{"id":152,"date":"2022-08-17T18:10:04","date_gmt":"2022-08-17T09:10:04","guid":{"rendered":"https:\/\/proteincomplex.wordpress.com\/?page_id=152"},"modified":"2026-04-17T10:10:59","modified_gmt":"2026-04-17T01:10:59","slug":"publication","status":"publish","type":"page","link":"https:\/\/www.pros.ehime-u.ac.jp\/protein-complex\/?page_id=152","title":{"rendered":"\u539f\u8457\u8ad6\u6587\u30fb\u5b66\u4f1a\u767a\u8868"},"content":{"rendered":"\n

\u539f\u8457\u8ad6\u6587\u30fb\u5b66\u4f1a\u767a\u8868<\/h2>\n\n\n\n

\u539f\u8457\u8ad6\u6587<\/span><\/h2>\n\n\n\n
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  1. Molecular interaction between T-lymphoma invasion and metastasis 2 and the PB1 domain of p67phox, Y. Tamura, Y. Adachi,<\/u><\/strong><\/strong> S. Hata, S. Terawaki<\/u><\/strong><\/strong>*<\/sup>, Research Square<\/em>, (2026), DOI: https:\/\/doi.org\/10.21203\/rs.3.rs-8955616\/v1<\/a>. (Preprint<\/em>)<\/li>\n\n\n\n
  2. Identification, functional characterization, and structural analysis of an atypical L-threonate 3-dehydrogenase, S. Watanabe,\u00a0H. Sato, T. Yokoi, S. Terawaki<\/u><\/strong>, J. Biol. Chem.<\/em>, (2026), 111280, doi: 10.1016\/j.jbc.2026.111280.<\/em>(\u30d7\u30ec\u30b9\u30ea\u30ea\u30fc\u30b9<\/a>)<\/li>\n\n\n\n
  3. Screening of one-bead one-compound cyclic peptide libraries using unpurified proteins from the wheat germ cell-free system to identify protein-protein interaction inhibitors, M. Hasegawa, A. Nozawa, Y. Tanaka, K. Kido, S. Terawaki<\/u><\/strong>, C. Takahashi, Y. Matsumoto, Y. Onda, K. Tanaka, T. Kishimoto, H. Sato, A. Takemiya, T. Sawasaki, Bioorg. & Med. Chem<\/em>., (2026), 133, 118492. doi: 10.1016\/j.bmc.2025.118492.<\/li>\n\n\n\n
  4. M. Akagashi, S. Watanabe, S. Kwiatkowski, J. Drozak, S. Terawaki<\/u><\/strong>, Y. Watanabe, Crystal structure of L-2-keto-3-deoxyfuconate 4-dehydrogenase reveals a unique binding mode as a \u03b1-furanosyl hemiketal of substrates, Sci. Rep<\/em>. (2024), 14(1), 14602<\/li>\n\n\n\n
  5. N. Nameki,  S. Terawaki<\/span><\/strong>,  M. Takizawa,  M. Kitamura, Y. Muto,  K. Kuwasako*<\/sup>, 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<\/em>. (2023), 173, (5), 203-216, https:\/\/doi.org\/10.1093\/jb\/mvad033<\/li>\n\n\n\n
  6. C. I. Kasano-Camones, M. Takizawa, N. Ohshima, C. Saito, W. Iwasaki, Y. Nakagawa, Y. Fujitani, R. Yoshida, Y. Saito, T. Izumi, S. Terawaki<\/span><\/strong>, M. Sakaguchi, F. J. Gonzalez, and Y. Inoue*<\/sup>, An HNF4\u03b1-PPAR\u03b1 regulatory cascade plays a critical role in driving NAFLD\/NASH progression, J. Biochem<\/em>. (2023), 173(5), 393\u2013411.<\/li>\n\n\n\n
  7. A. G. H. Rodrigo, N. Tomonobu, H. Yoneda, R. Kinoshita, Y. Mitsui, T. Sadahira, S. Terawaki<\/span><\/strong>, 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*<\/sup>. Toll-like receptor 4 promotes bladder cancer progression upon S100A8\/A9 binding, which requires TIRAP-mediated TPL2 activation, Biochem. Biophys. Res. Commun<\/em><\/em> 634 (2022) 83-91.<\/li>\n\n\n\n
  8. K. Yamanishi, M. Fiedler, S. Terawaki<\/u><\/strong>, Y. Higuchi, M. Bienz, and N. Shibata*<\/sup>. A direct heterotypic interaction between the DIX domains of Dishevelled and Axin mediates signaling to \u03b2-catenin. Sci. Signal<\/em>., 12(611). pii: eaaw5505 (2019).<\/li>\n\n\n\n
