Achievement

原著論文

  1. Matsumoto, G., Inobe, T., Amano, T., Murai, K., Nukina, N. and Mori, N. (2018) N-Acyldopamine induces aggresome formation without proteasome inhibition and enhances protein aggregation via p62/SQSTM1 expression. Scientific Reports, 8, 9585.
  2. Inobe, T.*, Tsukamoto, M., and Nozaki, M. (2018) Proteasome-mediated protein degradation is enhanced by fusion ubiquitin with unstructured degron. Biochem. Biophys. Res. Commun., 501, 948-954.
  3. Yu, H., Singh Gautam AK., Wilmington, SR., Wylie, D., Martinez-Fonts, K., Kago, G., Warburton, M., Chavali, S., Inobe, T., Finkelstein, I., Babu, MM., and Matouschek, A. (2016) Conserved sequence preferences contribute to substrate recognition by the proteasome. J. Biol. Chem.,291, 14526-39.
  4. Kurosawa, N., Wakata, Y., Inobe, T., Kitamura, H., Yoshioka, M., Matsuzawa, S., Kishi, Y., and Isobe, M. (2016) Novel method for the high-throughput production of phosphorylation site-specific monoclonal antibodies. Scientific Reports, 6, 25174.
  5. Inobe, T.* and Nozaki, M. (2016) Proteasomal degradation of damaged polyubiquitin. Biochem. Biophys. Res. Commun., 471, 34-40.
  6. Inobe, T.* and Nukina, N. (2016) Rapamycin-induced oligomer formation system of FRB-FKBP fusion proteins. J. Biosci. Bioeng., 122, 40-46.
  7. Inobe, T.* and Genmei, R. (2015) Inhibition of the 26S proteasome by peptide mimics of the coiled-coil region of its ATPase subunits. Biochem. Biophys. Res. Commun., 468, 143-150.
  8. Inobe, T.*, Nozaki, M. and Nukina, N. (2015) Artificial regulation of p53 function by modulating its assembly. Biochem. Biophys. Res. Commun., 467, 322-327.
  9. Takahashi, K., Matouschek, A. and Inobe, T.* (2015) Regulation of proteasomal degradation modulating an unstructured proteasomal initiation region of a substrate. ACS Chem. Biol. 10, 2537–2543.
  10. Inobe, T.* and Genmei, R. (2015) N-terminal coiled-coil structure of ATPase subunits of 26S proteasome is crucial for proteasome function. PLoS ONE, 10(7): e0134056.
  11. Fishbain, S., Inobe, T., Israeli, E., Chavali, S., Yu, H., Zokarkar, A., Babu, MM., and Matouschek, A.(2015) Sequence composition of disordered regions fine-tunes protein half-life. Nature Struct. Mol. Biol. 22, 214-221. [Impact factor: 11.633] Selected for News and Views
  12. Kraut, DA., Israeli, E., Schrader, E., Patil, A., Nakai, K., Nanavati, D., Inobe, T. and Matouschek, A. (2012) Sequence- and Species-Dependence of Proteasomal Processivity. ACS Chem. Biol. 7, 1444-1453. [Impact factor: 5.698]
  13. Chen, J., Makabe, K., Nakamura, T., Inobe, T. and Kuwajima, K. (2011) Dissecting a biomolecular process of MgATP2- binding to the chaperonin GroEL. J. Mol. Biol. 410, 343-356. [Impact factor: 4.303]
  14. Inobe, T., Fishbain, S., Prakash, S. and Matouschek, A. (2011) Defining the Geometry of the Two-component Proteasome Degron. Nature Chem. Biol. 7, 161-167. [Impact factor: 16.058]   Selected for Fuculty of 1000
  15. Prakash, S., Inobe, T., Hatch, A. J. and Matouschek, A. (2009) Substrate Selection by the Proteasome during Degradation of Protein Complexes. Nature Chem. Biol. 5, 29-36. [Impact factor: 16.058] Selected for News and Views
  16. Inobe, T., Kraut D. A. and Matouschek, A. (2008) How to pick a protein and pull at it (News and views). Nature Struct. Mol. Biol. 15, 1135-1136. [Impact factor: 12.273]
