki; Linda Rasubala; Kouhei Tsumoto; Izumi Kumagai; Eiji Kurimoto; Koichi Kato; Daisuke Kohda; Katsumi Maenaka
  PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 103, 44, 16412, 16417, Oct. 2006, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• MHC class I-like MILL molecules are beta(2)-microglobulin-associated, GPI-anchored glycoproteins that do not require TAP for cell surface expression
  Mizuho Kajikawa; Tomohisa Baba; Utano Tomaru; Yutaka Watanabe; Satoru Koganei; Sachiyo Tsuji-Kawahara; Naoki Matsumoto; Kazuo Yamamoto; Masaaki Miyazawa; Katsumi Maenaka; Akihiro Shizu; Masanori Kasahara
  JOURNAL OF IMMUNOLOGY, 177, 5, 3108, 3115, Sep. 2006, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Crystal structure of the human monocyte-activating receptor, "Group 2" leukocyte Ig-like receptor A5 (LILRA5/LIR9/ILT11)
  Mitsunori Shiroishi; Mizuho Kajikawa; Kimiko Kuroki; Toyoyuki Ose; Daisuke Kohda; Katsumi Maenaka
  JOURNAL OF BIOLOGICAL CHEMISTRY, 281, 28, 19536, 19544, Jul. 2006, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Expression of spider flagelliform silk protein in Bombyx mori cell line by a novel Bac-to-Bac/BmNPV baculovirus expression system
  Yungen Miao; Yuansong Zhang; Koichi Nakagaki; Tianfu Zhao; Aichun Zhao; Yan Meng; Masao Nakagaki; Enoch Y. Park; Katsumi Maenaka
  APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 71, 2, 192, 199, Jun. 2006, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Preparation and crystallization of the disulfide-linked HLA-G dimer
  M Shiroishi; D Kohda; K Maenaka
  BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1764, 5, 985, 988, May 2006, [Peer-reviewed]
  English, Scientific journal
• Preparation and crystallization of the disulfide-linked HLA-G dimer.
  Shiroishi M; Kohda D; Maenaka K
  Biochimica et biophysica acta, 1764, 5, 985, 988, May 2006, [Peer-reviewed], [International Magazine]
  English, Scientific journal, HLA-G is a non-classical MHC class I, which binds to inhibitory receptors, such as Leukocyte Ig-like receptors, to induce a wide range of tolerogenic immunological effects. HLA-G can be expressed as a disulfide-liked dimer both in solution and at the cell surface. However, the three-dimensional structure of the HLA-G dimer is unknown. Here, we report the crystallization of the disulfide-linked dimer form of HLA-G by adding dithiothreitol (DTT), enabling a 3.2-A data set to be collected. We also show that DTT promotes disulfide bond exchange of refolded HLA-G, whose free cysteine was protected, thus facilitating its dimerization. This technique could also be applied for disulfide-mediated dimer/multimer formation of refolded proteins harbouring free cysteines.
• Efficient leukocyte Ig-like receptor signaling and crystal structure of disulfide-linked HLA-G dimer
  M Shiroishi; K Kuroki; T Ose; L Rasubala; Shiratori, I; H Arase; K Tsumoto; Kumagai, I; D Kohda; K Maenaka
  JOURNAL OF BIOLOGICAL CHEMISTRY, 281, 15, 10439, 10447, Apr. 2006, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• 2P031 Crystallization of the catalytic subunit of archaeal oligosaccharyltransferase(29. Protein structure and dynamics (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
  Igura Mayumi; Maita Nobuo; Kamishikiryou Jun; Maenaka Katsumi; Kohda Daisuke
  Seibutsu Butsuri, 46, 2, S303, The Biophysical Society of Japan General Incorporated Association, 2006
  English
• 1P139 BmNPV expression system; Application to human natural killer cell receptors(4. Protein engineering,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
  Kajikawa Mizuho; Sasaki Kaori; Kuroki Kimiko; Motohashi Tomoko; Shimojima Tsukasa; Park Enoch Y.; Kohda Daisuke; Maenaka Katsumi
  Seibutsu Butsuri, 46, 2, S181, The Biophysical Society of Japan General Incorporated Association, 2006
  English
• 1P064 Comprehensive analysis of the MHCI binding of leukocyte immunoglobulin-like receptors using surface plasmon resonance technique(2. Protein function (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
  Kuroki Kimiko; Shiroishi Mitsunori; Fukunaga Yuko; Kohda Daisuke; Maenaka Katsumi
  Seibutsu Butsuri, 46, 2, S162, The Biophysical Society of Japan General Incorporated Association, 2006
  English
• 1P076 Molecular basis for recognition of E-cadherin by killer cell-lectin like receptor, KLRG1(2. Protein function (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
  Nakamura Seiko; Kuroki Kimiko; Ohki Izuru; Sasaki Kaori; Maruyama Takuma; Ito Masayuki; Ikura Mitsuhiko; Yamamoto Kazuo; Matsumoto Naoki; Kohda Daisuke; Maenaka Katsumi
  Seibutsu Butsuri, 46, 2, S165, The Biophysical Society of Japan General Incorporated Association, 2006
  English
• 1P088 N-linked protein glycosylation in hyperthermophilic archaeon Pyrococcus furiosus(2. Protein function (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
  Kamishikiryou Jun; Igura Mayumi; Maenaka Katsumi; Kohda Daisuke
  Seibutsu Butsuri, 46, 2, S168, The Biophysical Society of Japan General Incorporated Association, 2006
  English
• 1P027 Structual and biochemical studies of MHC class I recognition by human Leukocyte Ig-like receptors(1. Protein structure and dynamics (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
  Kuroki Kimiko; Shiroishi Mitsunori; Kajikawa Mizuho; Rasubala Linda; Kohda Daisuke; Maenaka Katsumi
  Seibutsu Butsuri, 46, 2, S153, The Biophysical Society of Japan General Incorporated Association, 2006
  English
• Crystallization and preliminary crystallographic analysis of the N-terminal domain of PriA from Escherichia coli.
  Sasaki K; Ose T; Tanaka T; Mizukoshi T; Ishigaki T; Maenaka K; Masai H; Kohda D
  Biochimica et biophysica acta, 1764, 1, 157, 160, Jan. 2006, [Peer-reviewed], [International Magazine]
  English, Scientific journal, PriA, a DEXH-type DNA helicase, binds specifically to the 3' end of DNA through its N-terminal domain, and is a candidate sensor protein that recognizes arrested DNA replication forks in bacteria. We crystallized an N-terminal fragment of PriA in the absence and the presence of oligonucleotides to elucidate the structural basis for the specific recognition of the 3' terminus of DNA.
• Entropically driven MHC class I recognition by human inhibitory receptor leukocyte Ig-like receptor B1 (LILRB1/ILT2/CD85j)
  M Shiroishi; K Kuroki; K Tsumoto; A Yokota; T Sasaki; K Amano; T Shimojima; Y Shirakihara; L Rasubala; PA van der Merwe; Kumagai, I; D Kohda; K Maenaka
  JOURNAL OF MOLECULAR BIOLOGY, 355, 2, 237, 248, Jan. 2006, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Extensive polymorphisms of LILRB1 (ILT2, LIR1) and their association with HLA-DRB1 shared epitope negative rheumatoid arthritis
  K Kuroki; N Tsuchiya; M Shiroish; L Rasubala; Y Yamashita; K Matsuta; T Fukazawa; M Kusaoi; Y Murakami; M Takiguchi; T Juji; H Hashimoto; D Kohda; K Maenaka; K Tokunaga
  HUMAN MOLECULAR GENETICS, 14, 16, 2469, 2480, Aug. 2005, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Expression, crystallization and preliminary diffraction studies of the Pseudomonas putida cytochrome P450cam operon repressor CamR
  K Maenaka; K Fukushi; H Aramaki; Y Shirakihara
  ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, 61, Pt 8, 796, 798, Aug. 2005, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Crystallization and preliminary X-ray analysis of mitochondrial presequence receptor Tom20 in complexes with a presequence from aldehyde dehydrogenase
  M Igura; T Ose; T Obita; C Sato; K Maenaka; T Endo; D Kohda
  ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, 61, Pt 5, 514, 517, May 2005, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Crystallization and preliminary X-ray analysis of the mRNA-binding domain of elongation factor SelB in complex with RNA
  L Rasubala; D Fourmy; T Ose; D Kohda; K Maenaka; S Yoshizawa
  ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, 61, Pt 3, 296, 298, Mar. 2005, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Structural basis for mRNA recognition by elongation factor SelB
  Satoko Yoshizawa; Linda Rasubala; Toyoyuki Ose; Daisuke Kohda; Dominique Fourmy; Katsumi Maenaka
  Nature Structural and Molecular Biology, 12, 2, 198, 203, 20 Feb. 2005, [Peer-reviewed]
  English, Scientific journal
• Structural basis for mRNA recognition by elongation factor SelB
  S Yoshizawa; L Rasubala; T Ose; D Kohda; D Fourmy; K Maenaka
  NATURE STRUCTURAL & MOLECULAR BIOLOGY, 12, 2, 198, 203, Feb. 2005, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Genetic variability of the major histocompatibility complex class I homologue encoded by human cytomegalovirus leads to differential binding to the inhibitory receptor ILT2
  M Vales-Gomez; M Shiroishi; K Maenaka; HT Reyburn
  JOURNAL OF VIROLOGY, 79, 4, 2251, 2260, Feb. 2005, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Efficient large-scale protein production of larvae and pupae of silkworm by Bombyx mori nuclear polyhedrosis virus bacmid system
  T Motohashi; T Shimojima; T Fukagawa; K Maenaka; EY Park
  BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 326, 3, 564, 569, Jan. 2005, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Crystal structure of a biologically functional form of PriB from Escherichia coli reveals a potential single-stranded DNA-binding site
  S Shioi; T Ose; K Maenaka; M Shiroishi; Y Abe; D Kohda; T Katayama; T Ueda
  BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 326, 4, 766, 776, Jan. 2005, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases
  T Kamura; K Maenaka; S Kotoshiba; M Matsumoto; D Kohda; RC Conaway; JW Conaway; KI Nakayama
  GENES & DEVELOPMENT, 18, 24, 3055, 3065, Dec. 2004, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• The inhibitory NK cell receptor CD94/NKG2A and the activating receptor CD94/NKG2C bind the top of HLA-E through mostly shared but partly distinct sets of HLA-E residues
  H Wada; N Matsumoto; K Maenaka; K Suzuki; K Yamamoto
  EUROPEAN JOURNAL OF IMMUNOLOGY, 34, 1, 81, 90, Jan. 2004, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Human inhibitory receptors Ig-like transcript 2 (ILT2) and ILT4 compete with CD8 for MHC class I binding and bind preferentially to HLA-G
  M Shiroishi; K Tsumoto; K Amano; Y Shirakihara; M Colonna; VM Braud; DSJ Allan; A Makadzange; S Rowland-Jones; B Willcox; EY Jones; PA van der Merwe; Kumagai, I; K Maenaka
  PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 100, 15, 8856, 8861, Jul. 2003, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Structure-guided design of sialic acid-based Siglec inhibitors and crystallographic analysis in complex with sialoadhesin
  NR Zaccai; K Maenaka; T Maenaka; PR Crocker; R Brossmer; S Kelm; EY Jones
  STRUCTURE, 11, 5, 557, 567, May 2003, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Systematic analysis of the combinatorial nature of epitopes recognized by TCR leads to identification of mimicry epitopes for glutamic acid decarboxylase 65-specific TCRs
  Y Uemura; S Senju; K Maenaka; LK Iwai; S Fujii; H Tabata; H Tsukamoto; S Hirata; YZ Chen; Y Nishimura
  JOURNAL OF IMMUNOLOGY, 170, 2, 947, 960, Jan. 2003, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Specificity, degeneracy, and molecular mimicry in antigen recognition by HLA-Class II restricted T cell receptors: Implications for clinical medicine
  Yasushi Uemura; Satoru Senju; Shinji Fujii; Leo Kei Iwai; Katsumi Maenaka; Hiroki Tabata; Takayuki Kanai; Yu-Zhen Chen; Yasuharu Nishimura
  Modern Rheumatology, 13, 3, 205, 214, 2003, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Crystallization and preliminary X-ray diffraction studies on the DNA-binding domain of the transcriptional activator protein PhoB from Escherichia coli
  K Shindoh; K Maenaka; T Akiba; H Okamura; Y Nishimura; K Makino; Y Shirakihara
  ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 58, Pt 10 Pt 2, 1862, 1864, Oct. 2002, [Peer-reviewed], [International Magazine]
  English, Scientific journal
• Molecular recognition by Ig-like receptors, KIRs and Fc gamma Rs
  K Maenaka; PA van der Merwe; DI Stuart; P Sondermann; EY Jones
  ACTIVATING AND INHIBITORY IMMUNOGLOBULIN-LIKE RECEPTORS, 45, 54, 2001, [Peer-reviewed]
  English, International conference proceedings
• Crystal structure of the human p58 killer cell inhibitory receptor (KIR2DL3) specific for HLA-Cw3-related MHC class I
  K Maenaka; T Juji; DI Stuart; EY Jones
  STRUCTURE WITH FOLDING & DESIGN, 7, 4, 391, 398, Apr. 1999, [Peer-reviewed]
  English, Scientific journal
• Redesigning of oligosaccharide binding sites of hen egg-white lysozyme and a homologous protein, α-lactalbumin
  I. Kumagai; K. Maenaka; H. Uchiyama; K. Watanabe; K. Miura
  Protein Engineering, Design and Selection, 6, 99, 1993, [Peer-reviewed]
  English, Scientific journal

• 増大特集 ワクチン開発 Ⅲ.シナジー拠点(北海道大学) クライオ電子顕微鏡を用いた構造ワクチン学研究
  前仲 勝実; 喜多 俊介; 福原 秀雄, 生体の科学, 76, 5, 432, 433, 15 Oct. 2025
  株式会社医学書院
• Self-assembly of chitin oligosaccharides and their derivatives: Mechanistic insights
  甲野裕之; 井筒歩夢; 長岡佑哉; 磯野拓也; 喜多俊介; 前仲勝実; 碓氷泰市; 工藤萌; 服部武史; 尾形慎, セルロース学会年次大会講演要旨集, 32nd, 2025
• Structural insights into silkworm vitellogenin
  喜多俊介; 沼田浩輝; 佐々木実奈; 安楽佑樹; 前仲勝実, 日本農芸化学会大会講演要旨集(Web), 2025, 2025
• 細胞表面タンパク質の弱い分子認識の定量化・構造解析
  森 遥史; 黒木 喜美子; 前仲 勝実, ファルマシア, 61, 3, 186, 190, 2025
  細胞表面タンパク質、特に免疫細胞表面受容体は、細胞の基本的機能を制御する重要な反応起点である。免疫システムは、これら活性型および抑制型受容体の速く弱い分子間相互作用の集積によって、シグナルバランスの調節し、生体恒常性維持を実現している。近年では、多様な免疫チェックポイント受容体を創薬標的として注目され、分子間相互作用定量解析と構造生物学的モデルを通した新規治療法やモダリティ創出が期待される。, 公益社団法人 日本薬学会, Japanese
• 細胞表面タンパク質の弱い分子認識の定量化・構造解析
  森遥史; 黒木喜美子; 前仲勝実, ファルマシア(Web), 61, 3, 2025
• Current status and prospects of the drug development and human resource development system at the Hokkaido University.
  前仲勝実; 前仲勝実, 日本薬学会年会要旨集(Web), 145th, 2025
• Antigen recognition mechanism of monoclonal antibodies that induce cell death in adult T-cell leukemia cells
  露木貴浩; 長郷巧太; POZA Pablo Adrian Guillen; 加藤いづみ; 喜多俊介; 鷲見正人; 黒木喜美子; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実; 前田直良; 前田直良, 日本薬学会年会要旨集(Web), 145th, 2025
• Quantification and structural analysis of weak intermolecular recognition of cell surface proteins
  前仲勝実; 前仲勝実, 日本薬学会年会要旨集(Web), 145th, 2025
• Compound screening for discovering existing drugs selectively targeting CSC-like cells
  藤田祥貴; 梁井史織; 鈴木華央; 乙黒聡子; 太田悠介; 野村尚生; 前仲勝実; 前仲勝実, 日本薬学会年会要旨集(Web), 145th, 2025
• Role of synaptic transmission in the signaling pathway of regulating aging in C. elegans
  中川健斗; 鈴木利治; 鈴木利治; 前仲勝実; 多留偉功, 日本薬学会年会要旨集(Web), 145th, 2025
• The antigen recognition mechanism of antibodies recognizing adult T-cell leukemia cells
  長郷巧太; 露木貴浩; POZA Pablo Adrian Guillen; 加藤いづみ; 喜多俊介; 鷲見正人; 黒木喜美子; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実; 前田直良, 日本薬学会年会要旨集(Web), 145th, 2025
• 成人T細胞白血病細胞に細胞死を誘導する新規モノクローナル抗体の分子認識機構
  露木貴浩; PABLO Adrian Guillen Poza; 加藤いづみ; 喜多俊介; 長郷巧太; 鷲見正人; 黒木喜美子; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実; 前田直良; 前田直良, 日本蛋白質科学会年会(Web), 25th, 2025
• 多様な免疫抑制タンパク質HLA-Gと受容体群の構造基盤と創薬応用
  黒木喜美子; 前仲勝実, 日本蛋白質科学会年会(Web), 25th, 2025
• SARS-CoV-2中和抗体の高機能化に向けた軽鎖組換え抗体の機能評価
  志田陽南子; 安楽佑樹; 熊谷拓大; 須川龍; 鷲見正人; 小野寺大志; 安達悠; 森山彩野; 高橋宜聖; 喜多俊介; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実, 日本蛋白質科学会年会(Web), 25th, 2025
• SARS-CoV-2BA.2.86及びJN.1Spike蛋白質の受容体結合ドメイン可動性に関する構造基盤
  矢島久乃; 安楽佑樹; 郭悠; 木村香菜子; PLIANCHAISUK Arnon; 奥村佳穂; 名倉淑子; 新勇介; 逸見拓矢; 黒田大祐; 高橋宜聖; 喜多俊介; 佐々木慈英; 澄田裕美; 伊東潤平; 前仲勝実; 佐藤佳; 橋口隆生, 日本蛋白質科学会年会(Web), 25th, 2025
• SARS-CoV-2中和抗体のフレームワーク領域を介した結合機構:分子動力学シミュレーションによる相互作用解析
  熊谷拓大; 安楽佑樹; PAN Xu; 志田陽南子; 安達悠; 森山彩野; 高橋宜聖; 喜多俊介; DOKAINISH Hisham M.; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実, 日本蛋白質科学会年会(Web), 25th, 2025
• 単粒子解析における中和抗体scFv化の粒子配向への影響
  染谷太陽; 谷秀顕; 安楽佑樹; 田所高志; 小野寺大志; 橋口隆生; 高橋宜聖; 喜多俊介; 前仲勝実; 前仲勝実, 日本蛋白質科学会年会(Web), 25th, 2025
• 免疫制御分子LILRA2のフィブリノーゲン認識機構の解明
  古川敦; WANG Jiaqi; 鈴木亮; 荒瀬尚; 平安恒幸; 前仲勝実, 日本蛋白質科学会年会(Web), 25th, 2025
• SARS-CoV-2オミクロンKP.2およびKP.3Sタンパク質のクライオ電子顕微鏡解析
  野間井智; 矢島久乃; 喜多俊介; 橋口隆生; 佐藤佳; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実, 日本蛋白質科学会年会(Web), 25th, 2025
• 中分子創薬が直面する課題とその克服に向けて 実験及びシミュレーションのための統合データベースの開発
  山田 一作; 木村 直貴; 野村 尚生; 乙黒 聡子; 宮地 弘幸; 重田 育照; 前仲 勝実, 薬学雑誌, 144, 5, 539, 543, May 2024
  (公社)日本薬学会, Japanese
• 【あなたのラボから薬を生み出す アカデミア創薬の実践 All JAPAN体制の先端技術支援を利用した創薬の最前線】(第2章)創薬標的タンパク質の構造解析と分子設計の革新的進歩 BSL3クライオ電子顕微鏡を用いた感染症創薬・ワクチン研究とその展望
  前仲 勝実; 福原 秀雄; Dokainish Hisham; 安楽 佑樹; 喜多 俊介, 実験医学, 42, 2, 246, 252, Feb. 2024
  (株)羊土社, Japanese
• 感染を制御する液性免疫 感染症に対する抗体医薬品の開発
  染谷太陽; 喜多俊介; 前仲勝実, 炎症と免疫, 32, 6, 464, 468, 2024
  東京 : 先端医学社, Japanese
• Immune response modulation by antibodies understood in the context of membrane structure biology.
  山本亮太; 黒木喜美子; DAVIS Simon J.; 前仲勝実, 月刊臨床免疫・アレルギー科, 82, 2, 123, 129, 2024
  東京 : 科学評論社, Japanese
• in vitro analysis for differentiation of cancer stem-like cells derived from commercially available cancer cell lines.
  野村尚生; 竹内若菜; 太田悠介; 梁井史織; 西拓海; 松永直哉; 前仲勝実; 前仲勝実, 日本癌学会学術総会抄録集(Web), 83rd, 2024
• Elucidation of the differentiation and early tumorigenesis mechanisms in cancer stem cell-like cells in xenograft models
  太田悠介; 竹内若菜; 梁井史織; 黒田京佑; 野村尚生; 野村尚生; 前仲勝実; 前仲勝実; 前仲勝実, 日本癌学会学術総会抄録集(Web), 83rd, 2024
• ウエストナイルウイルスサブユニットワクチンにおけるAS03様アジュバントの免疫賦活効果の検証
  井上敦子; 井上敦子; 板倉友香里; 齋藤慎二; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実; 澤洋文; 澤洋文; 澤洋文; 大場靖子; 大場靖子; 田畑耕史郎, 日本分子生物学会年会プログラム・要旨集(Web), 47th, 2024
• ER-localized enzyme highly expressed in cancer cells contributes to the Wnt/β-catenin pathway
  梁井史織; 梁井史織; 太田悠介; 野村尚生; 野村尚生; 前仲勝実; 前仲勝実; 前仲勝実, 日本癌学会学術総会抄録集(Web), 83rd, 2024
• The spike protein recognition mechanism of cross reactive SARS-CoV-2 neutralizing antibodies revealed by Cryo-EM
  前仲勝実; 前仲勝実, 日本抗体学会学術大会プログラム・抄録集(Web), 3rd, 2024
• 不飽和カルボニル化合物は肺小細胞がんSBC-3細胞に対してPKC依存的にフェロトーシスを誘導する
  東恒仁; 半田悠; 眞井洋輔; 前仲勝実; 田所高志, 日本薬理学雑誌, 159, Supplement, 2024
• Structural analysis of the Hepatitis B virus x protein (HBx)
  田中大貴; 喜多俊介; 佐々木実奈; 溝上雅史; 柴田幹大; 前仲勝実; 町田晋一, 日本ウイルス学会学術集会プログラム・予稿集(Web), 71st, 2024
• Discovery of anti-mpox virus agents by drug repurposing
  日紫喜隆行; 赤澤大輔; 森田武志; 大橋啓史; 朴ウンシル; 下島昌幸; 前田健; 海老原秀喜; 前仲勝実; 渡士幸一, 日本ウイルス学会学術集会プログラム・予稿集(Web), 71st, 2024
• 新規癌幹細胞様細胞株に対する選択的治療薬のスクリーニングの施行
  太田悠介; 梁井史織; 竹内若菜; 黒田京佑; 野村尚生; 野村尚生; 前仲勝実; 前仲勝実, 日本蛋白質科学会年会(Web), 24th, 2024
• イムペネマーゼ(IMP-1)型Metallo-β-lactamaseの構造解析に向けた取り組み
  須川龍; 喜多俊介; 前仲勝実; 池田朱里; 池田朱里; 本庄雅子; 本庄雅子; 浅見行弘; 浅見行弘; 砂塚敏明; 砂塚敏明; 廣瀬友靖; 廣瀬友靖; 鈴木智博; 鈴木智博, 日本蛋白質科学会年会(Web), 24th, 2024
• CD1d-アミド型抗原複合体のX線構造解析と示差走査熱量計による熱安定性解析
  宮内龍; 秋田穂; 日下裕規; 田所高志; 杉山成; 相羽俊彦; 相羽俊彦; 深瀬浩一; 村田道雄; 井貫晋輔; 井貫晋輔; 藤本ゆかり; 喜多俊介; 前仲勝実, 日本蛋白質科学会年会(Web), 24th, 2024
• HIV-2Nefタンパク質のCD3細胞内モチーフ結合解析
  古関亮太; 小澤偉大; 平尾憲吾; 田所高志; 鷲見正人; ANDREWS Sophie; ROWLAND-JONES Sarah; 黒木喜美子; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実, 日本蛋白質科学会年会(Web), 24th, 2024
• カイコ由来ビテロジェニンの構造基盤
  沼田浩輝; 喜多俊介; 佐々木実奈; 安楽佑樹; 前仲勝実, 日本蛋白質科学会年会(Web), 24th, 2024
• バイオ医薬品開発に向けた免疫抑制分子HLA-G2の発現系検討および機能解析
  山本亮太; 黒木喜美子; 渡邊紘士; 山田千聖; 前仲勝実, 日本蛋白質科学会年会(Web), 24th, 2024
• SARS-CoV-2中和抗体の高機能化に向けた軽鎖組換え抗体の作製および機能評価
  志田陽南子; 安楽佑樹; 喜多俊介; 安達悠; 高橋宜聖; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実, 日本蛋白質科学会年会(Web), 24th, 2024
• 成人T細胞白血病細胞増殖抑制抗体の抗原ペプチド認識の構造基盤
  露木貴浩; GUILLEN POZA Pablo Adrian; 加藤いづみ; 喜多俊介; 長郷巧太; 鷲見正人; 黒木喜美子; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実; 前田直良; 前田直良, 日本蛋白質科学会年会(Web), 24th, 2024
• 癌細胞における小胞体局在酵素のWnt/β-カテニン経路への寄与
  梁井史織; 太田悠介; 野村尚生; 前仲勝実, 日本蛋白質科学会年会(Web), 24th, 2024
• 免疫チェックポイント受容体BTLAに対する機能性抗体の分子認識
  竹川翔悟; 佐藤大悟; 岩森美樹; 伊東詩織; 田聡; 喜多俊介; PALUCH Chris; DAVIS Simon; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実; 黒木喜美子, 日本蛋白質科学会年会(Web), 24th, 2024
• 免疫チェックポイント分子HLA-Gに対する抗体の機能評価
  下柿元咲瑛; 森遥史; 栗城佑妃; 引地和馬; 赤岩愛記; 荒瀬尚; 古川敦; 古川敦; 前田直良; 黒木喜美子; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実, 日本蛋白質科学会年会(Web), 24th, 2024
• がん幹細胞様細胞株に対する選択的治療薬の創製
  太田悠介; 梁井史織; 竹内若菜; 黒田京佑; 野村尚生; 野村尚生; 前仲勝実; 前仲勝実; 前仲勝実, 日本生化学会大会(Web), 97th, 2024
• SARS-CoV-2に対するNOKS抗体の構造基盤
  岩切暢紀; 喜多俊介; 安楽佑樹; 橋口隆生; 安達悠; 小野寺大志; 高橋宜聖; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実, 日本蛋白質科学会年会(Web), 24th, 2024
• Structural insights into the ACE2-binding affinity of SARS-CoV-2 EG.5.1 spike protein harboring characteristic F456L mutation.
