原著論文・学会発表

原著論文

  1. N. Nameki,  S. Terawaki,  M. Takizawa,  M. Kitamura, Y. Muto,  K. Kuwasako*, Structural insights into recognition of SL4, the UUCG stem-loop, of human U1 snRNA by the ubiquitin-like domain, including the C-terminal tail in the SF3A1 subunit of U2 snRNP, J. Biochem. (2023), mvad033, https://doi.org/10.1093/jb/mvad033
  2. C. I. Kasano-Camones, M. Takizawa, N. Ohshima, C. Saito, W. Iwasaki, Y. Nakagawa, Y. Fujitani, R. Yoshida, Y. Saito, T. Izumi, S. Terawaki, M. Sakaguchi, F. J. Gonzalez, and Y. Inoue*, An HNF4α-PPARα regulatory cascade plays a critical role in driving NAFLD/NASH progression, J. Biochem. (2023), 173(5), 393–411,
  3. A. G. H. Rodrigo, N. Tomonobu, H. Yoneda, R. Kinoshita, Y. Mitsui, T. Sadahira, S. Terawaki, Y. Gohara, N. L. G. Y. Komalasari, F. Jiang, H. Murata, K. Yamamoto, J. Futami, A. Yamauchi, F. Kuribayashi, Y. Inoue, E. Kondo, S. Toyooka, M. Nishibori, M. Watanabe, Y. Nasu, M. Sakaguchi*. Toll-like receptor 4 promotes bladder cancer progression upon S100A8/A9 binding, which requires TIRAP-mediated TPL2 activation, Biochem. Biophys. Res. Commun 634 (2022) 83-91.
  4. K. Yamanishi, M. Fiedler, S. Terawaki, Y. Higuchi, M. Bienz, and N. Shibata*. A direct heterotypic interaction between the DIX domains of Dishevelled and Axin mediates signaling to β-catenin. Sci. Signal., 12(611). pii: eaaw5505 (2019).
  5. K. Yamanishi, W. Kumano, S. Terawaki, Y. Higuchi, N. Shibata*, Head-to-tail complex of Dishevelled and Axin-DIX domain: expression, purification, crystallographic studies and packing analysis, Protein Pept. Lett. 26, 792-797 (2019).
  6. K. Yamanishi, Y. Sin, S. Terawaki, Y. Higuchi, N. Shibata*, High-resolution structure of a Y27W mutant of the Dishevelled2 DIX domain, Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun75, 116-122 (2019).
  7. M. Hattori, O. Ishikawa, D. Oikawa, H. Amano, M. Yasuda, K Kaira, A. Ishida-Yamamoto, H. Nakano, D. Sawamura, S. Terawaki, K. Wakamatsu, F. Tokunaga, A. Shimizu*, In-frame Val(216)-Ser(217) deletion of KIT in mild piebaldism causes aberrant secretion and SCF response, J. Dermatol. Sci91, 35-42 (2018).
  8. S. Terawaki*, S. Fujita, T. Katsutani, K. Shiomi, K. Keino-Masu, M. Masu, K. Wakamatsu, N. Shibata, Y. Higuchi*, Structural basis for Ccd1 auto-inhibition in the Wnt pathway through homomerization of the DIX domain, Sci. Rep7, 7739 (2017).
  9. H. Wang, K. Hosoda, T. Ishii, R. Arai, T. Kohno, S. Terawaki and K. Wakamatsu*, Protein stabilizer, NDSB-195, enhances the dynamics of the β4-α2-loop of ubiquitin, J. Peptide. Sci., 22, 174-180 (2016).
  10. S. Terawaki, K. Kitano, M. Aoyama, T. Mori, and T. Hakoshima*, MT1-MMP recognition by ERM proteins and its implication in CD44 shedding, Genes Cells, 20, 847-859 (2015).
  11. S. Terawaki*, R. Matsubayashi, K. Hara, T. Onozuka, T. Kohno, and K. Wakamatsu,Biochemical characterization of a heterotrimeric Gi-protein activator peptide designed from the junction between the intracellular third loop and sixth transmembrane helix in the m4 muscarinic acetylcholine receptor, Biochem. Biophys. Res. Commun. 463, 64-69 (2015).
  12. S. Terawaki*, A. Yoshikane, Y. Higuchi, and K. Wakamatsu, Structural basis for cargo binding and autoinhibition of Bicaudal-D1 by a parallel coiled-coil with homotypic registry, Biochem. Biophys. Res. Commun. 460, 451-456 (2015).
  13. H. Wang, K. Hosoda, S. Terawaki, and K. Wakamatsu*, Refolding additive, dimethylbenzylammonium propane sulfonate (NDSB-256) accelerates Gly-Pro cis-trans Isomerization, Protein Pept. Lett. 22, 234-238 (2014)
