論文

  1. Heat-induced native dimerization prevents amyloid formation by variable domain from immunoglobulin light-chain REI. Nawata M, Tsutsumi H, Kobayashi Y, Unzai S, Mine S, Nakamura T, Uegaki K, Kamikubo H, Kataoka M, Hamada D. FEBS J. 2017 Sep;284(18):3114-3127. doi: 10.1111/febs.14181. Epub 2017 Aug 13.
  2. Cutting Edge: Class II-like Structural Features and Strong Receptor Binding of the Nonclassical HLA-G2 Isoform Homodimer. Kuroki K, Mio K, Takahashi A, Matsubara H, Kasai Y, Manaka S, Kikkawa M, Hamada D, Sato C, Maenaka K. J Immunol. 2017 May 1;198(9):3399-3403. doi: 10.4049/jimmunol.1601296. Epub 2017 Mar 27.
  3. Chiaki Ota, Masamichi Ikeguchi, Akiyoshi Tanaka and Daizo Hamada. Residual structures in the unfolded state of starch-binding domain of glucoamylase revealed by near-UV circular dichroism and protein engineering techniques. Biochim Biophys Acta. 2016 Oct;1864(10):1464-72. doi: 10.1016/j.bbapap.2016.05.002. Epub
  4. Bochao Wang, Mitsuhiro Nishimura, Huamin Tang, Akiko Kawabata, Nora F. Mahmoud, Zahra Khanlari, Daizo Hamada, Hiroki Tsuruta, Yasuko Mori. Crystal structure of human herpesvirus 6B tegument protein U14. PLoS Pathog. 12(5): e1005594. doi:10.1371/journal.ppat.1005594.
  5. Hideyuki Takahashi, Naoko Adachi, Toshihiko Shirafuji, Sally Danno, Takehiko Ueyama, Michele Vendruscolo, Anton N. Shuvaev, Takuya Sugimoto, Takahiro Seki, Daizo Hamada, Kazuhiro Irie, Hirokazu Hirai, Norio Sakai and Naoaki Saito. (2014) Identification and characterization of PKCgamma, implicated in SCA14, as an amyloidogenic protein. Hum Mol Genet. 24, 525-539. doi: 10.1093/hmg/ddu4727
  6. Yuta Kobayashi, Hirotaka Tsutsumi, Tetsuyuki Abe, Kyohei Ikeda, Yuki Tashiro, Satoru Unzai, Hironari Kamikubo, Mikio Kataoka, Hidekazu Hiroaki and Daizo Hamada. (2014) Decreased amyloidogenicity by mutational modulation of surface properties of the immunoglobulin light chain BRE variable domain. Biochemistry, 53, 5162-5173. DOI: 10.1021/bi5007892
  7. Mitsuhide Hamaguchi, Hironari Kamikubo, Kayo N. Suzuki, Yoshihisa Hagihara, Itaru Yanagihara, Ikuhiro Sakata, Mikio Kataoka & Daizo Hamada*. (2013) Structural basis of α-catenin recognition by EspB from enterohaemorrhagic E. coli based on hybrid strategy using low-resolution structural and protein dissection. PLoS ONE 8, e71618. doi:10.1371/journal.pone.0071618.
  8. Naokazu Inoue, Daizo Hamada, Hironari Kamikubo, Kunio Hirata, Mikio Kataoka, Masaki Yamamoto, Masahito Ikawa, Masaru Okabe & Yoshihisa Hagihara* (2013) Molecular dissection of IZUMO1, a sperm protein essential for sperm-egg fusion. Development, 140, 3221-3229.
  9. Naoko Iwaya, Hirotoshi Takasu, Natsuko Goda, Masahiro Shirakawa, Toshiki Tanaka, Daizo Hamada, Hidekazu Hiroaki*. (2013) MIT domain of Vps4 is a Ca2+-dependent phosphoinositide-binding domain. J. Biochem. 153, 473-481.
