博士（歯学）, The University of Osaka, Mar. 2024

構造活性相関

口腔外科

微生物学

X線結晶構造解析

量子化学

構造生物学

Life Science, Structural biochemistry

Life Science, Surgical dentistry

Life Science, Bacteriology

Oct. 2024, 両備檉園記念財団, 第46回 両備檉園記念財団 奨励賞
サングイニスレンサ球菌の線毛連結機構を基にした薬剤開発

Jul. 2024, 大阪大学 歯学会, 令和5年度 大阪大学歯学会 優秀研究奨励賞

Mar. 2024, 大阪大学, 令和5年度 研究科長賞（最優秀賞）

Apr. 2022, 口腔科学会, 第33回日本口腔科学会近畿地方部会 新人賞

Apr. 2022, 大阪大学, 令和3年度 研究科長賞（奨励賞)

Protein fractions associated with Prevotella intermedia suppress the growth of HSC-3 oral squamous cell carcinoma cells
Miyuki Kashiwabara; Machiko Kasai; Shintaro Nakano; Katsuki Takebe; Shiho Suzuki; Mariko Naito; Mikio Shoji; Ji-Won Lee; Tsukasa Akasaka; Yasuhiro Yoshida; Akira Hasebe; Yoichi Ohiro
Journal of Oral Biosciences, 68, 5, 100803, 100803, Elsevier BV, Oct. 2026, [Peer-reviewed]
English, Scientific journal

MetF‐Dependent Methionine Biosynthesis Is Required for Mycobacterium tuberculosis Survival and In Vivo Persistence
Ikue Tosa; Tomoki Kitahara; Katsuki Takebe; Masaaki Nakayama; Yuko Ito; Akihito Nishiyama; Shintaro Seto; Hotaka Kawai; Hiharu Inoue; Yuki Fukada; Yuki Nishiya; Hitoshi Nagatsuka; Takayuki Wada; Manabu Ato; Sohkichi Matsumoto; Naoya Ohara
MicrobiologyOpen, 15, 4, Wiley, 04 Aug. 2026, [Peer-reviewed]
English, Scientific journal, ABSTRACT

Methionine biosynthesis is essential for Mycobacterium tuberculosis , but the in vivo relevance of individual enzymes remains unclear. We performed transposon sequencing in Mycobacterium bovis BCG under methionine‐free conditions and identified metF as a major fitness determinant. To define enzyme‐specific functions, ΔmetE and ΔmetF mutants were generated in M. tuberculosis and evaluated using in vitro growth assays and a murine infection model. The ΔmetE mutant showed vitamin B ₁₂ ‐dependent growth in minimal medium but maintained normal growth in mice, indicating that its in vitro requirement does not translate to an in vivo defect. In contrast, ΔmetF exhibited strict methionine auxotrophy in vitro and completely failed to survive or persist in murine lungs and spleens. Structural modeling showed that MetF is distinct from human homologs, supporting selective inhibition. These findings demonstrate that MetF, but not MetE, is indispensable for M. tuberculosis survival in vivo and identify MetF as a promising metabolic drug target.

Bacterial collagenase harnesses collagen geometry for processive cleavage
Hiroya Oki; Katsuki Takebe; Adjoa Bonsu; Kazunori Fujii; Ryo Masuda; Nicholas Henderson; Takehiko Mima; Takaki Koide; Mahmoud Moradi; Osamu Matsushita; Joshua Sakon; Kazuki Kawahara
Nature Communications, Springer Science and Business Media LLC, 02 Apr. 2026, [Peer-reviewed]
English, Scientific journal, Abstract

Collagen, the major structural protein in the animal extracellular matrix, forms a triple helix that resists proteolysis and requires specialised enzymes for degradation. Flesh-eating bacteria secrete collagenases that unwind the collagen triple helix and processively trim Gly–X–Y triplet repeats, yet the molecular basis of this process has remained obscure. Here, cryo-electron microscopy reveals how  Hathewaya histolytica collagenase ColH engages its substrate and exploits the helix’s architecture for catalysis. ColH encircles a single collagen triple helix in a closed-ring conformation and, through dynamic domain motions, dehydrates and destabilises it. The enzyme undergoes substrate-assisted twisting to adopt a rigid ratcheted conformation, in which one chain is bent into a tripeptide-long ‘bight’ and threaded into the active site for cleavage, while two uncut strands are partitioned to non-catalytic sites. Release of the bight appears to reset the enzyme, with the uncut strands serving as guiding tracks. Repeated cycling between dynamic and rigid states likely enables triplet-by-triplet translocation, allowing ColH to harness collagen’s geometry for processive degradation. These findings reveal a bacterial strategy for collagen unwinding and cleavage distinct from that of mammalian collagenases, highlighting divergent evolutionary solutions for degrading one of nature’s most intractable substrates.

