KOJIMA Chojiro

Affiliation

Faculty of Engineering, Division of Materials Science and Chemical Engineering

Job Title

Professor

Date of Birth

1966

Research Fields, Keywords

NMR, Chemical Biology, Structural Biology, Biological Chemistry

Mail Address

E-mail address



写真a

The Best Research Achievement in Research Career 【 display / non-display

The Best Research Achievement in the last 5 years 【 display / non-display

Education 【 display / non-display

  • 1992.4
    -
    1995.3

    Osaka University   Department of Inorganic and Physical Chemistry   Doctor Course   Completed

  • 1990.4
    -
    1992.3

    Osaka University   Department of Inorganic and Physical Chemistry   Master Course   Completed

  • 1986.4
    -
    1990.3

    Osaka University   Department of Chemistry   Graduated

Degree 【 display / non-display

  • Doctor of Science - Osaka University

  • Master of Science - Osaka University

Campus Career 【 display / non-display

  • 2016.4
     
     

    Duty   Yokohama National UniversityFaculty of Engineering   Division of Materials Science and Chemical Engineering   Professor  

  • 2018.4
     
     

    Concurrently   Yokohama National UniversityGraduate school of Engineering Science   Department of Chemistry, Chemical Engineering and Life Science   Professor  

  • 2016.4
     
     

    Concurrently   Yokohama National UniversityCollege of Engineering Science   Department of Chemistry, Chemical Engineering and Life Science   Professor  

  • 2016.4
     
     

    Concurrently   Yokohama National UniversityGraduate School of Engineering   Department of Materials Science and Engineering   Professor  

External Career 【 display / non-display

  • 2016.5
     
     

    RIKEN   Quantitative Biology Center   Senior Visiting Scientist  

  • 2016.4
     
     

    Osaka University   Institute for Protein Research   Visiting Professor  

  • 2010.2
    -
    2016.3

    Osaka University   Institute for Protein Research   Associate Professor  

  • 2007.4
    -
    2010.2

    NAIST   Graduate School of Biological Sciences   Associate Professor  

  • 2005.4
    -
    2006.3

    Osaka University   Institute for Protein Research   Visiting Associate Professor  

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Academic Society Affiliations 【 display / non-display

  • 1991
     
     
     

    日本生物物理学会

Research Areas 【 display / non-display

  • Life Science / Structural biochemistry

 

Research Career 【 display / non-display

  • 創薬等ライフサイエンス研究のための相関構造解析プラットフォームによる支援と高度化(創薬基盤NMR技術の開発)

    The Other Research Programs  

    Project Year:

  • NMR分子置換法の開発

    Grant-in-Aid for Scientific Research  

    Project Year:

  • データベースを利用したNMR創薬支援パイプラインの開発

    Grant-in-Aid for Scientific Research  

    Project Year:

  • 病原体による宿主脂質ハイジャック機序の解明と創薬への応用(タンパク質-脂質間の物理的相互作用解析手法の改良・開発とLTPへの適用)

    JST Basic Research Programs (Core Research for Evolutional Science and Technology :CREST)  

    Project Year:

  • Fully automated NMR structure determination system for larger protein

    Grant-in-Aid for Scientific Research  

    Project Year:

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Books 【 display / non-display

  • 創薬研究のための相互作用解析パーフェクト(実験医学別冊)

    津本浩平(編),前仲勝実(編), 古板恭子, 児嶋長次郎, 児玉高志, 他( Role: Contributor ,  第1章「フラグメント創薬(FBDD)のための溶液NMR実験法(Ⅰ-8)」「水素-重水素交換質量分析(HDX-MS)実験法による相互作用部位の解析(Ⅱ-15)」)

    羊土社  ( ISBN:978-4-7581-2256-6

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    Total pages:368   Responsible for pages:86-98、160-167   Language:Japanese Book type:Scholarly book

Thesis for a degree 【 display / non-display

  • Precise structure determination of a DNA oligomer by NMR

    児嶋長次郎

    1995.3

    Doctoral Thesis   Single Work  

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    大阪大学理学研究科無機及び物理化学専攻
    DNAオリゴマーのNMR精密構造解析法の開発。

  • NMRを用いた核酸オリゴマーUASGの構造と運動性の解析

    児嶋長次郎

    1992.3

    Master Thesis   Single Work  

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    大阪大学理学研究科無機及び物理化学専攻
    GAL4蛋白質が結合するDNA配列UASGのNMR構造解析および運動性解析。

