原著論文 (* corresponding author)

  1. Hibino, E., Goda, N., Hisada, M., Tenno, T., and 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., RSC Food & Function, 13, 1953–1964, doi; 10.1039/D1FO03062K
  2. Matsuo, N., Goda, N., Tenno, T., and Hiroaki, H*. 2021, Cryoprotective activities of FK20, a human genome-derived intrinsically disordered peptide against cryosensitive enzymes without a stereospecific molecular interaction., Peer J Physical Chemistry, 3:e20, doi; 10.7717/peerj-pchem.20, https://peerj.com/articles/pchem-20/#
  3. Tenno, T., Kataoka, K., Goda, N.,and Hiroaki, H*. 2021. NMR-guided repositioning of non-steroidal anti-inflammatory drugs into tight junction modulators., Int J Mol Sci, 22(5), 2583, doi; 10.3390/ijms22052583
  4. Nakashima, M., Hisada, M., Goda, N., Tenno, T., Kotake, A., Inotsume, Y., Kameoka, I. and Hiroaki, H*. 2020, Opposing effect of naringenin and quercetin on the junctional compartment of MDCK II cells to modulate the tight junction., Nutrients, 12(11), 3285, doi; 10.3390/nu12113285, https://www.mdpi.com/2072-6643/12/11/3285
  5. 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). J. Pharmacol. 887, 173436, doi: 10.1016/j.ejphar.2020.173436, https://www.sciencedirect.com/science/article/pii/S0014299920305288
  6. Ikeda, K., Suzuki, S., Shigemitsu, Y., Tenno, T., Goda, N., Oshima, A., and 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, doi: 10.1038/s41598-020-69129-1, https://www.nature.com/articles/s41598-020-69129-1
  7. Iwaya, N., Goda, N., Matsuzaki, M., Narita, A., Shigemitsu, Y., Tenno, T., Abe, Y., Ueda, T., Hoshi, M., and Hiroaki, H.*, 2020, Principal Component Analysis of Data from NMR Titration Experiment of Uniformly 15N Labelled Amyloid Beta (1–42) Peptide with Osmolytes and Phenolic Compounds. Archives of Biochemistry and Biophysics. 690, 108446, doi: 10.1016/j.abb.2020.108446
  8. Moai, Y., Hiroaki, H., Obika, S., and Kodama, T.*, 2019, Synthesis of selenomethylene-locked nucleic acids (SeLNA) nucleoside unit bearing an adenine base, Nucleosides, Nucleotides and Nucleic Acids, 12, 1-10. doi: 10.1080/15257770.2019.1675169.
  9. 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
  10. 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
  11. 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.
  12. 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 
  13. Niwa, N., Shimizu, S., Maeda, Y., Hiroaki, H. and Ueno, Y.*, 2017, Benzene-Glycol Nucleic Acid (BGNA)-DNA Chimeras: Synthesis, Binding Properties, and Ability to Elicit Human RNase H Activity. RSC Advances. (2017), 7, 25378-25386. DOI: 10.1039/C7RA03896H
  14. Shimasaki, T., Ohtsuka, H., Naito, C., Tenno, T., Hiroaki, H., Murakami, H., Hirofumi Aiba, H*. 2017, Ecl1 is a zinc binding protein that is involved in the zinc-limitation dependent extension of chronological lifespan in fission yeast. Molecular Genetics and Genomics, 292(2):475-481. DOI: 10.1007/s00438-016-1285-x
  15. Shigemitsu, Y., Iwaya, N., Goda, N., Matsuzaki, M., Abe., Y., Narita, A., Tenno, T. Hoshi, M., and 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. Analytical Biochemistry,   Accepted. DOI: 10.1016/j.ab.2015.12.021