  野間井智; 安楽佑樹; 喜多俊介; 矢島久乃; 橋口隆生; 福原崇介; 佐藤佳; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実, 日本ウイルス学会学術集会プログラム・予稿集(Web), 71st, 2024
• 受容体結合に伴うSARS-CoV-2BA.2.86スパイク蛋白質のRBD-upトリガー構造
  矢島久乃; 安楽佑樹; 名倉淑子; 木村香菜子; 喜多俊介; 佐々木慈英; 佐藤佳; 前仲勝実; 橋口隆生, 日本蛋白質科学会年会(Web), 24th, 2024
• Structural basis for receptor recognition and neutralizing antibody evasion of SARS-CoV-2 BA.2.86 S protein
  矢島久乃; 安楽佑樹; 悠郭; 名倉淑子; 木村香菜子; 喜多俊介; PLIANCHAISUK Arnon; 奥村佳穂; 佐々木慈英; 伊東潤平; 前仲勝実; 佐藤佳; 橋口隆生, 日本ウイルス学会学術集会プログラム・予稿集(Web), 71st, 2024
• F456L変異を有するSARS-CoV-2EG.5.1Sタンパク質のACE2親和性に関する構造生物学的洞察
  野間井智; 安楽佑樹; 喜多俊介; 矢島久乃; 橋口隆生; 福原崇介; 佐藤佳; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実, 日本蛋白質科学会年会(Web), 24th, 2024
• NIV抗体とSARS-CoV-2スパイクタンパク質複合体構造に基づく中和機構の解明
  染谷太陽; 安楽佑樹; 福原秀雄; 森山彩野; 橋口隆生; 高橋宜聖; 喜多俊介; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実, 日本蛋白質科学会年会(Web), 24th, 2024
• 新型コロナウイルスに対する中和抗体の小型化
  喜多俊介; 染谷太陽; 安楽佑樹; 田所高志; 田所高志; 小野寺大志; 安達悠; 森山彩野; 湯本航平; 橋口隆生; 高橋宜聖; 前仲勝実; 前仲勝実, 日本抗体学会学術大会プログラム・抄録集(Web), 3rd, 2024
• 狂犬病ウイルスP蛋白質によるSTAT阻害機構解明のための,複合体クライオ電顕構造解析に向けた取り組み
  杉山葵; 南未来; 杉田征彦; 廣瀬未果; 喜多俊介; 喜多俊介; 有森貴夫; 高木淳一; 前仲勝実; 前仲勝実; 姚閔; 姚閔; 尾瀬農之; 尾瀬農之, 日本蛋白質科学会年会(Web), 24th, 2024
• 近赤外線光を活用した免疫療法による難治性がんに対する低分子抗体医薬品の開発
  楊一帆; 楊一帆; 田所高志; 中島孝平; 杉浦直樹; 森岡弘志; 前田直良; 小川美香子; 前仲勝実, 日本蛋白質科学会年会(Web), 24th, 2024
• 乳がん特異的キナーゼとアダプター蛋白質が形成する分子集合と酵素活性の相関を検証する
  武井梓穂; 宇賀神魁; 中迫純希; 松尾友樹; 神田諒; 川越聡一郎; 齋尾智英; 松田正; 前仲勝実; 姚閔; 尾瀬農之, 日本蛋白質科学会年会(Web), 24th, 2024
• コムギ胚芽無細胞共翻訳法による再構成ヌクレオソームの単粒子構造解析
  沖宗慶一; 東泰暉; 芳賀洵子; PETRA Banko; 森下了; 喜多俊介; 前仲勝実; 高須賀太一; 高須賀太一, 日本分子生物学会年会プログラム・要旨集(Web), 47th, 2024
• SARS-CoV-2BA.2.86S蛋白質の受容体結合ドメインの可動性に関する構造生物学的洞察
  矢島久乃; 安楽佑樹; 名倉淑子; 木村香菜子; 喜多俊介; PLIANCHAISUK Arnon; 奥村佳穂; 新勇介; 新勇介; 逸見拓矢; 黒田大祐; 高橋宣聖; 喜多俊介; 佐々木慈英; 澄田裕美; 伊東潤平; 前仲勝実; 佐藤佳; 橋口隆生, 日本分子生物学会年会プログラム・要旨集(Web), 47th, 2024
• Lipid antigen presentation of lipid-modified sphingolipids: lipid structures and immunomodulation
  末吉耕大; 川手菜々子; 平田菜摘; 井貫晋輔; 松丸尊紀; 日下裕規; 秋田穂; 喜多俊介; 前仲勝実; 藤本ゆかり, 日本糖質学会年会要旨集, 43rd, 2024
• CD1d-アミド型抗原複合体のX線結晶構造解析と示差走査熱量計による熱安定性解析
  宮内龍; 秋田穂; 日下裕規; 田所高志; 杉山成; 相羽俊彦; 相羽俊彦; 深瀬浩一; 村田道雄; 井貫晋輔; 井貫晋輔; 藤本ゆかり; 喜多俊介; 前仲勝実, 日本結晶学会年会講演要旨集, 2024, 2024
• SARS-CoV-2に対するNOKS抗体の構造基盤
  岩切暢紀; 喜多俊介; 安楽佑樹; 橋口隆生; 安達悠; 小野寺大志; 高橋宜聖; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実, 日本結晶学会年会講演要旨集, 2024, 2024
• Structural insight into NOKS antibodies against SARS-CoV-2
  岩切暢紀; 喜多俊介; 安楽佑樹; 橋口隆生; 安達悠; 小野寺大志; 高橋宜聖; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実, 日本生体防御学会学術総会講演抄録集, 35th (Web), 2024
• Structural analysis of SARS-CoV-2 using BSL3 cryo-EM
  福原秀雄; DOKAINISH Hisham; 喜多俊介; 田畑耕史郎; 田畑耕史郎; 高巣晃; HUISKONEN Juha; 安楽佑樹; 千田俊哉; 千田俊哉; 千田俊哉; STUART David; 佐々木道仁; 大場靖子; 鈴木定彦; 鈴木定彦; 澤洋文; 澤洋文; 前仲勝実; 前仲勝実; 前仲勝実, 日本生体防御学会学術総会講演抄録集, 35th (Web), 2024
• Structural insight into SARS-CoV-2 neutralizing antibodies
  喜多俊介; 安楽佑樹; 染谷太陽; 福原秀雄; 福原秀雄; 橋口隆生; 安達悠; 小野寺大志; 森山彩野; 高橋宜聖; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実, 日本生体防御学会学術総会講演抄録集, 35th (Web), 2024
• Single particle analysis of A/Singapore/GP1908/2015 (H1N1) influenza virus hemagglutinin
  小林颯太; 関屋俊輝; 喜多俊介; 新開大史; 喜田宏; 前仲勝実; 前仲勝実; 前仲勝実; 前仲勝実, 日本生体防御学会学術総会講演抄録集, 35th (Web), 2024
• Molecular basis of neutralizing antibodies to SARS-CoV-2
  喜多俊介; 前仲勝実, 量子ビームサイエンスフェスタ(Web), 2023, 2024
• Preparation of scFv antibody for reducing side effect
  石田知聖; 田所高志; 大村玲央; 冨田麻美; 杉山葵; 宮本和英; 前仲勝実, 日本薬学会年会要旨集(Web), 144th, 2024
• Wnt3a maturation by overexpressed ER-localized enzyme in cancer cells
  梁井史織; 太田悠介; 野村尚生; 前仲勝実; 前仲勝実, 日本薬学会年会要旨集(Web), 144th, 2024
• Academic drug discovery for pandemics: Basic research on infectious disease drug and vaccine development using BSL3 cryo-electron microscopy
  前仲勝実; 前仲勝実, 日本薬学会年会要旨集(Web), 144th, 2024
• X-ray crystallography of novel anti-proliferative monoclonal antibody against adult T-cell leukemia cells
  露木貴浩; POZA Pablo Adrian Guillen; 加藤いづみ; 喜多俊介; 黒木喜美子; 前仲勝実; 前田直良; 前田直良, 日本薬学会年会要旨集(Web), 144th, 2024
• Cryo-electron microscopy-based drug discovery for infectious disease
  前仲勝実; 前仲勝実, 日本薬学会年会要旨集(Web), 144th, 2024
• Structural basis for antiviral activity of a nucleoside analogue targeting dengue virus RNA-dependent RNA polymerase
  伊東詩織; 喜多俊介; 上村健太朗; 上村健太朗; 上村健太朗; 上村健太朗; 岩間湧希; 田所高志; 澤洋文; 澤洋文; 佐藤彰彦; 佐藤彰彦; 佐藤彰彦; 松田彰; 前仲勝実; 前仲勝実; 前仲勝実, 日本薬学会年会要旨集(Web), 144th, 2024
• Binding analysis of HIV-2 Nef protein with host CD3 intracellular motif
  古関亮太; 小澤偉大; 平尾憲吾; 田所高志; 鷲見正人; ANDREWS Sophie; SARAH Rowland-Jones; 黒木喜美子; 前仲勝実, 日本薬学会年会要旨集(Web), 144th, 2024
• Development of Novel Antibody Pharmaceuticals for Adult T-cell Leukemia Using Near-Infrared Light Immunotherapy
  YANG Yifan; YANG Yifan; 田所高志; 中島孝平; 杉浦直樹; 森岡弘志; 前田直良; 小川美香子; 前仲勝実, 日本薬学会年会要旨集(Web), 144th, 2024
• Structure Analysis of SARS-CoV-2 Spike Protein
  喜多俊介; 染谷太陽; 野間井智; 安楽佑樹; 前仲勝実, 日本結晶学会誌, 66, 2, 109, 114, 2024
  SARS-CoV-2 spike protein plays an important role in invading host cells. Spike protein is one of the targets of neutralizing antibodies, and thus is well studied for vaccine design and development of therapeutic antibodies. Here we review our research regarding the structure analysis of SARS-CoV-2 spike protein and spike-antibody complex with X-ray crystallography and cryo-EM., The Crystallographic Society of Japan, Japanese
• マルチバレント相互作用にフォーカスした生化学及び創薬の新展開 表面抗原を標的としたマルチバレント相互作用による機能制御 免疫抑制蛋白質や新型コロナウイルス中和抗体を例として
  前仲 勝実, 日本生化学会大会プログラム・講演要旨集, 96回, [1S11m, 01], Oct. 2023
  (公社)日本生化学会, Japanese
• 癌幹細胞様細胞の新規高純度株を用いた分化・初期腫瘍形成機構の検討
  太田 悠介; 竹内 若菜; 梁井 史織; 黒田 京佑; 野村 尚生; 前仲 勝実, 日本生化学会大会プログラム・講演要旨集, 96回, [1T14a, 503)], Oct. 2023
  (公社)日本生化学会, Japanese
• 癌細胞で高発現する小胞体局在酵素によるWnt3a成熟機構の解明
  梁井 史織; 太田 悠介; 野村 尚生; 前仲 勝実, 日本生化学会大会プログラム・講演要旨集, 96回, [2P, 489], Oct. 2023
  (公社)日本生化学会, Japanese
• 癌細胞株中に微量含まれる癌幹細胞様細胞株の生化学的特性の検討(Biochemical characteristics of a cancer stem-like cell included in trace amounts within commercial cancer cell lines)
  太田 悠介; 梁井 史織; 黒田 京佑; 竹内 若菜; 野村 尚生; 前仲 勝実, 日本癌学会総会記事, 82回, 996, 996, Sep. 2023
  (一社)日本癌学会, English
• 一本鎖抗体のVL領域に存在する2つのcis-Proを標的とした抗体工学研究
  楊一帆; 楊一帆; 岡崎匡; 田所高志; 喜多俊介; 佐藤卓史; 小橋川敬博; 前仲勝実; 森岡弘志, 日本蛋白質科学会年会プログラム・要旨集, 23rd (CD-ROM), Jun. 2023
• 新型コロナウイルスに対するscFv化抗体の機能評価
  染谷太陽; 谷秀顕; 安楽佑樹; 田聡; 福原秀雄; 福原秀雄; 野村尚生; 田所高志; 小野寺大志; 安達悠; 森山彩野; 湯本航平; 鈴木干城; 佐々木慈英; 橋口隆生; 高橋宜聖; 喜多俊介; 前仲勝実; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 23rd (CD-ROM), Jun. 2023
• N460K変異を有するSARS-CoV-2BA.2.75スパイクタンパク質のACE2親和性に関する構造的洞察
  安楽佑樹; 喜多俊介; 福原秀雄; 福原秀雄; 佐藤佳; 橋口隆生; 前仲勝実; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 23rd (CD-ROM), Jun. 2023
• クライオ電子顕微鏡構造解析と高速AFM観察から見えてきたABCトランスポーター(P-gp)の構造ダイナミクス
  濱口紀江; 濱口紀江; 安達成彦; 野中雄仁; 喜多俊介; 今野翔; 金岡優依; 守屋俊夫; 川崎政人; 安田賢司; 安西尚彦; 林良雄; 前仲勝実; 千田俊哉; 小笠原諭; 内橋貴之; 村田武士, 日本蛋白質科学会年会プログラム・要旨集, 23rd (CD-ROM), Jun. 2023
• Structure and solubility, passive diffusivity, cell membrane permeability, and P-gp substrate properties of optically active cyclopropane-containing cyclic peptides.
  宮地弘幸; 金光佳世子; 石井真由美; 渡邊恵里; 佐藤優希菜; 長田貴行; 山崎祐季; 柏木仁; 菅原満; 周東智; 重田育照; 渡邉瑞貴; 前仲勝実, 日本薬学会年会要旨集(Web), 143rd, 2023
• In silicoで改変したUT28KはSARS-CoV-2オミクロンBA.1に対して中和活性を回復した
  小澤龍彦; 小澤龍彦; 池田幸樹; CHEN Liuan; 鈴木理滋; 星野温; 野口映; 喜多俊介; 安楽佑樹; 五十嵐笑子; 佐賀由美子; 稲崎倫子; 民西俊太; 佐々木慈英; 桐田雄平; 福原秀雄; 前仲勝実; 橋口隆生; 福原崇介; 平林健一; 谷英樹; 岸裕幸; 岸裕幸; 仁井見英樹; 仁井見英樹, 日本抗体学会学術大会プログラム・抄録集(Web), 2nd, 2023
• IgA抗体の自己重合反応による四量体形成とその応用
  田畑耕史郎; 田畑耕史郎; 田畑耕史郎; 安楽佑樹; 多賀祐喜; 佐々木道仁; 佐々木道仁; 板倉友香里; 板倉友香里; 後藤希代子; 長谷川秀樹; 前仲勝実; 前仲勝実; 澤洋文; 澤洋文; 澤洋文; 福原秀雄; 大場靖子; 大場靖子; 鈴木忠樹, 日本抗体学会学術大会プログラム・抄録集(Web), 2nd, 2023
• Discovery of a broad-spectrum antiviral nucleoside analogue against positive-strand RNA viruses
  上村健太朗; 上村健太朗; 上村健太朗; 上村健太朗; 上村健太朗; 登治謙; 佐藤彰彦; 佐藤彰彦; 佐藤彰彦; 鳥羽晋輔; 鳥羽晋輔; 日下部伸治; 日下部伸治; 佐々木道仁; 田畑耕史郎; 大場靖子; 澤洋文; 澤洋文; 松浦善治; 松浦善治; 松田彰; 前仲勝実; 前仲勝実; 前仲勝実, 日本薬学会年会要旨集(Web), 143rd, 2023
• アダプター蛋白質介在に伴う,乳がん特異的キナーゼの活性亢進評価
  武井梓穂; 宇賀神魁; 中迫純希; 松尾友樹; 神田諒; 前仲勝実; 松田正; 姚閔; 尾瀬農之, 日本蛋白質科学会年会プログラム・要旨集, 23rd (CD-ROM), 2023
• Neutralization mechanism revealed by structural analysis of SARS CoV-2 spike protein complexed with antibodies
  山本旭麻; 東浦彰史; 下岡清美; 河野洋平; 喜多俊介; 安楽佑樹; 橋口隆生; 前仲勝実; 保田朋波流; 坂口剛正, 日本ウイルス学会学術集会プログラム・予稿集(Web), 70th, 2023
• Cryo-EM structure of SARS-CoV-2 XBB.1.5 spike protein and its ACE2 receptor recognition mechanism and structural comparison with XBB.1
  矢島久乃; 安楽佑樹; 喜多俊介; 佐々木慈英; 木村(寺角)香菜子; 前仲勝実; 佐藤佳; 福原崇介; 橋口隆生, 日本ウイルス学会学術集会プログラム・予稿集(Web), 70th, 2023
• Structural analysis of SARS-CoV-2 XBB.1 spike protein and ACE2 complex
  安楽佑樹; 喜多俊介; 矢島久乃; 佐藤佳; 橋口隆生; 前仲勝実, 日本ウイルス学会学術集会プログラム・予稿集(Web), 70th, 2023
• Analysis of the relationship between neutralizing activity and antigen recognition mechanism based on the structure of NIV antibody and SARS-CoV-2 spike protein complex.
  染谷太陽; 安楽佑樹; 森山彩野; 橋口隆生; 高橋宜聖; 喜多俊介; 前仲勝実, 日本ウイルス学会学術集会プログラム・予稿集(Web), 70th, 2023
• X-206 exhibits broad-spectrum and robust inhibition against infections by several drug-resistant isolates and variants of SARS-CoV-2.
  佐々木慈英; 岡部伊織; 佐藤彰彦; 佐藤彰彦; 佐藤彰彦; 児玉耕太; 乙黒聡子; 佐々木道仁; 大場靖子; 澤洋文; 澤洋文; 前仲勝実; 柳雄介; 橋口隆生, 日本ウイルス学会学術集会プログラム・予稿集(Web), 70th, 2023
• SARS-CoV-2中和抗体の一本鎖Fv断片を用いた構造解析
  田所高志; 田所高志; 喜多俊介; 染谷太陽; 安楽佑樹; 福原秀雄; 福原秀雄; 野村尚生; 小野寺大志; 森山彩野; 橋口隆生; 高橋宜聖; 前仲勝実; 前仲勝実, 日本結晶学会年会講演要旨集, 2023, 2023
• SARS-CoV-2スパイク蛋白質と広域中和抗体の複合体構造解析
  山本旭麻; 東浦彰史; 下岡清美; 河野洋平; 喜多俊介; 安楽佑樹; 野間井智; 橋口隆生; 前仲勝実; 保田朋波流; 坂口剛正, 日本結晶学会年会講演要旨集, 2023, 2023
• Screening of original HLA-G antibodies for induction of tumor immunity
  下柿元咲瑛; 黒木喜美子; 引地和馬; 赤岩愛記; 古川敦; 古川敦; 前田直良; 前仲勝実, 日本薬学会年会要旨集(Web), 143rd, 2023
• Synthesis of electron-deficient Cp^EIr(III) complex and its application for ether-directed C-H functionalization
  冨田永希; 小島正寛; 永島佑貴; 田中健; 杉山晴紀; 瀬川泰知; 古川敦; 前仲勝実; 前仲勝実; 前田理; 前田理; 吉野達彦; 吉野達彦; 松永茂樹; 松永茂樹, 日本薬学会年会要旨集(Web), 143rd, 2023
• Cigarette smoke gas phase induces ferroptosis via PKCβ in J774 macrophages
  Higashi Tsunehito; Handa Haruka; Mai Yosuke; Maenaka Katsumi; Tadokoro Takashi, Proceedings for Annual Meeting of The Japanese Pharmacological Society, 97, 3-B-P-069, 2023
  Cigarette smoking is a risk factor for various types of diseases including atherosclerosis, hypertension, chronic obstructive pulmonary disease, and respiratory infection. The respiratory infection caused by cigarette smoking is due to immune cell dysfunction by cigarette smoke, although its molecular mechanism remains to be clarified. The cigarette smoke can be divided into two phases: tar (particle) phase and gas phase. We have previously reported that gas phase extract of cigarette smoke (CSE) induces cell death. In this study, we have examined the effects of CSE on J774 macrophages. CSE and unsaturated carbonyl compounds, cytotoxic factors in the CSE, induced cell death in J774 macrophages. Ferrostatin-1 and liproxstatin-1, ferroptosis inhibitors, suppressed cell death caused by CSE and unsaturated carbonyl compounds. A broad-range protein kinase C (PKC) inhibitor Gö6983 suppressed CSE- and unsaturated carbonyl compounds-induced cell death. To identify PKC isoforms involved in the process, we have examined isoform-specific inhibitors. Enzastaurin, a PKCβ-specific inhibitor, suppressed the cell death. Enzastaurin also suppressed RSL3-induced ferroptosis. These results suggest that CSE and unsaturated carbonyl compounds induce PKCβ-dependent ferroptosis in J774 macrophages., Japanese Pharmacological Society, Japanese
• 【治療の可能性が広がる 抗体医薬 バイスペシフィック抗体、ADC、シングルドメイン抗体、機械学習…新技術と情報科学が実現した新時代のモダリティ】(第2章)疾患別のバイオロジー 感染症 SARS-CoV-2ウイルスの進化に対抗する抗体開発の現状と展望
  湯本 航平; 森山 彩野; 前仲 勝実; 高橋 宜聖, 実験医学, 40, 20, 3350, 3355, Dec. 2022
  (株)羊土社, Japanese
• 癌幹細胞形成におけるChitosan培養の効果
  黒田 京佑; 野村 尚生; 太田 悠介; 梁井 史織; 前仲 勝実, 日本生化学会大会プログラム・講演要旨集, 95回, 2P, 289, Nov. 2022
  (公社)日本生化学会, Japanese
• サイトメガロウイルス(CMV)眼感染症眼内液とCMV血症末梢血のCMV UL40多型の違いと眼内への感染進展における意義
  白根 茉利子; 八幡 信代; 元岡 大祐; 柴田 健輔; Khor Seik-Soon; 大前 陽輔; 柳井 亮二; 眞下 永; 蕪城 俊克; 森 康雄; 沼田 晃彦; 秋山 雅人; 長谷川 英一; 武田 篤信; 大黒 伸行; 前仲 勝実; 赤司 浩一; 徳永 勝士; 八幡 真人; 園田 康平, 日本臨床免疫学会総会プログラム・抄録集, 50回, 76, 76, Oct. 2022
  (一社)日本臨床免疫学会, Japanese
• X-ray crystal structure analysis of SARS-CoV-2 spike protein and neutralizing antibody NT-193 complex
  喜多俊介; 小野寺大志; 安達悠; 森山彩野; 野村尚生; 田所高志; 安楽佑樹; 湯本航平; 田聡; 福原秀雄; 鈴木干城; 橋口隆生; 高橋宜聖; 前仲勝実, 量子ビームサイエンスフェスタ(Web), 2021, Oct. 2022
• 汎SARS-CoV-2抗体の中和機構とBA.4/5変異株によるACE2受容体認識機構の構造基盤
  鈴木干城; 安楽佑樹; 木村香菜子; 喜多俊介; 佐々木慈英; 小澤龍彦; 仁井見英樹; 佐藤佳; 前仲勝実; 橋口隆生, 日本ウイルス学会学術集会プログラム・予稿集(Web), 69th, Sep. 2022
• VCP化合物による脊髄損傷後血液脊髄関門機能保護作用
  鈴木 裕貴; 角家 健; 五月女 慧人; 遠藤 健; 船木 智; 周東 智; 前仲 勝実; 岩崎 倫政, 日本整形外科学会雑誌, 96, 8, S1631, S1631, Sep. 2022
  (公社)日本整形外科学会, Japanese
• 次硝酸ビスマスの急性期脊髄損傷に対する神経保護効果とその機序の解明
  五月女 慧人; 角家 健; 鈴木 裕貴; 遠藤 健; 中川 慎介; 前仲 勝実; 岩崎 倫政, 日本整形外科学会雑誌, 96, 8, S1691, S1691, Sep. 2022
  (公社)日本整形外科学会, Japanese
• Planned serendipity in protein science
  前仲勝実, 医学のあゆみ, 282, 9, 801, 804, 27 Aug. 2022
  医歯薬出版(株), Japanese
• 電子不足Cp^EIr(III)錯体の合成及びエーテルを配向基として用いたC-H官能基化反応への応用
  冨田永希; 小島正寛; 永島佑貴; 田中健; 杉山晴紀; 杉山晴紀; 瀬川泰知; 瀬川泰知; 古川敦; 前仲勝実; 前仲勝実; 前田理; 前田理; 前田理; 吉野達彦; 吉野達彦; 松永茂樹; 松永茂樹, 次世代を担う有機化学シンポジウム講演要旨集, 20th, Jun. 2022
• Current status and prospects for the development of COVID-19 therapeutics at the Research center for Research and Education on Drug Discovery at Hokkaido University
  前仲勝実; 前仲勝実, 日本分析化学会有機微量分析研究懇談会・計測自動制御学会力学量計測部会合同シンポジウム講演要旨集, 89th-119th, Jun. 2022
• 平滑筋弛緩薬パパベリンの新規効能:血液脊髄関門保護を介した脊髄損傷に対する神経保護効果
  鈴木裕貴; 角家健; 五月女慧人; 遠藤健; 浅野毅; 前仲勝実; 中川慎介; 岩崎倫政, 日本整形外科学会雑誌, 96, 2, Jun. 2022
• X-ray crystal structure analysis of MHC class I like molecule CD1d in complex with glycolipids
  喜多俊介; 秋田穂; 日下裕規; TIAN Cong; 田所高志; 井貫晋輔; 新山真由美; 杉山成; 村田道雄; 藤本ゆかり; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 22nd (Web), Jun. 2022
• SARS-CoV-2 infection and development of neutralizing antibodies.