Papers 【 display / non-display

  • Cooperative regulation of PBI1 and MAPKs controls WRKY45 transcription factor in rice immunity

    NATURE COMMUNICATIONS   13   2397   2022.5  [Reviewed]

    DOI Web of Science

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    Authorship:Corresponding author   Language:English   Publishing type:Research paper (scientific journal)   Joint Work  

  • In-cell NMR as a sensitive tool to monitor physiological condition of Escherichia coli

    Scientific Reports (Nature Publisher Group)   10   2466   2020.2  [Reviewed]

    DOI Web of Science

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    Authorship:Last author, Corresponding author   Language:English   Publishing type:Research paper (scientific journal)   Joint Work  

  • Current NMR Techniques for Structure-Based Drug Discovery

    Toshihiko Sugiki, Kyoko Furuita, Toshimichi Fujiwara, Chojiro Kojima

    Molecules   23 ( 1 )   148   2018.1  [Reviewed]

    DOI

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    Authorship:Last author, Corresponding author   Language:English   Publishing type:Research paper (scientific journal)   Joint Work  

  • Substrate specificity of TOR complex 2 is determined by a ubiquitin-fold domain of the Sin1 subunit

    Hisashi Tatebe, Shinichi Murayama, Toshiya Yonekura, Tomoyuki Hatano, David Richter, Tomomi Furuya, … Show more authors

    eLife   6   e19594   2017.3  [Reviewed]

    DOI Web of Science

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:ELIFE SCIENCES PUBLICATIONS LTD   Joint Work  

    The target of rapamycin (TOR) protein kinase forms multi-subunit TOR complex 1 (TORC1) and TOR complex 2 (TORC2), which exhibit distinct substrate specificities. Sin1 is one of the TORC2-specific subunit essential for phosphorylation and activation of certain AGC-family kinases. Here, we show that Sin1 is dispensable for the catalytic activity of TORC2, but its conserved region in the middle (Sin1CRIM) forms a discrete domain that specifically binds the TORC2 substrate kinases. Sin1CRIM fused to a different TORC2 subunit can recruit the TORC2 substrate Gad8 for phosphorylation even in the sin1 null mutant of fission yeast. The solution structure of Sin1CRIM shows a ubiquitin-like fold with a characteristic acidic loop, which is essential for interaction with the TORC2 substrates. The specific substrate-recognition function is conserved in human Sin1CRIM, which may represent a potential target for novel anticancer drugs that prevent activation of the mTORC2 substrates such as AKT.

    Other Link: https://elifesciences.org/content/6/e19594

  • Bacterial effector modulation of host E3 ligase activity suppresses PAMP-triggered immunity in rice

    Kazuya Ishikawa, Koji Yamaguchi, Kazuaki Sakamoto, Satomi Yoshimura, Kento Inoue, Seiji Tsuge, Choj … Show more authors

    NATURE COMMUNICATIONS   5   5430   2014.11  [Reviewed]

    DOI Web of Science PubMed

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:NATURE PUBLISHING GROUP   Joint Work  

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Review Papers 【 display / non-display

  • オルガネラ間コンタクトを担うVAP蛋白質の構造と機能

    古板恭子, 児嶋長次郎

    酵素工学ニュース   Vol.81   12 - 16   2019.4

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    Language:Japanese   Publishing type:Article, review, commentary, editorial, etc. (bulletin of university, research institution)   Joint Work  

  • Amino Acid Selective 13C Labeling and 13C Scrambling Profile Analysis of Protein α and Side-Chain Carbons in Escherichia coli Utilized for Protein Nuclear Magnetic Resonance

    Toshihiko Sugiki and Kyoko Furuita and Toshimichi Fujiwara and Chojiro Kojima

    Biochemistry   57 ( 26 )   3576 - 3589   2018.7

    DOI

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    Language:English   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)   Publisher:American Chemical Society ({ACS})   Single Work  

  • Current NMR Techniques for Structure-Based Drug Discovery

    Toshihiko Sugiki, Kyoko Furuita, Toshimichi Fujiwara, and Chojiro Kojima

    Molecules   23 ( 1 )   148   2018.1  [Reviewed]  [Invited]

    DOI

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    Language:English   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)   Publisher:MDPI   Joint Work  