  16. Ohnishi, T., Yanazawa, M., Kitamura, Y., Sasahara, T., Nishiyama, T., Komura, H., Hiroaki, H., Fukazawa, Y., Kii, I., Kakita, A., Takeuchi, A., Ito, A., Takeda, H., Hirao, H., Inoue, M., Muramatsu, S., Matsui, K., Tada, M., Sato, M., Goda, N., Takino, N., Sakai, S., Arai, Y., Umetsu, Y., Takahashi, H., Hagiwara, M., Sawasaki, T., Iwasaki, G., Nakamura, Y., Nabeshima, Y., Teplow, T. B., and Hoshi, M.* 2015, Na,K-ATPasea3 Is a Death Target of Alzheimer Patient Amyloid-b Assembly. 2015, Proc. Natl. Acad. Sci. U.S.A., 112(32):E4465–E4474. DOI: 10.1073/pnas.1421182112
  17. Goda, N., Shimizu, K., Kuwahara, Y., Tenno, T., Noguchi,T., Ikegami, T., Ota, M., and Hiroaki, H*., A Method for Systematic Assessment of Intrinsically Disordered Protein Regions by NMR. 2015, Int J Mol Sci, 16 (7):15743-15760. DOI: 10.3390/ijms160715743
  18. Goda, N., Matsuo, N., Tenno, T., Ishino, S., Ishino, Y., Fukuchi, S., Ota, M., and Hiroaki, H*. 2015, An optimized Npro-based method for the expression and purification of intrinsically disordered proteins for an NMR study. Intrinsically Disordere Proteins, 3(1):1-6. DOI: 1080/21690707.2015.1011004
  19. 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 extended ligand-binding site. Protein Sci., 24(3):376-385 DOI: 10.1002/pro.2628
  20. Kobayashi, Y., Tsutsumi, H., Abe, T., Ikeda, K., Tashiro, Y., Unzai, S., Kamikubo,H., Kataoka, M., Hiroaki, H., and Hamada, D*. 2014., Decreased amyloidogenicity by mutational modulation of surface properties of the immunoglobulin light chain BRE variable domain. Biochemistry, 53(31):5162-5173. DOI: 10.1021/bi5007892
  21. Ishino, S., Yamagami, T., Kitamura, M., Kodera, N., Mori, T., Sugiyama, S., Ando, T., Goda, N., Tenno, T., Hiroaki, H., and 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. doi: 10.1074/jbc.M114.554998
  22. Fukuchi, S*., Amemiya, T., Sakamoto, S., Nobe, Y., Hosoda, K., Kado, Y., Murakami, D. S., Koike, R., Hiroaki, H., and Ota M*. 2013., IDEAL in 2014 illustrates interaction network composed of intrinsically disordered proteins and their binding partners. Nucleic Acids Res., 42:D320-325. doi: 10.1093/nar/gkt1010.
  23. Tenno, T., Goda, N., Umetsu, Y., Furuse, M., Ota, M., Kinoshita, K., and Hiroaki, H*. 2013. Accidental interaction between PDZ domains and diclofenac revealed by NMR-guided virtual screening. Molecules, 18:9567-9581. doi:10.3390/molecules18089567
  24. Iwaya, N., Takasu, H., Goda, N., Shirakawa, M., Tanaka, T., Hamada, D., and Hiroaki, H*. 2013. MIT domain of Vps4 is a Ca2+-dependent phosphoinositide-binding domain. J Biochem., 153(5):473-481.
  25. 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.
  26. Tsuruta, T., Umetsu, Y., Iwaya, N., Taniguchi, R., Goda, N., Tenno, T., Kuwahara, Y., and Hiroaki, H*., 2012. 1H, 13C, and 15N resonance assignment of the SPFH domain of human stomatin. NMR Assign, 6: 23-25.
  27. Iwaya,, Akiyama, K., Goda, N., Tenno, T., Fujiwara, Y., Hamada, D., Ikura, T., Shirakawa, M., and Hiroaki, H*. 2012. Effect of Ca2+ on microtubule severing enzyme katanin p60; insight into the substrate dependent activation mechanism. FEBS J., 279:1339–1352.