Insights into the taste of organic acids via TAS1Rs
Yuko Yamase; Katsuki Takebe; Kengo Horie; Yoshihiro Mitoh; Atsuko Yamashita; Ryusuke Yoshida
Journal of Oral Biosciences, 68, 1, 100731, 100731, Elsevier BV, Feb. 2026, [Peer-reviewed]
English, Scientific journal

Evaluation of Mycobacterium-derived plasmids for application in oral Actinomyces species
Sakiko Ohara; Yijuan Sheng; Yuki Nishiya; Ikue Tosa; Katsuki Takebe; Yuki Arimura; Hiroshi Mese; Naoko Ohara; Naoya Ohara
Journal of Oral Biosciences, 68, 1, 100718, 100718, Elsevier BV, Feb. 2026, [Peer-reviewed]
English, Scientific journal

MMP-3 cleavage of lamin a induces pro-migratory nuclear deformity, nucleophagy, and their autophagic secretion with extracellular vesicles in metastatic cancer.
Takanori Eguchi; Eman A Taha; Keisuke Nakano; Vikas Tiwari; Katsuki Takebe; Tomohiro Inoue; Lizi Xing; Chiharu Sogawa; Kuniaki Okamoto; Stuart K Calderwood
Cell communication and signaling : CCS, 15 Jan. 2026, [Peer-reviewed], [International Magazine]
English, Scientific journal

Calcium ions play a critical role in calcification of Corynebacterium matruchotii.
Naoko Ohara; Midori Ogawa; Katsuki Takebe; Ikue Tosa; Serina Ono; Mitsumasa Saito; Naoya Ohara
Scientific reports, 06 Jan. 2026, [Peer-reviewed], [International Magazine]
English, Scientific journal

PGN_0298 in the Assembly and Insertion Machinery (Aim) Operon Is Essential for the Viability of Porphyromonas gingivalis
Shintaro Ono; Katsuki Takebe; Ikue Tosa; Yuki Nishiya; Masaaki Nakayama; Takayuki Wada; Shogo Takashiba; Naoya Ohara
Microbiology and Immunology, Wiley, 02 Nov. 2025, [Peer-reviewed]
English, Scientific journal, ABSTRACT

Porphyromonas gingivalis is a typical periodontal pathogen, and one of its key virulence factors is the powerful protease gingipains. Gingipains are secreted via the type IX secretion system (T9SS) and are associated with the assembly and insertion machinery (Aim) operon (PGN_0296 to PGN_0301), which encodes both T9SS components and non‐T9SS proteins. In this study, we investigated PGN_0298, a gene of unknown function within this operon, to elucidate its role in P. gingivalis and to gain insights into its potential function through bioinformatics analyses. Our results demonstrated that PGN_0298 is essential for the viability of P. gingivalis , despite having limited direct association with T9SS. Sequence homology and structure predictions indicate that PGN_0298 encodes a putative isoprenyl transferase. The essentiality of PGN_0298 underscores its potential as a novel drug target for the treatment of periodontal disease., 46736003;47336923

Combined structural and FMO-based insights into shaft pilin polymerization mechanism in Streptococcus sanguinis.
Katsuki Takebe; Shuhei Miyakawa; Takeshi Sangawa; Mamoru Suzuki; Airi Matsumoto; Yuichi Oogai; Masaya Yamaguchi; Tomoko Sumitomo; Kaori Fukuzawa; Shigetada Kawabata; Masanobu Nakata
International journal of biological macromolecules, 148264, 148264, 12 Oct. 2025, [Peer-reviewed], [Lead author], [International Magazine]
English, Scientific journal, Bacterial pili are proteinaceous polymers that facilitate diverse biological functions. The SK36 strain of oral commensal bacterium Streptococcus sanguinis harbors sortase-assembled pili consisting of four proteins; PilA, PilB, PilC, and PilX. However, details regarding their structures and assembly mechanisms remain unclear. The crystal structures of recombinant PilA and PilB backbone pilins were examined at resolutions of 3.2 Å and 1.8 Å, respectively. Both exhibit a three-domain architecture (domains 1-3 from N- to C- terminus) with intramolecular isopeptide bonds in domains 2 and 3, and a positively charged, highly hydrophobic cleft in domain 1. Notably, while alignment along the same axis within the crystal was noted, their molecular orientations differ, as PilA maintains identical orientations (linear form), whereas PilB molecules are flipped 180° relative to each other (helical form). Both recognize the conserved ALLPNT sequence of domain 3 via the domain 1 cleft. Fragment molecular orbital calculations revealed no significant energetic differences between the linear and helical forms, with interactions predominantly mediated by C-terminal asparagine and threonine residues. Immunoblot analysis confirmed intermolecular isopeptide bond formation between threonine and conserved lysine residues at the domain 1-2 interface. The preceding glycine residue in the GALLPNT sequence may serve as a flexible pivot, enabling transitions between both forms. Since PilA, PilB, and PilC contain the GALLPNT sequence and could interconnect, the observations of domain 1-mediated recognition of the domain 3C-terminal region indicate a fundamental mechanism governing S. sanguinis pilus assembly. These findings provide molecular-based insight into sortase-mediated pilus biogenesis in Gram-positive bacteria., 49791674;49791788

Identification of PilX, pilus component of Streptococcus sanguinis
Li Yixuan; Masanobu Nakata; Hirono Migita; Airi Matsumoto; Yuichi Oogai; Katsuki Takebe; Masaya Yamaguchi; Nobuo Okahashi; Tomoko Sumitomo; Shigetada Kawabata
Journal of Oral Biosciences, 100664, 100664, Elsevier BV, Apr. 2025, [Peer-reviewed]
English, Scientific journal, 47336923

9型分泌装置の構造と歯周病原細菌の病原性における意義
武部克希
ファルマシア, 61, 3, 257, 257, Mar. 2025, [Peer-reviewed], [Lead author, Corresponding author]
Japanese