  17. Inobe, T., Takahashi, K., Maki, K., Enoki, S., Kamagata, K., Kadooka, A., Arai, M. and Kuwajima, K. (2008) Asymmetry of the GroEL-GroES Complex under Physiological Conditions as Revealed by Small-angle X-ray Scattering. Biophys. J. 94, 1392-1402. [Impact factor: 4.390]
  18. Enoki, S., Maki, K., Inobe, T., Takahashi, K., Kamagata, K., Oroguchi, T., Nakatani, H., Tomoyori, K. and Kuwajima, K. (2006) The Equilibrium Unfolding Intermediate Observed at pH 4 and Its Relationship with the Kinetic Folding Intermediates in Green Fluorescent Protein. J. Mol. Biol. 361, 969-982. [Impact factor: 4.303]
  19. Kuwajima, K., Inobe, T. and Arai, M. (2006) The allosteric Transition of the Chaperonin GroEL from Escherichia coli Studied by Solution X-ray Scattering. Macromol. Res. 14, 166-172. [Impact factor: 2.369]
  20. Iizuka, R., Yoshida, T., Ishii, N., Zako, T., Takahashi, K., Maki, K., Inobe, T., Kuwajima, K. and Yohda, M. (2005) Characterization of archaeal group II chaperonin-ADP-metal fluoride complexes: Implications that group II chaperonins operate as a “Two-stroke engine”. J. Biol. Chem. 280, 40375-40383.[Impact factor: 5.328]
  21. Akhtar, M. W., Srinivas, V., Raman, B., Ramakrishna, T., Inobe, T., Maki, K., Arai, M., Kuwajima, K. and Rao, C. M. (2004)Oligomeric Hsp33 with enhanced chaperone activity: Gel-filtration, cross-linking and SAXS analysis. J. Biol. Chem. 279, 55760-55769. [Impact factor: 5.328]
  22. Inobe, T. and Kuwajima, K. (2004) F value analysis of an allosteric transition of
    GroEL based on a single pathway model. J. Mol. Biol. 339, 199-205. [Impact factor: 4.303]
  23. Iizuka, R., So, S., Inobe, T., Yoshida, T., Zako, T., Kuwajima, K. and Yohda, M. (2004) Role of the helical protrusion in the conformational change and molecular chaperone activity of the archaeal group II chaperonin. J. Biol. Chem. 279, 18834-18839. [Impact factor: 5.328]
  24. Inobe, T., Kikushima, K., Makio, T., Arai, M. and Kuwajima, K. (2003) The allosteric transition of GroEL induced by metal fluoride ADP complexes. J. Mol. Biol. 329, 121-134. [Impact factor: 4.303]
  25. Arai, M., Inobe, T., Maki, K., Ikura, T., Kihara, H., Amemiya, Y. and Kuwajima, K. (2003) Denaturation and reassembly of chaperonin GroEL studied by solution X-ray scattering. Protein Science, 12, 672-680.  [Impact factor: 2.937]
  26. Inobe, T., Arai, M., Nakao, M., Ito, K., Kamagata, K., Makio, T., Amemiya, Y., Kihara, H. and Kuwajima, K. (2003) Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy. J. Mol. Biol. 327, 183-191. [Impact factor: 4.303]
  27. Kuwajima, K., Makio, T. and Inobe, T. (2002) Chaperone-affected folding of globular proteins. J. Biol. Phys. 28, 77-93.  [Impact factor: 0.646]
  28. Kuwajima, K., Arai, M., Inobe, T., Ito, K., Nakao, M., Maki, K., Kamagata, K., Kihara, H. and Amemiya Y. (2002) The use of the time-resolved X-ray solution scattering for studies of globular proteins. Spectroscopy, 16, 127-138. [Impact factor: 0.485]
  29. Arai, M., Ito, K., Inobe, T., Nakao, M., Maki, K., Kamagata, K., Kihara, H., Amemiya, Y. and Kuwajima, K. (2002) Fast compaction of α-lactalbumin during folding studied by stopped-flow X-ray scattering. J. Mol. Biol. 321, 121-132. [Impact factor: 4.303]
  30. Inobe, T., Makio, T., Takasu-Ishikawa, E., Terada, T. P. and Kuwajima, K. (2001). Nucleotide binding to the chaperonin GroEL: noncooperative binding of ATP analogs and ADP, and cooperative effect of ATP. Biochimica et Biophysica Acta, 1545, 160-173. [Impact factor: 3.078]