    A variety of nuclear magnetic resonance (NMR) applications have been developed for structure-based drug discovery (SBDD). NMR provides many advantages over other methods, such as the ability to directly observe chemical compounds and target biomolecules, and to be used for ligand-based and protein-based approaches. NMR can also provide important information about the interactions in a protein-ligand complex, such as structure, dynamics, and affinity, even when the interaction is too weak to be detected by ELISA or fluorescence resonance energy transfer (FRET)-based high-throughput screening (HTS) or to be crystalized. In this study, we reviewed current NMR techniques. We focused on recent progress in NMR measurement and sample preparation techniques that have expanded the potential of NMR-based SBDD, such as fluorine NMR (19F-NMR) screening, structure modeling of weak complexes, and site-specific isotope labeling of challenging targets.A variety of nuclear magnetic resonance (NMR) applications have been developed for structure-based drug discovery (SBDD). NMR provides many advantages over other methods, such as the ability to directly observe chemical compounds and target biomolecules, and to be used for ligand-based and protein-based approaches. NMR can also provide important information about the interactions in a protein-ligand complex, such as structure, dynamics, and affinity, even when the interaction is too weak to be detected by ELISA or fluorescence resonance energy transfer (FRET)-based high-throughput screening (HTS) or to be crystalized. In this study, we reviewed current NMR techniques. We focused on recent progress in NMR measurement and sample preparation techniques that have expanded the potential of NMR-based SBDD, such as fluorine NMR (19F-NMR) screening, structure modeling of weak complexes, and site-specific isotope labeling of challenging targets.

  • Protein 19F-labeling using transglutaminase for the NMR study of intermolecular interactions

    Yoshikazu Hattori and David Heidenreich and Yuki Ono and Toshihiko Sugiki and Kei-ichi Yokoyama and … Show more authors

    Journal of Biomolecular NMR   68 ( 4 )   271 - 279   2017.8

    DOI

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    Language:The in addition, foreign language   Publishing type:Article, review, commentary, editorial, etc. (bulletin of university, research institution)   Publisher:Springer Science and Business Media {LLC}   Single Work  

  • Lysine <sup>13</sup>C-Methylation NMR for Analyses of Interactions and Structural Changes

    HATTORI Yoshikazu,KOJIMA Chojiro

    Journal of the Biophysical Society of Japan   56 ( 5 )   288 - 289   2016.9  [Reviewed]  [Invited]

    DOI

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    Language:Japanese   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)   Publisher:The Biophysical Society of Japan   Joint Work  

    Other Link: https://www.jstage.jst.go.jp/article/biophys/56/5/56_288/_article/-char/ja/

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Presentations 【 display / non-display

  • 植物構造生物学研究と創薬

    児嶋長次郎  [Invited]

    植物科学シンポジウム2018 

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    Event date: 2018.12

    Language:Japanese   Presentation type:Oral presentation (general)  

    児嶋長次郎, “植物構造生物学研究と創薬”, 植物科学シンポジウム2018, Dec. 2018 (招待講演).
    https://bsw3.naist.jp/hashimoto/?page=1398

  • NMR tools developed for protein-drug and protein-protein interaction studies

    C. Kojima  [Invited]

    The 6th International Symposium on Drug Discovery and Design by NMR 

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    Event date: 2018.11

    Language:English   Presentation type:Oral presentation (general)  

    C. Kojima, “NMR tools developed for protein-drug and protein-protein interaction studies”, The 6th International Symposium on Drug Discovery and Design by NMR, Nov. 2018 (Invited Lecture).
    http://www.tsurumi.yokohama-cu.ac.jp/ynmr/workshop.html

Past of Collaboration and Commissioned Research 【 display / non-display

  • 低分子化合物ライブラリーを用いたフッ素NMRスクリーニング

    Funded Research offered by Enterprises  

    Project Year: 2015.11  -  2016.9 

 

Charge of on-campus class subject 【 display / non-display

  • 2022   基礎生化学

    College of Engineering Science

  • 2022   Structural Biochemistry

    College of Engineering Science

  • 2022   Physical Chemistry 1

    College of Engineering Science

  • 2022   Materials Engineering and its Social Roles

    Liberal Arts Education

 

Committee Memberships 【 display / non-display

  • 日本生物物理学会

    2017.4 - 2019.3  代議員

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    Committee type:Other 

  • 日本蛋白質科学会

    2015.6 - 2019.6  役員(選管、渉外)

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    Committee type:Other 

  • 日本核磁気共鳴学会

    2012.4 - 2018.3  評議員

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    Committee type:Other