Herbal medicine Ninjinyoeito inhibits RANKL-induced osteoclast differentiation and bone resorption activity by regulating NF-kB and MAPK pathway
Kaung Htike; Kunihiro Yoshida; Takanori Eguchi; Katsuki Takebe; Xueming Li; Yaxin Qu; Eiko Sakai; Takayuki Tsukuba; Kuniaki Okamoto
Journal of Oral Biosciences, Elsevier BV, Oct. 2024, [Peer-reviewed]
English, Scientific journal

New Catalytic Residues and Catalytic Mechanism of the RNase T1 Family
Katsuki Takebe; Mamoru Suzuki; Yumiko Hara; Takuya Katsutani; Naomi Motoyoshi; Tadashi Itagaki; Shuhei Miyakawa; Kuniaki Okamoto; Kaori Fukuzawa; Hiroko Kobayashi
ACS Bio & Med Chem Au, American Chemical Society (ACS), 20 Sep. 2024, [Peer-reviewed], [Lead author]
English, Scientific journal

Identification of the Acidification Mechanism of the Optimal pH for RNase He1
Katsuki Takebe; Mamoru Suzuki; Takeshi Sangawa; Naomi Motoyoshi; Tadashi Itagaki; Kana Kashima; Narikazu Uzawa; Hiroko Kobayashi
Biological and Pharmaceutical Bulletin, 46, 12, 1778, 1786, Pharmaceutical Society of Japan, 01 Dec. 2023, [Peer-reviewed], [Lead author]
English, Scientific journal

Analysis of FctB3 crystal structure and insight into its structural stabilization and pilin linkage mechanisms
Katsuki Takebe; Mamoru Suzuki; Takeshi Sangawa; Bernd Kreikemeyer; Masaya Yamaguchi; Narikazu Uzawa; Tomoko Sumitomo; Shigetada Kawabata; Masanobu Nakata
Archives of Microbiology, 206, 1, Springer Science and Business Media LLC, 23 Nov. 2023, [Peer-reviewed], [Lead author]
Scientific journal

Reconstruction of the lower lip after resection of its venous malformation using a labial mucosal advancement flap – A case report-
Yoshio Ueno; Kazuhide Matsunaga; Akinori Takeshita; Akari Teramoto; Katsuki Takebe; Hitomi Kajikawa; Yoshihiro Morita; Narikazu Uzawa
Journal of Oral and Maxillofacial Surgery, Medicine, and Pathology, 35, 6, 513, 517, Elsevier BV, Nov. 2023, [Peer-reviewed]
Scientific journal

Structural and Computational Analyses of the Unique Interactions of Opicapone in the Binding Pocket of Catechol O-Methyltransferase: A Crystallographic Study and Fragment Molecular Orbital Analyses
Katsuki Takebe; Mamoru Suzuki; Takao Kuwada-Kusunose; Satoko Shirai; Kaori Fukuzawa; Tomoko Takamiya; Narikazu Uzawa; Hiroshi Iijima
Journal of Chemical Information and Modeling, 63, 14, 4468, 4476, American Chemical Society (ACS), 12 Jul. 2023, [Peer-reviewed], [Lead author]
Scientific journal

Deep learning model for the automated evaluation of contact between the lower third molar and inferior alveolar nerve on panoramic radiography
Katsuki Takebe; Tomoaki Imai; Seiko Kubota; Ayano Nishimoto; Shigeki Amekawa; Narikazu Uzawa
Journal of Dental Sciences, 18, 3, 991, 996, Elsevier BV, Jul. 2023, [Peer-reviewed], [Lead author]
Scientific journal

GATA6 regulates expression of annexin A10 (ANXA10) associated with epithelial–mesenchymal transition of oral squamous cell carcinoma
Shun Takayama; Yoshihiro Morita; Ayano Nishimoto; Junya Nishimura; Katsuki Takebe; Satoko Kishimoto; Yuka Matsumiya-Matsumoto; Kazuhide Matsunaga; Tomoaki Imai; Narikazu Uzawa
Archives of Oral Biology, 144, 105569, 105569, Elsevier BV, Dec. 2022, [Peer-reviewed]
Scientific journal

Novel Functional Peptide for Next-Generation Vital Pulp Therapy
M. Watanabe; M. Okamoto; S. Komichi; H. Huang; S. Matsumoto; K. Moriyama; J. Ohshima; S. Abe; M. Morita; M. Ali; K. Takebe; I. Kozaki; A. Fujimoto; K. Kanie; R. Kato; K. Uto; M. Ebara; A. Yamawaki-Ogata; Y. Narita; Y. Takahashi; M. Hayashi
Journal of Dental Research, 102, 3, 322, 330, SAGE Publications, 22 Nov. 2022, [Peer-reviewed]
Scientific journal, Although vital pulp therapy should be performed by promoting the wound-healing capacity of dental pulp, existing pulp-capping materials were not developed with a focus on the pulpal repair process. In previous investigations of wound healing in dental pulp, we found that organic dentin matrix components (DMCs) were degraded by matrix metalloproteinase-20, and DMC degradation products containing protein S100A7 (S100A7) and protein S100A8 (S100A8) promoted the pulpal wound-healing process. However, the direct use of recombinant proteins as pulp-capping materials may cause clinical problems or lead to high medical costs. Thus, we hypothesized that functional peptides derived from recombinant proteins could solve the problems associated with direct use of such proteins. In this study, we identified functional peptides derived from the protein S100 family and investigated their effects on dental pulp tissue. We first performed amino acid sequence alignments of protein S100 family members from several mammalian sources, then identified candidate peptides. Next, we used a peptide array method that involved human dental pulp stem cells (hDPSCs) to evaluate the mineralization-inducing ability of each peptide. Our results supported the selection of 4 candidate functional peptides derived from proteins S100A8 and S100A9. Direct pulp-capping experiments in a rat model demonstrated that 1 S100A8-derived peptide induced greater tertiary dentin formation compared with the other peptides. To investigate the mechanism underlying this induction effect, we performed liquid chromatography–tandem mass spectrometry analysis using hDPSCs and the S100A8-derived peptide; the results suggested that this peptide promotes tertiary dentin formation by inhibiting inflammatory responses. In addition, this peptide was located in a hairpin region on the surface of S100A8 and could function by direct interaction with other molecules. In summary, this study demonstrated that a S100A8-derived functional peptide promoted wound healing in dental pulp; our findings provide insights for the development of next-generation biological vital pulp therapies.

