投稿者: tenno

蛋白質翻訳後修飾に関連する構造生物学

タンパク質がリボソームで合成された後、翻訳後修飾とよばれる化学修飾を受けることが知られています。リン酸化、メチル化、アセチル化など比較的小さな修飾から、糖鎖や脂肪酸さらにはタンパク質に及ぶ大きな修飾まであります。 “蛋白質翻訳後修飾に関連する構造生物学” の続きを読む

研究業績（個人：教員：天野剛志）

原著論文    R6/12/31現在
  1. Miura, K., Suzuki, Y., Ishida, K., Arakawa, M., Wu, H., Hujioka, Y., Emi, A., Maeda, K., Hamajima, R., Nakano, T., Tenno, T., Hiroaki, H., Morita, E.* (2023) Distinct motifs in the E protein are required for SARS-CoV-2 virus particle formation and lysosomal deacidification in host cells. J. Virol. 97(10) e0042623 DOI: 10.1128/jvi.00426-23
  2. Emoto, Y., Katayama, R., Hibino, E., Ishihara, S., Goda, N., Tenno, T., Kobashigawa, Y., Morioka, H., Hiroaki, H.* (2023) A Cost-Effective Immobilization Method for MBP Fusion Proteins on Microtiter Plates Using a Gelatinized Starch-Agarose Mixture and Its Application for Convenient Protein-Protein Interaction Analysis. Methods Protoc. 6, 44 DOI: 10.3990/mps6030044
  3. Nakashima, M., Goda, N., Tenno, T., Kotake, A., Inotsume, Y., Amaya, M., Hiroaki, H.* (2023) Pharmacologic Comparison of High-Dose Hesperetin and Quercetin on MDCK II Cell Viability, Tight Junction Integrity, and Cell Shape. Antioxidants 12(4), 952 DOI: 10.3390/antiox12040952
  4. Mizoguchi, T., Mikami, S., Yatou, M., Kondo, Y., Omaru, S., Kuwabara, S., Okura, W., Noda, S., Tenno, T., Hiroaki, H., Itoh, M.* (2023) Small-Molecule-Mediated Suppression of BMP Signaling by Selective Inhibition of BMP1-Dependent Chordin Cleavage. Int. J. Mol. Sci. 24, 4313 DOI: 10.3390/ijms24054313
  5. Katakoka, K., Suzuki, S., Tenno, T., Goda, N., Hibino, E., Oshima, A., Hiroaki, H.* (2022) A cryptic phosphate-binding pocket on the SPFH domain of human stomatin that regulates a novel fibril-like self-assembly. Curr. Res. Struct. Biol. 4, 158-166
  6. Hibino, E., Tenno, T., Hiroaki, H.* (2022) Relevance of Amorphous and Amyloid-Like Aggregates of the p53 Core Domain to Loss of Its DNA-Binding Activity. Front. Mol. Biosci. 9, 869851 DOI: 10.3389/fmolb/.2022.869851
  7. Hibino, E., Goda, N., Hisada, M., Tenno, T., Hiroaki, H.* (2022) Direct inhibition of the first PDZ domain of ZO-1 by glycyrrhizin is a possible mechanism of tight junction opening of Caco-2 cells. Food & Funct.13, 1953-1964 DOI: 10.1039/d1fo03062k
  8. Tenno, T., Kataoka, K., Goda, N., Hiroaki, H.* (2021) NMR-Guided Repositioning of Non-Steroidal Anti-Inflammatory Drugs into Tight Junction Modulators. Int. J. Mol. Sci., 22, 2583
  9. Matsuo, N., Goda, N., Tenno, T., Hiroaki, H.* (2021) Cryoprotective activities of FK20, a human genome-derived intrinsically disordered peptide against cryosensitive enzymes without a stereospecific molecular interaction. PeerJ Physical Chemistry 3, 20 DOI 10.7717/peerj-pchem.20
  10. Nakashima, M., Hisada, M., Goda, N., Tenno, T., Kotake, A., Inotsume, Y., Kameoka, I., Hiroaki, H.* (2020) Opposing Effect of Naringenin and Quercetin on the Junctional Compartment of MDCK II Cells to Modulate the Tight Junction. Nutrients 12, 3285
  11. Hisada, M., Hiranuma, M., Nakashima, M., Goda, N., Tenno, T., Hiroaki, H.* (2020) High dose of baicalin or baicalein can reduce tight junction integrity by partly targeting the first PDZ domain of zonula occludens-1 (ZO-1). Eur. J. Pharmacol.887, 173436
  12. Ikeda, K., Suzuki, S., Shigemitsu, Y., Tenno, T., Goda, N., Oshima, A., Hiroaki, H.* (2020) Presence of intrinsically disordered proteins can inhibit the nucleation phase of amyloid fibril formation of Aβ(1-42) in amino acid sequence independent manner. Sci. Rep. 10, 12334
  13. Iwaya, N., Goda, N., Matsuzaki, M., Narita, A., Shigemitsu, Y., Tenno, T., Abe, Y., Hoshi, M., Hiroaki, H.* (2020) Principal component analysis of data from NMR titration experiment of uniformly 15N labeled amyloid beta (1-42) peptide with osmolytes and phenolic compounds. Arch. Biochem. Biophys. 690, 108446
  14. 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
  15. 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
  16. 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.
  17. 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　
  18. 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
  19. 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
  20. 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
  21. 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
  22. 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.
  23. 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.
  24. 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.
  25. 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
  26. 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
  27. 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
  28. 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
  29. 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
  30. 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
  31. 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
  32. 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
  33. 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
  34. 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
  35. 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
  36. 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
  37. 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
  38. 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
  39. 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
  40. 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
  41. 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
  42. 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
  43. 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
  44. 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（2022）「溶液NMRを用いたタンパク質と化合物の弱い相互作用の探索・評価」B & I 80(2), 140-141
  • 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7285504号「頭皮状態改善剤及びそれを含有する化粧料」

　　  発明者　廣明秀一、天野剛志、中島美緒、佐々木瑞穂、谷口　優子

  • 特許第7304049号「タイトジャンクションの緩和剤、該緩和剤を含む化合物の吸収促進剤、並びに、該緩和剤を有効成分として含む医薬組成物、医薬部外品組成物、化粧品組成物及び食品組成物」

　　  発明者　廣明秀一、天野剛志、久田美咲

  • 特許第6760657号「タイトジャンクションの緩和剤・該緩和剤を含む薬剤吸収補助剤、及び該緩和剤を含む医薬組成物」

　　  発明者　廣明秀一、天野剛志、野田翔太

  • 特許第6587190号「タイトジャンクション形成制御剤及び該制御剤を含む医薬組成物」

　　  発明者　廣明秀一、天野剛志、中倉由香子、野田翔太

  • 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