  安楽佑樹; 喜多俊介; 福原秀雄; 前仲勝実, 月刊臨床免疫・アレルギー科, 77, 5, 604, 609, May 2022
  (有)科学評論社, Japanese
• Identification and characterization of novel receptors for HLA-G2
  渡邊紘士; 黒木喜美子; 前仲勝実, 日本薬学会年会要旨集(Web), 142年会, 26L, pm03S, Mar. 2022
  (公社)日本薬学会, Japanese
• Total synthesis and bioactivity of heat shock metabolites (HSM), maniwamycins produced by thermotolerant Streptomyces sp. JA74
  船山佳世; 齋藤駿; 加藤航; 新藤一敏; 川本芽子; 松原輝彦; 佐藤智典; 乙黒聡子; 前仲勝実; 井本正哉; 荒井緑, 日本薬学会年会要旨集(Web), 142年会, 27T, am06S, Mar. 2022
  (公社)日本薬学会, Japanese
• 5-Ethynylimidazole-4-carboxamide(EICA)ヌクレオチドプロドラッグの合成と抗デングウイルス活性
  日野谷 直人; 中村 元紀; 田良島 典子; 大場 靖子; 澤 洋文; 松田 彰; 前仲 勝実; 南川 典昭, 日本薬学会年会要旨集, 142年会, 28S, pm03S, Mar. 2022
  (公社)日本薬学会, Japanese
• 免疫系受容体の弱く速い結合を介したリガンド認識機構—Ligand recognition mechanisms by immune system receptors via weak and fast binding—特集 物質共生の観点からDDSを考える
  渡邊 紘士; 黒木 喜美子; 前仲 勝実, Drug delivery system : DDS : official journal of the Japan Society of Drug Delivery System / 日本DDS学会 編, 37, 2, 112, 121, Mar. 2022, [Peer-reviewed]
  日本DDS学会, Japanese
• プラス鎖RNAウイルスに対して広域的に抗ウイルス活性を示すヌクレオシドアナログの探索
  上村健太朗; 上村健太朗; 上村健太朗; 上村健太朗; 登治謙; 佐藤彰彦; 佐藤彰彦; 鳥羽晋輔; 鳥羽晋輔; 日下部伸治; 日下部伸治; 佐々木道仁; 田畑耕史郎; 大場靖子; 澤洋文; 松浦善治; 松浦善治; 松田彰; 前仲勝実; 前仲勝実, 日本ウイルス学会学術集会プログラム・予稿集(Web), 69th, 2022
• 分泌型IgA抗体の四量体形成分子機構の生化学的・構造生物学的解析
  田畑耕史郎; 田畑耕史郎; 福原秀雄; 福原秀雄; 安楽佑樹; 多賀祐喜; 佐々木道仁; 板倉友香里; 佐野芳; 上野朗; 相内章; 後藤希代子; 長谷川秀樹; 前仲勝実; 前仲勝実; 澤洋文; 澤洋文; 大場靖子; 鈴木忠樹, 日本ワクチン学会学術集会プログラム・抄録集, 26th, 2022
• Preparation and interaction analysis of highly functional antibody by rational design
  田所高志; 田所高志; 大村玲央; 冨田麻美; 坪井晴美; 中村光太; 前仲勝実, バイオメディカル分析科学シンポジウム講演要旨集, 34th, 2022
• 世界初IDP酵素の検証
  大和田ゆうき; 澤田光平; 荒井彩花; 田所高志; 南篤志; 前仲勝実; 久米田博之; 姚閔; 及川英秋; 尾瀬農之; 尾瀬農之, 日本結晶学会年会講演要旨集, 2022, 2022
• 強力な中和抗体NT-108によるSARS-CoV-2スパイクタンパク質認識の構造的基盤
  安楽佑樹; 小野寺大志; 喜多俊介; 安達悠; 森山彩野; 佐藤彰彦; 佐藤彰彦; 野村尚生; 田所高志; 田所高志; 湯本航平; 湯本航平; 伊東詩織; 田聡; 福原秀雄; 福原秀雄; 佐々木道仁; 大場靖子; 志和希; 岩田奈織子; 永田典代; 鈴木干城; 佐々木慈英; 関塚剛史; 登内奎介; 福士秀悦; 里深博幸; 香月康宏; 孫琳; 押村光雄; 黒田誠; 鈴木忠樹; 澤洋文; 橋口隆生; 高橋宜聖; 前仲勝実, 日本ウイルス学会学術集会プログラム・予稿集(Web), 69th, 2022
• Ligand recognition mechanisms by immune system receptors via weak and fast binding
  渡邊紘士; 黒木喜美子; 前仲勝実, Drug Delivery System, 37, 2, 112, 121, 2022, [Peer-reviewed]
  Immunoreceptors play an important role in maintaining homeostasis in the body by distinguishing between self and non-self, and by acting as a starting point for immune activation and inhibition signals. However, unlike soluble proteins such as antibodies, the binding affinity between immunoreceptors and their ligands is weak and especially, the dissociation is rapid, making accurate assessment of binding affinity difficult. In this review, we focused on this weak and fast interactions in ligand recognition by immunoreceptors and introduce kinetic, thermodynamic, and structural aspects of molecular recognition mechanisms using physicochemical and structural methods., THE JAPAN SOCIETY OF DRUG DELIVERY SYSTEM, Japanese
• Understanding the mechanism by which Ca²⁺ regulates ERp57-CNX complex formation
  金村進吾; 谷川雄哉; 伊藤大; LIN Yuxi; 松崎元紀; 黒木喜美子; 山口宏; 前仲勝実; LEE Young-Ho; 稲葉謙次; 奥村正樹, 日本分子生物学会年会プログラム・要旨集(Web), 44th, Dec. 2021
• Cryo-Electron Microscopes organized by Drug Discovery Base of Hokkaido University
  前仲勝実, 日本分子生物学会年会プログラム・要旨集(Web), 44th, Dec. 2021
• Thermal stability analysis of lipid antigen presenting molecule, CD1d
  秋田穂; 日下裕規; TIAN Cong; 田所高志; 井貫晋輔; 新山真由美; 杉山成; 村田道雄; 藤本ゆかり; 喜多俊介; 前仲勝実; 前仲勝実, 日本分子生物学会年会プログラム・要旨集(Web), 44th, Dec. 2021
• カルシウムイオンによるERp57-CNX複合体の構造機能調節
  谷川 雄哉; 金村 進吾; 伊藤 大; 林 雨曦; 松崎 元紀; 黒木 喜美子; 山口 宏; 前仲 勝実; 李 映昊; 稲葉 謙次; 奥村 正樹, 日本生化学会大会プログラム・講演要旨集, 94回, [3T14m, 245)], Nov. 2021
  (公社)日本生化学会, Japanese
• X-ray crystal structure analysis of lipid antigen presenting molecule CD1b in complex with endogenous ligand from silkworm
  TIAN Cong; KUSAKA Hiroki; TADOKORO Takashi; KITA Shunsuke; MAENAKA Katsumi, 日本結晶学会年会講演要旨集, 2021, Nov. 2021
• MHC classI様分子CD1dとアミド型α-GarCer複合体のX線結晶構造解析
  秋田穂; 日下裕規; 田聡; 田所高志; 井貫晋輔; 新山真由美; 杉山成; 村田道雄; 藤本ゆかり; 喜多俊介; 前仲勝実, 日本結晶学会年会講演要旨集, 2021, Nov. 2021
• MicroED法を用いたNi錯体の構造決定
  古川敦; 土井良平; 土井良平; 池本優真; 内山雅史; 小芝未希子; 前仲勝実; 佐藤美洋, 日本結晶学会年会講演要旨集, 2021, Nov. 2021
• 北大創薬センターの新型コロナウイルス治療薬開発の現状と展望
  前仲勝実, 日本薬学会九州支部大会講演要旨集, 38th (CD-ROM), Nov. 2021
• カルシウムイオンによるERp57-CNX複合体の構造機能調節
  谷川 雄哉; 金村 進吾; 伊藤 大; 林 雨曦; 松崎 元紀; 黒木 喜美子; 山口 宏; 前仲 勝実; 李 映昊; 稲葉 謙次; 奥村 正樹, 日本生化学会大会プログラム・講演要旨集, 94回, [3T14m, 245)], Nov. 2021
  (公社)日本生化学会, Japanese
• 新型コロナウイルスspike蛋白質と中和抗体NT-193複合体のX線結晶構造解析
  喜多俊介; 小野寺大志; 安達悠; 森山彩野; 野村尚生; 田所高志; 安楽佑樹; 湯本航平; 田聡; 福原秀雄; 鈴木干城; 佐々木慈英; 福士秀悦; 里深博幸; 香月康宏; 押村光雄; 橋口隆生; 高橋宜聖; 前仲勝実, 日本結晶学会年会講演要旨集, 2021, Sep. 2021
• 毒ヘビ由来Ca²⁺チャネル阻害型神経毒と毒ヘビ血清蛋白質の複合体構造
  田所高志; 岡部由紀; 松原永季; 喜多俊介; 尾瀬農之; 黒木喜美子; 前仲勝実; 寺田成之; 塩井(青木)成留実, 日本結晶学会年会講演要旨集, 2021, Aug. 2021
• Structure-based drug design for anti-viral drug development
  安楽佑樹; 喜多俊介; 前仲勝実, 医学のあゆみ, 278, 6, 532, 538, Aug. 2021
  医歯薬出版, Japanese
• 蛋白質科学を基盤としたアカデミア創薬の現状と展望:北大創薬センターの活動
  前仲勝実; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 21st, Jun. 2021
• カルシウムによるERp57-CNXの構造機能調節
  谷川雄哉; 金村進吾; 伊藤大; LIN Yuxi; 松崎元紀; 黒木喜美子; 山口宏; LEE Young-Ho; 前仲勝実; 稲葉謙次; 奥村正樹; 奥村正樹, 日本蛋白質科学会年会プログラム・要旨集, 21st, Jun. 2021
• Functional analysis of lipid loading into CD1b mediated by Saposin proteins
  TIAN Cong; KUSAKA Hiroki; TADOKORO Takashi; KITA Shunsuke; MAENAKA Katsumi, 日本蛋白質科学会年会プログラム・要旨集, 21st, Jun. 2021
• X-ray crystal structure analysis of lipid antigen presenting molecule CD1b
  TIAN Cong; KUSAKA Hiroki; TADOKORO Takashi; KITA Shunsuke; MAENAKA Katsumi, 量子ビームサイエンスフェスタ(Web), 2020, Mar. 2021
• Viral Biophysics: Contributions to Drug Modalities
  MAENAKA Katsumi; FUKUHARA Hideo; HASHIGUCHI Takao; CAAVEIRO Jose M. M.; NAGATOISHI Satoshi; KURODA Daisuke; TSUMOTO Kouhei, Seibutsu Butsuri, 61, 2, 082, 089, Mar. 2021
  Recent virological researches using biophysical methods, termed as virus biophysics or virophysics, largely contribute to the development of anti-viral drugs and vaccines. In this review, examples of structural and physicochemical analyses for representative viruses to develop drug modalities such as small compounds, antibodies, and vaccines are explained, and future direction of biophysical research for virus research is also discussed., The Biophysical Society of Japan General Incorporated Association, Japanese
• 免疫活性化受容体LILRA2のANGPTL6認識機構の解明(The understanding of binding mechanism of LILRA2 and ANGPTL6)
  王 嘉き; 古川 敦; 山崎 莉佳; 平安 恒幸; 門松 毅; 尾池 雄一; 荒瀬 尚; 前仲 勝実, 日本薬学会年会要旨集, 141年会, 28P01, 105S, Mar. 2021
  (公社)日本薬学会, English
• Viral Biophysics: Contributions to Drug Modalities
  前仲勝実; 福原秀雄; 橋口隆生; CAAVEIRO Jose M. M.; 長門石曉; 黒田大祐; 津本浩平; 津本浩平, 生物物理(Web), 61, 2, Mar. 2021
• 狂犬病ウイルスP蛋白質による宿主の免疫経路阻害機構の解明
  南未来; 杉山葵; 野間井智; JIANG Xinxin; 前仲勝実; YAO Min; 尾瀬農之, 日本蛋白質科学会年会プログラム・要旨集, 21st, 2021
• 病原性理解のためのLyssavirus P蛋白質C末端ドメイン構造解析
  杉山葵; 野間井智; JIANG Xinxin; 南未来; 前仲勝実; 伊藤直人; GOOLEY Paul R.; MOSELEY Gregory W.; YAO Min; 尾瀬農之; 尾瀬農之, 日本蛋白質科学会年会プログラム・要旨集, 21st, 2021
• 麻疹ウイルスVタンパク質によるType I IFN経路阻害機構の解明
  木本円花; 永野悠馬; 杉山葵; 姚閔; 田所高志; 前仲勝実; 尾瀬農之, 日本結晶学会年会講演要旨集, 2021, 2021
• 平滑筋弛緩薬パパベリンの新規効能:血液脊髄関門保護を介した脊髄損傷に対する神経保護効果
  鈴木裕貴; 角家健; 五月女慧人; 遠藤健; 浅野毅; 岩崎倫政; 中川慎介; 前仲勝実, 北海道整形災害外科学会, 139th, 2, S73, S73, 2021
  (公社)日本整形外科学会, Japanese
• Structural and Functional Basis for LILRB Immune Checkpoint Receptor Recognition of HLA-G isoforms
  黒木, 喜美子; 松原, 永季; 神田, 諒; 宮下, 尚之; 白石, 充典; 福永, 裕子; 上敷領, 淳; 福永, 淳; 福原, 秀雄; 廣瀬, 薫; Hunt, Joan S; 杉田, 有治; 喜多, 俊介; 尾瀬, 農之; 前仲, 勝実, Annual report of the Faculty of Pharmacy & Pharmaceutical Sciences, Fukuyama University, 38, 38, 35, 36, 25 Dec. 2020
  福山大学薬学部, Japanese
• COVID-19対策の創薬開発へ向けた北大創薬科学研究教育センターの取り組み
  前仲勝実, CBI学会大会, 2020 (CD-ROM), Oct. 2020
• Academic drug discovery with pharmaceutical modality in Center for Research and Education on Drug Discovery of Hokkaido University
  Maenaka Katsumi, Proceedings for Annual Meeting of The Japanese Pharmacological Society, 93, 2-S19-4, Mar. 2020
  Hokkaido University Institute of Pharmaceutical Sciences established an affiliated drug discovery science research and education center, Center for Research and Education on Drug Discovery of Hokkaido University (CRED), in 2011 to promote academia drug discovery research. We have set up over the last 8 years the ‘state of the art' instruments necessary for chemical screening, and provided the expertise for drug discovery to novice users, supported by the projects, such as "Basis for Supporting Innovative Drug Discovery and Life Science Research". We also organize a "Platform for medical care and drug discovery" network with related academic departments and universities, Hokkaido University hospital and pharmaceutical companies mainly in Hokkaido Area.
  
  We are proceeding drug discovery modality research using a seamless "from drug seeds to preclinical" development system with a cryo-electron microscope: (1) unique Hokkaido University chemical library (peptides, nucleic acids and natural compounds) and semi-automatic preparation system, (2) preparation technology of difficult-to-express proteins, (3) complete physicochemical measurement technology, (4) Integrated structural analysis technology with cryo EM.
  
  In this lecture, I would like to look back over the past eight years and introduce the current efforts of CRED with some specific examples including the cooperation with the Development Unit of Drug Discovery Initiative of the University of Tokyo to proceed ADME evaluation and derivative synthesis., Japanese Pharmacological Society, Japanese
• Academic drug discovery and future perspective of Cryo-EM in Hokkaido University
  前仲勝実, 日本薬学会年会要旨集(CD-ROM), 140th (Web), LS08, LS08, Mar. 2020
  (公社)日本薬学会, Japanese
• 血液脊髄関門機能保護を介した脊髄損傷治療薬の開発
  鈴木 裕貴; 角家 健; 遠藤 健; 袁 儒非; 浅野 毅; 前仲 勝実; 中川 慎介; 岩崎 倫政, Journal of Spine Research, 11, 3, 589, 589, Mar. 2020
  (一社)日本脊椎脊髄病学会, Japanese
• 〈Basic Science〉抑制化受容体と免疫応答 抑制化受容体の構造
  渡邊紘士; 黒木喜美子; 前仲勝実, 炎症と免疫, 29, 1, 2, 7, Feb. 2020
  (株)先端医学社, Japanese
• リッサウイルスP蛋白質C末端ドメインの構造比較
  杉山葵; 野間井智; 蒋欣欣; 南未来; 前仲勝実; 伊藤直人; GOOLEY Paul R.; MOSELEY Gregory W.; 姚閔; 尾瀬農之; 尾瀬農之, 日本結晶学会年会講演要旨集, 2020 (CD-ROM), 2020
• Drug development for spinal cord injury by targeting protection of blood-spinal cord barrier
  鈴木裕貴; 角家健; 遠藤健; 袁儒非; 浅野毅; 前仲勝実; 中川慎介; 岩崎倫政, Journal of Spine Research (Web), 11, 3, 2020
• Crystal structure analysis of the C-terminal domain of Duvenhage virus P protein
  杉山葵; 蒋欣欣; 前仲勝実; 姚閔; 尾瀬農之, 量子ビームサイエンスフェスタ(Web), 2019, 2020
• Quality control of major histocompatibility complex in the endoplasmic reticulum.
  金村進吾; 金村進吾; 松崎元紀; 前仲勝実; 稲葉謙次; 奥村正樹, 月刊臨床免疫・アレルギー科, 74, 5, 419, 426, 2020
  (有)科学評論社, Japanese
• LILRA2のリガンド認識機構の解明
  古川敦; 山崎莉佳; WANG Jiaqi; 平安恒幸; 湯本航平; 福原秀雄; 荒瀬尚; 前仲勝実, 日本生化学会大会(Web), 93rd, [2Z13, 659)], 2020
  (公社)日本生化学会, Japanese
• アカデミア創薬における小胞体ストレス応答性酵素を標的とした抗癌剤スクリーニング
  野村尚生; 松丸尊紀; 春山知樹; 前田直良; 奥村正樹; 金村進吾; 稻葉謙次; 田村保明; 前仲勝実, 日本分子生物学会年会プログラム・要旨集(Web), 42nd, Dec. 2019
• CD1dとアミド基導入抗原複合体のX線結晶構造解析
  喜多 俊介; 日下 裕規; 井貫 晋輔; Md. Imran Hossain; 花島 慎弥; 田所 高志; 新山 真由美; 杉山 成; 相羽 俊彦; 尾瀬 農之; 黒木 喜美子; 深瀬 浩一; 村田 道雄; 藤本 ゆかり; 前仲 勝実, 日本結晶学会 講演要旨集, Nov. 2019
• 免疫系受容体によるウイルス感染制御の構造基盤
  前仲 勝実, 日本小児感染症学会総会・学術集会プログラム・抄録集, 51回, 89, 89, Oct. 2019
  日本小児感染症学会, Japanese
• 免疫系受容体によるウイルス感染制御の構造基盤
  前仲 勝実, 日本小児感染症学会総会・学術集会プログラム・抄録集, 51回, 89, 89, Oct. 2019
  日本小児感染症学会, Japanese
• タンパク質の運命を制御する生体システムと疾病のフロンティア 小胞体ストレス応答性酸化還元調節酵素を標的とした創薬スクリーニング
  野村 尚生; 松丸 尊紀; 春山 知樹; 前田 直良; 奥村 正樹; 金村 進吾; 稲葉 謙次; 田村 保明; 前仲 勝実, 日本生化学会大会プログラム・講演要旨集, 92回, [2S03m, 05], Sep. 2019
  (公社)日本生化学会, Japanese
• 抗体医薬のための人工的三量体一本鎖Fvフラグメントの開発(Development of the engineered trimeric single-chain Fv fragment of the therapeutic antibody)
  Tadokoro Takashi; Nakamura Kota; Tsuboi Harumi; Maenaka Katsumi, 生物物理, 59, Suppl.1-2, S391, S391, Aug. 2019
  (一社)日本生物物理学会, English
• C型レクチン受容体Mincleリガンドとしての複合脂質:合成と機能解析
  松丸尊紀; 齋藤良太; 古川敦; 山崎晶; 前仲勝実; 藤本ゆかり, 日本化学会春季年会講演予稿集(CD-ROM), 99th, ROMBUNNO.2F6‐08, Mar. 2019
  Japanese
• SPECIFICITY OF ENDOGENOUS INHIBITOR FOR THE SNAKE NEUROTOXIN TRIFLIN: INTERACTION AND STRUCTURE ANALYSIS
  Narumi Shioi; Takashi Tadokoro; Yaopeng Hu; Lin Hai Kurahara; Keizo Hiraishi; Katsumi Maenaka; Isao Kuraoka; Shigeyuki Terada, TOXICON, 158, S34, S34, Feb. 2019
  English, Summary international conference
• WetとDryのコミュニケーションによるレジデンス化合物の検索
  児玉耕太; 児玉耕太; 斎尾智英; 福原秀雄; 乙黒聡子; 新妻清夏; 松丸尊紀; 松丸尊紀; 五十嵐学; 前仲勝実, 日本化学会春季年会講演予稿集(CD-ROM), 99th, 2019
• Crystal structure analysis of lipid presenting molecule CD1d
  喜多俊介; 日下裕規; HOSSAIN Md. Imran; 花島慎弥; 井貫晋輔; 田所高志; 新山真由美; 杉山成; 相羽俊彦; 相羽俊彦; 尾瀬農之; 黒木喜美子; 深瀬浩一; 藤本ゆかり; 村田道雄; 前仲勝実, 量子ビームサイエンスフェスタ(Web), 2018, 2019
• イヌジステンパーウイルス受容体結合タンパク質の構造と膜融合の活性化機構
  福原秀雄; 酒匂幸; 河村美尋; 梶川瑞穂; 橋口隆生; 竹田誠; PHILIPPE Plattet; 尾瀬農之; 前仲勝実, 日本ウイルス学会学術集会プログラム・予稿集(Web), 67th, 2019
• ヒトSLAMのアミノ最末端領域は麻疹ウイルスの受容体として機能するために重要である
  關文緒; 福原秀雄; 山本雄大; SUNDARAM Arulmozhiraja; 大石和恵; 丸山正; 常盤広明; 前仲勝実; 竹田誠, 日本ウイルス学会学術集会プログラム・予稿集(Web), 67th, 2019
• 小胞体ストレス応答性酸化還元調節酵素を標的とした創薬スクリーニング
  野村尚生; 松丸尊紀; 春山知樹; 前田直良; 奥村正樹; 金村進吾; 稲葉謙次; 田村保明; 前仲勝実, 日本生化学会大会(Web), 92nd, [2S03m, 05], 2019
  (公社)日本生化学会, Japanese
• 麻疹中和抗体のフラグメント化と物理化学的特性の解析
  田所高志; LUBNA Jahan Mst; 伊藤由梨; 田原舞乃; 橋口隆生; 竹田誠; 福原秀雄; 前仲勝実, 日本細胞生物学会大会(Web), 71st, ROMBUNNO.2P‐209 (WEB ONLY), 2019
  Japanese
• 狂犬病ウイルスP蛋白質によるJAK‐STATシグナル阻害機構の解明
  杉山葵; 蒋欣欣; 永野悠馬; 野間井智; 若原拓也; 前仲勝実; 姚閔; MOSLEY Gregory; 尾瀬農之, 日本細胞生物学会大会(Web), 71st, ROMBUNNO.2P‐005 (WEB ONLY), 2019
  Japanese
• 免疫受容体LILRA2のリガンド認識機構の解明
  山崎莉佳; 古川敦; 平安恒幸; 平安恒幸; 門松毅; 尾池雄一; 前仲勝実, 日本細胞生物学会大会(Web), 71st, ROMBUNNO.2P‐127 (WEB ONLY), 2019
  Japanese
• モリビリウイルス属の細胞侵入機構と創薬への取り組み
  前仲勝実; 前仲勝実; 前仲勝実, 生体分子科学討論会講演要旨集, 46th, 14, 2019
  Japanese
• IDPを使用した新規ペア型酵素の戦略
  澤田光平; 田所高志; 大和田ゆうき; 南篤志; 久米田博之; 斎尾智英; 姚閔; 及川英秋; 前仲勝実; 尾瀬農之; 尾瀬農之, 日本結晶学会年会講演要旨集, 2018, 32, 01 Nov. 2018
  Japanese
• [北大は新入生を歓迎する] ： 先生からのメッセージ
  北村, 清彦; 金沢, 英之; 岡田, 信弘; 鈴木, 恵二; 藤原, 正智; 岩﨑, 克則; 前仲, 勝実; 志村, 華子; 高見, 敏子; 渡辺, 将人; 東藤, 正浩, リテラポプリ, 44, 11, 14, 05 Oct. 2018
  Japanese
• NMRを用いた自然免疫受容体Mincleによる糖脂質認識機構の解析
  古川敦; 須知祐介; 久米田博之; 松丸尊紀; 齊藤貴士; 前仲勝実, Abstracts. Annual Meeting of the NMR Society of Japan, 57th, 178‐179, Oct. 2018
  Japanese
• 高精度分子シミュレーションに基づく中分子化合物の脂質二重膜透過解析
  清水奏; 清水奏; ARULMOZHIRAJA Sundaram; ARULMOZHIRAJA Sundaram; 山本雄大; 山本雄大; 前仲勝実; 前仲勝実; 常盤広明; 常盤広明, 日本薬学会関東支部大会講演要旨集, 62nd, 97, 10 Sep. 2018
  Japanese
• ヒト単純ヘルペスウイルス由来糖ペプチドと免疫受容体PILRα相互作用解析
  野村尚生; 柿田浩輔; 古川敦; 穴田仁洋; 橋下俊一; 松永茂樹; 齊藤貴士; 前仲勝実; 前仲勝実, Abstracts. Annual Meeting of the NMR Society of Japan, 57th, 198‐199, 03 Sep. 2018
  Japanese
• エポキシド加水分解機能を持つタンパク質の分子進化的考察
  飯淵 友直; 尾瀬 農之; 前仲 勝実; 及川 英秋; 園山 正史; 向井 有理, 日本生化学会大会プログラム・講演要旨集, 91回, [2P, 110], Sep. 2018
  (公社)日本生化学会, Japanese
• カイコ脂質輸送蛋白質の機能解析
  喜多 俊介; 日下 裕規; 前仲 勝実, 日本生化学会大会プログラム・講演要旨集, 91回, [3P, 070], Sep. 2018
  (公社)日本生化学会, Japanese
• 脂質抗原提示分子CD1dによる抗原認識機構の解析
  日下 裕規; 喜多 俊介; 大野 祐介; 木原 章雄; 尾瀬 農之; 黒木 喜美子; 前仲 勝実, 日本生化学会大会プログラム・講演要旨集, 91回, [3P, 090], Sep. 2018
  (公社)日本生化学会, Japanese
• エポキシド加水分解機能を持つタンパク質の分子進化的考察
  飯淵 友直; 尾瀬 農之; 前仲 勝実; 及川 英秋; 園山 正史; 向井 有理, 日本生化学会大会プログラム・講演要旨集, 91回, [2P, 110], Sep. 2018
  (公社)日本生化学会, Japanese
• 狂犬病ウイルスP蛋白質によるJAK‐STATシグナル阻害機構の解明
  杉山葵; JIANG Xinxin; 永野悠馬; 野間井智; 若原拓也; 前仲勝実; YAO Min; MOSLEY Gregory; 尾瀬農之, 日本蛋白質科学会年会プログラム・要旨集, 18th, 48, 23 May 2018
  Japanese
• 脂質抗原提示分子CD1dによる抗原認識における種差
  日下裕規; 喜多俊介; HOSSAIN Imran; 花島慎弥; 井貫晋輔; 新山真由美; 杉山成; 相羽俊彦; 尾瀬農之; 黒木喜美子; 深瀬浩一; 藤本ゆかり; 村田道雄; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 18th, 84, 23 May 2018
  Japanese
• 慢性炎症関連因子ANGPTL2の免疫細胞受容体LILRB2結合部位の同定
  荒牧峻彦; 黒木喜美子; 門松毅; 尾池雄一; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 18th, 146, 23 May 2018
  Japanese
• 毒ヘビ由来Ca2+チャネル阻害型神経毒と毒ヘビ血清蛋白質の複合体構造
  田所高志; 塩井(青木; 成留実; 岡部由紀; 松原永季; 喜多俊介; 尾瀬農之; 黒木喜美子; 前仲勝実; 寺田成之, 日本蛋白質科学会年会プログラム・要旨集, 18th, 10, 90, 23 May 2018, [International Magazine]
