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武部　克希 (タケベ　カツキ)

歯学研究院　口腔医学部門　口腔病態学分野講師

研究者基本情報

■ 学位
  • 博士（歯学）, 大阪大学, 2024年03月
■ URL
researchmap URLホームページURL■ ID 各種
研究者番号
  • 61000104
J-Global ID■ 研究キーワード・分野
研究キーワード
  • 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
研究分野
  • ライフサイエンス, 構造生物化学
  • ライフサイエンス, 外科系歯学
  • ライフサイエンス, 細菌学

経歴

■ 経歴
経歴
  • 2026年04月 - 現在
    北海道大学, 大学院歯学研究院 口腔医学専攻 口腔病態学講座 微生物学教室, 講師
  • 2024年04月 - 2026年03月
    岡山大学, 学術研究院医歯薬学域 歯科薬理学分野, 助教
  • 2020年04月 - 2024年03月
    大阪大学, 大学院歯学研究科顎口腔腫瘍学講座, 院生医員
学歴
  • 2020年04月 - 2024年03月, 大阪大学, 大学院歯学研究科, 口腔科学専攻, 日本国
  • 2013年04月 - 2019年03月, 大阪大学, 歯学部, 歯学科, 日本国

研究活動情報

■ 受賞
  • 2024年10月, 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
  • 2024年07月, 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
  • 2024年03月, 大阪大学, 令和5年度 研究科長賞（最優秀賞）
  • 2022年04月, 口腔科学会, 第33回日本口腔科学会近畿地方部会 新人賞
  • 2022年04月, 大阪大学, 令和3年度 研究科長賞（奨励賞)
■ 論文
  • 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, 2026年10月, ［査読有り］
    英語, 研究論文（学術雑誌）
  • 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, 2026年08月04日, ［査読有り］
    英語, 研究論文（学術雑誌）, 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, 2026年04月02日, ［査読有り］
    英語, 研究論文（学術雑誌）, 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, 2026年02月, ［査読有り］
    英語, 研究論文（学術雑誌）
  • 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, 2026年02月, ［査読有り］
    英語, 研究論文（学術雑誌）
  • 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, 2026年01月15日, ［査読有り］, ［国際誌］
    英語, 研究論文（学術雑誌）
  • 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, 2026年01月06日, ［査読有り］, ［国際誌］
    英語, 研究論文（学術雑誌）
  • 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, 2025年11月02日, ［査読有り］
    英語, 研究論文（学術雑誌）, 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, 2025年10月12日, ［査読有り］, ［筆頭著者］, ［国際誌］
    英語, 研究論文（学術雑誌）, 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, 2025年04月, ［査読有り］
    英語, 研究論文（学術雑誌）, 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, 2025年03月, ［査読有り］, ［筆頭著者, 責任著者］
    日本語
  • 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, 2024年10月, ［査読有り］
    英語, 研究論文（学術雑誌）
  • 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), 2024年09月20日, ［査読有り］, ［筆頭著者］
    英語, 研究論文（学術雑誌）
  • 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, 2023年12月01日, ［査読有り］, ［筆頭著者］
    英語, 研究論文（学術雑誌）
  • 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, 2023年11月23日, ［査読有り］, ［筆頭著者］
    研究論文（学術雑誌）
  • 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, 2023年11月, ［査読有り］
    研究論文（学術雑誌）
  • 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), 2023年07月12日, ［査読有り］, ［筆頭著者］
    研究論文（学術雑誌）
  • 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, 2023年07月, ［査読有り］, ［筆頭著者］
    研究論文（学術雑誌）
  • 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, 2022年12月, ［査読有り］
    研究論文（学術雑誌）
  • 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, 2022年11月22日, ［査読有り］
    研究論文（学術雑誌）, 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, 2021年06月27日, ［査読有り］
    研究論文（学術雑誌）, 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, 2021年06月01日, ［査読有り］
    研究論文（学術雑誌）, 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, 2020年05月01日, ［査読有り］
    研究論文（学術雑誌）
  • 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, 2019年12月01日, ［査読有り］
    研究論文（学術雑誌）
  • 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, 2018年10月04日, ［査読有り］
    研究論文（学術雑誌）, 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.
■ その他活動・業績
■ 講演・口頭発表等
  • 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, 2026年03月22日, 日本語, シンポジウム・ワークショップパネル（公募）
    2026年03月20日 - 2026年03月22日, ［招待講演］
  • 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, 2025年09月02日, 日本語, シンポジウム・ワークショップパネル（指名）
    2025年09月02日 - 2025年09月02日, 50122301, ［招待講演］
  • 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, 2025年05月30日, 日本語
    2025年05月29日 - 2025年05月31日, 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, 2024年10月06日
    2024年10月05日 - 2024年10月06日
  • 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, 2024年07月25日
    2024年07月25日, ［招待講演］
  • 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, 日本語
    2024年07月20日 - 2024年07月20日
  • 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, 2024年03月30日
    2024年03月28日 - 2024年03月31日, ［招待講演］
  • 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, 2023年11月10日
  • 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, 2023年09月16日
  • 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, 2023年05月
  • 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, 2022年10月
  • 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, 2022年04月
    ［招待講演］
  • 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, 2022年03月27日
  • 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, 2021年12月06日
  • 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, 2020年12月10日
■ 所属学協会
  • 2023年01月 - 現在
    口腔科学会
  • 2021年11月 - 現在
    日本薬学会
  • 2019年08月 - 現在
    日本口腔外科学会
  • 2018年05月 - 現在
    歯科基礎医学会
  • 2015年08月 - 現在
    日本結晶学会
■ 共同研究・競争的資金等の研究課題
■ 学術・社会貢献活動／その他
メディア報道
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