  9. K. Yamanishi, W. Kumano, S. Terawaki<\/u><\/strong>, Y. Higuchi, N. Shibata*<\/sup>, Head-to-tail complex of Dishevelled and Axin-DIX domain: expression, purification, crystallographic studies and packing analysis, Protein Pept. Lett.<\/em> 26, 792-797 (2019).<\/li>\n\n\n\n
  10. K. Yamanishi, Y. Sin, S. Terawaki<\/u><\/strong>, Y. Higuchi, N. Shibata*<\/sup>, High-resolution structure of a Y27W mutant of the Dishevelled2 DIX domain, Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun<\/em>. 75<\/strong>, 116-122 (2019).<\/li>\n\n\n\n
  11. M. Hattori, O. Ishikawa, D. Oikawa, H. Amano, M. Yasuda, K Kaira, A. Ishida-Yamamoto, H. Nakano, D. Sawamura, S. Terawaki<\/u><\/strong>, K. Wakamatsu, F. Tokunaga, A. Shimizu*<\/sup>, In-frame Val(216)-Ser(217) deletion of KIT in mild piebaldism causes aberrant secretion and SCF response, J. Dermatol. Sci<\/em>. 91<\/strong>, 35-42 (2018).<\/li>\n\n\n\n
  12. S. Terawaki<\/u><\/strong>*<\/sup>, S. Fujita, T. Katsutani, K. Shiomi, K. Keino-Masu, M. Masu, K. Wakamatsu, N. Shibata, Y. Higuchi*<\/sup>,\u3000Structural basis for Ccd1 auto-inhibition in the Wnt pathway through homomerization of the DIX domain, Sci. Rep<\/em>. 7<\/strong>, 7739 (2017).<\/li>\n\n\n\n
  13. H. Wang, K. Hosoda, T. Ishii, R. Arai, T. Kohno, S. Terawaki<\/u><\/strong> and K. Wakamatsu*<\/sup>, Protein stabilizer, NDSB-195, enhances the dynamics of the \u03b24-\u03b12-loop of ubiquitin, J. Peptide. Sci.<\/em>, 22, 174-180 (2016).<\/li>\n\n\n\n
  14. S. Terawaki<\/u><\/strong>, K. Kitano, M. Aoyama, T. Mori, and T. Hakoshima*<\/sup>, MT1-MMP recognition by ERM proteins and its implication in CD44 shedding, Genes Cells<\/em>, 20, 847-859 (2015).<\/li>\n\n\n\n
  15. S. Terawaki<\/u><\/strong>*<\/sup>, 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.<\/em> 463<\/strong>, 64-69 (2015).<\/li>\n\n\n\n
  16. S. Terawaki<\/u><\/strong>*<\/sup>, 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.<\/em> 460<\/strong>, 451-456 (2015).<\/li>\n\n\n\n
  17. H. Wang, K. Hosoda, S. Terawaki<\/u><\/strong>, and K. Wakamatsu*<\/sup>, Refolding additive, dimethylbenzylammonium propane sulfonate (NDSB-256) accelerates Gly-Pro cis-trans Isomerization, Protein Pept. Lett.<\/em> 22<\/strong>, 234-238 (2014)<\/li>\n\n\n\n
  18. S. Terawaki<\/u><\/strong>*<\/sup>, 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. Commun<\/em>. 70,<\/strong> 1103-1106 (2014)<\/li>\n\n\n\n
  19. S. Terawaki<\/u><\/strong>, K. Yano, T. Katsutani, K. Keino-Masu, M. Masu, Y. Shomura, H. Komori, N. Shibata, and Y. Higuchi*<\/sup>, Crystallographic characterization of the DIX domain of the Wnt signaling positive regulator Ccd1, Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun<\/em>. 67<\/strong>, 758-761 (2011)<\/li>\n\n\n\n
  20. S. Terawaki<\/u><\/strong>, K. Kitano, T. Mori, Y. Zhai, Y. Higuchi, N. Itoh, T. Watanabe, K. Kaibuchi, and T. Hakoshima*<\/sup>, The PHCCEx domain of Tiam1\/2 is a novel protein- and membrane-binding module, EMBO J<\/em>. 29<\/strong>, 236-250 (2010)<\/li>\n\n\n\n