  14. S. Terawaki*, H. Ootsuka, Y. Higuchi, and K, Wakamatsu, Crystallographic characterization of the C-terminal coiled-coil region of mouse Bicaudal-D1 (BICD1), Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun70, 1103-1106 (2014)
  15. S. Terawaki, K. Yano, T. Katsutani, K. Keino-Masu, M. Masu, Y. Shomura, H. Komori, N. Shibata, and Y. Higuchi*, Crystallographic characterization of the DIX domain of the Wnt signaling positive regulator Ccd1, Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun67, 758-761 (2011)
  16. S. Terawaki, K. Kitano, T. Mori, Y. Zhai, Y. Higuchi, N. Itoh, T. Watanabe, K. Kaibuchi, and T. Hakoshima*, The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding module, EMBO J29, 236-250 (2010)
  17. N. Shibata, H. Tamagaki, N. Hieda, K. Akita, H. Komori, Y. Shomura, S. Terawaki, K. Mori, N. Yasuoka, Y. Higuchi, and T. Toraya*, Crystal structure of ethanolamine ammonia-lyase complexed with coenzyme B12 analogs and substrates, J. Biol. Chem. 285, 26484-26493 (2010)
  18. N. Shibata, H. Tamagaki, S. Ohtsuki, N. Hieda, K. Akita, H. Komori, Y. Shomura, S. Terawaki, T. Toraya, N. Yasuoka, and Y. Higuchi*, Expression, crystallization and preliminary X-ray crystallographic study of ethanolamine ammonia-lyase from Escherichia coli, Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66, 709-711 (2010)
  19. S. Terawaki, K. Kitano, and T. Hakoshima, Crystallographic characterization of the membrane-targeting domains of the Rac-specific guanine nucleotide-exchange factors Tiam1 and Tiam2, Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64, 1039-1042 (2008)
  20. T. Mori, K. Kitano, S. Terawaki, R. Maesaki, Y. Fukami, and T. Hakoshima*, Structural Basis for CD44 Recognition by ERM Proteins, J. Biol. Chem. 283, 29602-29612 (2008)
  21. S. Terawaki, K. Kitano, M. Aoyama, and T. Hakoshima*, Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of membrane-type 1 matrix metalloproteinase (MT1-MMP), Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.64, 911-913 (2008)
  22. K. Kihira, S. Numata, M. Kitamura, J. Kondo, S. Terawaki, Y. Shomura, H. Komori, N. Shibata, and Y. Higuchi*, Crystallization and preliminary X-ray analysis of a class II release factor RF3 from a sulfate-reducing bacterium, Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64, 622-624 (2008)
  23. T. Mori, K. Kitano, S. Terawaki, R. Maesaki, and T. Hakoshima*, Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of adhesion molecule CD44, Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63, 844-847 (2007)
  24. Y. Takai, K. Kitano, S. Terawaki, R. Maesaki, and T. Hakoshima*, Structural basis of the cytoplasmic tail of adhesion molecule CD43 and its binding to ERM proteins, J. Mol. Biol. 381, 634-644 (2008)
  25. Y. Takai, K. Kitano, S. Terawaki, R. Maesaki, and T. Hakoshima*, Structural basis of PSGL-1 binding to ERM proteins, Genes Cells 12, 1329-1338 (2007)
  26. Y. Takai, K. Kitano, S. Terawaki, R. Maesaki, and T. Hakoshima*, Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1, Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63, 49-51 (2007)
  27. S. Terawaki, K. Kitano, and T. Hakoshima*, Structural basis for type II membrane protein binding by ERM proteins revealed by the radixin-neutral endopeptidase 24.11 (NEP) complex, J. Biol. Chem. 282, 19854-19862 (2007)
  28. S. Terawaki, R. Maesaki, and T. Hakoshima*, Structural basis for NHERF recognition by ERM proteins, Structure 14, 777-789 (2006)
  29. S. Terawaki, R. Maesaki, K. Okada, and T. Hakoshima*, Crystallographic characterization of the radixin FERM domain bound to the C-terminal region of the human Na+/H+-exchanger regulatory factor (NHERF), Acta Crystallogr. D Biol. Crystallogr59, 177-179 (2003)