*Corresponding author

著書

  1. Arai, M., Ito, K., Maki, K, Ikura, T., Inobe, T., Kihara, H., Amemiya, Y. and Kuwajima, K. (1999) Structural analysis of protein folding intermediates by solution X-ray scattering. In Old and New Views of Protein Folding (Kuwajima, K. and Arai, M. eds.) pp. 31-40, Elsevier Science, Amsterdam.

総説

  1. Inobe, T. and Matouschek A. (2014) Paradigms of protein degradation by the proteasome. Curr. Opin. Struct. Biol. 24, 156-164.
  2. 高橋一暢伊野部智由(2013) Unstructured領域を介したプロテアソームのタンパク質分解、生化学、85(11), 1020-1024.
  3. 伊野部智由(2011) 変性領域を介したプロテアソームの基質認識機構、生物物理,  51, 276-277.
  4. 伊野部智由(2011) プロテアソームによるタンパク質分解に必要な分解シグナルの配置、実験医学,  29, 2135-2138.
  5. 伊野部智由、貫名信行 (2010) 蛋白質分解系活性化による神経変性疾患治療、実験医学,  28, 788-794.
  6. Inobe, T. and Matouschek, A. (2008) Protein targeting to ATP-dependent proteases. Curr. Opin. Struct. Biol. 18, 43-51.

 

紀要等

  1. 伊野部智由:Midwest heat shock response and molecular chaperone meeting 報告記, Protein Community (特定領域研究「タンパク質の社会」領域ニュース) Vol. 1 (2008) 31-33.
  2. Inobe, T., Arai, M., Ito, K., Nakao, M., Kamagata, K., Amemiya, Y., Kihara, H. and Kuwajima, K. (2001) Nucleotide-induced structural change of GroEL studied by X-ray scattering. Photon Factory Activity Report 2000, p257.
  3. Inobe, T., Arai, M., Ito, K., Nakao, M., Amemiya, Y., Kihara, H. and Kuwajima, K. (2000) Nucleotide-induced structural change of GroEL studied by X-ray scattering. Photon Factory Activity Report 1999, p272.
  4. 伊野部智由、桑島邦博:GroELの協同性に関する「加水分解モデル」の顛末、CHAPERONE News Letter (特定領域研究「分子シャペロンによる細胞機能制御」領域ニュース) No. 8

 