  28. Fukuchi, S*., Sakamoto, S., Nobe, Y., Murakami, D. S., Amemiya, T., Hosoda, K., Koike, R. Hiroaki, H., and Ota, M*., 2012. IDEAL – Intrinsically Disordered proteins with Extensive Annotations and Literature. Nucleic Acids Research (database issue),. 40 (1):D507-511. (Epub 2011 Nov 8.)
  29. Hiroaki, H*., Umetsu, Y., Hoshi, M., Nabeshima, Y. and Kohda, D., 2011. A Simplified Recipe for Assigning Amide NMR Signals Using Combinatorial 14N Amino Acid Inverse-Labeling. J Structural Functional Genomics., 12 (3): 167-174.
  30. Hasegawa, J., Tokuda, E., Tenno, T., Tsujita, K., Sawai, H., Hiroaki, H., Takenawa, T. Itoh, T*. 2011. SH3YL1 regulates dorsal ruffle formation by a novel phosphoinositide–binding domain. J Cell Biol 193 (5):901-916.
  31. Fujiwara, Y., Fujiwara, K., Goda, N., Iwaya, N., Tenno, T., Shirakawa, M., Hiroaki, H*. 2011. Structure and function of the N-terminal nucleolin binding domain of nuclear Valocin containing protein like 2 (NVL2) harboring a nucleolar localization signal. 2011. J Biol Chem 286 (24):21732-21741.
  32. Umetsu, Y., Taniguchi, R., Satomura, R., Goda, N., Ikegami, T., Furuse, M., and Hiroaki, H*. 1H, 13C, and 15N resonance assignment of the first PDZ domain of mouse ZO-1. Biomol. NMR Assign 5 (2): 207-210.
  33. Umetsu, Y, Tenno, T., Goda, N., Shirakawa, M., Ikegami, T., and Hiroaki, H*. Structural difference of vasoactive intestinal peptide (VIP) in two distinct membrane mimicking conditions. BBA-Proteins Proteomics. 1814:724-730.
  34. Motono, C., Nakata, J., Koike, R., Shimizu, K., Shirota, M., Amemiya, T., Tomii, K., Nagano, N., Sakaya, N., Misoo, K., Sato, M., Kidera, A., Hiroaki, H., Shirai, T., Kinoshita, K., Noguchi, T., and Ota, M. 2010. SAHG, a comprehensive database of predicted structures of all human proteins. Nucleic Acids Res 39(suppl 1): D487-D493.
  35. Nishimasu, R., Komori, H., Higuchi, Y., Nishimasu, H., and Hiroaki, H*. Crystal structure of a PFU-PUL domain pair of Saccharomyces cerevisiae Doa1/Ufd3. Kobe J Med Sci 56: E125-E139.
  36. Ohnishi, H., Tochio, H., Kato, Z., Kimura, T., Hiroaki, H., Kondo, N., and Shirakawa, M. 2010. 1H, 13C, and 15N resonance assignment of the TIR domain of human MyD88. Biomol NMR Assign 4: 123-125.
  37. Iwaya, N., Kuwahara, Y., Fujiwara, Y., Goda, N., Tenno, T., Akiyama, K., Mase, S., Tochio, H., Ikegami, T., Shirakawa, M., and Hiroaki, H*. A common substrate recognition mode conserved between katanin p60 and VPS4 governs microtubule severing and membrane skeleton reorganization. J Biol Chem 285: 16822-16829.
  38. Jee, J., Mizuno, T., Kamada, K., Tochio, H., Chiba, Y., Yanagi, K., Yasuda, G., Hiroaki, H., Hanaoka, F., and Shirakawa, M. 2010. Structure and mutagenesis studies of the C-terminal region of licensing factor Cdt1 enable the identification of key residues for binding to replicative helicase Mcm proteins. J Biol Chem 285: 15931-15940.