  21. N. Shibata, H. Tamagaki, N. Hieda, K. Akita, H. Komori, Y. Shomura, S. Terawaki<\/u><\/strong>, K. Mori, N. Yasuoka, Y. Higuchi, and T. Toraya*<\/sup>, Crystal structure of ethanolamine ammonia-lyase complexed with coenzyme B12 analogs and substrates, J. Biol. Chem.<\/em> 285<\/strong>, 26484-26493 <\/em>(2010)<\/li>\n\n\n\n
  22. N. Shibata, H. Tamagaki, S. Ohtsuki, N. Hieda, K. Akita, H. Komori, Y. Shomura, S. Terawaki<\/u><\/strong>, T. Toraya, N. Yasuoka, and Y. Higuchi*<\/sup>, Expression, crystallization and preliminary X-ray crystallographic study of ethanolamine ammonia-lyase from Escherichia coli<\/em>, Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.<\/em> 66<\/strong>, 709-711 (2010)<\/li>\n\n\n\n
  23. S. Terawaki<\/u><\/strong>, 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.<\/em> 64<\/strong>, 1039-1042 (2008)<\/li>\n\n\n\n
  24. T. Mori, K. Kitano, S. Terawaki<\/u><\/strong>, R. Maesaki, Y. Fukami, and T. Hakoshima*<\/sup>, Structural Basis for CD44 Recognition by ERM Proteins, J. Biol. Chem.<\/em> 283<\/strong>, 29602-29612 (2008)<\/li>\n\n\n\n
  25. S. Terawaki<\/u><\/strong>, K. Kitano, M. Aoyama, and T. Hakoshima*<\/sup>, 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.<\/em>64<\/strong>, 911-913 <\/em>(2008)<\/li>\n\n\n\n
  26. K. Kihira, S. Numata, M. Kitamura, J. Kondo, S. Terawaki<\/u><\/strong>, Y. Shomura, H. Komori, N. Shibata, and Y. Higuchi*<\/sup>, 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.<\/em> 64<\/strong>, 622-624 (2008)<\/li>\n\n\n\n
  27. T. Mori, K. Kitano, S. Terawaki<\/u><\/strong>, R. Maesaki, and T. Hakoshima*<\/sup>, Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of adhesion molecule CD44, Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.<\/em> 63<\/strong>, 844-847 (2007)<\/li>\n\n\n\n
  28. Y. Takai, K. Kitano, S. Terawaki<\/u><\/strong>, R. Maesaki, and T. Hakoshima*<\/sup>, Structural basis of the cytoplasmic tail of adhesion molecule CD43 and its binding to ERM proteins, J. Mol. Biol.<\/em> 381<\/strong>, 634-644 (2008)<\/li>\n\n\n\n
  29. Y. Takai, K. Kitano, S. Terawaki<\/u><\/strong>, R. Maesaki, and T. Hakoshima*<\/sup>, Structural basis of PSGL-1 binding to ERM proteins, Genes Cells<\/em> 12<\/strong>, 1329-1338 (2007)<\/li>\n\n\n\n
  30. Y. Takai, K. Kitano, S. Terawaki<\/u><\/strong>, R. Maesaki, and T. Hakoshima*<\/sup>, 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.<\/em> 63<\/strong>, 49-51 (2007)<\/li>\n\n\n\n
  31. S. Terawaki<\/u><\/strong>, K. Kitano, and T. Hakoshima*<\/sup>, Structural basis for type II membrane protein binding by ERM proteins revealed by the radixin-neutral endopeptidase 24.11 (NEP) complex, J. Biol. Chem.<\/em> 282<\/strong>, 19854-19862 (2007)<\/li>\n\n\n\n
  32. S. Terawaki<\/u><\/strong>, R. Maesaki, and T. Hakoshima*<\/sup>, Structural basis for NHERF recognition by ERM proteins, Structure<\/em> 14<\/strong>, 777-789 <\/em>(2006)<\/li>\n\n\n\n
  33. S. Terawaki<\/u><\/strong>, R. Maesaki, K. Okada, and T. Hakoshima*<\/sup>, Crystallographic characterization of the radixin FERM domain bound to the C-terminal region of the human Na+<\/sup>\/H+<\/sup>-exchanger regulatory factor (NHERF), Acta Crystallogr. D Biol. Crystallogr<\/em>. 59<\/strong>, 177-179 (2003)<\/li>\n<\/ol>\n\n\n\n
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    \u8457\u66f8\u30fb\u89e3\u8aac<\/span><\/h2>\n\n\n\n