  ERp57, a member of the protein disulfide isomerase family, is a ubiquitous disulfide catalyst that functions in the oxidative folding of various clients in the mammalian endoplasmic reticulum (ER). In concert with ER lectin-like chaperones calnexin and calreticulin (CNX/CRT), ERp57 functions in virtually all folding stages from co-translation to post-translation, and thus plays a critical role in maintaining protein homeostasis, with direct implication for pathology. Here, we present mechanisms by which Ca2+ regulates the formation of the ERp57-calnexin complex. Biochemical and isothermal titration calorimetry analyses revealed that ERp57 strongly interacts with CNX via a non-covalent bond in the absence of Ca2+. The ERp57-CNX complex not only promoted the oxidative folding of human leukocyte antigen heavy chains, but also inhibited client aggregation. These results suggest that this complex performs both enzymatic and chaperoning functions under abnormal physiological conditions, such as Ca2+ depletion, to effectively guide proper oxidative protein folding. The findings shed light on the molecular mechanisms underpinning crosstalk between the chaperone network and Ca2+., Japanese
• NMRを用いた自然免疫受容体Mincleによる糖脂質認識機構の解析
  古川敦; 須知佑介; 久米田博之; 松丸尊紀; 齊藤貴士; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 18th, 120, 23 May 2018
  Japanese
• ヒトの自然免疫系を阻害する麻疹ウイルスV蛋白質の機能解析
  永野悠馬; 若原拓也; 秦玉瑩; 柳雄介; 前仲勝実; 尾瀬農之; 尾瀬農之, 日本蛋白質科学会年会プログラム・要旨集, 18th, 64, 23 May 2018
  Japanese
• Molecular recognition of Immune cell surface receptors toward various ligands
  前仲勝実, 日本比較免疫学会学術集会講演要旨, 30th, May 2018
• 新規Notch signaling阻害剤NSI-1の開発
  白石 昂也; 堺谷 政弘; 乙黒 聡子; 前仲 勝実; 中矢 正; 鈴木 利治, 日本薬学会年会要旨集, 138年会, 3, 128, 128, Mar. 2018
  (公社)日本薬学会, Japanese
• イヌジステンパーウイルスの株間の感染性の違いに着目したウイルスタンパク質と受容体の相互作用解析
  松尾 直也; 關 文緒; 中野 祥吾; 伊藤 創平; 前仲 勝実; 竹田 誠; 常盤 広明, 日本薬学会年会要旨集, 138年会, 3, 185, 185, Mar. 2018
  (公社)日本薬学会, Japanese
• HSV-1感染における糖ペプチドと免疫受容体PILRα相互作用解析
  野村 尚生; 柿田 浩輔; 古川 敦; 穴田 仁洋; 橋下 俊一; 松永 茂樹; 齊藤 貴士; 前仲 勝実, 日本薬学会年会要旨集, 138年会, 2, 245, 245, Mar. 2018
  (公社)日本薬学会, Japanese
• 細菌に分解された抗体の免疫活性化レセプターLILRA2による認識機構の解明
  山崎 莉佳; 古川 敦; 平安 恒幸; 荒瀬 尚; 前仲 勝実, 日本薬学会年会要旨集, 138年会, 2, 247, 247, Mar. 2018
  (公社)日本薬学会, Japanese
• PILRαによる糖ペプチド認識機構の解明
  古川 敦; 柿田 浩輔; 荒瀬 尚; 穴田 仁洋; 尾瀬 農之; 橋本 俊一; 前仲 勝実, 日本薬学会年会要旨集, 138年会, 2, 261, 261, Mar. 2018
  (公社)日本薬学会, Japanese
• イヌジステンパーウイルスの株間の感染性の違いに着目したウイルスタンパク質と受容体の相互作用解析
  松尾直也; 關文緒; 中野祥吾; 伊藤創平; 前仲勝実; 竹田誠; 常盤広明; 常盤広明, 日本薬学会年会要旨集(CD-ROM), 138th, 3, ROMBUNNO.26PA‐pm161S, 185, Mar. 2018
  (公社)日本薬学会, Japanese
• HSV‐1感染における糖ペプチドと免疫受容体PILRα相互作用解析
  野村尚生; 柿田浩輔; 古川敦; 穴田仁洋; 橋下俊一; 松永茂樹; 齊藤貴士; 前仲勝実; 前仲勝実, 日本薬学会年会要旨集(CD-ROM), 138th, 2, ROMBUNNO.28X‐am02, 245, Mar. 2018
  (公社)日本薬学会, Japanese
• 細菌に分解された抗体の免疫活性化レセプターLILRA2による認識機構の解明
  山崎莉佳; 古川敦; 平安恒幸; 荒瀬尚; 前仲勝実, 日本薬学会年会要旨集(CD-ROM), 138th, 2, ROMBUNNO.28X‐pm02S, 247, Mar. 2018
  (公社)日本薬学会, Japanese
• PILRαによる糖ペプチド認識機構の解明
  古川敦; 柿田浩輔; 荒瀬尚; 穴田仁洋; 尾瀬農之; 橋本俊一; 前仲勝実, 日本薬学会年会要旨集(CD-ROM), 138th, 2, ROMBUNNO.27PA‐am327, 261, Mar. 2018
  (公社)日本薬学会, Japanese
• B型肝炎治療 2018 核酸アナログ製剤によるIFN‐λ誘導とそれを標的としたB型肝炎治療薬の探索
  村田一素; 前仲勝実; 溝上雅史, Mebio, 35, 1, 80‐87, 87, 10 Jan. 2018
  (株)メジカルビュー社, Japanese
• Crystal structure and functional analyses of Rabies virus P protein mutants
  野間井智; 蒋欣欣; 永野悠馬; 杉山葵; 姚閔; GOOLEY Paul; MOSELEY Gregory; 前仲勝実; 尾瀬農之; 尾瀬農之, 量子ビームサイエンスフェスタ(Web), 2017, 2018
• 39. Insight into polyether natural product biosynthesis mechanism from biochemical, biophysical, and structural aspects of epoxide hydrolase family
  Sawada Kohei; Minami Atsushi; Kumeta Hiroyui; Saio Tomohide; Matsumaru Takanori; Oikawa Hideaki; Maenaka Katsumi; Ose Toyoyuki, Symposium on the Chemistry of Natural Products, symposium papers, 60, 229-234, 2018
  【背景】
  ポリエーテル化合物は，海産微細藻由来のブレベトキシン，放線菌由来のモネンシン，ラサロシド，キジマイシンなどに代表されるように様々な生物が多種多様な骨格を持つポリエーテルを生産している。これら天然物は連続したエーテル環を分子骨格に持ち，生理活性において重要な役割を果たしている。例えば，ポリエーテル骨格による金属イオンのキレーション機構が知られており2, 3, エーテル環上の酸素原子が特定の金属イオンをキレートして電荷を包み込み，外側に疎水性領域の炭素骨格を向ける。これによって細胞内外のイオンの透過性が増加し，抗菌活性などを示す（イオノフォア）。ポリエーテル骨格としては，テトラヒドロフラン（THF）やテトラヒドロピラン（THP）のようなエーテル環が数珠玉状（モネンシンなど），もしくは梯子状（ブレベトキシンなど）に連結されたものである。こうしたポリエーテル系天然物の生合成経路，特に多くの不斉点を有するエーテル環の構築機構は，有機化学的にも非常に興味が持たれてきた。ポリエーテル骨格の構築機構は1983年に提唱されたCane-Celmer-Westley (CCW)モデル「ポリエン-ポリエポキシド仮説」（1）において，環化機構が統一的に説明された。このモデルでは，鎖状ポリオレフィン前駆体がエポキシ化され，生成したポリエポキシドが位置選択的なエポキシド開環反応によりポリエーテル骨格が構築される。
  
  Scheme 1. Monensin B biosynthesis pathway catalyzed by MonBI and MonBII oligomer
  
  私達は，Monensin生合成をモデルケースとしてポリエーテル骨格構築機構の解明に取り組んできた。多様性を決定づけるエーテル環の導入は，エポキシド加水分解酵素ホモログである環化酵素が担うことが，最近は広く知られてる。Monensinの場合，その骨格を構築するために3 回の5-exo 環化反応が必要である (Scheme 1)。しかしながら，モネンシン生合成遺伝子クラスター中には、環化酵素と相同性を持つ遺伝子がmonBI, monBII の2つしか存在しないため、この2つの環化酵素がどのように3 回の環化反応を触媒するかを解明することが，複雑なポリエーテル骨格構築メカニズムを一般化することと同義であると考えた。組換え発現させたMonBI，, Symposium on the Chemistry of Natural Products Steering Committee, Japanese
• 【B型肝炎治療2018】 核酸アナログ製剤によるIFN-λ誘導とそれを標的としたB型肝炎治療薬の探索
  村田 一素; 前仲 勝実; 溝上 雅史, Mebio, 35, 1, 80, 87, Jan. 2018
  (株)メジカルビュー社, Japanese
• カイコ脂質輸送蛋白質の機能解析
  喜多 俊介; 日下 裕規; 前仲 勝実, 日本生化学会大会プログラム・講演要旨集, 91st, [3P, 070], 2018
  (公社)日本生化学会, Japanese
• 脂質抗原提示分子CD1dによる抗原認識機構の解析
  日下 裕規; 喜多 俊介; 大野 祐介; 木原 章雄; 尾瀬 農之; 黒木 喜美子; 前仲 勝実, 日本生化学会大会プログラム・講演要旨集, 91st, [3P, 090], 2018
  (公社)日本生化学会, Japanese
• 新規Notch signaling阻害剤NSI‐1の開発
  白石昂也; 堺谷政弘; 乙黒聡子; 前仲勝実; 前仲勝実; 中矢正; 鈴木利治, 日本薬学会年会要旨集(CD-ROM), 138th, 3, ROMBUNNO.26PA‐am139S, 128, 2018
  (公社)日本薬学会, Japanese
• ヌクレアーゼ抵抗性4’修飾型ヌクレオシドのアンチセンスgapmerへの導入
  平塚隆寛; 田所高志; 前仲勝実; 松田彰, 日本薬学会年会要旨集(CD-ROM), 138th, ROMBUNNO.26M‐pm06S, 2018
  Japanese
• 細菌によって分解された抗体と免疫活性化受容体LILRA2との特異的相互作用機構の解明
  山崎莉佳; 古川敦; 平安恒幸; 荒瀬尚; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 18th, 64, 2018
  Japanese
• 免疫制御分子PILRαと免疫細胞分化マーカーCD45の相互作用解析
  石塚幹広; 古川敦; 荒瀬尚; 前仲勝実, 日本生化学会大会(Web), 90th, ROMBUNNO.1P‐0031 (WEB ONLY), 0031], Dec. 2017
  生命科学系学会合同年次大会運営事務局, Japanese
• HLA‐Cw12拘束性HIV‐1ペプチドに対する宿主免疫受容体認識機構
  山下諒也; 黒木喜美子; 渡邊洋介; 阪田竜馬; 村越勇人; 赤星智寛; 滝口雅文; 前仲勝実, 日本生化学会大会(Web), 2017年度, [1P, 0139], Dec. 2017
  生命科学系学会合同年次大会運営事務局, Japanese
• 免疫補助制御分子CD160とリガンドHVEMの分子認識機構に向けた研究
  岩森美樹; 黒木喜美子; 齊藤貴士; 齊藤貴士; 阿部千紘; 小島理恵子; 前仲勝実, 日本生化学会大会(Web), 2017年度, [3P, 0103], Dec. 2017
  生命科学系学会合同年次大会運営事務局, Japanese
• ヒト免疫受容体NKRP1AによるリガンドLLT1の分子認識機構
  田所高志; 喜多俊介; 松原永季; 笠井宣征; 玉置貴晴; 岡部由紀; 日下裕規; 石山夢美; 福原秀雄; 上敷領淳; 尾瀬農之; 黒木喜美子; 前仲勝実, 日本生化学会大会(Web), 2017年度, [2P, 0185], Dec. 2017
  生命科学系学会合同年次大会運営事務局, Japanese
• PEG化タンパク質精製法の確立に向けた新規構造化PEG分子の設計と機能解析
  山田千聖; WAWRO Adam; WAWRO Adam; 黒木喜美子; 高橋愛実; 村岡貴博; 村岡貴博; 金原数; 金原数; 前仲勝実, 日本生化学会大会(Web), 2017年度, [3P, 0167], Dec. 2017
  生命科学系学会合同年次大会運営事務局, Japanese
• HIV-2 Nefタンパク質のX線結晶構造
  平尾 憲吾; 黒木 喜美子; Andrews Sophie; 尾瀬 農之; Rowland-Jones Sarah; 前仲 勝実, 生命科学系学会合同年次大会, 2017年度, [2P, 0091], Dec. 2017
  生命科学系学会合同年次大会運営事務局, English
• 単純ヘルペスウイルス由来糖蛋白質がヒト受容体を認識するメカニズム
  尾瀬農之; 石塚幹広; 古川敦; 黒木喜美子; 前仲勝実, 日本結晶学会年会講演要旨集, 2017, 47, 23 Nov. 2017
  Japanese
• 糖脂質α-GalCerを基盤とした脂質改変型CD1dリガンドの創製研究
  井貫 晋輔; 相羽 俊彦; 平田 菜摘; 柏原 瑛美; 喜多 俊介; 前仲 勝実; 深瀬 浩一; 藤本 ゆかり, エンドトキシン・自然免疫研究, 20, 64, 67, Oct. 2017
  日本エンドトキシン・自然免疫研究会, Japanese
• 狂犬病ウイルスの細胞吸着に関与する宿主因子の解析
  佐々木道仁; アニンディタ パウリナ; 伊藤直人; 杉山誠; 福原秀雄; 尾瀬農之; 尾瀬農之; 前仲勝実; 澤洋文; 澤洋文, 日本獣医学会学術集会講演要旨集, 160th, 400, 400, 30 Aug. 2017
  (公社)日本獣医学会, Japanese
• Examination of antiviral activity of 5-ethynyl-1-ribofuranosylimidazole-4-carboxamide(EICAR) against rabies virus in vitro(和訳中)
  Anindita Paulina Duhita; 佐々木 道仁; 伊藤 直人; 杉山 誠; 南川 典昭; 周東 智; 乙黒 聡子; 市川 聡; 松田 彰; 前仲 勝実; 大場 靖子; 澤 洋文, 日本獣医学会学術集会講演要旨集, 160回, 390, 390, Aug. 2017
  (公社)日本獣医学会, English
• In vitroでの狂犬病ウイルスに対する5-エチニル-1-リボフラノシルイミダゾール-4-カルボキサミド(EICAR)の抗ウイルス活性に関する検討(Examination of antiviral activity of 5-ethynyl-1-ribofuranosylimidazole-4-carboxamide(EICAR) against rabies virus in vitro)
  Anindita Paulina Duhita; 佐々木 道仁; 伊藤 直人; 杉山 誠; 南川 典昭; 周東 智; 乙黒 聡子; 市川 聡; 松田 彰; 前仲 勝実; 大場 靖子; 澤 洋文, 日本獣医学会学術集会講演要旨集, 160回, 390, 390, Aug. 2017
  (公社)日本獣医学会, English
• 狂犬病ウイルスの細胞吸着に関与する宿主因子の解析
  佐々木 道仁; アニンディ・タパウリナ; 伊藤 直人; 杉山 誠; 福原 秀雄; 尾瀬 農之; 前仲 勝実; 澤 洋文, 日本獣医学会学術集会講演要旨集, 160回, 400, 400, Aug. 2017
  (公社)日本獣医学会, Japanese
• ハブ血清蛋白質SSPの毒蛇CRISPsの阻害剤としての応用
  塩井成留実; 田所高志; 胡耀鵬; 倉原琳; 平石敬三; 前仲勝実, トキシンシンポジウム予稿集, 64th, 76‐79, 01 Jul. 2017
  Japanese
• WetとDryのコミュニケーションによるアカデミア創薬
  児玉耕太; 斉尾智英; 前仲勝実; 金城政孝, バイオサイエンスとインダストリー, 75, 4, 323, 325, Jul. 2017
  (一財)バイオインダストリー協会, Japanese
• 麻疹ウイルスV蛋白質C末端領域の構造的特徴
  永野悠馬; 若原拓也; 蒋欣欣; 柳雄介; 前仲勝実; 尾瀬農之, 日本蛋白質科学会年会プログラム・要旨集, 17th, 48, 22 May 2017
  Japanese
• 毒ヘビ神経毒とその内在性阻害蛋白質複合体の立体構造解析
  塩井(青木; 成留実; 田所高志; 胡耀鵬; 前仲勝実; 寺田成之, 日本蛋白質科学会年会プログラム・要旨集, 17th, 130, 22 May 2017
  Japanese
• 分泌タンパク質ANGPTL2を介したシグナル伝達を阻害可能な低分子化合物探索
  荒牧峻彦; 黒木喜美子; 門松毅; 尾池雄一; 尾瀬農之; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 17th, 147, 22 May 2017
  Japanese
• 細菌の抗体分解による免疫レセプター活性化の分子基盤
  山崎莉佳; 古川敦; 平安恒幸; 黒木喜美子; 荒瀬尚; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 17th, 64, 22 May 2017
  Japanese
• トラスツズマブ一本鎖Fv抗体断片の構築および高機能化
  田所高志; 中村光太; 坪井晴美; 前田龍; 尾瀬農之; 松田彰; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 17th, 148, 22 May 2017
  Japanese
• CD1dの一本鎖化による安定化と結晶構造解析
  日下裕規; 喜多俊介; HOSSAIN Imuran Md; 花島慎弥; 井貫晋輔; 新山真由美; 杉山成; 尾瀬農之; 黒木喜美子; 藤本ゆかり; 村田道雄; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 17th, 120, 22 May 2017
  Japanese
• インフルエンザウイルス細胞侵入において鍵となる宿主タンパク質の同定
  藤岡容一朗; 西出真也; 尾瀬農之; 加藤いづみ; 福原秀雄; 藤岡真理; 堀内浩水; 佐藤絢; NEPAL Prabha; 柏木彩花; WANG Jing; 堀口美香; PAUDEL Sarad; 南保明日香; 宮崎忠昭; 前仲勝実; 前仲勝実; 大場雄介, 日本細胞生物学会大会(Web), 69th, ROMBUNNO.T8‐04(P2‐028) (WEB ONLY), 61, May 2017
  (一社)日本細胞生物学会, Japanese
• インフルエンザウイルス細胞侵入において鍵となる宿主タンパク質の同定
  藤岡 容一朗; 西出 真也; 尾瀬 農之; 加藤 いづみ; 福原 秀雄; 藤岡 真理; 堀内 浩水; 佐藤 絢; Nepal Prabha; 柏木 彩花; Wang Jing; 堀口 美香; Paudel Sarad; 南保 明日香; 宮崎 忠昭; 前仲 勝実; 大場 雄介, 日本細胞生物学会大会講演要旨集, 69回, 61, 61, May 2017
  (一社)日本細胞生物学会, Japanese
• IFN‐lambdaを標的とした新規B型肝炎治療薬の探索
  村田一素; 村田一素; 前仲勝実; 溝上雅史, 肝臓, 58, Supplement 1, A45, 20 Apr. 2017
  Japanese
• B型肝炎研究の新展開 IFN-lambdaを標的とした新規B型肝炎治療薬の探索
  村田 一素; 前仲 勝実; 溝上 雅史, 肝臓, 58, Suppl.1, A45, A45, Apr. 2017
  (一社)日本肝臓学会, Japanese
• 脂質結合タンパク質の構造生物学 最近の展開 自然免疫受容体Mincleの糖脂質認識機構
  古川 敦; 須知 佑介; 池野 里紗; 松丸 尊紀; 上敷領 淳; 齊藤 貴士; 尾瀬 農之; 山崎 晶; 前仲 勝実, 日本薬学会年会要旨集, 137年会, 1, 136, 136, Mar. 2017
  (公社)日本薬学会, Japanese
• 脂質結合タンパク質の構造生物学 最近の展開 脂質抗原受容体CD1dの脂質認識部位に存在する親水性アミノ酸残基の機能解析とその制御
  井貫 晋輔; 相羽 俊彦; 平田 菜摘; 相原 瑛美; 市原 収; 吉留 大輔; 喜多 俊介; 前仲 勝実; 深瀬 浩一; 藤本 ゆかり, 日本薬学会年会要旨集, 137年会, 1, 137, 137, Mar. 2017
  (公社)日本薬学会, Japanese
• 脂質結合タンパク質の構造生物学 最近の展開 脂質-タンパク質相互作用の解明を目指した重原子化CD1dリガンドの合成と生理活性の評価
  花島 慎弥; Hossain Imran; 土川 博史; 村田 道雄; 日下 裕規; 喜多 俊介; 前仲 勝実, 日本薬学会年会要旨集, 137年会, 1, 137, 137, Mar. 2017
  (公社)日本薬学会, Japanese
• 次世代のアカデミア創薬を担う若手の力 抗がん剤を目指した若手研究者連携による創薬スクリーニング
  野村 尚生; 松丸 尊紀; 奥村 正樹; 稲葉 謙次; 田村 保明; 前仲 勝実, 日本薬学会年会要旨集, 137年会, 1, 142, 142, Mar. 2017
  (公社)日本薬学会, Japanese
• 脂質‐タンパク質相互作用の解明を目指した重原子化CD1dリガンドの合成と生理活性の評価
  花島慎弥; HOSSAIN Imran; HOSSAIN Imran; 土川博史; 村田道雄; 村田道雄; 日下裕規; 喜多俊介; 前仲勝実, 日本薬学会年会要旨集(CD-ROM), 137年会, 1, 137, 137, Mar. 2017
  (公社)日本薬学会, Japanese
• 脂質抗原受容体CD1dの脂質認識部位に存在する親水性アミノ酸残基の機能解析とその制御
  井貫晋輔; 相羽俊彦; 相羽俊彦; 平田菜摘; 相原瑛美; 市原収; 吉留大輔; 喜多俊介; 前仲勝実; 深瀬浩一; 藤本ゆかり, 日本薬学会年会要旨集(CD-ROM), 137年会, 1, 137, 137, Mar. 2017
  (公社)日本薬学会, Japanese
• Insight into the activation mechanism of Brk
  松尾友樹; 神田諒; 西條慎也; 清水伸隆; 前仲勝実; 尾瀬農之, 量子ビームサイエンスフェスタ(Web), 2016, 2017
• ヒストンメチル化酵素複合体構成因子EZH2-EED相互作用阻害剤の創製研究
  塩田勇介; 薬師寺文華; 加藤いづみ; 岡田ゆかり; 堀内正隆; 児玉耕太; 松田彰; 前仲勝実; 市川聡, メディシナルケミストリーシンポジウム講演要旨集, 35th, 2017
• 自然免疫受容体Mincleの糖脂質認識機構
  古川敦; 須知佑介; 池野里紗; 松丸尊紀; 上敷領淳; 齊藤貴士; 尾瀬農之; 山崎晶; 前仲勝実, 日本薬学会年会要旨集(CD-ROM), 137th, ROMBUNNO.S12‐1, 2017
  Japanese
• 抗がん剤を目指した若手研究者連携による創薬スクリーニング
  野村尚生; 松丸尊紀; 奥村正樹; 稲葉謙次; 田村保明; 前仲勝実, 日本薬学会年会要旨集(CD-ROM), 137th, ROMBUNNO.S13‐4, 2017
  Japanese
• 免疫受容体Mincleによる糖脂質認識機構のNMR解析
  齊藤貴士; 須知佑介; 古川敦; 前仲勝実, Abstracts. Annual Meeting of the NMR Society of Japan, 55th, 146‐147, 16 Nov. 2016
  Japanese
• 緑膿菌のレクチンLecA・LecB阻害剤リード化合物の創製研究
  大形悠梨子; 高木朋之; 阿部裕希; 加藤いづみ; 前仲勝実; 市川聡; 堺谷政弘, メディシナルケミストリーシンポジウム講演要旨集, 34th, 161, 11 Nov. 2016
  Japanese
• 糖脂質リガンドにおける脂質部位の構造展開を基盤とした新規CD1dリガンドの創製研究
  井貫晋輔; 相羽俊彦; 相羽俊彦; 平田菜摘; 柏原瑛美; 市原収; 吉留大輔; 喜多俊介; 前仲勝実; 深瀬浩一; 藤本ゆかり, メディシナルケミストリーシンポジウム講演要旨集, 34th, 139, 11 Nov. 2016
  Japanese
• 悪性脳腫瘍治療を指向した新規ベンゾオキサゾール誘導体の合成と活性評価
  林健人; 阿部祐希; 前田直良; 前仲勝実; 市川聡; 堺谷政弘, メディシナルケミストリーシンポジウム講演要旨集, 34th, 103, 11 Nov. 2016
  Japanese
• HLAの立体構造と免疫制御受容体の分子認識機構
  前仲勝実; 前仲勝実; 喜多俊介; 黒木喜美子, MHC (Web), 23, 2 Suppl, 63, 63, 15 Oct. 2016
  日本組織適合性学会, Japanese
• HLAの立体構造と免疫制御受容体の分子認識機構
  前仲 勝実; 喜多 俊介; 黒木 喜美子, MHC: Major Histocompatibility Complex, 23, 2Suppl., 63, 63, Oct. 2016
  日本組織適合性学会, Japanese
• HLAの立体構造と免疫制御受容体の分子認識機構
  前仲 勝実; 喜多 俊介; 黒木 喜美子, MHC: Major Histocompatibility Complex, 23, 2Suppl., 63, 63, Oct. 2016
  日本組織適合性学会, Japanese
• HLAの立体構造と免疫制御受容体の分子認識機構
  黒木喜美子; 黒木喜美子; 喜多俊介; 喜多俊介; 前仲勝実; 前仲勝実, MHC (Web), 23, 2, 80, 95, Sep. 2016
  Human Leukocyte Antigens (HLAs) are glycoproteins that exhibit unusually high genetic polymorphism as well as high polygenecity by forming a wide variety of gene families. HLAs generally display peptides derived from intracellular proteins to T cells, and furthermore, they interact with various immune cell surface receptors to control broad aspects of immune responses pleiotropically, resulting in the maintenance of homeostasis in our body. X-ray crystallography has remarkably contributed to understanding of precise mechanisms for these HLA interactions. In this issue, we describe molecular structures of HLAs and HLA-receptor complexes, showing how HLA molecules regulate immune responses, and further discuss about their relationship with diseases., 日本組織適合性学会, Japanese
• 脂質認識部位を制御する新規リガンドを用いたCD1dの機能解析
  平田菜摘; 相羽俊彦; 相羽俊彦; 内梨洋介; 市原収; 吉留大輔; 喜多俊介; 前仲勝実; 深瀬浩一; 井貫晋輔; 藤本ゆかり, 日本糖質学会年会要旨集, 35th, 115, 01 Aug. 2016
  Japanese
• アンジオポエチン様因子Angptl2の結晶構造解析および免疫受容体LILRB2との相互作用解析
  荒牧峻彦; 黒木喜美子; 門松毅; 寺田和豊; 尾池雄一; 尾瀬農之; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 16th, 104, 19 May 2016
  Japanese
• I型IFNシグナルを回避する麻疹ウイルスVタンパク質の分子基盤解析
  永野悠馬; 若原拓也; 野間井智; 市川聡; 柳雄介; 前仲勝実; 尾瀬農之, 日本蛋白質科学会年会プログラム・要旨集, 16th, 85, 19 May 2016
  Japanese
• 可溶性HLA‐Gの製剤化に向けて
  田所高志; 可野巧; 市川聡; 松田彰; 黒木喜美子; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 16th, 155, 19 May 2016
  Japanese
• 生体内AGE化タンパク質検出系の構築に向けた一本鎖抗体(scFv)の創製と評価
  福田夏希; 宮崎広海; 分山結加里; 中原悠介; 佐藤卓史; 小橋川敬博; 逢坂文那; 斉藤貴士; 前仲勝実; 野井健太郎; 小椋光; 中村照也; 山縣ゆり子; 森岡弘志, 日本蛋白質科学会年会プログラム・要旨集, 16th, 118, 19 May 2016
  Japanese
• カイコバキュロウイルスを用いた新規Bacmamの開発
  今井徳俊; 田所高志; 福原秀雄; 堀内正隆; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 16th, 78, 19 May 2016
  Japanese
• 免疫疾患患者血清中のHLA‐Gの定量に向けた抗HLA‐G抗体の特性評価
  目黒愛実; 古川敦; 黒木喜美子; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 16th, 81, 19 May 2016
  Japanese
• NMRを用いた自然免疫受容体Mincleの糖脂質認識機構の解析
  須知佑介; 古川敦; 齊藤貴士; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 16th, 50, 19 May 2016
  Japanese
• カイコバキュロウイルス発現系による急性骨髄性白血病に特異的なFLT3/ITDタンパク質の効率的な生産
  開俊樹; 菊池次郎; 喜多俊介; 前仲勝実; 古川雄祐; 柴山修哉, 日本農芸化学会大会講演要旨集(Web), 2016, 2C004 (WEB ONLY), 05 Mar. 2016
  Japanese
• 抗ウイルス感染症研究のフロンティア ウイルス侵入過程の重要性 モルビリウイルス属の細胞侵入機構の構造基盤と阻害剤開発
  前仲 勝実, 日本薬学会年会要旨集, 136年会, 1, 221, 221, Mar. 2016
  (公社)日本薬学会, Japanese
• ガレクチン‐3阻害剤の創薬研究
  渡邊友章; 大形悠梨子; 阿部祐希; 手塚洋平; 前田直良; 前仲勝実; 堺谷政弘, 日本薬学会年会要旨集(CD-ROM), 136th, 2, ROMBUNNO.29T‐PM10S, 127, Mar. 2016
  (公社)日本薬学会, Japanese
• 小胞体ストレスタンパク質を標的とした抗癌剤スクリーニング
  野村尚生; 鈴木華央; 松丸尊紀; 奥村正樹; 稲葉謙次; 田村保明; 前仲勝実, 日本薬学会年会要旨集(CD-ROM), 136th, 2, ROMBUNNO.28S‐PM06, 66, Mar. 2016
  (公社)日本薬学会, Japanese
• 単純ヘルペスウイルス感染阻害活性を示す糖ペプチドの合成研究
  柿田浩輔; 古川敦; 穴田仁洋; 南部寿則; 前仲勝実; 松永茂樹; 橋本俊一, 日本薬学会年会要旨集(CD-ROM), 136th, 2, ROMBUNNO.28AB‐PM065, 194, Mar. 2016
  (公社)日本薬学会, Japanese
• Development of novel CD1d ligands highly interacting with lipid binding sites
  Inuki Shinsuke; Aiba Toshihiko; Hirata Natsumi; Ichihara Osamu; Yoshidome Daisuke; Kita Shunsuke; Maenaka Katsumi; Fukase Koichi; Fujimoto Yukari, Symposium on the Chemistry of Natural Products, symposium papers, 58, Oral28, 2016
  The MHC class I-like molecule CD1d is a nonpolymorphic antigen-presenting glycoprotein, the ligands of which include glycolipids, such as a-GalCer (KRN7000). These ligands bind to the hydrophobic groove of CD1d (A’ pocket or F’ pocket), and then activate natural killer (NK) T cells by means of T cell receptor (TCR) recognition, leading to the secretion of various cytokines. We focused on a few polar residues in the A’ pocket of CD1d, a large hydrophobic lipid binding groove, and designed CD1d ligands that can interact with the hydrophilic residues through hydrogen bonds. A simple modification from a methylene to a polar functional group, an amide, in the long fatty acyl chain of a-GalCer significantly enhanced the CD1d recognition of glycolipid ligands. The WaterMap analysis predicted that the presence of amide groups significantly improved the hydration state of the hydrophilic region consisting of Gln14 and Ser28. Furthermore, Molecular dynamics (MD) simulations indicated that Gln14 and Ser28 can interact with the amide group through direct and water-bridged hydrogen bond. Taken together, we demonstrated that confined polar residues in the large hydrophobic area of the lipid binding pockets of mCD1d could be targeted to significantly influence the affinity between the protein and its ligands. These effects provide guidelines for ligand design in the context of lipid binding proteins., Symposium on the Chemistry of Natural Products Steering Committee, Japanese