  39. Kuwahara, Y., Unzai, S., Nagata, T., Hiroaki, Y., Yokoyama, H., Matsui, I., Ikegami, T., Fujiyoshi, Y., and Hiroaki, H*. Unusual thermal disassembly of the SPFH domain oligomer from Pyrococcus horikoshii. Biophys J 97: 2034-2043.
  40. 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.
  41. Ohnishi, H., Tochio, H., Kato, Z., Orii, K. E., Li, A., Kimura, T., Hiroaki, H., Kondo, N., and Shirakawa, M. 2009. Structural basis for the multiple interactions of the MyD88 TIR domain in TLR4 signaling. Proc Natl Acad Sci U S A 106: 10260-10265.
  42. Kuwahara, Y., Ohno, A., Morii, T., Yokoyama, H., Matsui, I., Tochio, H., Shirakawa, M., and Hiroaki, H*. The solution structure of the C-terminal domain of NfeD reveals a novel membrane-anchored OB-fold. Protein Sci 17: 1915-1924.
  43. Inomata, K., Ohki, I., Tochio, H., Fujiwara, K., Hiroaki, H., and Shirakawa, M. 2008. Kinetic and thermodynamic evidence for flipping of a methyl-CpG binding domain on methylated DNA. Biochemistry-US 47: 3266-3271.
  44. Goda, N., Tenno, T., Inomata, K., Shirakawa, M., Tanaka, T., and Hiroaki, H*. Intracellular protein delivery activity of peptides derived from insulin-like growth factor binding proteins 3 and 5. Exp Cell Res 314: 2352-2361.
  45. Tomida, J., Masuda, Y., Hiroaki, H., Ishikawa, T., Song, I., Tsurimoto, T., Tateishi, S., Shiomi, T., Kamei, Y., Kim, J., Kamiya, K., Vaziri, C., Ohmori, H., and Todo, T. 2008. DNA damage-induced ubiquitylation of RFC2 subunit of replication factor C complex. J Biol Chem 283: 9071-9079.
  46. Iwaya, N., Goda, N., Unzai, S., Fujiwara, K., Tanaka, T., Tomii, K., Tochio, H., Shirakawa, M., and Hiroaki, H*. Fine-tuning of protein domain boundary by minimizing potential coiled coil regions. J Biomol NMR 37: 53-63.
  47. Goda, N., Tenno, T., Inomata, K., Iwaya, N., Sasaki, Y., Shirakawa, M., and Hiroaki, H*. LBT/PTD dual tagged vector for purification, cellular protein delivery and visualization in living cells. Biochim Biophys Acta-Mol Cell Res 1773: 141-146.
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  57. Shiozawa, K., Maita, N., Tomii, K., Seto, A., Goda, N., Akiyama, Y., Shimizu, T., Shirakawa, M., and Hiroaki, H*. Structure of the N-terminal domain of PEX1 AAA-ATPase. Characterization of a putative adaptor-binding domain. J Biol Chem 279: 50060-50068.