  10. Kenji Sasahara, Koichi Morigaki, Takashi Okazaki & Daizo Hamada. Binding of islet amyloid polypeptide to supported lipid bilayers and amyloid aggregation at the membrane. (2012) Biochemistry, 51, 6908-6919.
  11. Naoko Iwaya Kohei Akiyama, Natsuko Goda, Takeshi Tenno, Yoshie Fujiwara, Daizo Hamada, Teikichi Ikura, Masahiro Shirakawa & Hidekazu Hiroaki. Effect of Ca2+ in the microtuble-severing enzyme p60-katanin. Insight into the substrate dependent activation mechanism. (2012) FEBS J. 279, 1339-1352.
  12. Kyoko Hiragami-Hamada, Kaori Shinmyozu, Daizo Hamada, Yoshiro Tatsu, Koichi Uegaki, Shinsuke Fujiwara & Jun-ichi Nakayama. N-terminal phosphorylation of HP1 promotes its chromatin binding. (2011). Mol. Cell. Biol. 31, 1186-1200.
  13. Daizo Hamada (2010) Cytoskeleton-modulating effectors of enteropathogenic and enterohemorrhagic Escherichia coli. FEBS J. 277, 2389.
  14. Daizo Hamada, Mitsuhide Hamaguchi, Kayo N. Suzuki, Ikuhiro Sakata & Itaru Yanagihara. (2010) Cytoskeleton-modulating effectors of enteropathogenic and enterohemorrhagic Escherichia coli: a case for EspB as an intrinsically less-ordered effector. FEBS J. 277, 2409-2415.
  15. Itaru Yanagihara, Kumiko Nakahira, Tsutomu Yamane, Shuji Kaida, Kouta Mayanagi, Daizo Hamada, Takashi Fukui, Kiyouhisa Ohnishi, Shin'ichiro Kajiyama, Toshiyuki, Shimizu, Mamoru Sato, Takahisa Ikegami, Mitsunori Ikeguchi, Takeshi Honda & Hiroshi Hashimoro. Structure and functional characterization of Vibrio parahaemolyticus thermostable direct hemolysin. (2010) J. Biol. Chem. 285, 16267-16274.
  16. Kenji Sasahara, Daniel Hall & Daizo Hamada Effect of lipid type on the binding of lipid vesicles to islet amyloid polypeptide amyloid fibrils. (2010) Biochemistry 49, 3040-3048.
  17. Daizo Hamada, Toshiki Tanaka, Gian Gaetano Tartaglia, Amol Pawar, Michele Vendruscolo, Mei Kawamura, Atsuo Tamura, Naoki Tanaka & Christopher M. Dobson. Competition between folding, native state dimerisation and amyloid aggregation in β-lactoglobulin. (2009). J. Mol. Biol. 386, 878-890.
  18. Mitsuhide Hamaguchi, Daizo Hamada, Kayo N. Suzuki, Ikuhiro Sakata & Itaru Yanagihara. Molecular basis of actin reorganization promoted by binding of enterohaemorrhagic Escherichia coli EspB to α-catenin. (2008). FEBS J. 275, 6260-6267.
  19. Naoki Tanaka, Ryoji Tanaka, Matsumi Tokuhara, Shigeru Kunugi, Yin-Fai Lee & Daizo Hamada. Amyloid fibril formation and chaperone-like activity of peptides from A-crystallin. (2008). Biochemisty, 47, 2961-2967.
  20. Daizo Hamada, Kouhei Tsumoto, Makoto Sawara, Naoki Tanaka, Kumiko Nakahira, Kentaro Shiraki & Itaru Yanagihara. Effect of an amyloidogenic sequence attached to yellow fluorescent protein. (2008). Proteins, 72, 811-821.
  21. Daizo Hamada, Takashi Higurashi, Tomoko Miyata, Kouta Mayanagi, Takashi Fukui, Tatsuya Iida, Takeshi Honda & Itary Yanagihara. Tetrameric structure of thermostable direct hemolysin from Vibrio parahaemolyticus revealed by ultracentrifugation, small angle X-ray scattering and electron microscopy. (2007). J. Mol. Biol. 365, 187-195.