• モルビリウイルス属の細胞侵入機構の構造基盤と阻害剤開発
  前仲勝実, 日本薬学会年会要旨集(CD-ROM), 136th, ROMBUNNO.S40‐4, 2016
  Japanese
• 麻疹ウイルスHタンパクの5つの主要な抗原エピトープ
  竹田誠; 田原舞乃; 前仲勝実, 日本小児感染症学会総会・学術集会プログラム・抄録集, 48th, 316, 2016
  Japanese
• ヘパラン硫酸を介した狂犬病ウイルスの細胞吸着機構の解析
  佐々木道仁; アニンディタ パウリナ; 伊藤直人; 杉山誠; 福原秀雄; 尾瀬農之; 前仲勝実; 大場靖子; 澤洋文; 澤洋文, 日本分子生物学会年会プログラム・要旨集(Web), 39th, ROMBUNNO.2P‐0314 (WEB ONLY), 2016
  Japanese
• HLA‐Cw12拘束性HIV‐1由来ペプチドの探索
  山下諒也; 黒木喜美子; 渡邊洋介; 小柳円; 滝口雅文; 前仲勝実, 日本分子生物学会年会プログラム・要旨集(Web), 39th, ROMBUNNO.1P‐0042 (WEB ONLY), 2016
  Japanese
• 狂犬病ウイルスGタンパク質特異的抗体の中和機構の解明
  有坂知朗; 荒牧峻彦; 青木亨丞; 伊藤直人; 杉山誠; 尾瀬農之; 福原秀雄; 前仲勝実, 日本分子生物学会年会プログラム・要旨集(Web), 39th, ROMBUNNO.1P‐0598 (WEB ONLY), 2016
  Japanese
• 糖鎖を作る・読む・壊す分子システム ヒト免疫系受容体PILRの糖ペプチド認識機構
  前仲 勝実, 日本生化学会大会・日本分子生物学会年会合同大会講演要旨集, 88回・38回, [1S2, 5], Dec. 2015
  (公社)日本生化学会, English
• PEG化タンパク質の精製に向けた新規PEG化試薬の設計
  山田 千聖; Wawro Adam; 黒木 喜美子; 高橋 愛実; 村岡 貴博; 金原 数; 前仲 勝実, 日本生化学会大会・日本分子生物学会年会合同大会講演要旨集, 88回・38回, [2P0459], [2P0459], Dec. 2015
  (公社)日本生化学会, English
• 構造分子生物学・生化学の進展 糖脂質認識C型レクチン受容体Mincleの構造解析と新規アジュバント探索
  古川 敦; 上敷領 淳; 須知 裕介; 池野 里紗; 松丸 尊紀; 児玉 耕太; 尾瀬 農之; 山崎 晶; 前仲 勝実, 日本生化学会大会・日本分子生物学会年会合同大会講演要旨集, 88回・38回, [3W7, 6], Dec. 2015
  (公社)日本生化学会, English
• (プロ)レニン受容体の調製と機能評価系の構築
  石山夢美; 喜多俊介; 田所高志; 笠井宣征; 北辻千展; KRAYUKHINA Elena; KRAYUKHINA Elena; 内山進; 神田敦宏; 石田晋; 黒木喜美子; 前仲勝実, 日本生化学会大会(Web), 88回・38回, [2P1235], [2P1235], Dec. 2015
  (公社)日本生化学会, Japanese
• Lectin‐like transcript1(LLT1)C型レクチン様ドメインの結晶構造解析
  喜多俊介; 田所高志; 松原永季; 笠井宣征; 玉置貴晴; 岡部由紀; 日下裕規; 石山夢美; 福原秀雄; 上敷領淳; KRAYUKHINA Elena; KRAYUKHINA Elena; 内山進; 尾瀬農之; 黒木喜美子; 前仲勝実, 日本生化学会大会(Web), 88回・38回, [3T17p, 02(3P0328)], Dec. 2015
  (公社)日本生化学会, Japanese
• カイコバキュロウイルスを用いた新規Bacmamの開発
  今井徳俊; 田所高志; 堀内正隆; 福原秀雄; 前仲勝実, 日本生化学会大会(Web), 88th, 3P0912 (WEB ONLY), [3P0912], Dec. 2015
  (公社)日本生化学会, Japanese
• Crystal structure of human CD1d-β2m produced by silkworm-baculovirus expression system
  Kita S; Kusaka H; Yoshida K; Kasai Y; Niiyama M; Hanashima S; Sugiyama S; Murata M; Kuroki K; Maenaka K, CD1-MR1-2015, Nov. 2015
  English, Summary international conference
• THE IMMUNOSUPPRESSIVE EFFECT OF HLA-G2/G6 HOMODIMER IN COLLAGEN-INDUCED ARTHRITIS MICE
  Ami Takahashi; Kimiko Kuroki; Katsumi Maenaka, TISSUE ANTIGENS, 86, 2, 78, 78, Aug. 2015
  English, Summary international conference
• MECHANISMS REPROGRAMMING B CELLS BY HLA-G AND THEIR SIGNATURE IN KIDNEY TRANSPLANT PATIENTS
  Maureen Ezeakile; Vera Portik-Dobos; Daniel D. Horuzsko; Rajan Kapoor; Katsumi Maenaka; Carlos F. Zayas; Laura L. Mulloy; Anatolij Horuzsko, TISSUE ANTIGENS, 86, 2, 90, 91, Aug. 2015
  English, Summary international conference
• 構造生物学が推進する医薬基盤とその応用 抑制型免疫受容体PILRαによるヘルペスウイルス1型由来O型糖鎖およびペプチド配列の同時認識と創薬
  尾瀬農之; 古川敦; 黒木喜美子; 前仲勝実, 医学のあゆみ, 254, 8, 559, 565, Aug. 2015
  医歯薬出版(株), Japanese
• 単純ヘルペスウイルス感染阻害活性を有する糖ペプチドの設計と合成
  柿田浩輔; 羽鳥菜々生; 古川敦; 山田友樹; 穴田仁洋; 南部寿則; 前仲勝実; 橋本俊一, 日本糖質学会年会要旨集, 34th, 252, 01 Jul. 2015
  Japanese
• 可溶性HLA‐G分子の効率的生産に向けてのアプローチ
  可野巧; 田所高志; 市川聡; 松田彰; 黒木喜美子; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 15th, 115, 26 May 2015
  Japanese
• ポリエーテル化合物生合成酵素の結晶構造解析
  尾瀬農之; 笈川あずさ; 野間井智; 澤田光平; 道仙卓也; 南篤志; 及川英秋; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 15th, 67, 26 May 2015
  Japanese
• マウス由来TMPRSS2の相互作用解析に向けたタンパク質発現系の構築
  宮本優介; 福原秀雄; 竹田誠; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 15th, 115, 26 May 2015
  Japanese
• 毒ヘビがもつ自己の毒に対する内在性阻害タンパク質Small Serum Proteinの機能と構造解析
  塩井(青木; 成留実; 塩井誠次郎; 田所高志; 黒木喜美子; 前仲勝実; 寺田成之, 日本蛋白質科学会年会プログラム・要旨集, 15th, 78, 26 May 2015
  Japanese
• ヒト免疫受容体NKRP1AによるリガンドLLT1の分子認識機構の解明
  田所高志; 喜多俊介; 松原永季; 笠井宣征; 玉置貴晴; 岡部由紀; 日下裕規; 石山夢美; 福原秀雄; 上敷領淳; 尾瀬豊之; 黒木喜美子; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 15th, 145, 26 May 2015
  Japanese
• カイコバキュロウイルス発現系を用いた麻疹ウイルスHタンパク質およびヒト免疫受容体SLAMの調製と相互作用解析
  今井徳俊; 田所高志; 吉田康貴; 喜多俊介; 黒木喜美子; 橋口隆生; 柳雄介; 竹田誠; 福原秀雄; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 15th, 114, 26 May 2015
  Japanese
• 単純ヘルペスウイルス侵入阻害糖ペプチドの最適化を目指した熱力学的相互作用解析およびX線結晶構造解析
  山田友樹; 古川敦; 柿田浩輔; 坂本二郎; 前田直良; 逢坂文那; 斉藤貴士; 黒木喜美子; 荒瀬尚; 穴田仁洋; 尾瀬農之; 橋本俊一; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 15th, 90, 26 May 2015
  Japanese
• 脂質抗原提示分子CD1dの結晶構造解析
  日下裕規; 喜多俊介; 吉田康貴; 笠井宜征; 新山真由美; 杉山成; 村田道雄; 黒木喜美子; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 15th, 89, 26 May 2015
  Japanese
• JAK‐STAT経路を阻害するウイルスタンパク質の機能・構造解析
  永野悠馬; 野間井智; 前仲勝実; 柳雄介; 尾瀬農之, 日本蛋白質科学会年会プログラム・要旨集, 15th, 88, 26 May 2015
  Japanese
• カイコ幼虫を用いた活性型PKBの発現と精製
  前崎綾子; 佐藤亮介; 田岡万悟; 金場哲平; 朝野維起; 藤田千春; 藤原俊伸; 伊藤隆; 礒辺俊明; 箱嶋敏雄; 前仲勝実; 三島正規, 日本蛋白質科学会年会プログラム・要旨集, 15th, 123, 26 May 2015
  Japanese
• アンジオポエチン様因子Angptl2の発現系構築と免疫受容体LILRB2との相互作用解析
  荒牧峻彦; 黒木喜美子; 門松毅; 寺田和豊; 尾池雄一; 尾瀬農之; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 15th, 138, 26 May 2015
  Japanese
• ハーセプチン抗体Fv断片の相互作用解析および熱安定性解析
  中村光太; 田所高志; 前田龍; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 15th, 114, 26 May 2015
  Japanese
• 脂質活性構造研究の最前線 免疫系受容体MincleとMCLの糖脂質認識の分子基盤
  前仲 勝実, 日本薬学会年会要旨集, 135年会, 1, 93, 93, Mar. 2015
  (公社)日本薬学会, Japanese
• 動き出した創薬オープンイノベーションネットワーク 北海道大学スクリーニング拠点の現状と展望
  前仲 勝実, 日本薬学会年会要旨集, 135年会, 1, 155, 155, Mar. 2015
  (公社)日本薬学会, Japanese
• 単純ヘルペスウイルスがペア型レセプターPILRαを利用するメカニズム
  尾瀬農之; 黒木喜美子; 山口宗親; 田畑栄一; 真板宣夫; 梶川瑞穂; 中村聖子; WANG Jing; 佐藤毅史; 荒瀬尚; 前仲勝実, 物構研サイエンスフェスタ要旨集, 3rd, 79, 2015
  Japanese
• ゲノム網羅的解析によるB型肝炎ウイルス感染の病態関連遺伝子の同定と新規診断法の開発 HLA等機能解析
  前仲勝実, ゲノム網羅的解析によるB型肝炎ウイルス感染の病態関連遺伝子の同定と新規診断法の開発に関する研究 平成26年度 委託業務成果報告書, 59, 60, 2015
  Japanese
• 北海道大学スクリーニング拠点の現状と展望
  前仲勝実, 日本薬学会年会要旨集(CD-ROM), 135th, ROMBUNNO.S20-2, 2015
  Japanese
• 免疫系受容体MincleとMCLの糖脂質認識の分子基盤
  前仲勝実, 日本薬学会年会要旨集(CD-ROM), 135th, ROMBUNNO.S02-3, 2015
  Japanese
• 高収率な一本鎖抗体のデザインに向けた検討
  山下駿; 山上紗矢佳; 逢坂文那; 齊藤貴士; 片岡千和; 澤田石一之; 前仲勝実; 小橋川敬博; 森岡弘志, 日本薬学会九州支部大会講演要旨集, 31st, 90, 21 Nov. 2014
  Japanese
• クロマチンリモデリング関連因子間の相互作用解析
  谷口岳史; 辻美保子; 森田和美; 阿川大貴; 諏訪喜昭; 小橋川敬博; 池鯉鮒麻美; 中村照也; 逢坂文那; 齊藤貴士; 前仲勝実; 菅野新一郎; 安井明; 山縣ゆり子; 森岡弘志, 日本薬学会九州支部大会講演要旨集, 31st, 43, 21 Nov. 2014
  Japanese
• 麻疹ウイルスHタンパク質を標的とした侵入阻害剤の開発
  東端将哲; 福原秀雄; 逢坂文那; 橋口隆生; 柳雄介; 竹田誠; 児玉耕太; 齊藤貴士; 前仲勝実, 日本ウイルス学会学術集会プログラム・抄録集, 62nd, 204, 31 Oct. 2014
  Japanese
• 犬ジステンパーウイルスエンベロープタンパク質HおよびFの相互作用解析と電子顕微鏡による構造解析
  依田芽生; 福原秀雄; 武田森; 三尾和弘; PLATTET Philippe; 竹田誠; 前仲勝実, 日本ウイルス学会学術集会プログラム・抄録集, 62nd, 218, 31 Oct. 2014
  Japanese
• ムンプスウイルス感染におけるHeat Shock Protein70の役割
  加藤大志; 喜多俊介; 久保田耐; 中津祐一郎; 前仲勝実; 木所稔; 竹田誠, 日本ウイルス学会学術集会プログラム・抄録集, 62nd, 220, 31 Oct. 2014
  Japanese
• イヌジステンパーウイルスH蛋白質におけるP541S変異が受容体SLAMとの相互作用に及ぼす影響
  吉田康貴; 酒井宏治; 喜多俊介; 福原秀雄; 柳雄介; 竹田誠; 前仲勝実, 日本ウイルス学会学術集会プログラム・抄録集, 62nd, 219, 31 Oct. 2014
  Japanese
• 単純ヘルペスウイルス1型感染阻害物質の探索
  前田直良; 古川敦; 坂本二郎; 黒木喜美子; 尾瀬農之; 柿田浩輔; 穴田仁洋; 橋本俊一; 有井潤; 加藤哲久; 川口寧; 荒瀬尚; 前仲勝実, 日本ウイルス学会学術集会プログラム・抄録集, 62nd, 273, 31 Oct. 2014
  Japanese
• II型膜貫通型セリンプロテアーゼTMPRSS2は,HA開裂部位にmono‐basicなアミノ酸配列をもつA型インフルエンザウイルスに対する肺内必須活性化酵素である
  酒井宏治; 網康至; 田原舞乃; 久保田耐; 安楽正輝; 中島典子; 高下恵美; 関塚剛史; 駒瀬勝啓; 信澤枝里; 小田切孝人; 前仲勝実; 黒田誠; 長谷川秀樹; 河岡義裕; 田代眞人; 竹田誠, 日本ウイルス学会学術集会プログラム・抄録集, 62nd, 155, 31 Oct. 2014
  Japanese
• 構造細胞生物学の展開 医薬イノベーションの起爆剤としての構造 糖脂質・糖ペプチドを認識する免疫系受容体の構造生物学的研究
  前仲 勝実, 日本生化学会大会プログラム・講演要旨集, 87回, [2S06p, 4], Oct. 2014
  (公社)日本生化学会, Japanese
• マラリア原虫におけるアピコプラストTic22とトランジット配列の複合体形成
  逢坂文那; 山田友樹; 松丸尊紀; 前仲勝実; 齊藤貴士, 日本生化学会大会(Web), 87th, 4P-234 (WEB ONLY), 234], Oct. 2014
  (公社)日本生化学会, Japanese
• Molecular basis for HLA class I assodations with autoimmune diseases
  前仲勝実; 黒木喜美子, 日本脊椎関節炎学会誌, 6, 1, 33, 38, Oct. 2014
  ヒト白血球抗原(HLA)-B27は、多集団において、リウマチ性疾患の一つである強直性脊椎炎(AS)患者のほぼ90%が陽性であること、HLA-B27遺伝子導入ラット・マウスがAS様症状を示すことから、AS病因遺伝子として強く示唆されてきた。HLA-B27ホモ二量体と類似したホモ二量体を形成するHLA-Gの分子形態とも比較しながら、その分子構造基盤につき考察し、AS発症の機序について述べた。, 日本脊椎関節炎学会, Japanese
• 自己免疫疾患に関わるHLAクラスI分子による免疫制御の分子基盤
  前仲 勝実; 黒木 喜美子, 日本脊椎関節炎学会誌, 6, 1, 33, 38, Oct. 2014
  ヒト白血球抗原(HLA)-B27は、多集団において、リウマチ性疾患の一つである強直性脊椎炎(AS)患者のほぼ90%が陽性であること、HLA-B27遺伝子導入ラット・マウスがAS様症状を示すことから、AS病因遺伝子として強く示唆されてきた。HLA-B27ホモ二量体と類似したホモ二量体を形成するHLA-Gの分子形態とも比較しながら、その分子構造基盤につき考察し、AS発症の機序について述べた。, 日本脊椎関節炎学会, Japanese
• Application of the silkworm expression system for the structural biology: a case study of human CD1d-β2m
  Kita S; Kusaka H; Yoshida K; Kasai Y; Niiyama M; Sugiyama S; Murata M; Kuroki K; Maenaka K, ICCBM15, Sep. 2014
  English, Summary international conference
• 抗ヘルペスウイルス活性をもつシアル酸含有糖ペプチドおよび類縁体の合成
  柿田浩輔; 羽鳥菜々生; 坂本二郎; 古川敦; 穴田仁洋; 南部寿則; 前仲勝実; 橋本俊一, 日本糖質学会年会要旨集, 33rd, 140, 23 Jul. 2014
  Japanese
• Structural Analysis for the Interaction of sialic T antigen glycopeptide of HSV-1 with Entry Receptor PILR alpha
  Takao Nomura; Jiro Sakamoto; Fumina Oosaka; Kosuke Kakita; Atsushi Furukawa; Masahiro Anada; Shunichi Hashimoto; Kimiko Kuroki; Toyoyuki Ose; Hisashi Arase; Takashi Saitoh; Katsumi Maenaka, PROTEIN SCIENCE, 23, 230, 230, Jul. 2014
  English, Summary international conference
• 熱力学的解析から見えてきた一本鎖抗体の効率的生産へ向けてのアプローチ
  山下駿; 山上紗矢佳; 逢坂文那; 斉藤貴士; 片岡千和; 澤田石一之; 前仲勝実; 小橋川敬博; 森岡弘志, 日本蛋白質科学会年会プログラム・要旨集, 14th, 112, 26 May 2014
  Japanese
• 表面蛋白質の発現ストラテジー
  前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 14th, 39, 26 May 2014
  Japanese
• C型レクチン様受容体MincleとMCLの糖脂質認識機構
  古川敦; 上敷領淳; 森大輝; 豊永憲司; 岡部由紀; 藤司亜也; 神田諒; 三宅靖延; 尾瀬農之; 山崎晶; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 14th, 121, 26 May 2014
  Japanese
• 「構造生物学と免疫」MHCクラスI受容体の構造生物学
  黒木喜美子; 前仲勝実, JSI Newsl, 22, 2, 22, 09 Apr. 2014
  Japanese
• 創薬研究の基盤となる相互作用解析 一本鎖抗体の実用化に向けた構造機能解析
  森岡 弘志; 小橋川 敬博; 諏訪 喜昭; 山下 駿; 山本 珠実; 福田 夏希; 二階堂 里那; 中原 悠介; 龍野 友花; 斉藤 貴士; 逢坂 文那; 手塚 洋平; 前仲 勝実; 澤田石 一之; 片岡 千和, 日本薬学会年会要旨集, 134年会, 1, 242, 242, Mar. 2014
  (公社)日本薬学会, Japanese
• 含リン脱離基法を機軸とする抗ヘルペスウイルス活性をもつ糖ペプチドの立体選択的合成
  柿田浩輔; 羽鳥菜々生; 穴田仁洋; 南部寿則; 前仲勝実; 橋本俊一, 日本薬学会年会要旨集(CD-ROM), 134th, 2, ROMBUNNO.29PMS-079, 247, Mar. 2014
  (公社)日本薬学会, Japanese
• アカデミア創薬実現に必要な10の視点 5.合理的創薬と構造解析
  齊藤貴士; 堺谷政弘; 前仲勝実, 実験医学, 32, 2, 222, 229, 01 Feb. 2014
  Japanese
• 【研究成果を薬につなげるアカデミア創薬の戦略と実例】 (第1章)アカデミア創薬実現に必要な10の視点 合理的創薬と構造解析
  齊藤 貴士; 堺谷 政弘; 前仲 勝実, 実験医学, 32, 2, 222, 229, Feb. 2014
  (株)羊土社, Japanese
• 一本鎖抗体の実用化に向けた構造機能解析
  森岡弘志; 小橋川敬博; 諏訪喜昭; 山下駿; 山本珠実; 福田夏希; 二階堂里那; 中原悠介; 龍野友花; 斉藤貴士; 逢坂文那; 手塚洋平; 前仲勝実; 澤田石一之; 片岡千和, 日本薬学会年会要旨集(CD-ROM), 134th, ROMBUNNO.S50-5, 2014
  Japanese
• 単純ヘルペスウイルスがペア型レセプターPILRαを利用する分子基盤
  尾瀬農之; 黒木喜美子; 山口宗親; 田畑栄一; 真板宣夫; 梶川瑞穂; 中村聖子; WANG Jing; 佐藤毅史; 荒瀬尚; 前仲勝実, 日本結晶学会年会講演要旨集, 2014, 110, 2014
  Japanese
• 糖脂質・糖ペプチドを認識する免疫系受容体の構造生物学的研究
  前仲勝実, 日本生化学会大会(Web), 87th, 2S06P-4 (WEB ONLY), 2014
  Japanese
• NMRによるヒトCD160細胞外ドメインの立体構造解析
  阿部千紘; 黒木喜美子; 小島理恵子; 齊藤貴士; 前仲勝実, 日本分子生物学会年会プログラム・要旨集(Web), 37th, 1P-0723 (WEB ONLY), 2014
  Japanese
• 一本鎖抗体の高収率化クローンの溶液挙動および耐熱性の解析
  山下駿; 山上紗矢佳; 逢坂文那; 齊藤貴士; 片岡千和; 澤田石一之; 前仲勝実; 小橋川敬博; 森岡弘志, 日本分子生物学会年会プログラム・要旨集(Web), 37th, 1P-0936 (WEB ONLY), 2014
  Japanese
• クロマチンリモデリング複合体形成の構造生物学的研究
  谷口岳史; 辻美保子; 森田和美; 阿川大貴; 諏訪喜昭; 小橋川敬博; 池鯉鮒麻美; 中村照也; 逢坂文那; 齊藤貴士; 前仲勝実; 菅野新一郎; 安井明; 山縣ゆり子; 森岡弘志, 日本分子生物学会年会プログラム・要旨集(Web), 37th, 3P-0138 (WEB ONLY), 2014
  Japanese
• HEK293細胞を用いたHLA‐Cw12拘束性HIV‐1由来免疫制御ペプチドの探索
  渡邊洋介; 黒木喜美子; 小柳円; 滝口雅文; 前仲勝実, 日本分子生物学会年会プログラム・要旨集(Web), 37th, 1P-0721 (WEB ONLY), 2014
  Japanese
• 合理的HIVワクチン設計のためのgp120エピトープ探索系の確立に向けて
  阪田竜馬; 黒木喜美子; 前仲勝実, 日本分子生物学会年会プログラム・要旨集(Web), 37th, 1P-0722 (WEB ONLY), 2014
  Japanese
• 2SBP-02 Structural basis for glycolipid recognition mechanism by C-type lectin like receptor, Mincle(New Development of Structural Cell Biology in Signal Transduction,Symposium,The 52th Annual Meeting of the Biophysical Society of Japan(BSJ2014))
  Furukawa Atsushi; Kamishikiryo Jun; Ose Toyoyuki; Yamasaki Sho; Maenaka Katsumi, Seibutsu Butsuri, 54, 1, S131, 2014
  一般社団法人 日本生物物理学会, English
• Activity of Regional Branch
  前仲 勝実; 寺本 央, Seibutsu Butsuri, 53, 6, 334, 335, 25 Nov. 2013
  The Biophysical Society of Japan General Incorporated Association, Japanese
• マウスリゾチームにおける部位特異的なアスパラギン残基のラセミ化機構の解析
  藤田玲奈; 斎藤貴士; 前仲勝実; 林いづみ; 白石充典; 阿部義人; 植田正, 日本薬学会九州支部大会講演要旨集, 30th, 159, 20 Nov. 2013
  Japanese
• ウイルスの膜融合に関与するTMPRSS2タンパク質の調製と結晶化
  佐藤亮; 福原秀雄; 竹田誠; 前仲勝実, 日本ウイルス学会学術集会プログラム・抄録集, 61st, 419, 29 Oct. 2013
  Japanese
• 単純ヘルペスウイルス1型(HSV‐1)のglycoprotein B(gB)とmyelin associated glycoprotein(MAG)との相互作用解明
  青木亨丞; 福原秀雄; 黒木喜美子; 武田森; 末永忠広; 荒瀬尚; 前仲勝実, 日本ウイルス学会学術集会プログラム・抄録集, 61st, 329, 29 Oct. 2013
  Japanese
• 受容体結合領域を含む複数の主要エピトープを変化させた麻疹ウイルスの解析
  田原舞乃; 酒井宏治; 駒瀬勝啓; 前仲勝実; 竹田誠, 日本ウイルス学会学術集会プログラム・抄録集, 61st, 225, 29 Oct. 2013
  Japanese
• Nectin4を介するモルビリウイルスの細胞侵入機構の解明
  陳甦ルイ; 福原秀雄; 伊藤由梨; 酒匂幸; 橋口隆生; 梶川瑞穂; 柳雄介; 竹田誠; 前仲勝実, 日本ウイルス学会学術集会プログラム・抄録集, 61st, 315, 29 Oct. 2013
  Japanese
• 1回膜貫通型 受容体の遺伝子:KIR,LILR,PILR 免疫系細胞表面のペア型受容体
  黒木喜美子; 前仲勝実, 生体の科学, 64, 5, 490, 491, 15 Oct. 2013
  株式会社医学書院, Japanese
• monensin生合成酵素の結晶構造解析
  道仙卓也; 南篤志; 笈川あずさ; 佐藤恭平; 前仲勝実; 及川英秋; 尾瀬農之, 日本結晶学会年会講演要旨集, 2013, 75, 12 Oct. 2013
  Japanese
• 【細胞表面受容体】 構造的特徴:1回膜貫通型 受容体の遺伝子:KIR,LILR,PILR 免疫系細胞表面のペア型受容体
  黒木 喜美子; 前仲 勝実, 生体の科学, 64, 5, 490, 491, Oct. 2013
  (公財)金原一郎記念医学医療振興財団, Japanese
• Nectin4は上皮に局在する犬ジステンパーウイルス特異的受容体である
  PRATAKPIRIYA Watanyoo; 關文緒; 大槻紀之; 酒井宏治; 福原秀雄; 片本宏; 平井卓哉; TECHANGAMSUWAN Somporn; LAN Nguyen; 前仲勝実; 竹田誠; 山口良二, 日本獣医学会学術集会講演要旨集, 156th, 215, 215, 30 Aug. 2013
  (公社)日本獣医学会, Japanese
• MurDの大量発現系の構築と結晶化
  笈川あずさ; 北辻千展; 尾瀬農之; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 13th, 123, 31 May 2013
  Japanese
• C型レクチン様受容体Mindeの糖脂質認識機構
  古川敦; 上敷領淳; 岡部由紀; 神田涼; 豊永憲司; 森大輝; 三宅靖延; 山崎晶; 尾瀬農之; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 13th, 115, 31 May 2013
  Japanese
• モネンシン生合成酵素の結晶構造解析
  尾瀬農之; 笈川あずさ; 南篤志; 佐藤恭平; 及川英秋; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 13th, 122, 31 May 2013
  Japanese
• 樹状細胞免疫受容体DCIRの発現・精製およびX線結晶構造解析
  福原秀雄; 松原永季; 神田諒; 矢部力朗; 海部知則; 尾瀬農之; 岩倉洋一郎; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 13th, 119, 31 May 2013
  Japanese
• バキュロウイルス‐カイコ発現系を用いて産生したヒトチロシナーゼの性質
  梅田彩奈; 佐藤正幸; 忠平和子; 日下部宜宏; PARK Enock Y; 前仲勝実; 蜷木理; 殿塚隆史; 西河淳, 日本農芸化学会大会講演要旨集(Web), 2013, 2C16A15 (WEB ONLY), 05 Mar. 2013
  Japanese
• パラミクソウイルス侵入機構と阻害剤開発
  東端将哲; 福原秀雄; 齊藤貴士; 陳甦ぜい; 逢坂文那; 児玉耕太; 尾瀬農之; 前仲勝実, 日本薬学会年会要旨集(CD-ROM), 133年会, 1, 100, 100, Mar. 2013
  (公社)日本薬学会, Japanese
• 創薬を指向した構造生物学の最前線 パラミクソウイルス侵入機構と阻害剤開発
  東端 将哲; 福原 秀雄; 齊藤 貴士; 陳 甦へい; 逢坂 文那; 児玉 耕太; 尾瀬 農之; 前仲 勝実, 日本薬学会年会要旨集, 133年会, 1, 100, 100, Mar. 2013
  (公社)日本薬学会, Japanese
• 細胞外マトリックス分子/ケモカインを標的とした成人T細胞白血病制御法の開発
  前田直良; 上出利光; 服部俊夫; 前仲勝実; 大橋貴, 金沢大学がん進展制御研究所がんの転移・薬剤耐性に関わる先導的研究拠点, 2012, 183, 185, 2013
  Japanese
• 重症呼吸器ウイルス感染症のサーベイランス・病態解明及び制御に関する研究 呼吸器感染ヒトパラミクソウイルス全般の病態解明・制御に関する研究 呼吸器感染症ウイルス増殖におけるTMPRSS2の役割ならびに膜融合タンパクP3位保存グルタミンの重要性について
  竹田誠; 安部昌子; 田原舞乃; 酒井宏治; 白戸憲也; 松山州徳; 加納和彦; 野田雅博; 木村博一; 網康至; 加藤篤; 水田克巳; 前仲勝実; 福原秀雄; 江角眞理子, 重症呼吸器ウイルス感染症のサーベイランス・病態解明及び制御に関する研究 平成24年度 総括・分担研究報告書, 139, 148, 2013
  Japanese
• 新型インフルエンザ等新興・再興感染症研究事業 早期麻疹排除及び排除状態の維持に関する研究 麻疹ウイルスの抗原エピトープの構造解析と効果的なワクチン維持のための研究
  前仲勝実, 早期麻疹排除及び排除状態の維持に関する研究 平成22-24年度 総合研究報告書 平成24年度 総括・分担研究報告書, 173, 176, 2013
  Japanese
• 免疫系受容体LILRファミリーの構造と創薬への試み
  前仲勝実, 千里ライフサイエンスセミナー講演要旨集, 2013, 16, 17, 2013
  Japanese
• HIV由来ペプチドライブラリーを用いたHLA‐Cw12拘束性免疫制御ペプチドの同定
  渡邊洋介; 黒木喜美子; 小柳円; 滝口雅文; 前仲勝実, 日本分子生物学会年会プログラム・要旨集(Web), 36th, 3P-0758 (WEB ONLY), 2013
  Japanese
• 結晶構造解析に向けた,乳がん特異的キナーゼBrkとアダプタータンパク質STAP‐2の機能解析
  神田諒; 関根勇一; 前仲勝実; 松田正; 尾瀬農之, 日本分子生物学会年会プログラム・要旨集(Web), 36th, 2P-0302 (WEB ONLY), 2013
  Japanese
• Entry mechanism of morbillivirus family
  Hideo Fukuhara; Surui Chen; Shin Takeda; Katsumi Maenaka, Yakugaku Zasshi, 133, 5, 549, 559, 2013
  The Pharmaceutical Society of Japan, Japanese, Book review
• Structural biology for drug development
  Katsumi Maenaka; Koichi Kato, Yakugaku Zasshi, 133, 5, 507, 507, 2013
  公益社団法人 日本薬学会, Japanese
• Entry mechanism of morbillivirus family
  Hideo Fukuhara; Surui Chen; Shin Takeda; Katsumi Maenaka, Yakugaku Zasshi, 133, 5, 549, 559, 2013
  (公社)日本薬学会, Japanese, Book review
• カニクイザルで致死的感染症を起こしたジステンパーウイルスのサルレセプターの効率的な利用:ジステンパーウイルスはヒトへの脅威となり得るのか?