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  1. Hibino, E.* and Hiroaki, H.*, Potential of rescue and reactivation of tumor suppressor p53 for cancer therapy, 2022, Biophys. Rev., (invited review)(available online), DOI:10.1007/s12551-021-00915-5
  2. Hiroaki, H., Kohda, D*. Chapter 20: Protein-ligand interactions studied by NMR, in “Experimental Approaches of NMR Spectroscopy ‐ Methodology and Application to Life Science and Materials Science” (Springer), edited by The NMR Society of Japan, 2017: 579-600. ISBN 978-981-10-5965-0
  3. Shigemitsu, Y., Hiroaki, H*. Common molecular pathogenesis of disease-related intrinsically disordered proteins revealed by NMR analysis, 2018, J Biochemistry, 163(1), (invited review) :11–17. DOI:10.1093/jb/mvx056
  4. Hiroaki, H*., Application of NMR in Drug Discovery, 2016, Special Periodical Reports; Nuclear Magnetic Resonance Volume 45 (Royal Society of Chemistry) : 217–239 (invited review)
  5. Hiroaki, H*., Recent applications of isotopic labeling for protein NMR in drug discovery. Expert Opinion on Drug Discovery, invited review, 8(5):523-536. DOI:10.1517/17460441.2013.779665
  6. Uesugi, S*., Odai, O., Kodama, H., Hiroaki, H., Sakata, T., and Tanaka, T. Hammerhead-type RNA Enzyme and its Derivatives Which Consist of Three RNA Oligomer Strands. Structure, & Function, (Adenine Press) Volume 2: Proteins 165-172.(1992)


  1. 技術情報協会 疾患の原因遺伝子・タンパク質の解析と診断・治療技術の開発(2022)
    担当項目 第2章タンパク質解析による疾患原因の解明とその手法 第1節 「タンパク質構造解析による発症原因・関連メカニズムの解明」,印刷中
  2. 生物物理 (日本生物物理学会誌) 2022, 62(1), 39-42
    NMR から見たアミロイド β ペプチドの線維化機構解析
  3. 医歯薬出版株式会社 医学のあゆみ, 2021, 278(6), 653-662
    天然変性タンパク質と創薬 (「特集 構造生命科学による創薬への挑戦」
  4. 東京化学同人 相分離生物学の全貌(現代化学増刊46) (2020), 124-128
    担当項目 第III部 天然変性タンパク質
  5. 技術情報協会 In silico創薬におけるスクリーニングの高速化・効率化技術 編 (2018)
    担当項目 第一章 第8節NMRによるin-silicoスクリーニング計算結果の検証
  6. 再生医療(日本再生医療学会雑誌) 2015, 14(3), 52-53
    用語解説 「天然変性蛋白質」 (2015)
  7. 生化学 2013, 85(8), 679-686
    特集「タンパク質構造機能相関再考」~ NMRで見るタンパク質-低分子相互作用 (2013)
  8. 融合領域レビュー 2013, 2, e003, DOI: 10.7875/leading.author.2.e003)
    立体構造が明らかにしたGタンパク質共役型受容体の刺激受容のしくみ (2013)
  9. 羊土社 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 竹縄忠臣・伊藤俊樹編(2011)
    担当項目 第2章 タンパク質取扱いの基礎技術(1.タンパク質の定量法、2.タンパク質の濃縮法(各種濃縮法)、3.タンパク質の透析法、4.タンパク質の保存法)、第3章 タンパク質精製法(1.タンパク質の抽出と分画、2-4. 疎水性クロマトグラフィー、4.構造研究のためのタンパク質精製前処理 NMR、X線解析に必要なタンパク質) p21-37, p49-52, p65-68, p98-102
  10. 講談社サイエンティフィク タンパク質の立体構造入門 藤博幸編(2010)
    担当項目 3 立体構造決定法・NMR
  11. 呼吸 (Respiration Research) 2010, 29(6), 571-578
  12. JSBi 日本バイオインフォマティクス学会ニュースレター 2009, 19, 5-6
  13. 講談社サイエンティフィク 分光測定入門シリーズ8 核磁気共鳴分光法 日本分光学会編(2009)
    担当項目 第一章 NMRの原理
  14. 生化学 2008, 80(10), 948-958.
    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
  15. 蛋白質核酸酵素2008, 53(2),256-264.
    天野剛志・廣明 秀一*
  16. 蛋白質核酸酵素2007, 52(4), 381-388.
    シリーズ実験キット解体新書・第12回・戻れ!活性よ、構造よ -リフォールディングキットの中身と原理
    清水真人・廣明 秀一(編著)
  17. 蛋白質核酸酵素2007, 52(3), 279-286.
    清水真人・廣明 秀一(編著)
  18. 蛋白質核酸酵素2007, 52(2), 183-190.
    清水真人・廣明 秀一(編著)
  19. 蛋白質核酸酵素2007, 52(1), 85-92.