Biofilm Spreading by the Adhesin-Dependent Gliding Motility of Flavobacterium johnsoniae: 2. Role of Filamentous Extracellular Network and Cell-to-Cell Connections at the Biofilm Surface
Keiko Sato; Masami Naya; Yuri Hatano; Naoki Kasahata; Yoshio Kondo; Mari Sato; Katsuki Takebe; Mariko Naito; Chikara Sato
International Journal of Molecular Sciences, 22, 13, 6911, 6911, MDPI AG, 27 Jun. 2021, [Peer-reviewed]
Scientific journal, Flavobacterium johnsoniae forms a thin spreading colony on nutrient-poor agar using gliding motility. As reported in the first paper, WT cells in the colony were sparsely embedded in self-produced extracellular polymeric matrix (EPM), while sprB cells were densely packed in immature biofilm with less matrix. The colony surface is critical for antibiotic resistance and cell survival. We have now developed the Grid Stamp-Peel method whereby the colony surface is attached to a TEM grid for negative-staining microscopy. The images showed that the top of the spreading convex WT colonies was covered by EPM with few interspersed cells. Cells exposed near the colony edge made head-to-tail and/or side-to-side contact and sometimes connected via thin filaments. Nonspreading sprB and gldG and gldK colonies had a more uniform upper surface covered by different EPMs including vesicles and filaments. The EPM of sprB, gldG, and WT colonies contained filaments ~2 nm and ~5 nm in diameter; gldK colonies did not include the latter. Every cell near the edge of WT colonies had one or two dark spots, while cells inside WT colonies and cells in SprB-, GldG-, or GldK-deficient colonies did not. Together, our results suggest that the colony surface structure depends on the capability to expand biofilm.

Crystal structure of the C-terminal domain of envelope protein VP37 from white spot syndrome virus reveals sulphate binding sites responsible for heparin binding
Wasusit Somsoros; Takeshi Sangawa; Katsuki Takebe; Jakrada Attarataya; Kanokpan Wongprasert; Saengchan Senapin; Triwit Rattanarojpong; Mamoru Suzuki; Pongsak Khunrae
Journal of General Virology, 102, 6, Microbiology Society, 01 Jun. 2021, [Peer-reviewed]
Scientific journal, White spot syndrome virus (WSSV) is the most virulent pathogen causing high mortality and economic loss in shrimp aquaculture and various crustaceans. Therefore, the understanding of molecular mechanisms of WSSV infection is important to develop effective therapeutics to control the spread of this viral disease. In a previous study, we found that VP37 could bind with shrimp haemocytes through the interaction between its C-terminal domain and heparin-like molecules on the shrimp cells, and this interaction can also be inhibited by sulphated galactan. In this study, we present the crystal structure of C-terminal domain of VP37 from WSSV at a resolution of 2.51 Å. The crystal structure contains an eight-stranded β-barrel fold with an antiparallel arrangement and reveals a trimeric assembly. Moreover, there are two sulphate binding sites found in the position corresponding to R213 and K257. In order to determine whether these sulphate binding sites are involved in binding of VP37 to heparin, mutagenesis was performed to replace these residues with alanine (R213A and K257A), and the Surface Plasmon Resonance (SPR) system was used to study the interaction of each mutated VP37 with heparin. The results showed that mutants R213A and K257A exhibited a significant loss in heparin binding activity. These findings indicated that the sites of R213 and K257 on the C-terminal domain of envelope protein VP37 are essential for binding to sulphate molecules of heparin. This study provides further insight into the structure of C-terminal domain of VP37 and it is anticipated that the structure of VP37 might be used as a guideline for development of antivirus agent targeting on the VP37 protein.

Crystal Structure of Catechol -O-Methyltransferase Complexed with Nitecapone
Hiroshi Iijima; Katsuki Takebe; Mamoru Suzuki; Hiroko Kobayashi; Tomoko Takamiya; Hiroaki Saito; Norio Niwa; Takao Kuwada-Kusunose
Chemical and Pharmaceutical Bulletin, 68, 5, 447, 451, Pharmaceutical Society of Japan, 01 May 2020, [Peer-reviewed]
Scientific journal

X-Ray Crystallographic Structure of Hericium erinaceus Ribonuclease, RNase He1 in Complex with Zinc
Hiroko Kobayashi; Takeshi Sangawa; Katsuki Takebe; Naomi Motoyoshi; Tadashi Itagaki; Mamoru Suzuki
Biological and Pharmaceutical Bulletin, 42, 12, 2054, 2061, Pharmaceutical Society of Japan, 01 Dec. 2019, [Peer-reviewed]
Scientific journal