      \n
    1. \u5bfa\u8107\u614e\u4e00\u3001BioID\u6cd5\u306b\u7528\u3044\u308b\u9175\u7d20\u306e\u69cb\u9020\u7684\u7279\u5fb4\u3001\u5b9f\u9a13\u533b\u5b66\u5225\u518a\u6700\u5f37\u306e\u30b9\u30c6\u30c3\u30d7UP\u30b7\u30ea\u30fc\u30ba\u300c\u30ea\u30a2\u30eb\u306a\u76f8\u4e92\u4f5c\u7528\u3092\u6349\u3048\u308b\u8fd1\u63a5\u4f9d\u5b58\u6027\u6a19\u8b58\u30d7\u30ed\u30c8\u30b3\u30fc\u30eb\u300d, 2024(9\u670824\u65e5\u767a\u520a)<\/li>\n\n\n\n
    2. \u5bfa\u8107\u614e\u4e00\u3001\u30b5\u30ea\u30c9\u30de\u30a4\u30c9\u8a98\u5c0e\u4f53\u304c\u3082\u305f\u3089\u3059\u30e6\u30d3\u30ad\u30c1\u30f3\u30ea\u30ac\u30fc\u30bc\u57fa\u8cea\u8a8d\u8b58\u306e\u5909\u63db\u6a5f\u69cb\u3001\u30d5\u30a1\u30eb\u30de\u30b7\u30a2\u3001Vol. 52\u3001 12\u30011157\u30012016<\/li>\n<\/ol>\n<\/div>\n\n\n\n
      \n

      \u5b66\u4f1a\u767a\u8868<\/span> (\u4e0b\u7dda\u306f\u7814\u7a76\u5ba4\u6240\u5c5e\u8005)<\/h2>\n\n\n\n
        \n
      1. \u25cb\u5bfa\u8107\u614e\u4e00<\/span>\u3001\u964d\u65d7\u5927\u5cb3\u3001\u9ad8\u6a4b\u5343\u4f73\u5b50\u3001\u8db3\u7acb\u88d5\u7f8e\u5b50<\/span>\u3001\u91ce\u6fa4\u5f70\u3001\u6fa4\u5d0e\u9054\u4e5f, BioID\u6cd5\u306b\u7528\u3044\u308b\u8fd1\u4f4d\u4f9d\u5b58\u6027\u30d3\u30aa\u30c1\u30f3\u5316\u9175\u7d20AirID\u306eX\u7dda\u7d50\u6676\u69cb\u9020\u89e3\u6790, \u7b2c97\u56de\u65e5\u672c\u751f\u5316\u5b66\u4f1a\u5927\u4f1a\u30012025\u5e7411\u6708\u3001\u4eac\u90fd\u3000(\u30dd\u30b9\u30bf\u30fc\u767a\u8868&\u4e00\u822c\u53e3\u982d\u767a\u8868)<\/li>\n\n\n\n
      2. \u25cb\u6c38\u91ce \u8056\u967d<\/span>\u3001\u8db3\u7acb\u88d5\u7f8e\u5b50<\/span>\u3001\u5bfa\u8107\u614e\u4e00<\/span>, Wnt\u30b7\u30b0\u30ca\u30eb\u4f1d\u9054\u56e0\u5b50\u306b\u7279\u7570\u7684\u306a\u30aa\u30ea\u30b4\u30de\u30fc\u5f62\u6210\u5236\u5fa1\u6a5f\u69cb\u306e\u69cb\u9020\u751f\u7269\u5b66\u7684\u89e3\u6790\u3001\u7b2c97\u56de\u65e5\u672c\u751f\u5316\u5b66\u4f1a\u5927\u4f1a\u30012025\u5e7411\u6708\u3001\u4eac\u90fd\u3000(\u30dd\u30b9\u30bf\u30fc\u767a\u8868&\u4e00\u822c\u53e3\u982d\u767a\u8868)<\/li>\n\n\n\n
      3. \u25cb\u4f0a\u6771\u6d77\u6597<\/span>\u3001\u6c38\u91ce \u8056\u967d<\/span>\u3001\u5bfa\u8107\u614e\u4e00<\/span>\u3001Wnt\u30b7\u30b0\u30ca\u30eb\u5236\u5fa1\u56e0\u5b50Axin\u306e\u30ea\u30f3\u9178\u5316\u4f9d\u5b58\u7684\u306a\u5206\u5b50\u6a5f\u80fd\u5236\u5fa1\u306e\u751f\u5316\u5b66\u7684\u89e3\u6790\u3001\u7b2c97\u56de\u65e5\u672c\u751f\u5316\u5b66\u4f1a\u5927\u4f1a\u30012025\u5e7411\u6708\u3001\u4eac\u90fd\u3000(\u30dd\u30b9\u30bf\u30fc\u767a\u8868)<\/li>\n\n\n\n
      4. \u25cb<\/span>\u8db3\u7acb\u88d5\u7f8e\u5b50<\/span>, \u5c0f\u6fa4\u660e\u5948<\/span>, \u85e4\u5ca1\u8ce2\u771f<\/span>\u3001\u5357\u51fa\u5343\u5c0b<\/span>\u3001\u9ad8\u6a4b\u5b8f\u9686\u3001\u6fa4\u5d0e\u9054\u4e5f\u3001\u5bfa\u8107\u614e\u4e00<\/span>\u3001Cytohesin\u306e\u30b3\u30a4\u30eb\u30c9\u30b3\u30a4\u30eb\u30c9\u30e1\u30a4\u30f3\u3092\u4ecb\u3057\u305f\u6a19\u7684\u5206\u5b50\u8a8d\u8b58\u6a5f\u69cb\u306e\u69cb\u9020\u751f\u7269\u5b66\u7684\u89e3\u6790\u3001\u7b2c97\u56de\u65e5\u672c\u751f\u5316\u5b66\u4f1a\u5927\u4f1a\u30012025\u5e7411\u6708\u3001\u4eac\u90fd\u3000(\u30dd\u30b9\u30bf\u30fc\u767a\u8868&\u4e00\u822c\u53e3\u982d\u767a\u8868)<\/li>\n\n\n\n