  酒井宏治; 關文緒; 網康至; 田原舞乃; 中津祐一郎; 大槻紀之; 福原秀雄; 福士秀悦; 吉河智城; 西條政幸; 森川茂; 前仲勝実; 山口良二; 駒瀬勝啓; 竹田誠, 日本ウイルス学会学術集会プログラム・抄録集, 60th, 282, 31 Oct. 2012
  Japanese
• 野外イヌジステンパーウイルスはヒトNectin4を受容体として利用できる
  大槻紀之; 関塚剛史; 關文緒; 酒井宏治; 久保田耐; 福原秀雄; 前仲勝実; 山口良二; 黒田誠; 竹田誠, 日本ウイルス学会学術集会プログラム・抄録集, 60th, 381, 31 Oct. 2012
  Japanese
• 麻疹ウイルス単一血溝型決定の分子基盤
  田原舞乃; BRINDLEY Melinda A; 福原秀雄; 酒井宏治; 大野真治; 駒瀬勝啓; ROTA Paul A; PLEMPER Richard K; 前仲勝実; 竹田誠, 日本ウイルス学会学術集会プログラム・抄録集, 60th, 282, 31 Oct. 2012
  Japanese
• イヌジステンパーウイルスの上皮および中枢神経感染におけるイヌNectin4の利用
  關文緒; PRATAKPIRIYA Watanyoo; 大槻紀之; 酒井宏治; 福原秀雄; 前仲勝実; 山口良二; 竹田誠, 日本ウイルス学会学術集会プログラム・抄録集, 60th, 381, 31 Oct. 2012
  Japanese
• オステオポンチン-インテグリン相互作用を分子標的とした成人T細胞白血病に対する抗体免疫療法(Osteopontin-integrin interaction as a molecular target for antibody-mediated immunotherapy in adult T-cell leukemia)
  前田 直良; 大橋 貴; 浩 日勒; 服部 俊夫; 高橋 弥生; 張替 秀郎; 長谷川 寛雄; 藤井 雅寛; 前仲 勝実; 上出 利光, 日本癌学会総会記事, 71回, 117, 117, Aug. 2012
  日本癌学会, English
• Structural Biologyとがん治療創薬 ヒトKiller cell Ig-like receptor群のNK細胞アロ反応性の構造基盤(Structural biology and cancer therapy Structural basis for natural killer cell alloreactivity of human killer cell Ig-like receptors)
  前仲 勝実, 日本癌学会総会記事, 71回, 227, 228, Aug. 2012
  日本癌学会, English
• HIV由来変異ペプチドによる宿主免疫の二重逃避機構
  黒木喜美子; 前仲勝実, 月刊臨床免疫・アレルギー科, 58, 2, 210, 216, Aug. 2012
  科学評論社, Japanese
• 麻疹ウイルス及び犬ジステンパーウイルスH蛋白質の構造学的研究
  尾瀬農之; 橋口隆生; 酒匂幸; 伊藤由梨; 福原秀雄; 黒木喜美子; 柳雄介; 竹田誠; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 12th, 83, 31 May 2012
  Japanese
• 機能および構造解析に向けた細胞表面蛋白質の調製法
  福原秀雄; 橋口隆生; 黒木喜美子; 尾瀬農之; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 12th, 19, 31 May 2012
  Japanese
• ヤツメウナギ由来可変性リンパ球受容体VLRCの結晶構造
  神田諒; 須藤洋一; 笠松純; 笠原正典; 前仲勝実; 尾瀬農之, 日本蛋白質科学会年会プログラム・要旨集, 12th, 117, 31 May 2012
  Japanese
• 【抗ウイルス薬-最新の動向-】 麻疹ウイルスと受容体との複合体の立体構造と今後の展望
  前仲 勝実; 橋口 隆生; 柳 雄介, 日本臨床, 70, 4, 695, 703, Apr. 2012
  (株)日本臨床社, Japanese
• 麻疹ウイルスと受容体との複合体の立体構造と今後の展望 (特集 抗ウイルス薬) -- (新規抗ウイルス薬の開発動向と展望)
  前仲 勝実; 橋口 隆生; 柳 雄介, 日本臨床, 70, 4, 695, 703, Apr. 2012
  日本臨床社, Japanese
• 抗ウイルス薬 IV.特論 麻疹ウイルスと受容体との複合体の立体構造と今後の展望
  前仲勝実; 前仲勝実; 橋口隆生; 橋口隆生; 柳雄介, 日本臨床, 70, 4, 695-703, 703, 01 Apr. 2012
  Japanese
• ロバスト設計最適化支援ツールを用いたin silicoスクリーニング
  児玉耕太; 山口政隆; 小川修一; 尾瀬農之; 前仲勝実, 日本薬学会年会要旨集, 132nd, 4, 115, 05 Mar. 2012
  Japanese
• ウイルス感染機構の構造基盤と創薬への展開
  前仲勝実; 前仲勝実, 日本薬学会年会要旨集, 132nd, 1, 99, 05 Mar. 2012
  Japanese
• 創薬に向けた構造生物学 ウイルス感染機構の構造基盤と創薬への展開
  前仲 勝実, 日本薬学会年会要旨集, 132年会, 1, 99, 99, Mar. 2012
  (公社)日本薬学会, Japanese
• オステオポンチン‐インテグリン相互作用を標的とした新規成人T細胞白血病治療法の開発
  前田直良; 大橋貴; CHAGAN‐YASUTAN Haorile; 服部俊夫; 高橋弥生; 張替秀郎; 長谷川寛雄; 藤井雅寛; 前仲勝実; 上出利光, 日本生体防御学会学術総会講演抄録集, 23rd, 66, 2012
  Japanese
• 早期麻疹排除及び排除状態の維持に関する研究 麻疹ウイルスの抗原エピトープの構造解析と効果的なワクチン維持のための研究
  前仲勝実, 早期麻疹排除及び排除状態の維持に関する研究 平成23年度 総括・分担研究報告書, 114, 117, 2012
  Japanese
• 樹状細胞免疫受容体DCIRの結晶化と構造解析
  福原秀雄; 松原永季; 神田諒; 矢部力朗; 海部知則; 上敷領淳; 尾瀬農之; 岩倉洋一郎; 前仲勝実, 日本分子生物学会年会プログラム・要旨集(Web), 35th, 1P-0056 (WEB ONLY), 2012
  Japanese
• ヒト免疫制御受容体LILRB1とリガンドHLA‐Gの複合体の結晶構造解析
  黒木喜美子; 松原永季; 神田諒; 上敷領淳; 尾瀬農之; 福永裕子; 前仲勝実, 日本分子生物学会年会プログラム・要旨集(Web), 35th, 1P-0060 (WEB ONLY), 2012
  Japanese
• 各臓器移植についての拒絶反応の解説・移植の新しい治療法の紹介 第5回 NKレセプターとHLAの最前線
  黒木喜美子; 北辻千展; 前仲勝実, MHC, 18, 3, 215, 233, Dec. 2011
  日本組織適合性学会, Japanese
• 各臓器移植についての拒絶反応の解説・移植の新しい治療法の紹介(第5回) NKレセプターとHLAの最前線
  黒木 喜美子; 北辻 千展; 前仲 勝実, MHC: Major Histocompatibility Complex, 18, 3, 215, 233, Dec. 2011
  ナチュラルキラー(NK)細胞上には多数のNKレセプターが存在し, 自然免疫で中心的な役割を果たすNK細胞の傷害活性を制御している. ヒトNKレセプターは, 構造上免疫グロブリン(Ig)様レセプターに属するkiller cell immunoglobulin(Ig)-like receptor群, leukocyte Ig-like receptor群およびC型レクチン様レセプターに属するNKG2/CD94群に分類され, いずれも活性型と抑制型が存在するペア型レセプターの一員である. 抑制型NKレセプターの多くはMHCクラスIをリガンドとして認識し, 正常な自己細胞に対してNK細胞が傷害しないように制御しているが, 活性型NKレセプターのリガンドについては未だ不明な点も多い. 本稿では特にMHCクラスIをリガンドとするNKレセプターに焦点を当て, その機能, 構造, 疾患との関連について最近の知見を概説する. 「1. はじめに」 NK細胞は末梢血リンパ球の約10〜15%を占め, ウイルス感染など生体防御の最前線において, IL-2, IL-15, IL-18などのサイトカインや細胞表面レセプター群を介するシグナル伝達によって活性化し, 自然免疫において重要な役割を担っている., 日本組織適合性学会, Japanese
• gamma/deltaT細胞とNK細胞 ヒトCD161(NKRP1A/KLRB1)とリガンドLLT1の分子認識機構(Molecular basis for LLT1 recognition by human CD161 (NKRP1A/KLRB1))
  黒木 喜美子; 上敷領 淳; 福原 秀雄; 岡部 由紀; 前仲 勝実, 日本免疫学会総会・学術集会記録, 40, 77, 77, Nov. 2011
  (NPO)日本免疫学会, English
• SrcおよびAuroraキナーゼ2重阻害による滑膜肉腫の相乗的in vivo抗腫瘍効果(Dual inhibition of Src and Aurora kinases abrogates tumor growth, invasion, and angiogenesis of synovial sarcoma in vivo)
  津田 真寿美; 新井 隆太; 渡部 琢哉; 尾瀬 農之; 小布施 力史; 前仲 勝実; 三浪 明男; 大場 雄介, 日本癌学会総会記事, 70回, 274, 274, Sep. 2011
  日本癌学会, English
• 抗ジンセノシドRe小型化抗体の作製及び酵素免疫吸着測定法(ELISA)の開発
  坂元政一; PONGKITWITOON Benyakan; 田中宏幸; 森元聡; 前仲勝実; 柴田攻, コロイドおよび界面化学討論会講演要旨集, 63rd, 512, 22 Aug. 2011
  Japanese
• Leukocyte Immunoglobulin‐Like Receptor(LILR)ファミリーの分子認識
  黒木喜美子; 前仲勝実, 生化学, 83, 8, 715, 726, Aug. 2011
  (公社)日本生化学会, Japanese
• BmNPVバクミドシステムを用いたカイコでの膜タンパク質の発現
  佐々木香織; 梶川瑞穂; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 11th, 152, 27 May 2011
  Japanese
• 表面タンパク質の不安定な複合体の分子解析法
  前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 11th, 34, 27 May 2011
  Japanese
• T細胞機能の誘導と抑制 HVEMとその受容体CD160によるT細胞の制御
  小島理恵子; 前仲勝実, 月刊臨床免疫・アレルギー科, 55, 5, 515, 520, 25 May 2011
  (有)科学評論社, Japanese
• T cell regulation by CD160-HVEM interaction
  小島 理恵子; 前仲 勝実, Clinical immunology & allergology, 55, 5, 515, 520, May 2011
  科学評論社, Japanese
• EPITOPE MAPPING OF A NOVEL B27-SPECIFIC ANTIBODY
  Joanna L. Giles; Kirsty McHugh; Katilin DiGleria; Jackie Shaw; Simon Kollnberger; Katsumi Maenaka; Osiris Marroquin; Christoph Renner; Paul Bowness, RHEUMATOLOGY, 50, 140, 141, Apr. 2011
  English, Summary international conference
• 多様な形態を有するHLA‐G蛋白質とヒト免疫制御受容体との分子認識
  黒木喜美子; 福永裕子; 上敷領淳; 白石充典; 尾瀬農之; 前仲勝実, 日本薬学会年会要旨集, 131年会, 1, 188, 188, Mar. 2011
  (公社)日本薬学会, Japanese
• 生命現象を担う生体分子に着目した創薬と臨床応用 多様な形態を有するHLA-G蛋白質とヒト免疫制御受容体との分子認識
  黒木 喜美子; 福永 裕子; 上敷領 淳; 白石 充典; 尾瀬 農之; 前仲 勝実, 日本薬学会年会要旨集, 131年会, 1, 188, 188, Mar. 2011
  (公社)日本薬学会, Japanese
• SU6656 suppresses human synovial sarcoma progression through Src and Aurora kinase inhibition
  Arai Ryuta; Tsuda Masumi; Watanabe Takuya; Ose Toyoyuki; Obuse Chikashi; Maenaka Katsumi; Minami Akio; Ohba Yusuke, 日本分子生物学会年会プログラム・要旨集(Web), 34th, WEB ONLY 2P-0690, 2011
  Summary national conference
• ヤツメウナギ由来可変性リンパ球受容体の結晶学的研究
  神田諒; 須藤洋一; 笠松純; 笠原正典; 前仲勝実; 尾瀬農之, 日本結晶学会年会講演要旨集, 2011, 90, 2011
  Japanese
• 麻疹ウイルスH蛋白質と受容体の複合体構造
  尾瀬農之; 橋口隆生; 久保田万理恵; 真板宣夫; 柳雄介; 前仲勝実, 日本結晶学会年会講演要旨集, 2011, 87, 2011
  Japanese
• 抑制型レセプターCD160によるHVEM認識の分子基盤
  小島理恵子; 梶川瑞穂; 白石充典; 黒木喜美子; 前仲勝実, 日本分子生物学会年会プログラム・要旨集(Web), 34th, 2T7PI-2 (WEB ONLY), 2011
  Japanese
• CDV‐Hの結晶構造解析と機能解析
  伊藤由梨; 福原秀雄; 酒匂幸; 橋口隆生; 梶川瑞穂; 竹田誠; 柳雄介; 尾瀬農之; 前仲勝実, 日本結晶学会年会講演要旨集, 2011, 90, 2011
  Japanese
• 免疫抑制分子HLA‐Gダイマーの局所投与による関節炎抑制効果の検討
  黒木喜美子; 岡部由紀; 廣瀬薫; 福永裕子; 小柳悟; 大戸茂弘; 前仲勝実, 日本分子生物学会年会プログラム・要旨集(Web), 34th, 2P-0444 (WEB ONLY), 2011
  Japanese
• 早期麻疹排除及び排除状態の維持に関する研究 麻疹ウイルスの抗原エピトープの構造解析と効果的なワクチン維持のための研究
  前仲勝実, 早期麻疹排除及び排除状態の維持に関する研究 平成22年度 総括・分担研究報告書, 117, 120, 2011
  Japanese
• ヒト免疫制御受容体LILRB1とリガンドHLA‐Gの複合体の結晶構造解析
  松原永季; 黒木喜美子; 上敷領淳; 尾瀬農之; 前仲勝実, 日本結晶学会年会講演要旨集, 2011, 95, 2011
  Japanese
• HIV由来変異ペプチドによるKIR2DL1を介した免疫逃避機構の分子基盤
  黒木喜美子; 上敷領淳; 尾瀬農之; THANANCHAI Hathairat; MAKADZANGE Tariro; ROWLAND‐JONES Sarah; DONG Tao; 前仲勝実, 日本結晶学会年会講演要旨集, 2011, 94, 2011
  Japanese
• HIV由来ペプチドライブラリーを用いたHLA‐Cw4拘束性免疫制御ペプチドの同定
  黒木喜美子; 福永裕子; 尾瀬豊之; 前仲勝実, 生化学, 83回・33回, 1P, 1023, Dec. 2010
  (公社)日本生化学会, Japanese
• 構造細胞生物学の新展開 モルビリウイルス属の細胞侵入機構と免疫制御の構造基盤
  前仲 勝実, 日本生化学会大会・日本分子生物学会年会合同大会講演要旨集, 83回・33回, 4W16, 6, Dec. 2010
  (公社)日本生化学会, Japanese
• 麻疹ウイルスと受容体SLAMの相互作用と膜融合
  橋口隆生; 白銀勇太; 前仲勝実; 柳雄介, 日本ウイルス学会学術集会プログラム・抄録集, 58th, 147, 15 Oct. 2010
  Japanese
• HSV‐1のエンベロープ蛋白質gBペプチドおよびペア型レセプターPILRαの複合体結晶構造解析
  尾瀬農之; 山口宗親; WAN Jing; 黒木喜美子; 田畑栄一; 真板宣夫; 中村聖子; 梶川瑞穂; 白鳥行大; 佐藤毅史; 荒瀬尚; 前仲勝実, 日本ウイルス学会学術集会プログラム・抄録集, 58th, 420, 15 Oct. 2010
  Japanese
• モルビリウイルス属ワクチンの有効性の構造基盤
  前仲勝実, 日本ウイルス学会学術集会プログラム・抄録集, 58th, 155, 15 Oct. 2010
  Japanese
• イヌジステンパーウイルスHタンパク質と受容体SLAMとの分子認識
  伊藤由梨; 福原秀雄; 酒匂幸; 橋口隆生; 梶川瑞穂; 竹田誠; 柳雄介; 前仲勝実, 日本ウイルス学会学術集会プログラム・抄録集, 58th, 247, 15 Oct. 2010
  Japanese
• クラスI認識受容体の構造とリガンド認識
  黒木喜美子; 福永裕子; 上敷領淳; 白石充典; 尾瀬農之; 前仲勝実, MHC, 17, 2, 136, 136, Aug. 2010
  日本組織適合性学会, Japanese
• NKおよびクラスI認識受容体研究の最前線 クラスI認識受容体の構造とリガンド認識
  黒木 喜美子; 福永 裕子; 上敷領 淳; 白石 充典; 尾瀬 農之; 前仲 勝実, MHC: Major Histocompatibility Complex, 17, 2, 136, 136, Aug. 2010
  日本組織適合性学会, Japanese
• 新規CRISP蛋白質の発見と毒蛇血清蛋白質SSP‐2との相互作用領域の解析
  塩井(青木; 成留実; 清村康子; 黒木喜美子; 前仲勝実; 寺田成之, 日本蛋白質科学会年会プログラム・要旨集, 10th, 73, 15 May 2010
  Japanese
• LILR1/HLA‐GとLILR82/HLA‐G複合体の結合機構の違い
  宮下尚之; 黒木喜美子; 前仲勝実; 杉田有治, 日本蛋白質科学会年会プログラム・要旨集, 10th, 66, 15 May 2010
  Japanese
• 麻疹ウイルスによる細胞侵入機構の構造基盤
  橋口隆生; 尾瀬農之; 上敷領淳; 柳雄介; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 10th, 32, 15 May 2010
  Japanese
• 活性化型受容体LILRA1‐MHC相互作用を介した免疫反応制御の分子基盤
  上敷領淳; 黒木喜美子; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 10th, 163, 15 May 2010
  Japanese
• 細胞表面において生体防御に関わる分子認識の構造生物学
  福原秀雄; 橋口隆生; 黒木喜美子; 白石充典; 佐々木香織; 梶川瑞穂; 尾瀬農之; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 10th, 32, 15 May 2010
  Japanese
• HLA-B27 FORMS HEAVY CHAIN HOMODIMERS IN VITRO AND IN VIVO THAT BIND TO CELLULAR RECEPTORS INCLUDING LILR AND KIR FAMILY MEMBERS
  Kirsty McHugh; Joanna Giles; Simon Kollnberger; Kimiko Kuroi; Katsumi Maenaka; Paul Bowness, RHEUMATOLOGY, 49, I50, I50, Apr. 2010
  English, Summary international conference
• モルビリウイルス属の細胞侵入機構と免疫制御の構造基盤
  前仲勝実, 生化学, ROMBUNNO.4W16-6, 2010
  Japanese
• HLA多型が寄与する自己免疫疾患の発症機序の解明 HLA‐B27の構造的分子特性の解析と免疫制御機構の解明
  前仲勝実, HLA多型が寄与する自己免疫疾患の発症機序の解明 平成21年度 総括・分担研究報告書, 18, 21, 2010
  Japanese
• ペア型レセプターPILRα及びHSV‐1のエンベロープ蛋白質gB模倣ペプチド複合体結晶構造
  尾瀬農之; 山口宗親; 黒木喜美子; 田畑栄一; 真板宣夫; 梶川瑞穂; 中村聖子; WANG Jing; 佐藤毅史; 荒瀬尚; 前仲勝実, 日本結晶学会年会講演要旨集, 2010, 97, 2010
  Japanese
• 蚕バイオテクノロジー : タンパク質生産工場として(第61回大会シンポジウム報告)
  朴 龍洙; 前仲 勝実, 生物工学会誌 : seibutsu-kogaku kaishi, 87, 11, 539, 539, 25 Nov. 2009
  公益社団法人日本生物工学会, Japanese
• CD160‐HVEM相互作用を中心としたT細胞制御機構の分子基盤
  小島理恵子; 梶川瑞穂; 白石充典; 黒木喜美子; 前仲勝実, 日本免疫学会総会・学術集会記録, 39, 161, 161, Nov. 2009
  (NPO)日本免疫学会, Japanese
• T細胞補助シグナル CD160-HVEM相互作用を中心としたT細胞制御機構の分子基盤
  小島 理恵子; 梶川 瑞穂; 白石 充典; 黒木 喜美子; 前仲 勝実, 日本免疫学会総会・学術集会記録, 39, 161, 161, Nov. 2009
  (NPO)日本免疫学会, Japanese
• イヌジステンパーウイルスHタンパク質と受容体SLAMとの分子認識
  酒匂幸; 橋口隆生; 竹田誠; 柳雄介; 前仲勝実, 日本ウイルス学会学術集会プログラム・抄録集, 57th, 276, 01 Oct. 2009
  Japanese
• 麻疹ウイルスHタンパク質と受容体SLAMの複合体の結晶構造と麻疹ウイルスの細胞侵入機構
  橋口隆生; 尾瀬農之; 上敷領淳; 竹田誠; 前仲勝実; 柳雄介, 日本ウイルス学会学術集会プログラム・抄録集, 57th, 149, 01 Oct. 2009
  Japanese
• Paired Immunoglobulin(Ig)Like type 2 Receptor(PILR)αによるGlycoprotein B(gB)認識機構の解明
  山口宗親; 黒木喜美子; 田畑栄一; 真板宣夫; 梶川瑞穂; 尾瀬農之; 中村聖子; 王静; 佐藤毅; 荒瀬尚; 前仲勝実, 日本ウイルス学会学術集会プログラム・抄録集, 57th, 149, 01 Oct. 2009
  Japanese
• 真正細菌におけるセレノシステイン特異的翻訳伸長因子SelBとSECIS mRNAの相互作用基盤
  尾瀬農之; RASUBALA Linda; 神田大輔; SOLER Nicolas; 吉澤聡子; FOURMY Dominique; 前仲勝実, 生化学, ROMBUNNO.2S8A-2, 25 Sep. 2009
  Japanese
• 翻訳されうる21番目のアミノ酸、セレノシステインを含有するタンパク質研究のブレーク・スルー 真正細菌におけるセレノシステイン特異的翻訳伸長因子SelBとSECIS mRNAの相互作用基盤
  尾瀬 農之; Rasubala Linda; 神田 大輔; Soler Nicolas; 吉澤 聡子; Fourmy Dominique; 前仲 勝実, 日本生化学会大会プログラム・講演要旨集, 82回, 2S8a, 2, Sep. 2009
  (公社)日本生化学会, Japanese
• BmNPVバクミドを用いたヒト膜タンパク質受容体のカイコ個体での生産
  梶川瑞穂; 佐々木香織; 黒木喜美子; 橋口隆生; 岡部由紀; 福原秀雄; 竹田誠; 柳雄介; 脇本義太郎; 豊岡勝; 武田茂樹; 本橋智子; 霜島司; PARK Enoch Y; 前仲勝実, 日本生物工学会大会講演要旨集, 61st, 281, 25 Aug. 2009
  Japanese
• 皮膚免疫に重要な役割を果たすと推定される新しいMHCクラスI様分子の解析
  吉田繁; 富居一範; 梶川瑞穂; 近藤瑞穂; 大塚紀幸; 前仲勝実; 笠原正典, MHC, 16, 2, 178, 178, 25 Aug. 2009
  日本組織適合性学会, Japanese
• 3S13p03 Silkworm expression of human membrane receptors using BmNPV bacmid
  KAJIKAWA Mizuho; SASAKI Kaori; KUROKI Kimiko; HASHIGUCHI Takao; OKABE Yuki; HUKUHARA Hideo; TAKEDA Makoto; YANAGI Yusuke; WAKIMOTO Yoshitarou; TOYOOKA Masaru; TAKEDA Shigeki; MOTOHASHI Tomoko; SHIMOJIMA Tsukasa; PARK Enoch Y; MAENAKA Katsumi, 日本生物工学会大会講演要旨集, 21, 0, 281, 25 Aug. 2009
  公益社団法人日本生物工学会, Japanese
• HIVペプチドの変異によるNK細胞受容体を介した免疫逃避の分子基盤
  前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 9th, 45, 24 Apr. 2009
  Japanese
• CD160‐HVEM相互作用を中心としたT細胞活性制御の分子基盤
  小島理恵子; 梶川瑞穂; 白石充典; 黒木喜美子; 前仲勝実, 日本分子生物学会年会講演要旨集, 32nd, Vol.1, 63, 2009
  Japanese
• HLA多型が寄与する自己免疫疾患の発症機序の解明 HLA‐B27の構造的分子特性の解析と免疫制御機構の解明
  前仲勝実, HLA多型が寄与する自己免疫疾患の発症機序の解明 平成20年度 総括・分担研究報告書, 16, 19, 2009
  Japanese
• マウスMHCクラスIb分子MILL2の結晶構造解析
  梶川瑞穂; 尾瀬農之; 笠原正典; 前仲勝実, 生化学, 81回・31回, 2T20-1, 1, Nov. 2008
  (公社)日本生化学会, Japanese
• シグナル伝達タンパク質の分子認識研究の新展開 麻疹ウイルス受容体結合タンパク質の立体構造
  前仲 勝実, 日本生化学会大会・日本分子生物学会年会合同大会講演要旨集, 81回・31回, 3S16, 2, Nov. 2008
  (公社)日本生化学会, Japanese
• Association of LILRA2 (ILT1, LIR7) splice site polymorphism with systemic lupus erythematosus and microscopic polyangiitis (vol 9, page 214, 2008)