Immunoglobulin‐like domains of the cargo proteins are essential for protein stability during secretion by the type IX secretion system
Keiko Sato; Shinji Kakuda; Hideharu Yukitake; Yoshio Kondo; Mikio Shoji; Katsuki Takebe; Yuka Narita; Mariko Naito; Daisuke Nakane; Yoshimitsu Abiko; Koichi Hiratsuka; Mamoru Suzuki; Koji Nakayama
Molecular Microbiology, 110, 1, 64, 81, Wiley, 04 Oct. 2018, [Peer-reviewed]
Scientific journal, Summary

The periodontal pathogen Porphyromonas gingivalis secretes many potent virulence factors using the type IX secretion system (T9SS). T9SS cargo proteins that have been structurally determined by X‐ray crystallography are composed of a signal peptide, functional domain(s), an immunoglobulin (Ig)‐like domain and a C‐terminal domain. Role of the Ig‐like domains of cargo proteins in the T9SS has not been elucidated. Gingipain proteases, which are cargo proteins of the T9SS, were degraded when their Ig‐like domains were lacking or truncated. The degradation was dependent on the activity of a quality control factor, HtrA protease. Another T9SS cargo protein, HBP35, which has a thioredoxin domain as a functional domain, was analyzed by X‐ray crystallography, revealing that HBP35 has an Ig‐like domain after the thioredoxin domain and that the hydrophobic regions of the thioredoxin domain and the Ig‐like domain face each other. HBP35 with substitution of hydrophobic amino acids in the Ig‐like domain was degraded depending on HtrA. These results suggest that the Ig‐like domain mediates stability of the cargo proteins in the T9SS.

Structural analysis of inactive hyaluronidase of Streptococcus pyogenes
山口 雅也; 東 孝太郎; 武部 克希; 中田 匡宣; 住友 倫子; 川端 重忠, 日本細菌学雑誌, 79, 2, 268, 268, Jul. 2024
日本細菌学会, English

Porphyromonas gingivalis新規オペロンに存在するOmp様タンパク質の構造解析と役割
CHEN Yujiang; 武部克希; 佐藤啓子; 中山真彰; 加島佳奈; ZHANG Mingzheng; 岡元邦彰; 門脇知子; 大原直也; 大原直也, Journal of Oral Biosciences Supplement (Web), 2024, 2024

Identification of drugs with anticancer activity in acidic environment by drug repositioning
千田正; 武部克希; 武部克希; 鵜澤成一, 日本口腔科学会学術集会プログラム・抄録集, 78th, 2024

Structure and antitumor activity of 12-residue variants of RNase He1 derived from Yamabushitake mushrooms.
小林弘子; 武部克希; 千田正; 元吉尚美; 板垣正; 鵜澤成一; 鈴木守, 日本薬学会年会要旨集(Web), 144th, 2024

Reaction mechanism of COMT and conformational changes induced by enhancer molecules.
武部克希; 桑田(楠瀬)隆生; 鈴木守; 飯島洋; 飯島洋, 日本薬学会年会要旨集(Web), 144th, 2024

COMT-Ligand Molecular Interactions Based on Crystal Structures and Quantum Chemical Calculations
福澤薫; 白井智子; 武部克希; 高谷大輔; 飯島洋; 飯島洋, 日本薬学会年会要旨集(Web), 144th, 2024

Streptococcus sanguinisが産生する線毛タンパク質のX線結晶構造解析
武部 克希; 鈴木 守; 東 孝太郎; 山口 雅也; 住友 倫子; 川端 重忠; 中田 匡宣, Journal of Oral Biosciences Supplement, 2023, [P1, 25], Sep. 2023
(一社)歯科基礎医学会, Japanese

パノラマX線画像における下顎智歯-下歯槽管頬舌的位置関係の自動判定深層学習モデル構築の試み
桂 尚[渕端]; 武部 克希; 窪田 星子; 西元 彩乃; 今井 智章; 鵜澤 成一, 日本口腔科学会雑誌, 72, 2, 89, 89, Jul. 2023
(NPO)日本口腔科学会, Japanese

A study of the effectiveness of preoperative PCE chemotherapy for resectable oral cancer
竹下彰範; 松永和秀; 森田祥弘; 松宮由香; 梶川ひとみ; 西元彩乃; 武部克希; 千田正; 柏木孝文; 加島佳奈; 紀之定紘子; 芝原巧; 菊池菫; 鵜澤成一, 日本口腔腫瘍学会総会・学術大会プログラム・抄録集, 41st, 2023

ヤマブシタケ由来RNase He1改変体のX線構造解析と抗腫瘍活性
武部克希; 千田正; 森田祥弘; 西村遵也; 西元彩乃; 鵜澤成一; 小林弘子, 日本口腔科学会学術集会プログラム・抄録集, 77th, 2023

Conformational plasticity of catechol O-methyltransferase.
飯島洋; 武部克希; 鈴木守; 桑田(楠瀬)隆生; 高宮知子; 鵜澤成一, 日本薬学会年会要旨集(Web), 143rd, 2023

Investigation of amino acid residues involved in the optimum pH of RNase He1 from Yamabushitake
小林弘子; 武部克希; 元吉尚美; 板垣正; 鵜澤成一; 鈴木守, 日本薬学会年会要旨集(Web), 143rd, 2023

Labial mucosal advancement flapを用いて口唇再建を行った下唇血管腫の1例
寺本 朱里; 上野 祥夫; 松永 和秀; 竹下 彰範; 武部 克希; 梶川 ひとみ; 鵜澤 成一, 日本口腔科学会雑誌, 71, 2, 100, 101, Jul. 2022
(NPO)日本口腔科学会, Japanese