      5. \u25cbMasaya Nagano<\/span>, Yumiko Adachi<\/span>, Shin-ichi Terawaki<\/span>, Cryo-EM analysis of Axin2 homooligomer involved in the termination of the Wnt\/beta-catenin pathway, Protein Island Matsuyama 2025 (PIM2025)<\/em>\u3001Matsuyama, Japan, September (2025). (\u30dd\u30b9\u30bf\u30fc\u767a\u8868)<\/li>\n\n\n\n
      6. \u25cb\u8db3\u7acb\u88d5\u7f8e\u5b50<\/span>\u3001\u85e4\u5ca1\u8ce2\u771f<\/span>\u3001\u5357\u51fa\u5343\u5c0b<\/span>\u3001\u5bfa\u8107\u614e\u4e00<\/span>\u3001Cytohesin1\u306e\u30b3\u30a4\u30eb\u30c9\u30b3\u30a4\u30eb\u9818\u57df\u3092\u4ecb\u3057\u305f\u7d30\u80de\u5c40\u5728\u5236\u5fa1\u306e\u69cb\u9020\u751f\u7269\u7684\u89e3\u6790\u3001\u7b2c96\u56de\u65e5\u672c\u751f\u5316\u5b66\u4f1a\u5927\u4f1a\u30012024\u5e7411\u6708\u3001\u6a2a\u6d5c\u3000(\u30dd\u30b9\u30bf\u30fc\u767a\u8868)<\/li>\n\n\n\n
      7. \u25cb\u6c38\u91ce \u8056\u967d<\/span>\u3001\u8db3\u7acb\u88d5\u7f8e\u5b50<\/span>\u3001\u5bfa\u8107\u614e\u4e00<\/span>\u3001Wnt\u30b7\u30b0\u30ca\u30eb\u4f1d\u9054\u306e\u6291\u5236\u56e0\u5b50Axin2\u304c\u5f62\u6210\u3059\u308b\u30db\u30e2\u30aa\u30ea\u30b4\u30de\u30fc\u306e\u30af\u30e9\u30a4\u30aa\u96fb\u5b50\u9855\u5fae\u93e1\u89e3\u6790\u3001\u7b2c96\u56de\u65e5\u672c\u751f\u5316\u5b66\u4f1a\u5927\u4f1a\u30012024\u5e7411\u6708\u3001\u6a2a\u6d5c\u3000(\u30dd\u30b9\u30bf\u30fc\u767a\u8868&\u4e00\u822c\u53e3\u982d\u767a\u8868)<\/li>\n\n\n\n
      8. \u25cbYumiko Adachi<\/span>, Shin-ichi Terawaki<\/span>, Tatsuya Sawasaki, Cryo-EM analysis of the Dvl1-DIX homo-oligomer, Protein Island Matsuyama 2024 (PIM2024)<\/em>\u3001Matsuyama, Japan, November (2024). (\u30dd\u30b9\u30bf\u30fc\u767a\u8868)<\/li>\n\n\n\n
      9. \u25cb\u8db3\u7acb\u88d5\u7f8e\u5b50<\/span>\u3001\u5bfa\u8107\u614e\u4e00<\/span>\u3001\u6fa4\u5d0e\u9054\u4e5f\u3001Wnt\u30b7\u30b0\u30ca\u30eb\u4f1d\u9054\u7d4c\u8def\u5236\u5fa1\u56e0\u5b50Dvl1 DIX\u30c9\u30e1\u30a4\u30f3\u306e\u7acb\u4f53\u69cb\u9020\u89e3\u6790\u3001\u5148\u7aef\u30e2\u30c7\u30eb\u52d5\u7269\u652f\u63f4\u30d7\u30e9\u30c3\u30c8\u30d5\u30a9\u30fc\u30e0\u82e5\u624b\u652f\u63f4\u8b1b\u7fd2\u4f1a\u30012024\u5e748\u6708\u3001\u611b\u77e5\u3000(\u30dd\u30b9\u30bf\u30fc\u767a\u8868\uff06\u30b7\u30e7\u30fc\u30c8\u30c8\u30fc\u30af)<\/li>\n\n\n\n
      10. \u25cb\u6851\u8feb\u9999\u5948\u5b50\uff0c\u5bfa\u8107\u614e\u4e00<\/span>\uff0c\u7027\u6fa4\u5c06\u884c\uff0c\u5317\u6751\u307e\u3069\u304b\uff0c\u6b66\u85e4\u88d5\uff0c\u884c\u6728\u4fe1\u4e00\u3001Structural basis for the interaction between the UUCG stem-loop of human U1 snRNA and the ubiquitin like domain of the SF3A1 subunit in U2 snRNP\u3001\u65e5\u672cRNA\u5b66\u4f1a\u30012024\u5e746\u6708\u3001\u6771\u4eac(\u30dd\u30b9\u30bf\u30fc\u767a\u8868)<\/li>\n\n\n\n
      11. \u25cb\u5bfa\u8107\u614e\u4e00<\/span>\u3001\u884c\u6728\u4fe1\u4e00\u3001\u7027\u6fa4\u5c06\u884c\u3001\u5317\u6751\u307e\u3069\u304b\u3001\u6b66\u85e4\u88d5\u3001\u6851\u8feb\u9999\u5948\u5b50\u3001\u30d2\u30c8U2 snRNP\u306e\u30b5\u30d6\u30e6\u30cb\u30c3\u30c8SF3A1\u306eubiquitin-like\u30c9\u30e1\u30a4\u30f3\u3068U1 snRNA\u306estem-loop 4\u3068\u306e\u8907\u5408\u4f53\u306eX\u7dda\u7d50\u6676\u69cb\u9020\u89e3\u6790\u3001\u7b2c96\u56de\u65e5\u672c\u751f\u5316\u5b66\u4f1a\u5927\u4f1a\u30012023\u5e7411\u6708\u3001\u798f\u5ca1\u3000(\u30dd\u30b9\u30bf\u30fc\u767a\u8868)<\/li>\n\n\n\n