著書・解説

  1. 寺脇慎一、サリドマイド誘導体がもたらすユビキチンリガーゼ基質認識の変換機構、ファルマシア、Vol. 52、 12、1157、2016

学会発表・講演・セミナーなど

  1. 寺脇慎一、プロテオサイエンスセンターにおける構造生物学研究の展開、2024年2月27日、愛媛
  2. 寺脇慎一、タンパク質の構造解析、PIM2023技術講習会、2023年11月、愛媛
  3. 寺脇慎一、行木信一、瀧澤将行、北村まどか、武藤裕、桑迫香奈子、ヒトU2 snRNPのサブユニットSF3A1のubiquitin-likeドメインとU1 snRNAのstem-loop 4との複合体のX線結晶構造解析、第96回日本生化学会大会、2023年11月、福岡 (ポスター発表)
  4. 寺脇慎一、クライオ電子顕微鏡およびX線結晶解析を用いたタンパク質の立体構造解析、第2回PRiME共同研究発表会 技術紹介、2023年9月、愛媛
  5. S. Terawaki, N. Nameki, M. Takizawa, M. Kitamura, Y. Muto, K. Kuwasako, X-ray crystallography of the ubiquitin-like domain in the SF3A1 subunit of human U2 snRNP complexed with SL4, the UUCG stem-loop, of U1 snRNA, Protein Island Matsuyama 2023 (PIM2023), Matsuyama, Japan, September (2023). (ポスター発表)
  6. L. X Xiaoxia, H. Sakamoto, R. Kubota, S. Terawaki, N. Shinzawa, K. Hikosaka, Challenges in isolation of mitochondrial ribosomes from the malaria parasite, Protein Island Matsuyama 2023 (PIM2023)、Matsuyama, Japan, September (2023). (ポスター発表)
  7. 寺脇慎一、藤田祥平、中込蒼一朗、石渡拓也、清水結加、笠野一郎、井上裕介、塩見健輔、桝正幸、柴田直樹、樋口芳樹、若松馨、Axinオリゴマーの構造変化を介したWntシグナル伝達制御の構造基盤、第95回日本生化学会大会、2022年11月、名古屋 (一般口頭発表、ポスター発表)
  8. 寺脇慎一、動的なオリゴマー形成を介する細胞シグナル伝達の構造生物学、愛媛大学 291回 応用化学セミナー、2022年、愛媛
  9. S. Terawaki, K. Wakamatsu, K. Shiomi, M. Masu, N. Shibata, Y. Higuchi, Structural basis for dynamic oligomerization of Wnt signaling regulators, Protein Island Matsuyama 2022 (PIM2022), Matsuyama, Japan, September (2022).
  10. 寺脇慎一、動的オリゴマー形成を介する細胞シグナル伝達の構造生物学、群馬大学Sメンブレンプロジェクト若手研究者発表会、2022年、群馬
  11. S. Terawaki, K. Wakamatsu, K. Shiomi, M. Masu, N. Shibata, Y. Higuchi, Structural basis of the molecular interaction of Axin with Coiled-coil DIX1 by heterotypic oligomerization of DIX domain, 3SAP(New perspectives on Wnt signaling, unveiled by structural and cell biology), Joint Annual Meeting of 71st JSCB & 19th PSSJ, Kobe, Japan, June (2019).
  12. 寺脇慎一、Wntシグナル伝達で機能する動的オリゴマーの構造生物学、第24回生体調節研究所・工学部合同生命科学セミナー、2017年、群馬
  13. 寺脇慎一、放射光を利用した構造生物学研究の推進と創薬基盤の創出、群大・KEK連携シンポジウム「量子ビームを用いた先端科学の展開と産業応用への期待」における講演、2017年、群馬
  14. S. Terawaki, S. Fujita, K. Shiomi, K. Keino-Masu, M. Masu, K. Wakamatsu, N. Shibata, and Y. Higuchi, Structural basis of Wnt signaling regulation by dynamic polymerized proteins, 13st Conference of the Asian Crystallographic Association (AsCA2015), Kolkata, India, December (2015). Invited lecture
  15. 寺脇慎一、生命科学におけるX線結晶解析法の進歩と課題、群馬県高等学校教育研究会理化学部会・日本化学会関東支部理科教育談話会における講演、2105年、群馬
  16. 寺脇慎一、Wntシグナル伝達で機能する動的オリゴマー形成因子の構造生物学、群馬大学 第9回医
  17. 寺脇慎一、「細胞接着分子及びWnt受容体の足場蛋白質の構造生物学的研究」、第15回生体調節研究所・工学部合同生命科学セミナー、2012年、群馬
  18. 寺脇慎一、構造生物学 〜蛋白質構造に基づくシグナル伝達の理解〜、名古屋大学大学院医学研究科 グローバルCOEプログラム 「機能分子医学への神経疾患・腫瘍の融合拠点」 系統講義ベーシックサイエンスコース特別講義、2012、名古屋

アウトリーチ活動

  1. 寺脇慎一、タンパク質の姿・形と機能、高大連携活動出張講義、2022年11月16日