    シリーズ実験キット解体新書・第9回・細胞破砕 自由自在!
    清水真人・廣明 秀一(編著)
  20. 蛋白質核酸酵素2006, 51(15), 2375-2382.
    清水真人・廣明 秀一(編著)
  21. 蛋白質核酸酵素2006, 51(13), 1869-1878.
    清水真人・廣明 秀一(編著)
  22. 蛋白質核酸酵素2006, 51(12), 1781-1790.
    清水真人・廣明 秀一(編著)
  23. 蛋白質核酸酵素2006, 51(11), 1623-1630.
    清水真人・廣明 秀一(編著)
  24. JSBi 日本バイオインフォマティクス学会ニュースレター 2006, 13, 6-7.
    廣明 秀一*
  25. 蛋白質核酸酵素2006, 51(9), 1095-1102.
    清水真人・廣明 秀一(編著)
  26. 共立出版 バイオインフォマティクス事典 日本バイオインフォマティクス学会編
    担当項目 1.核磁気共鳴法 2.X線解析 3.生体分子の構造決定法 (2006)
    廣明 秀一*
  27. バイオテクノロジージャーナル 2006, 6(4), 453-456
    廣明 秀一*
  28. 蛋白質核酸酵素2006, 51(8), 997-1004.
    清水真人・廣明 秀一(編著)
  29. 実験医学 2006, 24(11), 1675-1680
    天野剛志・合田名都子・廣明 秀一
  30. 蛋白質核酸酵素2006, 51(7), 887-894.
    清水真人・廣明 秀一(編著)
  31. 蛋白質核酸酵素2006, 51(1), 61-71.
    清水真人・廣明 秀一(編著)
  32. 生物物理 2006, 46(3), 159-163
    ペルオキシソーム因子PEX1 ATPaseのN末端ドメインの立体構造が示したAAA ATPase間の進化的類縁関係
    廣明 秀一・塩澤久美子・富井健太郎*
  33. 分光研究 2006, 55(1), 54-66
    講座-磁気共鳴分光. I.NMRの原理
    廣明 秀一
  34. 生物薬科学実験講座 核酸I・広川書店2004
    第一章 核酸の合成 : 3 DNAの化学合成,  pp80-119
    廣明 秀一・上杉 晴一*
  35. 蛋白質核酸酵素2004, 49(12), 2587-2594.
    タンパク質ドメイン研究のための迅速なベクター構築法 (新実験講座)
    天野 剛志・合田 名都子・廣明 秀一
  36. ゲノミクス・プロテオミクスの新展開「生物情報の解析と応用」 今中忠行監修 エヌティーエス 2004
    第二編プロテオミクス・第三節2 p657-p661
    廣明 秀一
  37. 分子生物学イラストレイテッド・改訂第2版 羊土社 2002年
    第8章 分子生物学の新領域 1.構造生物学 p380-387
    渡邊 太一・廣明 秀一・白川 昌宏
  38. 蛋白質核酸酵素 2001 Oct;46(13):1936-1942
    廣明 秀一
  39. 蛋白質核酸酵素 2001 Feb;46(2):167-168
    くり返し構造のもたらす多様性 TPRドメインの複合体、結晶構造2題
    廣明 秀一
  40. 生物工学会誌 2000 Oct;78(10):428-431
    廣明 秀一


  1. Urata, H., Shimizu, H., Hiroaki, H., Kohda, D., and Akagi, M. “Characterization of DNA, RNA and DNA/RNA duplexes containing an L-nucleotide.” Nucleic Acids Res Supp 1, 243-244 (2001).
  2. Fujii, S., Tanaka, Y., Uesugi, S., Tanaka, T., Sakata, T., and Hiroaki, H. “Conformational features of the four successive non-Watson-Crick base pairs in RNA duplex.” Nucleic Acids Symp Ser 27, 63-64 (1992).