X-Ray Crystallographic Structure of RNase He1 in Complex with guanosine from Hericium erinaceus (Yamabushitake)
小林弘子; 寒川剛; 武部克希; 元吉尚美; 板垣正; 鵜澤成一; 鈴木守, 日本薬学会年会要旨集(Web), 142年会, 28PO5, 01, Mar. 2022
(公社)日本薬学会, Japanese

Correspondence to postoperative recurrence and metastasis high risk cases in our department
竹下彰範; 松永和秀; 加藤逸郎; 今井智章; 森田祥弘; 松宮由香; 千田正; 梶川ひとみ; 武部克希; 鵜澤成一, 日本口腔腫瘍学会総会・学術大会プログラム・抄録集, 40th, 2022

Enhancement of COMT reaction by an enhancer compound: A crystallographic study.
飯島洋; 武部克希; 桑田(楠瀬)隆生; 鈴木守; 高宮知子; 鵜澤成一, 日本薬学会年会要旨集(Web), 142nd, 2022

Crystal structures of COMT-opicapone complex: opicapone can form stable complexes either with SAM(substrate) and SAH(Product)
武部克希; 桑田(楠瀬)隆夫; 鈴木守; 高宮知子; 鵜澤成一; 飯島洋, 日本薬学会年会要旨集(Web), 142nd, 2022

パノラマX線画像における下顎智歯と下歯槽管接触の自動判定深層学習モデルの構築
武部克希; 今井智章; 窪田星子; 窪田星子; 西元彩乃; 鵜澤成一, 日本口腔科学会雑誌(Web), 71, 1, 2022

化膿レンサ球菌の不活性型ヒアルロン酸分解酵素の結晶構造解析と活性型変異体の構造予測(Structural analysis of Streptococcus pyogenes hyaluronidase and in silico analysis based on structural models)
東 孝太郎; 山口 雅也; 中田 匡宣; 武部 克希; 住友 倫子; 鈴木 守; 川端 重忠, Journal of Oral Biosciences Supplement, 2021, 181, 181, Oct. 2021
(一社)歯科基礎医学会, Japanese

口腔癌の術前末梢血単核細胞を用いた腫瘍浸潤リンパ球のフェノタイプ予測
梶川 ひとみ; 武部 克希; 松永 和秀; 鵜澤 成一, 日本口腔科学会雑誌, 70, 2, 145, 145, Jul. 2021
(NPO)日本口腔科学会, Japanese

口腔扁平上皮癌における腫瘍内T細胞と腫瘍浸潤様式の関連性
梶川 ひとみ; 武部 克希; 松永 和秀; 鵜澤 成一, 頭頸部癌, 47, 2, 227, 227, May 2021
(一社)日本頭頸部癌学会, Japanese

口腔扁平上皮癌における腫瘍浸潤様式と腫瘍免疫学的因子の関連性の検討
梶川 ひとみ; 武部 克希; 松永 和秀; 鵜澤 成一; 和田 尚, 日本がん免疫学会総会プログラム・抄録集, 25回, 111, 111, May 2021
日本がん免疫学会, Japanese

微生物の分子論(遺伝子・タンパク質・情報伝達・代謝・各種オミクス等) 結晶構造解析に基づく化膿レンサ球菌におけるヒアルロン酸分解酵素の分子機構解明
東 孝太郎; 山口 雅也; 中田 匡宣; 武部 克希; 住友 倫子; 鈴木 守; 川端 重忠, 日本細菌学雑誌, 76, 1, 53, 53, Feb. 2021
日本細菌学会, Japanese

抗菌薬標的タンパク質の生化学 歯周病細菌叢の病原性を抑える試み
佐藤 啓子; 納屋 昌実; 近藤 好夫; 武部 克希; 内藤 真理子; 鈴木 守; 今田 勝巳; 石川 岳志; 佐藤 主税, 日本細菌学雑誌, 76, 1, 40, 40, Feb. 2021
日本細菌学会, Japanese

Activated regulatory T cells correlates with mode of invasion in oral squamous cell carcinoma
梶川ひとみ; 武部克希; 松永和秀; 鵜澤成一, 日本口腔腫瘍学会総会・学術大会プログラム・抄録集, 39th, 2021

Structural analysis of Streptococcus pyogenes hyaluronidase and in silico analysis based on structural models
東孝太郎; 山口雅也; 中田匡宣; 武部克希; 住友倫子; 鈴木守; 川端重忠, Journal of Oral Biosciences Supplement (Web), 2021, 2021

COMTと阻害剤の相互作用における官能基の寄与のFMO法による評価
白井智子; 山本亜美; 古石誉之; 米持悦生; 武部克希; 鵜澤成一; 飯島洋; 福澤薫, 構造活性相関シンポジウム講演要旨集(CD-ROM), 49th, 2021

FMO法によるCOMTと阻害剤の相互作用におけるニトロ基の寄与の評価
白井智子; 山本亜美; 古石誉之; 米持悦生; 武部克希; 飯島洋; 福澤薫, 日本薬学会関東支部大会講演要旨集(CD-ROM), 65th, 2021

Crystal structure of COMT/nitecapone complex and a suggestion for design of non-nitrocatechol type inhibitor.
天野雅之; 武部克希; 鈴木守; 楠瀬隆生; 松本和樹; 茂庭歩美; 小林弘子; 齋藤弘明; 高宮知子; 丹羽典朗; 飯島洋, 日本薬学会年会要旨集(Web), 140年会, 28K, pm05S, Mar. 2020
(公社)日本薬学会, Japanese