      12. \u25cbS. Terawaki<\/span>, 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)<\/em>, Matsuyama, Japan, September (2023). (\u30dd\u30b9\u30bf\u30fc\u767a\u8868)<\/li>\n\n\n\n
      13. \u25cbL. X Xiaoxia, H. Sakamoto, R. Kubota, S. Terawaki<\/span>, N. Shinzawa, K. Hikosaka, Challenges in isolation of mitochondrial ribosomes from the malaria parasite, Protein Island Matsuyama 2023 (PIM2023)<\/em>\u3001Matsuyama, Japan, September (2023). (\u30dd\u30b9\u30bf\u30fc\u767a\u8868)<\/li>\n\n\n\n
      14. \u25cb\u5bfa\u8107\u614e\u4e00<\/span>\u3001\u85e4\u7530\u7965\u5e73\u3001\u4e2d\u8fbc\u84bc\u4e00\u6717\u3001\u77f3\u6e21\u62d3\u4e5f\u3001\u6e05\u6c34\u7d50\u52a0\u3001\u7b20\u91ce\u4e00\u90ce\u3001\u4e95\u4e0a\u88d5\u4ecb\u3001\u5869\u898b\u5065\u8f14\u3001\u685d\u6b63\u5e78\u3001\u67f4\u7530\u76f4\u6a39\u3001\u6a0b\u53e3\u82b3\u6a39\u3001\u82e5\u677e\u99a8\u3001Axin\u30aa\u30ea\u30b4\u30de\u30fc\u306e\u69cb\u9020\u5909\u5316\u3092\u4ecb\u3057\u305fWnt\u30b7\u30b0\u30ca\u30eb\u4f1d\u9054\u5236\u5fa1\u306e\u69cb\u9020\u57fa\u76e4\u3001\u7b2c95\u56de\u65e5\u672c\u751f\u5316\u5b66\u4f1a\u5927\u4f1a\u30012022\u5e7411\u6708\u3001\u540d\u53e4\u5c4b\u3000(\u4e00\u822c\u53e3\u982d\u767a\u8868\u3001\u30dd\u30b9\u30bf\u30fc\u767a\u8868)<\/li>\n\n\n\n
      15. \u25cbS. Terawaki<\/u>, K. Wakamatsu, K. Shiomi, M. Masu, N. Shibata, Y. Higuchi, Structural basis for dynamic oligomerization of Wnt signaling regulators, Protein Island Matsuyama 2022 (PIM2022)<\/em>, Matsuyama, Japan, September (2022).<\/li>\n\n\n\n
      16. \u25cbS. Terawaki<\/u>, 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<\/sup> PSSJ<\/em>, Kobe, Japan, June (2019).<\/li>\n\n\n\n
      17. \u25cbS. Terawaki<\/u>, 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)<\/em>, Kolkata, India, December (2015). Invited lecture<\/em><\/li>\n<\/ol>\n<\/div>\n\n\n\n
        \n

        \u8b1b\u6f14<\/span>\u30fb\u30bb\u30df\u30ca\u30fc\u306a\u3069<\/h2>\n\n\n\n
          \n
        1. \u8db3\u7acb\u88d5\u7f8e\u5b50<\/span>\u3001Cytohesin\u306ecoiled-coil\u30c9\u30e1\u30a4\u30f3\u306e\u6a19\u7684\u5206\u5b50\u8a8d\u8b58\u306e\u69cb\u9020\u751f\u7269\u5b66\u7684\u89e3\u6790\u3001\u5fdc\u7528\u5316\u5b66\u30bb\u30df\u30ca\u30fc\u30012025\u5e7412\u6708\u3001\u611b\u5a9b<\/li>\n\n\n\n
        2. \u5bfa\u8107\u614e\u4e00<\/span>\u3001AirID\u306e\u69cb\u9020\u89e3\u6790\u3001PIM2025\u6280\u8853\u8b1b\u7fd2\u4f1a\u30012025\u5e7411\u6708\u3001\u611b\u5a9b<\/li>\n\n\n\n
        3. \u5bfa\u8107\u614e\u4e00<\/span>\u3001\u30b3\u30a4\u30eb\u30c9\u30b3\u30a4\u30eb\u3092\u4ecb\u3057\u305f\u30b7\u30b0\u30ca\u30eb\u4f1d\u9054\u5236\u5fa1\u306e\u69cb\u9020\u751f\u7269\u5b66\u7684\u7814\u7a76\u3001\u30d7\u30ed\u30c6\u30aa\u5275\u85ac\u30bb\u30df\u30ca\u30fc\u30012025\u5e7410\u6708\u3001\u611b\u5a9b<\/li>\n\n\n\n
        4. \u5bfa\u8107\u614e\u4e00<\/span>\u3001BioID\u9175\u7d20\u306e\u69cb\u9020\u89e3\u6790\u3001PIM2024\u6280\u8853\u8b1b\u7fd2\u4f1a\u30012024\u5e7412\u6708\u3001\u611b\u5a9b<\/li>\n\n\n\n