  K. Mamegano; K. Kuroki; R. Miyashita; M. Kusaoi; S. Kobayashi; K. Matsuta; K. Maenaka; M. Colonna; S. Ozaki; H. Hashimoto; Y. Takasaki; K. Tokunaga; N. Tsuchiya, GENES AND IMMUNITY, 9, 7, 650, 650, Oct. 2008
  English, Others
• “21番目のアミノ酸”セレノシステインを取り込むための分子基盤
  尾瀬農之; RASUBALA Linda; 神田大輔; SOLER Nicolas; 吉澤聡子; FOURMY Dominique; 前仲勝実, 補体シンポジウム講演集, 45th, 194, 194, Jul. 2008
  (一社)日本補体学会, Japanese
• 麻疹ウイルスHタンパク質のX線結晶構造解析
  橋口隆生; 梶川瑞穂; 真板宣夫; 竹田誠; 黒木喜美子; 佐々木香織; 柳雄介; 前仲勝実, 補体シンポジウム講演集, 45, 61, 61, Jul. 2008
  (一社)日本補体学会, Japanese
• ウイルス認識の分子基盤 麻疹ウイルスHタンパク質のX線結晶構造解析
  橋口 隆生; 梶川 瑞穂; 真板 宣夫; 竹田 誠; 黒木 喜美子; 佐々木 香織; 柳 雄介; 前仲 勝実, 補体シンポジウム講演集, 45, 61, 61, Jul. 2008
  (一社)日本補体学会, Japanese
• X-ray crystallographic analysis of measles virus hemagglutinin
  HASHIGUCHI Takao; MAENAKA Katsumi; YANAGI Yusuke, Virus, 58, 1, 1, 10, 22 Jun. 2008, [Domestic magazines]
  X-ray crystallographic analyses, together with nuclear magnetic resonance, have revealed three-dimensional structures of many important viral proteins, thereby allowing us to better understand the interactions between viral and host cell molecules. In this review, we summarize the recently determined crystal structure of the measles virus (MV) attachment protein hemagglutinin. Based on this structural information, we also discuss how the MV hemagglutinin interacts with various cellular receptors and why MV vaccines have been effective for many years without inducing escape mutant viruses. Other topics discussed are a putative MV receptor present on polarized epithelial cells and the protein expression system using a cultured human cell line 293SGnTI(-), which is suitable for X-ray crystallographic analyses., 日本ウィルス学会, Japanese
• 複数の結合様式を介したミトコンドリアTom20によるプレ配列の認識機構
  齊藤貴士; 井倉真由美; 尾瀬農之; 前仲勝実; 神田大輔, 日本蛋白質科学会年会プログラム・要旨集, 8th, 19, 23 May 2008
  Japanese
• DNAのメチル化シグナルを見分ける分子メカニズム―メチル化及び非メチル化CpG結合ドメインの立体構造解析より―
  大木出; 真板宣夫; 前仲勝実; 神田大輔, 日本蛋白質科学会年会プログラム・要旨集, 8th, 81, 23 May 2008
  Japanese
• BmNPVバクミドとカイコ個体を用いたヒトGタンパク質共役型受容体の生産
  梶川瑞穂; 佐々木香織; 脇本義太郎; 豊岡勝; 武田茂樹; 本橋智子; 霜島司; PARK Enoch Y; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 8th, 124, 23 May 2008
  Japanese
• Asn結合型糖鎖修飾を決定するオリゴ糖転移酵素・膜タンパク質の大腸菌による発現
  井倉真由美; 上敷領淳; NYIRENDA James; 前仲勝実; 神田大輔, 日本蛋白質科学会年会プログラム・要旨集, 8th, 81, 23 May 2008
  Japanese
• BmNPVバクミドシステムによるヒト免疫細胞表面レセプターの発現と糖鎖解析
  佐々木香織; 梶川瑞穂; 矢木宏和; 近藤幸子; 黒木喜美子; 本橋智子; 霜島司; PARK Enoch Y; 加藤晃一; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 8th, 98, 23 May 2008
  Japanese
• 免疫学 HLA‐G―副作用の少ない生物学的製剤の可能性
  黒木喜美子; 前仲勝実, 医学のあゆみ, 224, 11, 874, 875, Mar. 2008
  医歯薬出版(株), Japanese
• BmNPVバクミドシステムによるヒト免疫細胞表面レセプターの発現と糖鎖解析
  佐々木香織; 梶川瑞穂; 矢木宏和; 近藤幸子; 黒木喜美子; 本橋智子; 霜島司; PARK Enoch Y; 加藤晃一; 前仲勝実, 生化学, 4P-0214, 2008
  Japanese
• 麻疹ウイルス受容体結合タンパク質の立体構造
  前仲勝実, 生化学, 3S16-2, 2008
  Japanese
• 【ウイルス学・構造生物学】結晶構造が解き明かす麻疹ウイルスワクチン成功の理由
  橋口隆生; 柳雄介; 前仲勝実, メディカルバイオ, 5, 1, 10, 11, 01 Jan. 2008
  (株)オーム社, Japanese
• 構造基盤解析に向けたミトコンドリアTom20‐プレ配列ペプチド複合体の安定化
  齊藤貴士; 井倉真由美; 尾瀬農之; 帯田孝之; 小島理恵子; 前仲勝実; 神田大輔, Abstr Annu Meet NMR Soc Jpn, 46th, 164, 165, 11 Sep. 2007
  Japanese
• アスパラギン結合型糖鎖修飾を決定するオリゴ糖転移酵素の構造生化学
  井倉真由美; 上敷領淳; 真板宣夫; 山田真希; 前仲勝実; 神田大輔, 日本糖質学会年会要旨集, 27th, 65, 10 Jul. 2007
  Japanese
• 超好熱性古細菌Pyrococcus furiosusのN型糖鎖生合成機構の解明
  上敷領淳; 井倉真由美; 山田真希; 前仲勝実; 神田大輔, 日本蛋白質科学会年会プログラム・要旨集, 7th, 63, 07 May 2007
  Japanese
• Asn結合型糖鎖修飾を決定するオリゴ糖転移酵素の構造生物学研究
  井倉真由美; 真板宣夫; 上敷領淳; 山田真希; 前仲勝実; 神田大輔, 日本蛋白質科学会年会プログラム・要旨集, 7th, 28, 07 May 2007
  Japanese
• PriAタンパク質によるDNA3′末端の塩基非選択的認識機構の解明
  佐々木香織; 尾瀬農之; 岡本直明; 田中卓; 前仲勝実; 正井久雄; 斉藤美保子; 白井剛; 神田大輔, 日本蛋白質科学会年会プログラム・要旨集, 7th, 50, 07 May 2007
  Japanese
• ペア型レセプターPaired Ig‐Like type2 Receptor(PILR)の構造解析
  田畑栄一; 黒木喜美子; 梶川瑞穂; 白鳥行大; 荒瀬尚; 神田大輔; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 7th, 79, 07 May 2007
  Japanese
• ミトコンドリアTom20によるプレ配列の動的認識機構:緩和解析からのアプローチ
  齊藤貴士; 井倉真由美; 尾瀬農之; 帯田孝之; 小島理恵子; 前仲勝実; 神田大輔, 日本蛋白質科学会年会プログラム・要旨集, 7th, 38, 07 May 2007
  Japanese
• Entropically Driven Receptor-Ligand Interaction; Molecular recognition of Human Inhibitory Receptor Leukocyte Immunoglobulin-Like Receptors (LILRs)
  SHIROISHI Mitsunori; KUROKI Kimiko; KOHDA Daisuke; MAENAKA Katsumi, Biophysics, 47, 2, 93, 99, Mar. 2007
  Protein-protein and protein-nucleic acid interactions are fundamental in self and non-self recognition in immune system. Leukocyte immunoglobulin-like receptor B1 (LILRB1) and LILRB2 are human inhibitory receptors which recognize major histocompatibility complex (MHC) class I molecules and take part in immune regulation. In this review, we demonstrated detailed thermodynamic and kinetic studies of interactions between LILRs and MHC class I molecules, and structural analyses by X-ray crystallography and NMR. Our data shows the binding mode involving some conformational adjustment without a v..., 日本生物物理学会, Japanese
• クロマチン構造制御に関わる新規CpG配列結合ドメインのDNA認識の分子メカニズム
  大木出; 前仲勝実; 神田大輔, 生化学, 1P-0034, 2007
  Japanese
• Asn結合型糖鎖修飾を決定するオリゴ糖転移酵素の構造生物学研究
  井倉真由美; 真板宣夫; 上敷領淳; 山田真希; 前仲勝実; 神田大輔, 生化学, 4P-0096, 2007
  Japanese
• 難治性血管炎に関する調査研究 日本人顕微鏡的多発血管炎の疾患感受性遺伝子に関する研究
  土屋尚之; 宮下リサ; 豆ケ野剛一; 徳永勝士; 川崎綾; 黒木喜美子; 前仲勝実; COLONNA Marco; 小林茂人; 橋本博史; 尾崎承一, 難治性血管炎に関する調査研究 平成18年度総括・分担研究報告書, 43, 48, 2007
  Japanese
• ペア型レセプターPaired Ig‐Like type2 Receptor(PILR)のCD99認識機構の分子基盤
  田畑栄一; 黒木喜美子; 梶川瑞穂; WANG Jing; 荒瀬尚; 神田大輔; 前仲勝実, 生化学, 1P-0043, 2007
  Japanese
• Structural basis for the DNA recognition of PriA protein in the stalled DNA replication fork
  佐々木香織; 田中卓; 正井久雄; 前仲勝実; 神田大輔, 生化学, 1P-0701, 2007
  Japanese
• クロマチン工学への応用に向けたキネトコアタンパク質複合体の再構成
  堀哲也; 真柳浩太; 前仲勝実; 保木裕子; 佐渡敬; 岡田聖裕; 深川竜郎, 生化学, 2P-0788, 2007
  Japanese
• ジスルフィド結合で拘束したTom20‐プレ配列複合体の動的振る舞い
  斉藤貴士; 伊倉真由美; 小島理恵子; 帯田孝之; 前仲勝実; 神田大輔, Abstr Annu Meet NMR Soc Jpn, 45th, 244, 245, 20 Nov. 2006
  Japanese
• Molecular basis for LILR recognition of HLA-G and its dimer
  M. Shiroishi; K. Kuroki; T. Ose; L. Rasubala; I. Shiratori; H. Arase; D. Kohda; K. Maenaka, TISSUE ANTIGENS, 68, 4, CP6, CP6, Oct. 2006
  English, Summary international conference
• ペア型レセプターPaired Ig‐Like type2Receptor(PILR)の構造解析
  田畑栄一; 黒木喜美子; 白鳥行大; 荒瀬尚; 神田大輔; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 6th, 96, 31 Mar. 2006
  Japanese
• BmNPVバクミドシステムを用いたカイコ個体でのヒト免疫細胞表面レセプターKIRの大量発現
  佐々木香織; 梶川瑞穂; 黒木喜美子; 本橋智子; 霜島司; 朴龍洙; 神田大輔; 前仲勝実, 日本蛋白質科学会年会プログラム・要旨集, 6th, 62, 31 Mar. 2006
  Japanese
• Molecular Basis for the Selenocysteine Incorporation
  OSE Toyoyuki; RASUBALA Linda; YOSHIZAWA Satoko; FOURMY Dominique; KOHDA Daisuke; MAENAKA Katsumi, Biophysics, 46, 2, 102, 105, 25 Mar. 2006
  日本生物物理学会, Japanese
• Crystallization and preliminary crystallographic analysis of the N-terminal domain of PriA from Escherichia coli
  K Sasaki; T Ose; T Tanaka; T Mizukoshi; T Ishigaki; K Maenaka; H Masai; D Kohda, BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1764, 1, 157, 160, Jan. 2006
  English
• 大腸菌プライモソーム形成に関わるタンパク質PriBの立体構造とDNAとの相互作用
  塩井誠次郎; 阿部義人; 竹縄太一; 前仲勝実; 神田大輔; 片山勉; 植田正, 日本分子生物学会年会講演要旨集, 28th, 56, 25 Nov. 2005
  Japanese
• ミトコンドリアプレ配列認識のためのTom20タンパク質の動的構造
  井倉真由美; 帯田孝之; 尾瀬農之; 遠藤斗志也; 前仲勝実; 神田大輔, 日本分子生物学会年会講演要旨集, 28th, 602, 25 Nov. 2005
  Japanese
• MHCクラスI様分子MILLの構造・機能解析
  梶川瑞穂; 笠原正典; 神田大輔; 前仲勝実, 日本分子生物学会年会講演要旨集, 28th, 282, 25 Nov. 2005
  Japanese
• NK細胞抑制型レセプターKLRG1(Killer Cell Lectin‐Like Receptor G1)によるKLRG1リガンド認識の構造基盤
  中村聖子; 黒木喜美子; 佐々木香織; 丸山拓馬; 伊藤昌之; 山本一夫; 松本直樹; 神田大輔; 前仲勝実, 日本分子生物学会年会講演要旨集, 28th, 572, 25 Nov. 2005
  Japanese
• カイコ個体を用いたタンパク質の大量発現用バクミドの開発及び応用
  PARK Enoch Y; 前仲勝実, 日本分子生物学会年会講演要旨集, 28th, 48, 25 Nov. 2005
  Japanese
• E.coli由来PriAのN末端ドメインによるDNA3′末端認識の構造的基盤
  佐々木香織; 尾瀬農之; 田中卓; 岡本直明; 前仲勝実; 正井久雄; 神田大輔, 日本分子生物学会年会講演要旨集, 28th, 393, 25 Nov. 2005
  Japanese
• Killer cell lectin‐like receptor G1(KLRG1)が認識するKLRG1リガンド上領域の同定
  丸山拓馬; 松本直樹; 伊藤昌之; 中村聖子; 黒木喜美子; 前仲勝実; 山本一夫, 日本免疫学会総会・学術集会記録, 35, 97, 97, Nov. 2005
  (NPO)日本免疫学会, Japanese
• 白血球抑制性受容体LILRB1とMHCクラスIとのFCSおよびNMRを用いた相互作用解析
  黒木喜美子; 白石充典; RASUBALA Linda; 小林佐代子; 梶川瑞穂; 田畑栄一; 福永裕子; 岡本直明; 神田大輔; 前仲勝実, 日本免疫学会総会・学術集会記録, 35, 99, 99, Nov. 2005
  (NPO)日本免疫学会, Japanese
• HLA‐GダイマーのLILR/LIR/ILTレセプターを介した強いシグナル伝達とその構造基盤
  前仲勝実; 白石充典; 黒木喜美子; RASUBALA Linda; 白鳥行大; 荒瀬尚; 神田大輔, 日本免疫学会総会・学術集会記録, 35, 99, 99, Nov. 2005
  (NPO)日本免疫学会, Japanese
• NK細胞抑制型レセプターKLRG1(Killer Cell Lectin‐Like Recepter G1)によるKLRG1リガンド認識の構造基盤
  中村聖子; 黒木喜美子; 佐々木香織; 丸山拓馬; 伊藤昌之; 山本一夫; 松本直樹; 神田大輔; 前仲勝実, 日本免疫学会総会・学術集会記録, 35, 98, 98, Nov. 2005
  (NPO)日本免疫学会, Japanese
• 白血球抑制性受容体LILRB1とMHCクラスIとの蛍光相関分光法(FCS)およびNMRを用いた相互作用解析
  黒木喜美子; 白石充典; RASUBALA Linda; 小林佐代子; 梶川瑞穂; 田畑栄一; 福永裕子; 岡本直明; 神田大輔; 前仲勝実, 日本分子生物学会年会講演要旨集, 35, 99, 99, Nov. 2005
  (NPO)日本免疫学会, Japanese
• 関節リウマチ(RA)関連Leukocyte Immunoglobulin-like Receptor(LILR)B1ハプロタイプの構造・発現解析
  黒木 喜美子; 白石 充典; リンダ・ラスバラ; 土屋 尚之; 神田 大輔; 徳永 勝士; 前仲 勝実, 日本リウマチ学会総会・学術集会・国際リウマチシンポジウムプログラム・抄録集, 49回・14回, 211, 211, Apr. 2005
  (一社)日本リウマチ学会, Japanese
• 大腸菌由来PriAとオリゴヌクレオチドとの複合体の結晶化
  佐々木香織; 尾瀬農之; 岡本直明; 田中卓; 正井久雄; 前仲勝実; 神田大輔, 日本分子生物学会年会プログラム・講演要旨集, 27th, 618, 25 Nov. 2004
  Japanese
• ラットTom20タンパク質とALDHプレ配列複合体のX線結晶構造解析
  井倉真由美; 帯田孝之; 尾瀬農之; 遠藤斗志也; 前仲勝実; 神田大輔, 日本分子生物学会年会プログラム・講演要旨集, 27th, 732, 25 Nov. 2004
  Japanese
• ヒト免疫細胞受容体ILT/LIR/CD85ファミリーのリガンド認識の分子的基盤
  白石充典; 黒木喜美子; 小島恵理子; 津本浩平; 熊谷泉; 神田大輔; 前仲勝実, 日本分子生物学会年会プログラム・講演要旨集, 27th, 354, 25 Nov. 2004
  Japanese
• ミトコンドリア・プレ配列受容体Tom20‐ALDHプレ配列複合体の結晶構造と緩和解析
  帯田孝之; 井倉真由美; 尾瀬農之; 前仲勝実; 遠藤斗志也; 神田大輔, NMR討論会講演要旨集, 43rd, 212, 213, 10 Nov. 2004
  Japanese
• ヒト免疫細胞抑制型受容体ILT4のリガンド認識の分子的基盤
  白石充典; 津本浩平; 栗本英治; 加藤晃一; 熊谷泉; 神田大輔; 前仲勝実, 日本免疫学会総会・学術集会記録, 34, 230, 230, 05 Nov. 2004
  (NPO)日本免疫学会, Japanese
• 関節リウマチ(RA)関連Leukocyte Immunoglobulin‐like Receptor(LIR)1ハプロタイプの構造・発現解析
  黒木喜美子; 土屋尚之; 白石充典; RASUBALA L; 山下由美; 小池隆夫; 神田大輔; 徳永勝士; 前仲勝実, 日本免疫学会総会・学術集会記録, 34, 162, 162, Nov. 2004
  (NPO)日本免疫学会, Japanese
• Leukocyte Ig‐like receptor群の構造解析
  前仲勝実, 医学のあゆみ, 209, 13, 1033, 1034, 26 Jun. 2004
  医歯薬出版(株), Japanese
• ヒト免疫細胞抑制型受容体ILT2,4の相互作用解析
  白石充典; 津本浩平; 熊谷泉; 白木原康雄; 前仲勝実, 生化学, 76, 3, 320, 320, 25 Mar. 2004
  (公社)日本生化学会, Japanese
• 第三のナイシン類縁体,ナイシンQ
  米山史紀; 深尾匡憲; 帯田孝之; 善藤威史; 前仲勝実; 中山二郎; 神田大輔; 園元謙二, 日本農芸化学会大会講演要旨集, 2004, 162, 05 Mar. 2004
  Japanese
• NK細胞表面レセプター群の分子認識
  前仲勝実, 生化学, 76, 2, 135, 140, 25 Feb. 2004
  コレクション : 国立国会図書館デジタルコレクション > デジタル化資料 > 雑誌, (公社)日本生化学会, Japanese
• Molecular recognitions of natural killer cell receptors
  K Maenaka, SEIKAGAKU, 76, 2, 135, 140, Feb. 2004, [Domestic magazines]
  Japanese
• ヒト免疫細胞受容体ILT2,4の相互作用解析
  白石充典; ラスバラ リンダ; 津本浩平; 熊谷泉; 神田大輔; 前仲勝実, 日本免疫学会総会・学術集会記録, 33, 318, 318, 05 Nov. 2003
  (NPO)日本免疫学会, Japanese
• NMRを用いたempty MHCクラスIタンパク質の動的構造解析
  栗本英治; 山口芳樹; 前仲勝実; 神田大輔; 加藤晃一, 日本免疫学会総会・学術集会記録, 33, 324, 324, 05 Nov. 2003
  (NPO)日本免疫学会, Japanese
• Distinct associations of the leukocyte immunoglobulin-like receptor (LIR)1 and LIR6 polymorphisms with susceptibility to rheumatoid arthritis (RA) and systemic lupus erythematosus (SLE).
  K Kuroki; N Tsuchiya; K Maenaka; L Rasubala; M Shiroishi; Y Yamashita; K Matsuta; T Fukazawa; D Kohda; T Koike; T Juji; H Hashimoto; K Tokunaga, ARTHRITIS AND RHEUMATISM, 48, 9, S197, S197, Sep. 2003
  English, Summary international conference
• Structural analysis of ligand-free MHC class I protein by NMR spectroscopy
  Kurimoto E; Yamaguchi Y; Igaki T; Maenaka K; Kato K, Biophysics, 43, 1, S41, S41, 25 Aug. 2003
  日本生物物理学会, Japanese
• Structure-guided design of sialic acid-based Siglec inhibitors and crystallographic analysis in complex with sialoadhesin
  NR Zaccai; K Maenaka; T Maenaka; PR Crocker; R Brossmer; S Kelm; EY Jones, STRUCTURE, 11, 5, 557, 567, May 2003
  English
• Structure-guided design of sialic acid-based Siglec inhibitors and crystallographic analysis in complex with sialoadhesin
  NR Zaccai; K Maenaka; T Maenaka; PR Crocker; R Brossmer; S Kelm; EY Jones, STRUCTURE, 11, 5, 557, 567, May 2003
  English
• Bacmidを用いたBmNPVバキュロウイルス外来遺伝子発現系の構築
  本橋智子; 霜島司; 前仲勝実; 朴龍しゅ, 日本農芸化学会大会講演要旨集, 2003, 154, 05 Mar. 2003
  Japanese
• Yasushi Uemura, Satoru Senju, Katsumi Maenaka, Leo Kei Iwai, Shinji Fujii, Hiroki Tabata, Hirotake Tsukamoto, Shinya Hirata, Yu-Zhen Chen & Yasuharu Nishimura. Systematic analysis of the combinatorial nature of epitopes recognized by TCR leads to i・・・
  J. Immunol, 170, 947, 960, 2003
  Yasushi Uemura, Satoru Senju, Katsumi Maenaka, Leo Kei Iwai, Shinji Fujii, Hiroki Tabata, Hirotake Tsukamoto, Shinya Hirata, Yu-Zhen Chen & Yasuharu Nishimura. Systematic analysis of the combinatorial nature of epitopes recognized by TCR leads to identification of mimicry epitopes for glutamic acid decarboxylase 65-specific TCRs.
