原著論文 H30/9/27現在
- Hiroaki, H.*, Satomura, K., Goda, N., Nakakura, Y., Hiranuma, M., Tenno, T., Hamada, D., Ikegami, T., 2018., Spatial overlap of claudin- and phosphatidylinositol phosphate-binding sites on the first PDZ domain of zonula occludens 1 studied by NMR, Molecules, 23(10), 2465; doi: 10.3390/molecules23102465
- Hori, K., Ajioka, K., Goda, N., Shindo, A., Takagishi, M., Tenno, T., and Hiroaki, H.*, 2018, Discovery of Potent Disheveled/Dvl Inhibitors Using Virtual Screening Optimized With NMR-Based Docking Performance Index., Frontiers in Pharmacology. 9, Article 983, doi:3389/fphar.2018.00983
- Okazaki, H., Matsuo, N., Tenno, T., Goda, N., Shigemtsu, Y., Ota, M., and Hiroaki, H*, 2018, Using 1HN amide temperature coefficients to define intrinsically disordered regions: An alternative NMR method. Protein Science, published online, doi: 1002/pro.3485.
- Matsuo, N., Goda, N., Shimizu, K., Tenno, T., Fukuchi, F., Ota, M. and Hiroaki, H.*, 2018, Discovery of Cryoprotective Activity of Human-genome derived Intrinsically Disordered Proteins. Int J Mol Sci,, 19(2), 401; doi: 10.3390/ijms19020401
- Shigemitsu, Y., Iwaya, N., Goda, N., Matsuzaki, M., Tenno, T., Narita, A., Hoshi, M., Hiroaki, H. (2016) Nuclear magnetic resonance evidence for the dimer formation of beta amyloid peptide 1-42 in 1,1,1-3,3,3-hexafluoro-2-propanol. Anal. Biochem. 498, 59-67
- Goda, N., Shimizu, K., Kuwahara, Y., Tenno, T., Noguchi, T., Ikegami, T., Ota, M., Hiroaki, H. (2015) A Method for Systematic Assessment of Intrinsically Disordered Protein Region by NMR. Int. J. Mol. Sci. 16, 15743-15760
- Goda, N., Matsuo, N., Tenno, T., Ishino, S., Fukuchi, S., Ota, M., Hiroaki, H. (2015) An optimized Npro-based method for the expression and purification of intrinsically disordered proteins for an NMR study. Intrinsically Diord. Proteins 3(1), 1-6, DOI: 10.1080/21690707.2015.1011004
- Fujiwara, Y., Goda, N., Tamashiro, T., Narita, H., Satomura, K., Tenno, T., Nakagawa, A., Oda, M., Suzuki, M., Sakisaka, T., Takai, Y., Hiroaki, H. (2015) Crystal structure of afadin PDZ domain-nectin-3 complex shows the structural plasticity of the ligand-binding site. Protein Sci. 24(3), 376-385
- Ishino, S., Yamagami, T., Kitamura, M., Kodera, N., Mori, T., Sugiyama, S., Ando, T., Goda, N., Tenno, T., Hiroaki, H., Ishino, Y. (2014) Multiple Interactions of the Intrinsically Disordered Region between the Helicase and Nuclease Domains of the Archaeal Hef Protein. J. Biol. Chem. 289(31), 21627-21639.
- Tenno, T., Goda, N., Umetsu, Y., Ota, M., Kinoshita, K., and Hiroaki, H. (2013) Accidental Interaction between PDZ Domains and Diclofenac Revealed by NMR-Assisted Vritual Screening. Molecules, 18, 9567-9581.
- Ota, M., Koike, R., Amemiya, T., Tenno, T., Romero, P.R., Hiroaki, H., Dunker, A.K., and Fukuchi, S. (2013) An assignment of intrinsically disordered regions of proteins based on NMR structures. J Structural Biol., 181:29-36.