COMT/阻害剤複合体の結晶構造解析及び,量子化学計算による相互作用解析
武部克希; 福澤薫; 鈴木守; 桑田(楠瀬)隆生; 鵜澤成一; 飯島洋, 構造活性相関シンポジウム講演要旨集(CD-ROM), 48th, 2020

9型分泌装置分泌タンパク質のImmunoglobulin-like domainsは細胞内構造安定性に関与する
佐藤啓子; 角田真二; 武部克希; 鈴木守, KEK Progress Report (Web), 2019-7, 2019

化膿レンサ球菌におけるヒアルロン酸分解酵素の分子系統解析およびタンパク質構造解析
東 孝太郎; 武部 克希; 山口 雅也; 住友 倫子; 中田 匡宣; 鈴木 守; 川端 重忠, Journal of Oral Biosciences Supplement, 2018, 351, 351, Sep. 2018
(一社)歯科基礎医学会, Japanese

Streptococcus sanguinisが産生するSrtCのX線結晶構造
武部克希; 中田匡宣; 川端重忠; 鈴木守, 日本結晶学会年会講演要旨集, 2018, 2018

化膿レンサ球菌におけるヒアルロン酸分解酵素の分子系統解析およびタンパク質構造解析
東孝太郎; 武部克希; 山口雅也; 住友倫子; 中田匡宣; 鈴木守; 川端重忠, Journal of Oral Biosciences Supplement (Web), 2018, 2018

ヤマブシタケ由来RNase He1のZn複合体のX線構造解析
小林 弘子; 元吉 尚美; 板垣 正; 武部 克希; 寒川 剛; 鈴木 守, 日本薬学会年会要旨集, 137年会, 3, 129, 129, Mar. 2017
(公社)日本薬学会, Japanese

M3型化膿レンサ球菌が産生する線毛タンパク質FctA3の結晶構造解析
寒川剛; 武部克希; 中田匡宣; 川端重忠; 鈴木守, 日本結晶学会年会講演要旨集, 2016, 2016

細胞接着因子Nectin-1/3ヘテロ複合体の立体構造解析
寒川剛; 武部克希; 勝谷拓也; 鈴木守, 日本蛋白質科学会年会プログラム・要旨集, 16th, 2016

細胞接着因子ネクチンのヘテロ複合体の結晶構造解析
寒川剛; 武部克希; 勝谷拓也; 鈴木守, 日本結晶学会年会講演要旨集, 2015, 2015

X線構造解析を基軸とした 微生物タンパク質の構造及び機能解析
武部 克希; 宮川 柊兵; 小林 弘子; 中田 匡宣
日本細菌学会 総会, 22 Mar. 2026, Japanese, Public symposium
20 Mar. 2026 - 22 Mar. 2026, [Invited]

構造生物学の手法と CCN2 の結晶化
武部克希; 青山絵理子; 滝川正春
第 16 回日本 CCN ファミリー研究会, 02 Sep. 2025, Japanese, Nominated symposium
02 Sep. 2025 - 02 Sep. 2025, 50122301, [Invited]

構造生物学に基づいた歯周病菌に存在するシャペロン様タンパク 質の機能解明
武部 克希; 佐藤 啓子; 宮川 柊兵; 土佐 郁恵; Yujiang Chen; 加島 佳奈; 大原 直也
第98回日本細菌学会総会, 30 May 2025, Japanese
29 May 2025 - 31 May 2025, 46736003

細菌性コラゲナーゼの基質ほぐし及び切断機構について
武部 克希; 美間 健彦; 沖 大也; 河原 一樹; 松下 治
第77回日本細菌学会中国・四国支部総会, 06 Oct. 2024
05 Oct. 2024 - 06 Oct. 2024

COMT(カテコール-O-メチル基転移酵素)阻害剤の複合体 X 線結晶構造解析 及び、FMO(Fragment molecular orbital)法を用いた活性中心における 相互作用評価
武部克希
大阪大学歯学会 第 137 回例会 優秀研究奨励賞 受賞講演, 25 Jul. 2024
25 Jul. 2024, [Invited]

RNase T1ファミリーの新規触媒残基および、RNase活性と抗腫瘍活性の関係性
武部 克希; 宮川 柊兵; 原 由美子; 鈴木 守; 板垣 正; 元吉 尚美; 福澤 薫; 岡元 邦彰; 小林 弘子
第41回創薬・薬理フォーラム岡山, Japanese
20 Jul. 2024 - 20 Jul. 2024

COMTの反応機構と賦活化物質による立体構造変化
武部 克希; 桑田-楠瀬 隆生; 鈴木 守; 飯島 洋
日本薬学会第144回, 30 Mar. 2024
28 Mar. 2024 - 31 Mar. 2024, [Invited]

パノラマ X 線画像における下顎智歯-下歯槽管接触関係の自動判定深層学習モデル構築の試み
武部克希; 西元彩乃; 桂(渕端)尚; 窪田星子; 今井智章; 鵜澤成一
.第68回 日本口腔外科学会 総会, 10 Nov. 2023

Streptococcus sanguinis が産生する線毛タンパク質のX線結晶構造解析
武部 克希; 鈴木 守; 東 孝太郎; 山口 雅也; 住友 倫子; 川端 重忠; 中田 匡宣
第65回歯科基礎医学会, 16 Sep. 2023