招待講演

  1. Inobe, T. (2018) Regulation of proteasomal degradation. The 18th KIAS Conference on “Protein Structure and Function” (KIAS, Seoul, Korea, Nov. 15-17).
  2. Inobe, T. (2016) Regulation of proteasomal degradation. 第54回日本生物物理学会年会(つくば国際会議場、11月25〜27日)
  3. 伊野部智由(2013)プロテアソームによる新規蛋白質分解制御法、日本バイオマテリアル学会北陸若手研究発表会(富山大学、12月16日)
  4. Inobe, T. (2013) Protein unfolding for proteasome-mediated degradation. International Symposium on Protein Folding and its Biological Significance (Okazaki Conference Center, Okazaki, Japan, March 4-6).
  5. Inobe, T., Takahashi, K., and Matouschek A.  (2012) Fluctuation-mediated regulation of the protein degradation by the proteasome. The 6th International Symposium “Molecular Science of Fluctuations toward Biological Functions” (KyotoTerrsa, Kyoto, Japan, Dec. 5-6).
  6. 伊野部智由(2011)プロテアソームによる蛋白質アンフォールディングと分解:その初期過程、日本物理学会2011年秋季大会(富山大学、9月21日〜24日)
  7. Inobe, T., Fishbain, S., Prakash, S., and Matouschek, A. (2010) Defining the geometry of the two-component proteasome degron. 48th Annual Meeting of the Biophysical Society of Japan (Sendai, Japan, Sept. 20)
  8. Inobe, T., Fishbain, S., Prakash, S. and Matouschek, A. (2010) Molecular mechanism of protein unfolding in the cell. The 10th Annual Meeting of The Protein Science Society of Japan (Sapporo, Japan, June. 16-18)
  9. Inobe, T., Prakash, S. and Matouschek, A. (2009) Selecting proteins for degradation: The initiation step. Cold Spring Harbor Laboratory Meeting: The Ubiquitin Family (Cold Spring Harbor Laboratory, New York, U.S.A., April 21-25, 2009).
  10. Inobe, T., Prakash, S., Tian, L. and Matouschek, A. (2007) Selecting proteins for degradation: The initiation step. The 12th Annual Midwest Stress Response and Molecular Chaperone Meeting (Northwestern University, Evanston, U.S.A., February 3, 2007).

国際学会発表

  1. Inobe, T. (2018) Regulation of proteasomal degradation. The 18th KIAS Conference on “Protein Structure and Function” (KIAS, Seoul, Korea, Nov. 15-17).
  2. Inobe, T., Takahashi, K., and Tsukamoto, M.(2018) Regulation of proteasomal degradation by utilizing the unstructured region. International Symposium on “Proteins; from the Cradle to the Grave” (Enryakuji Kaikan (Shiga), Japan, Aug. 26-29).
  3. Inobe, T., and Takahashi, K. (2016) Regulation of proteasomal degradation by molecular chaperone. Nascent Chain Biology Meeting 2016 (Lake Kawaguchi, Japan, Sep. 1-3).
  4. Inobe, T., Takahashi, K., Matouschek A. and Nukina N.  (2012) Selective proteasomal degradation of the mutant huntingtin protein by an artificial adapter protein. FASEB Science Research Conference “Protein Folding in the Cell” (Saxtons River, Vermont, July 29- Aug. 8).
  5. Inobe, T. and Takahashi, K. (2012) Fluctuation-mediated substrate recognition by the proteasome. The 5th International Symposium on Molecular Science of Fluctuations toward Biological Functions (Nara, Japan, Jan. 7-8).
  6. Inobe, T., Prakash, S. and Matouschek, A. (2009) How does the proteasome Select proteins for degradation? (Poster) The 14th Annual Midwest Stress Response and Molecular Chaperone Meeting (Northwestern University, Evanston, U.S.A., January 17, 2009).
  7. Inobe, T. and Kuwajima, K. (2004) F value analysis of an allosteric transition of GroEL based on a single-pathway model. (Poster) Molecular Chaperone & the Heat Shock Response (Cold Spring Harbor Laboratory, New York, May 5-9, 2004).
  8. Inobe, T. and Kuwajima, K. (2004) F value analysis of an allosteric transition of GroEL based on a single-pathway model. (Poster) The 1st Pacific-Rim International Conference on Protein Science (Yokohama, April 14-18, 2004).
  9. Inobe, T., Arai, M., Kikushima, K., Makio, T., Nakao, M., Kamagata, K. and Kuwajima, K. (2003) Molecular mechanism of the allosteric transiton of GroEL. (Poster) 17th Symposium of the Protein Society (Boston, July 26-30, 2003).
  10. Inobe, T., Arai, M., Ito, K., Nakao, M., Kamagata, K., Amemiya, Y., Kihara, H. and Kuwajima, K. (2002) Nucleotide-induced structural change of GroEL studied by X-ray scattering. (Poster) Molecular Chaperone & the Heat Shock Response (Cold Spring Harbor Laboratory, New York, May 1-5, 2002).
  11. Inobe, T., Kikushima, K., Kadooka, A., Makio, T. and Kuwajima, K. (2001) Cooperative structural changes of the chaperonin GroEL by ADP-phosphate analog complexes. (Poster) 4th International Conference on Biological Physics (Kyoto, July 30-August 3, 2001).
  12. Inobe, T., Makio, T., Takasu-Ishikawa, E., Terada, T. P., Arai, M., Ito, K., Nakao, M., Kihara, H., Amemiya, Y. and Kuwajima, K. (2000) Non-cooperative Nucleotide binding and the ATP-induced Cooperative Transition of Chaperonin GroEL (Poster) Molecular Chaperone & the Heat Shock Response (Cold Spring Harbor Laboratory, New York, May 3-7, 2000).