  3. Uesugi, S., Kodama, H., Hiroaki, H., and Odai, O. “Properties of hammerhead-type RNA enzyme derivatives which contain a G-to-I replacement in the loop region.” Nucleic Acids Symp Ser 27, 13-14 (1992).
  4. Fujii, S., Tanaka, Y., Tomita, K., Sakata, T., Hiroaki, H., Tanaka, T., and Uesugi, S. “Molecular structure of extraordinarily stable RNA: model building and X-ray analysis.” Nucleic Acids Symp Ser 25, 181-182 (1991).
  5. Hiroaki, H., Uesugi, S., and Fujii, S. “The molecular recognition mechanism of DNA by bleomycin.” Nucleic Acids Symp Ser 25, 147-148 (1991).
  6. Hiroaki, H., Ebata, T., Uesugi, S., and Fujii, S. “Base recognition mechanism of bleomycin: solution structure of d(GGGGAGCTCCCC)2 based on 1H-NMR and restrained molecular dynamics.” Nucleic Acids Symp Ser 22, 53-54 (1990).
  7. Uesugi, S., Odai, O., Hiroaki, H., Kodama, H., Sakata, T., and Tanaka, T. “Conformation and properties of hammerhead-type RNA enzymes.” Nucleic Acids Symp Ser 22, 41-42 (1990).
  8. Ebata, T., Hiroaki, H., Uesugi, S., and Sugiura, Y. “Identification of DNA degradation products by antitumor antibiotic, esperamicin.” Nucleic Acids Symp Ser 22, 19-20 (1990).
  9. Odai, O., Sakata, T., Orita, M., Hiroaki, H., Uesugi, S., and Tanaka, T. “Synthesis and properties of RNA with catalytic activity.” Nucleic Acids Symp Ser 21, 105-106 (1989).
  10. Uesugi, S., Oda, Y., Hiroaki, H., and Ikehara, M. “NMR studies on DNA hairpin structures with a five nucleotide loop.” Nucleic Acids Symp Ser 21, 65-66 (1989).


  1. 7WH3 Solution structure of human stomatin SPFH domain in a phosphate buffer (2021)
  2. 6LCB Crystal structure of human Dishevelled1 PDZ domain with its inhibitor NPL3009 (2019)
  3. 6LCA Crystal structure of human Dishevelled1 PDZ domain homotrimer (2019)
  4. 3VQG Crystal Structure Analysis of the PDZ Domain Derived from the Tight Junction Regulating Protein (2012)
  5. 3VGF  Crystal Structure Analysis of the PDZ Domain Derived from the Tight Junction Regulating Protein (2012)
  6. 3AXA Crystal structure of afadin PDZ domain in complex with the C-terminal peptide from nectin-3 (2011)
  7. 2RRM Interplay between phosphatidyl-inositol-phosphates and claudins upon binding to the 1st PDZ domain of zonula occludens 1 (2011)
  8. 2RRH NMR structure of vasoactive intestinal peptide in Methanol (2010)
  9. 2RRI NMR structure of vasoactive intestinal peptide in DPC Micelle (2010)
  10. 2RRE Structure and function of the N-terminal nucleolin binding domain of nuclear valocine containing protein like 2 (NVL2) harboring a nucleolar localization signal (2010)
  11. 2RQQ Structure of C-terminal region of Cdt1 (2009)
  12. 2RPA The solution structure of N-terminal domain of microtubule severing enzyme (2008)
  13. 2RPB The solution structure of membrane protein (SPFH domain PH0470) (2008)