- Iwaya, N., Akiyama, K., Goda, N., Tenno, T., Fujiwara, Y., Hamada, D., Ikura, T., Shirakawa, M., and Hiroaki, H. (2012) Effect of Ca2+ on the microtubule-severing enzyme p60-katanin Insight into the substrate-dependent activation mechanism. FEBS J., 279(7), 1339-1352
- Isogai, S., Morimoto, D., Arita, K., Unzai, S., Tenno, T., Hasegawa, J., Sou, Y.-S., Komatsu, M., Tanaka, K., Shirakawa, M., and Tochio, H. (2011) Crystal Structure of the Ubiquitin-associated (UBA) Domain of p62 and Its Interaction with Ubiquitin. J. Biol. Chem., 286(36), 31864-31874
- Fujiwara, Y., Fujiwara, K., Goda, N., Iwaya, N., Tenno, T., Shirakawa, M., and Hiroaki, H. (2011) Structure and Function of the N-terminal Nucleolin Binding Domain of Nuclear Valocin-containing Protein-like 2 (NVL2) Harboring a Nuclear Localization Signal. J. Biol. Chem., 286(24), 21732-21741
- Hasegawa, J., Tokuda, E., Tenno, T., Tsujita, K., Sawai, H., Hiroaki, H., Takenawa, T., and Itoh T. (2011) SH3YL1 regulates dorsal ruffle formation by a novel phosphoinositide-binding domain. J. Cell Biol., 193(5), 901-916
- Umetsu, Y., Tenno, T., Goda, N., Shirawaka, M., Ikegami, T., and Hiroaki, H. (2011) Structural difference of vasoactive intestinal peptide in two distinct membrane-mimicking environments. Biochim. Biophys. Acta, 1814(5), 724-730
- Morimoto, D., Isogai, S., Tenno, T., Tochio, H., Shirakawa, M., Ariyoshi, M. (2010) Purification, crystallization and preliminary crystallographic studies of Lys48-linked polyubiquitin chains. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66, 834-837
- Igarashi, R., Sakai, T., Hara, H., Tenno, T., Tanaka, T., Tochio, H., Shirakawa, M. (2010) Distance determination in proteins inside Xenopus laevis oocytes by double electron-electron resonance experiments. J. Am. Chem. Soc. 132, 8228-8229
- Iwaya, N., Kuwahara, Y., Fujiwara, Y., Goda, N., Tenno, T., Akiyama, K., Mase, S., Tochio, H., Ikegami, T., Shirakawa, M., and Hiroaki, H. (2010) A Common Substrate Recognition Mode Conserved between Katanin p60 and VPS4 Governs Microtuble Severing and Membrane Skeleton Reorganization. J. Biol. Chem. 285, 16822-16829
- Inomata, K., Ohno, A., Tochio, H., Isogai, S., Tenno, T., Nakase, I., Takeuchi, T., Futaki, S., Ito, Y., Hiroaki, H., and Shirakawa, M. (2009) High-resolution multi-dimensional NMR spectroscopy of proteins in human cells. Nature, 458, 106-109
- Goda, N., Tenno, T., Inomata, K., Shirakawa, M., Tanaka, T., and Hiroaki, H. (2008) Intracellular protein delivery activity of peptides derived from insulin-like growth factor binding protein 3 and 5. Exp. Cell Res. 314, 2352-2361
- Sakai, T., Tochio, H., Inomata, K., Sasaki, Y., Tenno, T., Tanaka, T., Kokubo, T., Hiroaki, H., and Shirakawa, M. (2007) Fluoroscopic assessment of protein leakage during Xenopus oocytes in-cell NMR experiment by co-injected EGFP. Anal. Biochem.371, 247-249