ヤマブシタケ由来 RNase He1 改変体のX 線構造解析と抗腫瘍活性
武部克希; 千田正; 森田祥弘; 西村遵也; 西元彩乃; 鵜澤成一; 小林弘子
第77回 日本口腔科学会, May 2023

Investigation of hydrogen bond network in the active center of catechol O-methyltransferase by X-ray crystallography and FMO method
Katsuki Takebe; Tomoko Shirai; Yuma Handa; Kaori Fukuzawa; Mamoru Suzuki; Takao Kuwada-Kusunose; Tokomo Takamiya; Narikazu Uzawa; Hiroshi Iijima
CBI学会2022年大会, Oct. 2022

パノラマ X 線画像における下顎智歯-下歯槽管接触関係の自動判定深層学習モデル構築の試み.
武部 克希; 今井 智章; 窪田 星子; 西元 彩乃; 鵜澤 成一
第76回 日本口腔科学会, Apr. 2022
[Invited]

COMT（カテコールO-メチル基転移酵素）-新規阻害剤の複合体の構造解析: Opicaponeは基質（SAM）、生成物（SAH）とも安定な複合体を形成する
武部克希; 桑田(楠瀬) 隆夫; 鈴木 守; 高宮 知子; 鵜澤 成一; 飯島 洋
日本薬学会第142年会, 27 Mar. 2022

パノラマX線画像における下顎智歯と下歯槽管接触の自動判定深層学習モデルの構築
武部克希; 今井智章; 西元彩乃; 窪田星子; 鵜澤成一
第33回日本口腔科学会近畿地方会, 06 Dec. 2021

COMT/阻害剤複合体の結晶構造解析及び、量子化学計算による相互作用解析
武部克希; 福澤薫; 鈴木守; 楠瀬隆生; 鵜澤成一; 飯島洋
第48 回構造活性相関シンポジウム, 10 Dec. 2020

Jan. 2023 - Present
口腔科学会

Nov. 2021 - Present
日本薬学会

Aug. 2019 - Present
日本口腔外科学会

May 2018 - Present
歯科基礎医学会

Aug. 2015 - Present
日本結晶学会

Transgelinの骨組織新規メカノ応答分子としての役割
科学研究費助成事業
Apr. 2026 - Mar. 2029
池亀 美華
日本学術振興会, 基盤研究(C), 岡山大学, 26K12601

膜タンパク質RELTのリガンド同定と構造解析によるエナメル質形成不全症の病態解明
科学研究費助成事業
Apr. 2026 - Mar. 2029
池田 淳史
日本学術振興会, 基盤研究(C), 岡山大学, Coinvestigator, 26K12903

歯周病原細菌P. gingivalisにおける，BamA類似タンパクの機能および病原性の解明
科学研究費助成事業
Apr. 2026 - Mar. 2029
小野 晋太郎
日本学術振興会, 基盤研究(C), 岡山大学, Coinvestigator, 26K12634

軟骨成長・アンチエイジング因子CCN2の健康維持への応用に向けた分子基盤の解明
科学研究費助成事業
Apr. 2025 - Mar. 2028
滝川 正春
日本学術振興会, 基盤研究(B), 岡山大学, Coinvestigator, 25K03047

歯周病細菌主要病原因子ジンジパインの宿主直接作用と必須新奇オペロンの解明
科学研究費助成事業
Apr. 2024 - Mar. 2028
大原 直也
日本学術振興会, 基盤研究(B), 岡山大学, 24K02614

膜ダイナミクスをターゲットとしたがん骨転移ニッチモデルと病態制御機構の開発
科学研究費助成事業
Apr. 2024 - Mar. 2027
岡元 邦彰
日本学術振興会, 基盤研究(C), 岡山大学, 24K13239

Roles of cancer extracellular vesicles in hijacking macrophages and metastatic niche formation
Grants-in-Aid for Scientific Research
01 Apr. 2023 - 31 Mar. 2026
江口 傑徳; 高橋 賢; 河合 穂高; 岡元 邦彰; 冨樫 庸介; 武部 克希
Japan Society for the Promotion of Science, Grant-in-Aid for Scientific Research (B), Okayama University, 23K28000

レンサ球菌線毛先端蛋白質の構造解析に立脚した細胞付着機構の解明及び感染制御創薬
科学研究費助成事業
Apr. 2025 - Mar. 2026
武部 克希
日本学術振興会, 若手研究, Principal investigator, 25K20246

サングイニスレンサ球菌の線毛連結機構の解明及び、連結阻害に基づく感染制御の創薬
科学研究費助成事業
Jul. 2024 - Mar. 2026
武部 克希
日本学術振興会, 研究活動スタート支援, 岡山大学, Principal investigator, 24K23551

サングイニスレンサ球菌の線毛連結機構を基にした薬剤開発
Oct. 2024
武部 克希
両備檉園記念財団, 第46回 両備檉園記念財団 奨励賞, 両備檉園記念財団, Principal investigator

病原細菌がコラーゲンを壊すしくみを発見！「移植再生医療」や「新薬開発」への応用に期待【岡山大学】
21 Apr. 2026
Other than myself
RSK山陽放送
[Media report]

組織侵襲性細菌が組織を壊す仕組みを解明 移植再生医療に応用の可能性も
Apr. 2026
KSB瀬戸内海放送
[Paper]

組織侵襲性細菌が組織を壊す仕組みを解明！ ～移植再生医療に応用の可能性～
北海道大学
[Internet]