  14. 2Z5V Solution structure of the TIR domain of human MyD88 (2007)
  15. 2EXD NfeD domain isolated from PH0471 membrane protein of unknown function (2005)
  16. 2D2P pituitary adenylate cyclase activating peptide 38 (PACAP38) (2005)
  17. 2D07 Thymine deglycosylase with SUMO-3 (2005)
  18. 1WYW Thymine deglycosylase with SUMO-1 (2005)
  19. 1WR1   The complex sturcture of Dsk2p UBA with ubiquitin (2004)
  20. 1WR0   The solution structure of human Vps4B MIT domain (2004)
  21. 1WLF   Structure Of The N-Terminal Domain Of Pex1 AAA-ATPase: Characterization Of A Putative Adaptor-Binding Domain (2004)
  22. 1UEL   Solution Structure Of Ubiquitin-Like Domain Of Hhr23B Complexed With Ubiquitin-Interacting Motif Of Proteasome Subunit S5A (2003)
  23. 1GD5   Solution Structure Of the PX domain from Human p47phox NADPH oxidase. (2001)
  24. 413D   A’-form RNA double helix in the Single Crystal Structure of r(UGAGCUUCGGCUC). (1998)
  25. 373D   A’-RNA conformation in the Crystal Structure of r(UGAGCUUCGGCUC). (1998)備考 p56Lck SH3 domainの溶液構造については企業での研究のためPDBにdepositしていない。


  1. 特願2021-168639 「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、
    出願日:2021/10/14 (株式会社日華化学との共同出願)
  2. 特願2018-209383 「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、化粧品組成物および食品組成物」、発明者: 廣明秀一、天野剛志、久田美咲、
  3. 特願2017-235036 「Wntシグナル伝達系阻害剤、該阻害剤を有効成分として含む医薬組成物」、発明者: 廣明秀一、天野剛志、進藤麻子、高岸麻紀、堀公則、
  4. 特許6760657 [特願2017-520717] 「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、
    出願日:2016/5/24 (再表)
  5. 特許6587190 [特願2016-535943] 「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、
    出願日:2015/7/22 (再表)
  6. 特許6643761 [特願2016-503988] 「タンパク質凍結保存用保護剤」、発明者: 廣明秀一、天野名都子、松尾直紀、太田元規、福地佐斗志、岩村佳奈、
    出願日:2015/1/6 (再表)
  7. 米国特許 US. Patent 8415146                        許可日2013年4月9日
    「Vector and utilization of the same」
    発明者             廣明秀一 合田名都子 天野剛志
  8. 特許第4647871号(特願2001-544328) 許可日2010年12月17日、
    発明者                  廣明秀一 神田大輔、
    出願日 2000/12/01
  9. 特許第4487036号(特願2003-308773)許可日2010年4月9日
    発明者             廣明秀一 合田名都子 天野剛志、
    出願日    2004/08/31
  10. 欧州特許番号 No.1669445 (独・仏で成立、ドイツ特許番号 60 2004 017 488.2-08)
    発明者             廣明秀一 合田名都子 天野剛志
    出願日    2004/08/31
  11. 特願2004-350635  「ヒトVps4bのMITドメインと二価または三価の金属イオン複合体の構造的特徴およびヒトVps4bのMITドメインによるホスファチジルイノシトールリン酸認識機構」
    発明者             白川昌宏 廣明秀一 高須博敏
    出願日    2004/12/03
  12. 特願2004-231652  「酵母DSK2のユビキチン結合ドメインとモノユビキチンとの複合体の構造的特徴および酵母DSK2のユビキチン結合ドメインによるモノユビキチン認識機構」
    発明者             白川昌宏 廣明秀一 大野綾子
    出願日    2004/08/06
  13. PCT/JP2004/12523 「新規ベクター及びその利用」
    発明者             廣明秀一 合田名都子 天野剛志
    出願日    2004/08/31
  14. 特願2003-308773  「新規ベクター及びその利用」
    発明者             廣明秀一 合田名都子 天野剛志
    出願日    2004/08/31
  15. 特願平11-346193  「タンパク質の構造座標及びNMR化学シフトならびにそれらの使用」
    発明者             神田大輔 廣明秀一 住本英樹
    出願日    2000/12/01
Updated: 2022/03/03 — 16:42