        5. \u5bfa\u8107\u614e\u4e00<\/span>\u3001\u30d7\u30ed\u30c6\u30aa\u30b5\u30a4\u30a8\u30f3\u30b9\u30bb\u30f3\u30bf\u30fc\u306b\u304a\u3051\u308b\u69cb\u9020\u751f\u7269\u5b66\u7814\u7a76\u306e\u5c55\u958b\u3001\u30d7\u30ed\u30c6\u30aa\u5275\u85ac\u30bb\u30df\u30ca\u30fc\u30012024\u5e742\u670827\u65e5\u3001\u611b\u5a9b<\/li>\n\n\n\n
        6. \u5bfa\u8107\u614e\u4e00<\/span>\u3001\u30bf\u30f3\u30d1\u30af\u8cea\u306e\u69cb\u9020\u89e3\u6790\u3001PIM2023\u6280\u8853\u8b1b\u7fd2\u4f1a\u30012023\u5e7411\u6708\u3001\u611b\u5a9b<\/li>\n\n\n\n
        7. \u5bfa\u8107\u614e\u4e00<\/span>\u3001\u30af\u30e9\u30a4\u30aa\u96fb\u5b50\u9855\u5fae\u93e1\u304a\u3088\u3073X\u7dda\u7d50\u6676\u89e3\u6790\u3092\u7528\u3044\u305f\u30bf\u30f3\u30d1\u30af\u8cea\u306e\u7acb\u4f53\u69cb\u9020\u89e3\u6790\u3001\u7b2c2\u56dePRiME\u5171\u540c\u7814\u7a76\u767a\u8868\u4f1a \u6280\u8853\u7d39\u4ecb\u30012023\u5e749\u6708\u3001\u611b\u5a9b<\/li>\n\n\n\n
        8. \u5bfa\u8107\u614e\u4e00<\/span>\u3001\u52d5\u7684\u306a\u30aa\u30ea\u30b4\u30de\u30fc\u5f62\u6210\u3092\u4ecb\u3059\u308b\u7d30\u80de\u30b7\u30b0\u30ca\u30eb\u4f1d\u9054\u306e\u69cb\u9020\u751f\u7269\u5b66\u3001\u611b\u5a9b\u5927\u5b66 291\u56de \u5fdc\u7528\u5316\u5b66\u30bb\u30df\u30ca\u30fc\u30012022\u5e74\u3001\u611b\u5a9b<\/li>\n\n\n\n
        9. \u5bfa\u8107\u614e\u4e00<\/span>\u3001\u52d5\u7684\u30aa\u30ea\u30b4\u30de\u30fc\u5f62\u6210\u3092\u4ecb\u3059\u308b\u7d30\u80de\u30b7\u30b0\u30ca\u30eb\u4f1d\u9054\u306e\u69cb\u9020\u751f\u7269\u5b66\u3001\u7fa4\u99ac\u5927\u5b66S\u30e1\u30f3\u30d6\u30ec\u30f3\u30d7\u30ed\u30b8\u30a7\u30af\u30c8\u82e5\u624b\u7814\u7a76\u8005\u767a\u8868\u4f1a\u30012022\u5e74\u3001\u7fa4\u99ac<\/li>\n\n\n\n
        10. \u5bfa\u8107\u614e\u4e00<\/span>\u3001Wnt\u30b7\u30b0\u30ca\u30eb\u4f1d\u9054\u3067\u6a5f\u80fd\u3059\u308b\u52d5\u7684\u30aa\u30ea\u30b4\u30de\u30fc\u306e\u69cb\u9020\u751f\u7269\u5b66\u3001\u7b2c24\u56de\u751f\u4f53\u8abf\u7bc0\u7814\u7a76\u6240\u30fb\u5de5\u5b66\u90e8\u5408\u540c\u751f\u547d\u79d1\u5b66\u30bb\u30df\u30ca\u30fc\u30012017\u5e74\u3001\u7fa4\u99ac<\/li>\n\n\n\n
        11. \u5bfa\u8107\u614e\u4e00<\/span>\u3001\u653e\u5c04\u5149\u3092\u5229\u7528\u3057\u305f\u69cb\u9020\u751f\u7269\u5b66\u7814\u7a76\u306e\u63a8\u9032\u3068\u5275\u85ac\u57fa\u76e4\u306e\u5275\u51fa\u3001\u7fa4\u5927\u30fbKEK\u9023\u643a\u30b7\u30f3\u30dd\u30b8\u30a6\u30e0\u300c\u91cf\u5b50\u30d3\u30fc\u30e0\u3092\u7528\u3044\u305f\u5148\u7aef\u79d1\u5b66\u306e\u5c55\u958b\u3068\u7523\u696d\u5fdc\u7528\u3078\u306e\u671f\u5f85\u300d\u306b\u304a\u3051\u308b\u8b1b\u6f14\u30012017\u5e74\u3001\u7fa4\u99ac<\/li>\n\n\n\n
        12. \u5bfa\u8107\u614e\u4e00<\/span>\u3001\u751f\u547d\u79d1\u5b66\u306b\u304a\u3051\u308bX\u7dda\u7d50\u6676\u89e3\u6790\u6cd5\u306e\u9032\u6b69\u3068\u8ab2\u984c\u3001\u7fa4\u99ac\u770c\u9ad8\u7b49\u5b66\u6821\u6559\u80b2\u7814\u7a76\u4f1a\u7406\u5316\u5b66\u90e8\u4f1a\u30fb\u65e5\u672c\u5316\u5b66\u4f1a\u95a2\u6771\u652f\u90e8\u7406\u79d1\u6559\u80b2\u8ac7\u8a71\u4f1a\u306b\u304a\u3051\u308b\u8b1b\u6f14\u30012105\u5e74\u3001\u7fa4\u99ac<\/li>\n\n\n\n
        13. \u5bfa\u8107\u614e\u4e00<\/span>\u3001Wnt\u30b7\u30b0\u30ca\u30eb\u4f1d\u9054\u3067\u6a5f\u80fd\u3059\u308b\u52d5\u7684\u30aa\u30ea\u30b4\u30de\u30fc\u5f62\u6210\u56e0\u5b50\u306e\u69cb\u9020\u751f\u7269\u5b66\u3001\u7fa4\u99ac\u5927\u5b66 \u7b2c9\u56de\u533b<\/li>\n\n\n\n
