2024/06/09 更新

写真a

タケベ カツキ
武部 克希
Takebe Katsuki
所属
医歯薬学域 助教
職名
助教
外部リンク

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 / 外科系歯学

  • ライフサイエンス / 構造生物化学

  • ライフサイエンス / 細菌学

経歴

  • 岡山大学   学術研究院医歯薬学域 歯科薬理学分野   助教

    2024年4月 - 現在

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  • 大阪大学   大学院歯学研究科顎口腔腫瘍学講座   院生医員

    2020年4月 - 2024年3月

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所属学協会

  • 口腔科学会

    2023年1月 - 現在

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  • 日本薬学会

    2021年11月 - 現在

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  • 日本口腔外科学会

    2019年8月 - 現在

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  • 歯科基礎医学会

    2018年5月 - 現在

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  • 日本結晶学会

    2015年8月 - 現在

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論文

  • Identification of the Acidification Mechanism of the Optimal pH for RNase He1 査読

    Katsuki Takebe, Mamoru Suzuki, Takeshi Sangawa, Naomi Motoyoshi, Tadashi Itagaki, Kana Kashima, Narikazu Uzawa, Hiroko Kobayashi

    Biological and Pharmaceutical Bulletin   46 ( 12 )   1778 - 1786   2023年12月

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    担当区分:筆頭著者   記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:Pharmaceutical Society of Japan  

    DOI: 10.1248/bpb.b23-00511

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  • Analysis of FctB3 crystal structure and insight into its structural stabilization and pilin linkage mechanisms 査読

    Katsuki Takebe, Mamoru Suzuki, Takeshi Sangawa, Bernd Kreikemeyer, Masaya Yamaguchi, Narikazu Uzawa, Tomoko Sumitomo, Shigetada Kawabata, Masanobu Nakata

    Archives of Microbiology   206 ( 1 )   2023年11月

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    担当区分:筆頭著者   掲載種別:研究論文(学術雑誌)   出版者・発行元:Springer Science and Business Media LLC  

    DOI: 10.1007/s00203-023-03727-1

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    その他リンク: https://link.springer.com/article/10.1007/s00203-023-03727-1/fulltext.html

  • Reconstruction of the lower lip after resection of its venous malformation using a labial mucosal advancement flap – A case report- 査読

    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   2023年11月

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    掲載種別:研究論文(学術雑誌)   出版者・発行元:Elsevier BV  

    DOI: 10.1016/j.ajoms.2023.03.004

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  • 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 査読

    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   2023年7月

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    担当区分:筆頭著者   掲載種別:研究論文(学術雑誌)   出版者・発行元:American Chemical Society (ACS)  

    DOI: 10.1021/acs.jcim.3c00331

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  • Deep learning model for the automated evaluation of contact between the lower third molar and inferior alveolar nerve on panoramic radiography 査読

    Katsuki Takebe, Tomoaki Imai, Seiko Kubota, Ayano Nishimoto, Shigeki Amekawa, Narikazu Uzawa

    Journal of Dental Sciences   18 ( 3 )   991 - 996   2023年7月

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    担当区分:筆頭著者   掲載種別:研究論文(学術雑誌)   出版者・発行元:Elsevier BV  

    DOI: 10.1016/j.jds.2022.12.008

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  • GATA6 regulates expression of annexin A10 (ANXA10) associated with epithelial–mesenchymal transition of oral squamous cell carcinoma 査読

    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   2022年12月

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    掲載種別:研究論文(学術雑誌)   出版者・発行元:Elsevier BV  

    DOI: 10.1016/j.archoralbio.2022.105569

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  • Novel Functional Peptide for Next-Generation Vital Pulp Therapy 査読

    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   2022年11月

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    掲載種別:研究論文(学術雑誌)   出版者・発行元:SAGE Publications  

    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.

    DOI: 10.1177/00220345221135766

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    その他リンク: http://journals.sagepub.com/doi/full-xml/10.1177/00220345221135766

  • 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 査読

    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   2021年6月

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    掲載種別:研究論文(学術雑誌)   出版者・発行元:MDPI AG  

    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.

    DOI: 10.3390/ijms22136911

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  • Crystal structure of the C-terminal domain of envelope protein VP37 from white spot syndrome virus reveals sulphate binding sites responsible for heparin binding 査読

    Wasusit Somsoros, Takeshi Sangawa, Katsuki Takebe, Jakrada Attarataya, Kanokpan Wongprasert, Saengchan Senapin, Triwit Rattanarojpong, Mamoru Suzuki, Pongsak Khunrae

    Journal of General Virology   102 ( 6 )   2021年6月

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    掲載種別:研究論文(学術雑誌)   出版者・発行元:Microbiology Society  

    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.

    DOI: 10.1099/jgv.0.001611

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  • Crystal Structure of Catechol -O-Methyltransferase Complexed with Nitecapone 査読

    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   2020年5月

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    掲載種別:研究論文(学術雑誌)   出版者・発行元:Pharmaceutical Society of Japan  

    DOI: 10.1248/cpb.c20-00011

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  • X-Ray Crystallographic Structure of Hericium erinaceus Ribonuclease, RNase He1 in Complex with Zinc 査読

    Hiroko Kobayashi, Takeshi Sangawa, Katsuki Takebe, Naomi Motoyoshi, Tadashi Itagaki, Mamoru Suzuki

    Biological and Pharmaceutical Bulletin   42 ( 12 )   2054 - 2061   2019年12月

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    掲載種別:研究論文(学術雑誌)   出版者・発行元:Pharmaceutical Society of Japan  

    DOI: 10.1248/bpb.b19-00532

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  • Immunoglobulin‐like domains of the cargo proteins are essential for protein stability during secretion by the type IX secretion system 査読

    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   2018年10月

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    掲載種別:研究論文(学術雑誌)   出版者・発行元:Wiley  

    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.

    DOI: 10.1111/mmi.14083

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    その他リンク: https://onlinelibrary.wiley.com/doi/full-xml/10.1111/mmi.14083

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MISC

  • 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   2021年2月

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    記述言語:日本語   出版者・発行元:日本細菌学会  

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講演・口頭発表等

  • COMTの反応機構と賦活化物質による立体構造変化 招待

    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3月30日 

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    開催年月日: 2024年3月28日 - 2024年3月31日

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  • 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 

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  • 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9月16日 

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  • 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5月 

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  • 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 

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  • 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. 招待

    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4月 

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  • 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3月27日 

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  • 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6日 

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  • 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 

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受賞

  • 令和5年度 研究科長賞(最優秀賞)

    2024年3月   大阪大学  

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  • 第33回日本口腔科学会近畿地方部会 新人賞

    2022年4月   口腔科学会  

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  • 令和3年度 研究科長賞(奨励賞)

    2022年4月   大阪大学  

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共同研究・競争的資金等の研究

  • 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

    研究課題/領域番号:24K02614  2024年04月 - 2028年03月

    日本学術振興会  科学研究費助成事業  基盤研究(B)

    大原 直也

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    配分額:18590000円 ( 直接経費:14300000円 、 間接経費:4290000円 )

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  • 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

    研究課題/領域番号:24K13239  2024年04月 - 2027年03月

    日本学術振興会  科学研究費助成事業  基盤研究(C)

    岡元 邦彰

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    配分額:4550000円 ( 直接経費:3500000円 、 間接経費:1050000円 )

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