その他

国内学会発表16回

アウトリーチ活動

  1. 伊野部 智由「最近のアカデミック・キャリアアップ事情」、富山大学男女共同参画推進室セミナー「留学して研究するということin 五福」(富山大学、2012年7月18日)
  2. RIKEN RESEARCH, Research highlights “Maintaining a proper distance – A protein-devouring enzyme complex uses two different mechanisms to determine which targets to destroy-” 執筆協力(2011年5月)

受賞

  • 2017年 富山県ひとづくり財団 第34回「とやま賞」
  • 2009年 Northwestern University IBiS Postdoctral Travel Award

科学研究費補助金,各種外部資金の獲得状況

  • 2018年度 日本応用酵素協会 2018年度酵素研究助成
  • 2018年度~2019年度 科学研究費補助金 新学術領域研究(研究領域提案型)
  • 2017年度~2018年度 高橋産業経済研究財団 平成29, 30年度研究助成金
  • 2017年度~2018年度 科学研究費補助金 新学術領域研究(研究領域提案型)
  • 2016年度 金原一郎記念医学医療振興財団 第31回基礎医学医療研究助成金
  • 2016年度 ほくぎん若手研究者助成金
  • 2015年度~2016年度 科学研究費補助金 新学術領域研究(研究領域提案型)
  • 2014年度 鈴木謙三記念医科学応用研究財団 調査研究助成
  • 2014年度 ホクト生物科学振興財団 研究奨励金
  • 2014年度 旭硝子財団 研究奨励
  • 2014年度~2015年度 科学研究費補助金 若手研究(B)
  • 2014年度 倉田記念科学技術財団 倉田奨励金
  • 2013年度 内藤記念科学振興財団 内藤記念科学奨励金・研究助成
  • 2013年度 稲盛財団 研究助成金
  • 2013年度 ノバルティス科学振興財団 ノバルティス研究奨励金
  • 2012年度 アステラス病態代謝研究会 研究助成
  • 2012年度 持田記念医学薬学振興財団 研究助成
  • 2012年度 武田科学振興財団 ライフサイエンス研究奨励
  • 2011年度~2012年度 科学研究費補助金 新学術領域研究(研究領域提案型)
  • 2010年度~2011年度 科学研究費補助金 若手研究(B)
  • 2009年4月~2012年3月 理化学研究所基礎科学特別研究員
  • 2009年4月 Northwestern Univ. IBiS Postdoctral Travel Award
  • 2007年10月~2009年9月 日本学術振興会海外特別研究員
  • 2004年10月~2007年9月 Human Frontier Science Program Long-term Fellowship
  • 2004年4月(辞退)日本学術振興会海外特別研究員
  • 2003年5月 加藤記念国際交流助成
  • 2001年5月 東京大学大学院学生学術研究奨励金
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