        14. \u5bfa\u8107\u614e\u4e00<\/span>\u3001\u300c\u7d30\u80de\u63a5\u7740\u5206\u5b50\u53ca\u3073Wnt\u53d7\u5bb9\u4f53\u306e\u8db3\u5834\u86cb\u767d\u8cea\u306e\u69cb\u9020\u751f\u7269\u5b66\u7684\u7814\u7a76\u300d\u3001\u7b2c15\u56de\u751f\u4f53\u8abf\u7bc0\u7814\u7a76\u6240\u30fb\u5de5\u5b66\u90e8\u5408\u540c\u751f\u547d\u79d1\u5b66\u30bb\u30df\u30ca\u30fc\u30012012\u5e74\u3001\u7fa4\u99ac<\/li>\n\n\n\n
        15. \u5bfa\u8107\u614e\u4e00<\/span>\u3001\u69cb\u9020\u751f\u7269\u5b66\u3000\u301c\u86cb\u767d\u8cea\u69cb\u9020\u306b\u57fa\u3065\u304f\u30b7\u30b0\u30ca\u30eb\u4f1d\u9054\u306e\u7406\u89e3\u301c\u3001\u540d\u53e4\u5c4b\u5927\u5b66\u5927\u5b66\u9662\u533b\u5b66\u7814\u7a76\u79d1 \u30b0\u30ed\u30fc\u30d0\u30ebCOE\u30d7\u30ed\u30b0\u30e9\u30e0 \u300c\u6a5f\u80fd\u5206\u5b50\u533b\u5b66\u3078\u306e\u795e\u7d4c\u75be\u60a3\u30fb\u816b\u760d\u306e\u878d\u5408\u62e0\u70b9\u300d \u7cfb\u7d71\u8b1b\u7fa9\u30d9\u30fc\u30b7\u30c3\u30af\u30b5\u30a4\u30a8\u30f3\u30b9\u30b3\u30fc\u30b9\u7279\u5225\u8b1b\u7fa9\u30012012\u3001\u540d\u53e4\u5c4b<\/li>\n<\/ol>\n<\/div>\n\n\n\n
          \n

          \u30a2\u30a6\u30c8\u30ea\u30fc\u30c1\u6d3b\u52d5<\/span><\/h2>\n\n\n\n
            \n
          1. \u5bfa\u8107\u614e\u4e00\u3001\u30bf\u30f3\u30d1\u30af\u8cea\u306e\u59ff\u30fb\u5f62\u3068\u6a5f\u80fd\u3001\u9ad8\u5927\u9023\u643a\u6d3b\u52d5\u51fa\u5f35\u8b1b\u7fa9\u30012022\u5e7411\u670816\u65e5<\/li>\n<\/ol>\n<\/div>\n\n\n\n

            <\/p>\n","protected":false},"excerpt":{"rendered":"

            \u539f\u8457\u8ad6\u6587\u30fb\u5b66\u4f1a\u767a\u8868 \u539f\u8457\u8ad6\u6587 \u8457\u66f8\u30fb\u89e3\u8aac \u5b66\u4f1a\u767a\u8868 (\u4e0b\u7dda\u306f\u7814\u7a76\u5ba4\u6240\u5c5e\u8005) \u8b1b\u6f14\u30fb\u30bb\u30df\u30ca\u30fc\u306a\u3069 \u30a2\u30a6\u30c8\u30ea\u30fc\u30c1\u6d3b\u52d5<\/p>\n","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"sidebar-footer-only","meta":{"footnotes":""},"class_list":["post-152","page","type-page","status-publish","hentry"],"jetpack_sharing_enabled":true,"_links":{"self":[{"href":"https:\/\/www.pros.ehime-u.ac.jp\/protein-complex\/index.php?rest_route=\/wp\/v2\/pages\/152","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.pros.ehime-u.ac.jp\/protein-complex\/index.php?rest_route=\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/www.pros.ehime-u.ac.jp\/protein-complex\/index.php?rest_route=\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/www.pros.ehime-u.ac.jp\/protein-complex\/index.php?rest_route=\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/www.pros.ehime-u.ac.jp\/protein-complex\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=152"}],"version-history":[{"count":66,"href":"https:\/\/www.pros.ehime-u.ac.jp\/protein-complex\/index.php?rest_route=\/wp\/v2\/pages\/152\/revisions"}],"predecessor-version":[{"id":1505,"href":"https:\/\/www.pros.ehime-u.ac.jp\/protein-complex\/index.php?rest_route=\/wp\/v2\/pages\/152\/revisions\/1505"}],"wp:attachment":[{"href":"https:\/\/www.pros.ehime-u.ac.jp\/protein-complex\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=152"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}