- Goda, N., Tenno, T., Inomata, K., Iwaya, N., Sasaki, Y., Shirakawa, M., and Hiroaki, H. (2007) LBT/PTD dual tagged vector for purification, cellular protein delivery and visualization in living cells. Biochim. Biophys. Acta 1773, 141-146
- Hara, H., Tenno, T., and Shirakawa, M. (2007) Distance determination in human ubiquitin by pulsed double electron-electron resonance and double quantum coherence ESR methods. J. Magn. Reson. 184, 78-84
- Sakai, T., Tochio, H., Tenno, T., Ito, Y., Kokubo, T., Hiroaki, H., and Shirakawa, M. (2006) In-cell NMR spectroscopy of proteins inside Xenopus laevis oocytes. J. Biomol. NMR, 36, 179-188
- Ohno, A., Jee, J.-G., Fujiwara, K., Tenno, T., Goda, N., Tochio, H., Kobayashi, H., Hiroaki, H., and Shirakawa, M. (2005) Structure of the UBA Domain of Dsk2p in Complex with Ubiquitin: Molecular Determinants for Ubiquitin Recognition.Structure, 13, 521-532
- Tenno, T., Fujiwara, K., Tochio, H., Iwai, K., Morita, E. H., Hayashi, H., Murata, S., Hiroaki, H., Sato, M., Tanaka, K., and Shirakawa, M. (2004) Structural basis for distinct roles of Lys 63- and Lys48-linked polyubiquitin chains. Genes Cells, 9, 865-875
- Nomura, M., Kobayashi, T., Kohono, T., Fujiwara, K., Tenno, T., Shirakawa, M., Ishizaki, I., Yamamoto, K., Matsuyama, T., Mishima, M., Kojima, C. (2004) Paramagnetic NMR study of Cu2+-IDA complex localization on a protein surface and its application to elucidate long distance information. FEBS Lett., 566(1-3), 157-161
- Tenno, T., Goda, N., Tateishi, Y., Tochio, T., Mishima, M., Hayashi, H., Shirakawa, M., and Hiroaki, H. (2004) High-throughput construction method of expression vector of peptides for NMR study suited for isotopic labeling. Protein Eng. Des. Sel., 17, 305-314
- Goda, N., Tenno, T., Takasu, H., Hiroaki, H., and Shirakawa, M. (2004) The PRESAT-vector: Asymmetric T-vector for high-throughput screening of soluble protein domains for structural proteomics. Protein Sci., 13, 652-658
- Fujiwara, K., Tenno, T., Sugasawa, K., Jee, J.-G., Ohki, I., Kojima, C., Tochio, H., Hiroaki, H., Hanaoka, F., and Shirakawa M. (2004) Structure of the Ubiquitin-interacting Motif of S5a Bound to the Ubiquitin-like Domain of HR23B. J. Biol. Chem.,279, 4760-4767
日本語総説
- 天野剛志、廣明秀一(2013)「立体構造が明らかにしたGタンパク質共役受容体の刺激受容のしくみ」領域融合レビュー 2, e003
- 天野剛志、廣明秀一、白川昌宏(2008)「クラスB GPCR細胞外ドメインのペプチドリガンド分子認識機構」 生化学 80, 948-958
- 天野剛志、廣明秀一 (2008)「進むG蛋白質共役型受容体の立体構造解析:展望と課題」 蛋白質核酸酵素 53, 256-264
- 天野剛志、合田名都子、廣明秀一(2006)Close Up実験法「高効率かつ高速な融合タンパク質発現ベクターの構築法」 実験医学 24, 1675-1680
- 天野剛志、合田名都子、廣明秀一 (2004)「蛋白質ドメイン研究のための迅速なベクター構築法」 蛋白質核酸酵素 19, 2587-2594
著書
- 竹縄忠臣・伊藤俊樹編(2011)実験医学別冊 実験ハンドブックシリーズ改訂 タンパク質実験ハンドブック 羊土社
- 担当項目 第3章 III)ゲル濾過クロマトグラフィー、V)リガンドアフィニティークロマトグラフィー、VI)金属アフィニティークロマトグラフィー、VII)抗体アフィニティークロマトグラフィー(p60-64、p68-83)
特許
- 特許第4487036号 「新規ベクター及びその利用」
- 特許番号No.1669445(フランス)
- 特許番号60 2004 017 488.2-08(ドイツ)
発明者 廣明秀一、合田名都子、天野剛志
出願日 2004/8/31