• Mitsunori Shiroishi, Kouhei Tsumoto, Kimie Amano, Yasuo Shirakihara, Marco Colonna, Veronique M. Braud, David S. J. Allan, Azure Makadzange, Sarah Rowland-Jones, Benjamin Willcox, E. Yvonne Jones, P. Anton van der Merwe, Izumi Kumagai, & Katsumi Ma・・・
  Proc. Natl. Acad. Sci. USA, 100, 8856, 61, 2003
  Mitsunori Shiroishi, Kouhei Tsumoto, Kimie Amano, Yasuo Shirakihara, Marco Colonna, Veronique M. Braud, David S. J. Allan, Azure Makadzange, Sarah Rowland-Jones, Benjamin Willcox, E. Yvonne Jones, P. Anton van der Merwe, Izumi Kumagai, & Katsumi Maenaka. Human inhibitory receptors ILT2 and ILT4 compete with CD8 for MHC class I binding and bind preferentially to HLA-G
• Specificity, degeneracy, and molecular mimicry in antigen recognition by HLA-Class II restricted T cell receptors: Implications for clinical medicine
  Yasushi Uemura; Satoru Senju; Shinji Fujii; Leo Kei Iwai; Katsumi Maenaka; Hiroki Tabata; Takayuki Kanai; Yu-Zhen Chen; Yasuharu Nishimura, Modern Rheumatology, 13, 3, 205, 214, 2003
  English, Book review
• Haruka Wada, Naoki Matsumoto, Katsumi Maenaka, Kazuhiro Suzuki and Kazuo Yamamoto. Two HLA-E Mutants Segregate the Inhibitory NK Cell Receptor CD94/NKG2A and the Activating Receptor CD94/NKG2C, Both of Whichi Bind the Top of HLA-E
  Eur. J. Immunol, In the press, 2003
• Yasushi Uemura, Satoru Senju, Katsumi Maenaka, Leo Kei Iwai, Shinji Fujii, Hiroki Tabata, Hirotake Tsukamoto, Shinya Hirata, Yu-Zhen Chen & Yasuharu Nishimura. Systematic analysis of the combinatorial nature of epitopes recognized by TCR leads to i・・・
  J. Immunol, 170, 947, 960, 2003
  Yasushi Uemura, Satoru Senju, Katsumi Maenaka, Leo Kei Iwai, Shinji Fujii, Hiroki Tabata, Hirotake Tsukamoto, Shinya Hirata, Yu-Zhen Chen & Yasuharu Nishimura. Systematic analysis of the combinatorial nature of epitopes recognized by TCR leads to identification of mimicry epitopes for glutamic acid decarboxylase 65-specific TCRs.
• Mitsunori Shiroishi, Kouhei Tsumoto, Kimie Amano, Yasuo Shirakihara, Marco Colonna, Veronique M. Braud, David S. J. Allan, Azure Makadzange, Sarah Rowland-Jones, Benjamin Willcox, E. Yvonne Jones, P. Anton van der Merwe, Izumi Kumagai, & Katsumi Ma・・・
  Proc. Natl. Acad. Sci. USA, 100, 8856, 61, 2003
  Mitsunori Shiroishi, Kouhei Tsumoto, Kimie Amano, Yasuo Shirakihara, Marco Colonna, Veronique M. Braud, David S. J. Allan, Azure Makadzange, Sarah Rowland-Jones, Benjamin Willcox, E. Yvonne Jones, P. Anton van der Merwe, Izumi Kumagai, & Katsumi Maenaka. Human inhibitory receptors ILT2 and ILT4 compete with CD8 for MHC class I binding and bind preferentially to HLA-G
• Specificity, degeneracy, and molecular mimicry in antigen recognition by HLA-Class II restricted T cell receptors: Implications for clinical medicine
  Yasushi Uemura; Satoru Senju; Shinji Fujii; Leo Kei Iwai; Katsumi Maenaka; Hiroki Tabata; Takayuki Kanai; Yu-Zhen Chen; Yasuharu Nishimura, Modern Rheumatology, 13, 3, 205, 214, 2003
  English, Book review
• Haruka Wada, Naoki Matsumoto, Katsumi Maenaka, Kazuhiro Suzuki and Kazuo Yamamoto. Two HLA-E Mutants Segregate the Inhibitory NK Cell Receptor CD94/NKG2A and the Activating Receptor CD94/NKG2C, Both of Whichi Bind the Top of HLA-E
  Eur. J. Immunol, In the press, 2003
• Systematic analysis of the combinatorial nature of epitopes recognized by TCR leads to identification of mimicry epitopes for GAD65 specific TCRs
  Uemura, Y; Senju, S; Maenaka, K; Iwai, L.K; Fujii, S; Tabata, H; Tsukamoto, H; Hirata, S; Chen, Y-Z; Nishimura, Y, J. Immunol., 170, 947, 960, 960, 2003
• エピトープ発現ライブラリーを用いたGAD65自己反応性TCRの認識エピトープの多様性に関する解析
  植村靖史; 千住覚; 前仲勝実; 藤井慎嗣; 塚本博丈; CHEN Y‐C; 西村泰治, 日本免疫学会総会・学術集会記録, 32, 278, 278, 31 Oct. 2002
  (NPO)日本免疫学会, Japanese
• Crystallization and preliminary X-ray diffraction studies on the DNA-binding domain of the transcriptional activator protein PhoB from Escherichia coli
  K Shindoh; K Maenaka; T Akiba; H Okamura; Y Nishimura; K Makino; Y Shirakihara, ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 58, 1862, 1864, Oct. 2002
  English
• バキュロウィルスBmNPV外来遺伝子発現系における効率的ベクターの構築
  本橋智子; PARK E Y; 前仲勝実, 日本生物工学会大会講演要旨集, 2002, 66, 66, 25 Sep. 2002
  日本生物工学会, Japanese
• 461 Construction of efficient expression vector in BmNPV (bacurovirus) expression system
  Motohashi Tomoko; Park Enoch Y; Maenaka Katsumi, 日本生物工学会大会講演要旨集, 14, 0, 66, 66, 25 Sep. 2002
  公益社団法人日本生物工学会, Japanese
• ヒト免疫細胞抑制型受容体ILT2,4の相互作用解析
  白石充典; 前仲勝実; 白木原康雄; JONES Y; VAN DER MERWER A; 津本浩平; 熊谷泉, 生化学, 74, 8, 957, 957, 25 Aug. 2002
  (公社)日本生化学会, Japanese
• ヒト白血球抗原(HLA)とNK細胞受容体の相互作用の熱量計を用いた解析
  郷田秀一郎; 津本浩平; 横田亜紀子; 白石充典; 前仲勝実; 熊谷泉, 生化学, 74, 8, 871, 871, 25 Aug. 2002
  (公社)日本生化学会, Japanese
• HLA typing in a Kenyan cohort identifies novel class I alleles that restrict cytotoxic T cell response to local HIV-1 clades.
  AIDS in press, 16, 1899, 1904, 2002
• HLA typing in a Kenyan cohort identifies novel class I alleles that restrict cytotoxic T cell response to local HIV-1 clades.
  AIDS in press, 2002
• 免疫グロブリン様レセプター群のリガンド認識に関する速度論的熱力学的解析
  前仲 勝実; 白石 充典; 津本 浩平; Anton van; der Merwe; David Stuart; Yvonne Jones; Peter Sondermann; 熊谷 泉; 白木原 康雄, 日本免疫学会総会・学術集会記録, 31, 233, 233, Dec. 2001
  (NPO)日本免疫学会, Japanese
• The human low affinity Fc gamma receptors IIa, IIb, and III bind IgG with fast kinetics and distinct thermodynamic properties
  K Maenaka; PA van der Merwe; DI Stuart; EY Jones; P Sondermann, JOURNAL OF BIOLOGICAL CHEMISTRY, 276, 48, 44898, 44904, Nov. 2001
  English
• The human low affinity Fc gamma receptors IIa, IIb, and III bind IgG with fast kinetics and distinct thermodynamic properties
  K Maenaka; PA van der Merwe; DI Stuart; EY Jones; P Sondermann, JOURNAL OF BIOLOGICAL CHEMISTRY, 276, 48, 44898, 44904, Nov. 2001
  English
• 免疫グロブリン様レセプター群のリガンド認識に関する速度論的熱力学的解析
  前仲勝実; 白石充典; 津本浩平; VAN DER MERWE A; STUART D; JONES Y; SONDERMANN P; 熊谷泉; 白木原康雄, 日本免疫学会総会・学術集会記録, 31, 233, 31 Oct. 2001
  Japanese
• MHCクラスI分子及びヒトNK細胞阻害受容体(KIR)の効率的な巻き戻しと相互作用の熱力学的解析
  郷田秀一郎; 横田亜紀子; 白石充典; 津本浩平; 前仲勝実; 熊谷泉, 日本生物物理学会年会講演予稿集, 39th, S47, Oct. 2001
  Japanese
• 不溶性か粒から巻き戻した各種受容体細胞外ドメインの機能評価
  北村武; 郷田秀一郎; 津本浩平; 前仲勝実; 三沢悟; 熊谷泉, 日本生物物理学会年会講演予稿集, 39th, S47, Oct. 2001
  Japanese
• Ig‐like receptor群の分子認識機構
  前仲勝実, MHC, 8, 2, 104, 30 Sep. 2001
  Japanese
• Effective refolding of MHC class I molecule(Cw7)and killer cell inhibitory receptor(KIR2DL2)and their interaction
  Goda S; Yokota A; Shiroishi M; Tsumoto K; Maenaka K; Kumagai I, Biophysics, 41, 1, S47, 10 Sep. 2001
  日本生物物理学会, Japanese
• Assessment of function for several receptor extracellular domains refolded from inclusion bodies
  Kitamura T; Goda S; Tsumoto K; Maenaka K; Misawa S; Kumagai I, Biophysics, 41, 1, S47, 10 Sep. 2001
  日本生物物理学会, Japanese
• MHCと移植 Ig-like receptor群の分子認識機構
  前仲 勝実, MHC: Major Histocompatibility Complex, 8, 2, 104, 104, Sep. 2001
  日本組織適合性学会, Japanese
• 不溶性か粒で調製した各種受容体細胞外ドメインの効率よい巻き戻し系の構築
  北村武; 郷田秀一郎; 津本浩平; 前仲勝実; 三沢悟; 熊谷泉, 生化学, 73, 8, 959, 25 Aug. 2001
  Japanese
• Molecular recognition by immunologically relevant receptors.
  前仲勝実, 蛋白質 核酸 酵素, 46, 11, 1805, 1811, 10 Aug. 2001
  Japanese
• 【新世紀における蛋白質科学の進展】 生命現象の理解と医療・創薬に向けて 生体防御 免疫系レセプターの分子認識
  前仲 勝実, 蛋白質・核酸・酵素, 46, 11, 1805, 1811, Aug. 2001
  免疫系レセプターの機能制御を理解するには,細胞表面レセプターの分子認識を解析することが必須であるが,ようやく最近,いくつかのレセプターについて機能と構造の両面からの統合的な解析が報告されてきた.その例として,自然免疫にかかわるナチュラルキラー(NK)細胞に発現するkiller cell Ig-like receptor(KIR)の主要組織適合性抗原(MHC)クラスIに対する分子認識の著者等の研究を中心に,同じくMHCを認識し,適応免疫にかかわるレセプター(T細胞レセプター,CD8など)や他のレセプターと比較しながら,多様な免疫系レセプターの分子認識について概説した, 共立出版(株), Japanese
• 免疫系レセプターの分子認識 (新世紀における蛋白質科学の進展) -- (第3部 生命現象の理解と医療・創薬に向けて)
  前仲 勝実, 蛋白質核酸酵素, 46, 11, 1427, 1428,1805〜1811, Aug. 2001
  共立出版, Japanese
• Detection of autoantibodies to killer immunoglobulin-like receptors using recombinant fusion proteins for two killer immunoglobulin-like receptors in patients with systemic autoimmune diseases
  T Matsui; M Otsuka; K Maenaka; H Furukawa; T Yabe; K Yamamoto; K Nishioka; T Kato, ARTHRITIS AND RHEUMATISM, 44, 2, 384, 388, Feb. 2001
  English
• 免疫系レセプターの分子認識
  蛋白質核酸酵素 増刊号「新世紀における蛋白質科学の進展」, 46(11)、1805-1811, 2001
• ヒトMHCクラスI HLA-B*5101とHIV由来の免疫優性エピトープペプチドの複合体のX線結晶構造解析
  前仲 勝実; 前仲 太恵子; 冨山 宏子; 滝口 雅文; David Stuart; Yvonne Jones, 日本免疫学会総会・学術集会記録, 30, 315, 315, Nov. 2000
  (NPO)日本免疫学会, Japanese
• ヒトMHCクラスI HLA‐B5101とHIV由来の免疫優性エピトープペプチドの複合体のX線結晶構造解析
  前仲勝実; 前仲太恵子; 冨山宏子; 滝口雅文; STUART D; JONES Y, 日本免疫学会総会・学術集会記録, 30, 315, 26 Sep. 2000
  Japanese
• Autoantibodies to Killer Immunoglobulin-like Receptors (KIRS) in systemic autoimmune diseases.
  T Matsui; K Maenaka; H Furukawa; T Yabe; K Yamamoto; K Nishioka; T Kato, ARTHRITIS AND RHEUMATISM, 43, 9, S330, S330, Sep. 2000
  English, Summary international conference
• Nonstandard peptide binding revealed by crystal structures of HLA-B*5101 complexed with HIV immunodominant epitopes
  K Maenaka; T Maenaka; H Tomiyama; M Takiguchi; DI Stuart; EY Jones, JOURNAL OF IMMUNOLOGY, 165, 6, 3260, 3267, Sep. 2000
  English
• ヒトkiller cell Ig‐like receptorの分子認識機構
  前仲勝実; VAN DER MERWE A; 前仲太恵子; 白木原康雄; STUART D; JONES Y, 生化学, 72, 8, 1029, 1029, 25 Aug. 2000
  (公社)日本生化学会, Japanese
• Crystallization and preliminary diffraction studies of cam repressor(CamR)for the camphor catabolism operon.
  Maenaka K; Fukushi K; Aramaki H; Shirakihara Y, Biophysics, 40, 1, S195, 05 Aug. 2000
  日本生物物理学会, Japanese
• ヒトkiller cell immunoglobulin(Ig)‐like receptorの構造と機能
  前仲勝実; VAN DER MERWE A; 十字猛夫; 前仲太恵子; 白木原康雄; STUART D; JONES Y, タンパク質構造討論会講演要旨集, 51st, 325, 07 Jun. 2000
  Japanese
• Classical and nonclassical class I major histocompatibility complex molecules exhibit subtle conformational differences that affect binding to CD8 alpha alpha
  GF Gao; BE Willcox; Wyer, JR; JM Boulter; CA O'Callaghan; K Maenaka; DI Stuart; EY Jones; PA Van Der Merwe; JI Bell; BK Jakobsen, JOURNAL OF BIOLOGICAL CHEMISTRY, 275, 20, 15232, 15238, May 2000
  English
• MHC superfamily structure and the immune system
  K Maenaka; EY Jones, CURRENT OPINION IN STRUCTURAL BIOLOGY, 9, 6, 745, 753, Dec. 1999
  English
• Killer cell immunoglobulin receptors and T cell receptors bind peptide-major histocompatibility complex class I with distinct thermodynamic and kinetic properties
  K Maenaka; T Juji; T Nakayama; Wyer, JR; GF Gao; T Maenaka; NR Zaccai; A Kikuchi; T Yabe; K Tokunaga; K Tadokoro; DI Stuart; EY Jones; PA van der Merwe, JOURNAL OF BIOLOGICAL CHEMISTRY, 274, 40, 28329, 28334, Oct. 1999
  English
• Crystal structure of the human p58 killer cell inhibitory receptor (KIR2DL3) specific for HLA-Cw3-related MHC class I
  Katsumi Maenaka; Takeo Juji; David I. Stuart; E. Yvonne Jones, Structure, 7, 4, 391, 398, 15 Apr. 1999
  Current Biology Ltd, English
• ヒトkiller cell Ig-like receptor(KIR)の構造と機能
  構造生物, 5, 5-15, 1999
• Structural and functional effect of Trp-62 -> Gly and Asp-101 -> Gly substitutions on substrate-binding modes of mutant hen egg-white lysozymes
  K Maenaka; M Matsushima; G Kawai; A Kidera; K Watanabe; R Kuroki; Kumagai, I, BIOCHEMICAL JOURNAL, 333, 71, 76, Jul. 1998
  English
• Crystallization and preliminary diffraction studies of the extracellular region of human p58 killer cell inhibitory receptor (KIR2)
  K Maenaka; T Juji; K Tadokoro; K Harlos; DI Stuart; EY Jones, ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 54, 433, 435, May 1998
  English
• Structural analysis of mutant hen egg-white lysozyme preferring a minor binding mode
  K Maenaka; M Matsushima; G Kawai; K Watanabe; R Kuroki; Kumagai, I, BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1384, 1, 23, 31, Apr. 1998
  English
• Antibody engineering by phage display
  KUMAGAI Izumi; TSUMOTO Kouhei; MAENAKA Katsumi, Biophysics, 213, 219-222, 5, 219, 222, 25 Sep. 1997
  一般社団法人日本生物物理学会, Japanese
• The human natural killer gene complex (NKC) is located on chromosome 12p13.1-p13.2
  Y Suto; T Yabe; K Maenaka; K Tokunaga; K Tadokoro; T Juji, IMMUNOGENETICS, 46, 2, 159, 162, 1997
  English
• The 1.8-angstrom X-ray structure of the Escherichia coli PotD protein complexed with spermidine and the mechanism of polyamine binding
  S Sugiyama; Y Matsuo; K Maenaka; DG Vassylyev; M Matsushima; K Kashiwagi; K Igarashi; K Morikawa, PROTEIN SCIENCE, 5, 10, 1984, 1990, Oct. 1996
  English
• Development of a novel phage display system and its application to conversion of molecular recognition activities of proteins
  Kumagai, I; K Tsumoto; K Maenaka, PROTEIN ENGINEERING, 9, 9, 3, 3, Sep. 1996
  English, Summary international conference
• ヒトNKクラスIレセプターの大腸菌での発現とファージ表面への提示
  前仲 勝実; 西村 元子; 菊地 安希子; 中山 貴博; 斎藤 彰一; 屋部 登志雄; 熊谷 泉; 田所 憲治; 十字 猛夫, 日本分子生物学会年会プログラム・講演要旨集, 19, 0, 527, 527, 01 Aug. 1996
  Japanese
• ファージペプチドライブラリーを用いたヒト赤血球GPA分子上の抗体認識エピトープの解析
  屋部 登志雄; 古田 大; 前仲 勝実; 津本 浩平; 田所 憲治; 内川 誠; 熊谷 泉; 十字 猛夫, 日本分子生物学会年会プログラム・講演要旨集, 19, 0, 720, 720, 01 Aug. 1996
  Japanese
• 抗原のファージ提示による抗原抗体反応の解析
  津本 浩平; 前仲 勝実; 熊谷 泉, 日本分子生物学会年会プログラム・講演要旨集, 19, 0, 720, 720, 01 Aug. 1996
  Japanese
• Chromosomal localization of the human natural killer cell class I receptor family genes to 19q13.4 by fluorescence in situ hybridization
  Y Suto; K Maenaka; T Yabe; M Hirai; K Tokunaga; K Tadokoro; T Juji, GENOMICS, 35, 1, 270, 272, Jul. 1996
  English
• Expression of human NK class I receptor in Escherichia coli and presentation to phage surface.
  前仲勝実; 西村元子; 菊地安希子; 中山貴博; 斎藤彰一; 屋部登志雄; 熊谷泉; 田所憲治; 十字猛夫, 日本分子生物学会年会プログラム・講演要旨集, 19th, 7, 527, 1039, Jul. 1996
  (公社)日本生化学会, Japanese
• 抗原のファージ提示による抗原抗体反応の解析
  津本浩平; 前仲勝実; 熊谷泉, 日本分子生物学会年会プログラム・講演要旨集, 19th, 720, Jul. 1996
  Japanese
• ファージペプチドライブラリーを用いたヒト赤血球GPA分子上の抗体認識エピトープの解析
  屋部登志雄; 古田大; 前仲勝実; 津本浩平; 田所憲治; 内川誠; 熊谷泉; 十字猛夫, 日本分子生物学会年会プログラム・講演要旨集, 19th, 720, Jul. 1996
  Japanese
• Evolution engineering of enzyme molecules based on the catalytic mechanism.
  前仲勝実; 熊谷泉, 化学, 51, 6, 398, 399, Jun. 1996
  Japanese
• 触媒機構に基づく酵素分子の進化工学 (1996年の化学-6-)
  前仲 勝実; 熊谷 泉, 化学, 51, 6, 398, 399, Jun. 1996
  資料形態 : テキストデータ プレーンテキスト, 化学同人, Japanese
• 触媒機構に基づく酵素分子の進化工学
  化学6, 398-399, 1996
• A stable phage-display system using a phagemid vector: Phage display of hen egg-white lysozyme (HEL), Escherichia coli alkaline, phosphatase, and anti-HEL monoclonal antibody, HyHEL10
  K Maenaka; M Furuta; K Tsumoto; K Watanabe; Y Ueda; Kumagai, I, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 218, 3, 682, 687, Jan. 1996
  English
• Display of protease inhibitor on filamentous phage coat protein.
  津本浩平; 前仲勝実; 田口精一; 百瀬春生; 熊谷泉, 日本分子生物学会年会プログラム・講演要旨集, 18th, 524, Nov. 1995
  Japanese
• NK細胞受容体の繊維状ファージ表面への提示の試み
  前仲勝実; 西村元子; 斉藤彰一; 屋部登志雄; 田所憲治; 熊谷泉; 十字猛夫, 日本免疫学会総会・学術集会記録, 25, 424, Oct. 1995
  Japanese
• 安定なファージ提示系の開発と抗体工学への応用
  熊谷泉; 前仲勝実; 津本浩平, 日本免疫学会総会・学術集会記録, 25, 424, Oct. 1995
  Japanese
• B‐LCLを標的細胞として測定したNK細胞のアロ特異的細胞障害活性
  斉藤彰一; 西村元子; 前仲勝実; 屋部登志雄; 田所憲治; 十字猛夫, 日本免疫学会総会・学術集会記録, 25, 286, Oct. 1995
  Japanese
• Development of the stable phagemid pIII display system of proteins on the surface of the filamentous phage
  K Maenaka; K Tsumoto; Y Ueda; M Furuta; K Watanabe; Kumagai, I, PROTEIN ENGINEERING, 8, 9, 43, 43, Sep. 1995
  English, Summary international conference
• DISSECTION OF PROTEIN-CARBOHYDRATE INTERACTIONS IN MUTANT HEN EGG-WHITE LYSOZYME COMPLEXES AND THEIR HYDROLYTIC ACTIVITY
  K MAENAKA; M MATSUSHIMA; H SONG; F SUNADA; K WATANABE; KUMAGAI, I, JOURNAL OF MOLECULAR BIOLOGY, 247, 2, 281, 293, Mar. 1995
  English
• Development of the stable phagemid pIII display system of proteins on the surface of the filamentous phage
  Maenaka K; Tsumoto K; Ueda Y; Furuta M; Watanabe K; Kumagai I, Protein Eng., 9, 965, 1995
• STRUCTURAL-CHANGES OF ACTIVE-SITE CLEFT AND DIFFERENT SACCHARIDE BINDING MODES IN HUMAN LYSOZYME CO-CRYSTALLIZED WITH HEXA-N-ACETYL-CHITOHEXAOSE AT PH 4.0
  HW SONG; K INAKA; K MAENAKA; M MATSUSHIMA, JOURNAL OF MOLECULAR BIOLOGY, 244, 5, 522, 540, Dec. 1994
  English
• CONTRIBUTION TO ANTIBODY-ANTIGEN INTERACTION OF STRUCTURALLY PERTURBED ANTIGENIC RESIDUES UPON ANTIBODY-BINDING
  K TSUMOTO; Y UEDA; K MAENAKA; K WATANABE; K OGASAHARA; K YUTANI; KUMAGAI, I, JOURNAL OF BIOLOGICAL CHEMISTRY, 269, 46, 28777, 28782, Nov. 1994
  English
• Display of hen egg-white lysozyme on the surface of filamentous phage.
  前仲勝実; 津本浩平; 上田能孝; 渡辺公綱; 熊谷泉, 日本分子生物学会年会プログラム・講演要旨集, 17th, 394, Nov. 1994
  Japanese
• ニワトリ卵白リゾチームTrp62改変体の基質類似体との複合体のX線結晶解析
  前仲勝実; 松島正明; 宋海衛; 渡辺公綱; 熊谷泉, 日本蛋白工学会年会プログラム・要旨集, 6th, 10, May 1994
  Japanese
• FUNCTIONAL AND STRUCTURAL ROLE OF A TRYPTOPHAN GENERALLY OBSERVED IN PROTEIN-CARBOHYDRATE INTERACTION - TRP-62 OF HEN EGG-WHITE LYSOZYME
  K MAENAKA; G KAWAI; K WATANABE; F SUNADA; KUMAGAI, I, JOURNAL OF BIOLOGICAL CHEMISTRY, 269, 10, 7070, 7075, Mar. 1994
  English
• Special issue : New generation of protein crystallography.Present state and future of protein crystallography methodology.Progress of diffraction datum collection methods.More fast and more beautiful.
  松島 正明; 熊谷 泉; 前仲 勝実, Biophysics, 33, 6, 311, 313, 25 Nov. 1993
  記事分類: 物理学--分子・物性--結晶, 日本生物物理学会, Japanese
• Special issue : New generation of protein crystallography.Present state and future of protein crystallography methodology.Progress of diffraction datum collection methods.More fast and more beautiful.
  松島 正明; 熊谷 泉; 前仲 勝実, Seibutsu Butsuri, 33, 311-313, 6, 7, 9, 01 Nov. 1993
  記事分類: 物理学--分子・物性--結晶, The Biophysical Society of Japan General Incorporated Association, Japanese
• Functional analysis of c-type lysozyme by protein engineering
  Maenaka Katsumi; Kumagai Izumi, Biophysics, 33, 4, 219, 224, 25 Jul. 1993
  Protein engineering studies of the recombinant c-type lysozymes have provided incisive probes into the roles of individual amino acid residues in the enzymes. The amino acid replacements in the active site cleft of the lysozymes by site-directed mutagenesis and functional analyses of these mutant enzymes were summerized and discussed., 日本生物物理学会, Japanese
• EFFECTS OF SUBSITE ALTERATIONS ON SUBSTRATE-BINDING MODE IN THE ACTIVE-SITE OF HEN EGG-WHITE LYSOZYME
  KUMAGAI, I; K MAENAKA; F SUNADA; S TAKEDA; K MIURA, EUROPEAN JOURNAL OF BIOCHEMISTRY, 212, 1, 151, 156, Feb. 1993
  English
• Effects of subsite alterations on substrate‐binding mode in the active site of hen egg‐white lysozyme
  Izumi KUMAGAI; Katsumi MAENAKA; Futoshi SUNADA; Shigeki TAKEDA; Kin‐ichiro MIURA, European Journal of Biochemistry, 212, 1, 151, 156, 1993
  English
• REDESIGNING OF OLIGOSACCHARIDE BINDING-SITES OF HEN EGG-WHITE LYSOZYME AND A HOMOLOGOUS PROTEIN, ALPHA-LACTALBUMIN
  KUMAGAI, I; K MAENAKA; H UCHIYAMA; K WATANABE; K MIURA, PROTEIN ENGINEERING, 6, 99, 99, 1993
  English, Summary international conference
• Interaction between a recombinant Fv fragment and its antigen protein: Effect of structural conversions of the antigenic epitope
  Tsumoto K; Ueda Y; Maenaka K; Ogawawara K; Yutani K; Watanabe K; Kumagai I, Protein Eng., 7, 1010, 1993
• ニワトリリゾチームの基質結合部位の構造改変 機能変換とエピトーブ構造の解析
  熊谷泉; 前仲勝実; 上田能孝; 津本浩平; 河合剛太; 渡辺公綱; 三浦謹一郎, タンパク質構造討論会講演要旨集, 43rd, 73, 76, Sep. 1992
  Japanese
• ニワトリリゾチームTrp62改変体のNMRによる構造解析
  前仲勝実; 砂田太; 河合剛太; 渡辺公綱; 三浦謹一郎; 熊谷泉, 生体分子の構造と機能に関する討論会講演要旨集, 19th, 18, 19, Jul. 1992
  Japanese