  22. Atsushi Tabata, Fumihiko Namba, Minoru Yamada, Taeko Hasegawa, Kumiko Nakahira, Daizo Hamada, Hiroyuki Kitajima, Eiichiro Fukusaki & Itaru Yanagihara. Expression and purification of recombinant human annexin A2 in Pichia pastoris and utility of expression product for detecting annexin A2 antibody. (2006). J. Biosci. Bioeng. 101, 190-197.
  23. 濵田大三「アミロイド線維から機能性タンパク質ナノ繊維へ」生物工学 特集 (2006) 84, 398-400.
  24. Takashi Fukui, Kentaro Shiraki, Daizo Hamada, Koji Hara, Tomoko Miyata, Shinsuke Fujiwara, Kouta Mayanagi, Keiko Yanagihara, Testuya Iida, Eiichiro Fukusaki, Tadayuki Imanaka, Takeshi Honda & Itaru Yanagihara. (2005). Thermostable direct hemolysin of Vibrio parahaemolyticus is a bacterial reversible amyloid toxin. Biochemistry, 44, 9825-9832.
  25. Tomoaki Kato, Daizo Hamada, Takashi Fukui, Makoto Hayashi, Takeshi Honda, Yoshikatsu Murooka & Itaru Yanagihara. (2005). A pH-dependent conformational change in EspA, a component of the Escherichia coli O157:H7 type III secretion system. FEBS J. 272, 2773-2783.
  26. Yoshiaki Furukawa, Tadato Ban, Daizo Hamada, Koichi Ishimori, Yuji Goto & Isao Morishima. (2005). Electron transfer reaction in a single protein molecule observed by total intrenal reflection fluorescence microscopy. J. Am. Chem. Soc. 127, 2098-2103.
  27. Daizo Hamada, Tomoaki Kato, Takahisa Ikegami, Kayo N. Suzuki, Makoto Hayashi, Yoshikatsu Murooka, Takeshi Honda, & Itaru Yanagihara. EspB from enterohaemorrhagic Escherichia coli is a natively partially folded protein. (2005). FEBS J. 272, 756-768
  28. Tadato Ban, Masaru Hoshino, Satoshi Takahashi, Daizo Hamada, Kazuhito Hasegawa, Hironobu Naiki & Yuji Goto. (2004). Direct observation of A amyloid fibril growth and inhibition. J. Mol. Biol. 344, 757-767.
  29. Minoru Yamada, Koji Inui, Daizo Hamada, Kumiko Nakahira, Keiko Yanagihara, Norio Sakai, Toshinori Nishigaki, Keiichi Ozono & Itaru Yanagihara. (2004). Analysis of recombinant human saposin A expressed by Pichia pastoris. Biochem. Biophys. Res. Commin. 318, 588-593.
  30. Daizo Hamada, Itaru Yanagihara & Kouhei Tsumoto. (2004). Engineering amyloidgenicity toward development of nanofibrillar materials. Trends in Biotechnology, 22, 93-97.
  31. Lesley H. Greene, Daizo Hamada, Stephen J. Eyles & Keith Brew. (2003). Conserved signature proposed for folding in the lipocalin superfamily. FEBS Letters, 553, 39-44.
  32. Tadato Ban, Daizo Hamada, Kazuhiro Hasegawa, Hironobu Naiki & Yuji Goto. (2003). Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence. J. Biol. Chem. 278, 16462-16465.
  33. 濵田大三「アミロイド?形成機構と新規材料としての可能性」生物物理 (2003) 43(245), 4-8.
  34. Daizo Hamada & Christopher M. Dobson. (2002) A kinetic study of β-lactoglobulin amyloid fibril formation promoted by urea. Protein Sci. 11, 2417-2426.
  35. Masahiro Maeda, Daizo Hamada, Masaru Hoshino, Yayoi Onda, Toshiharu Hase & Yuji Goto. (2002) Partially folded structure of flavin adenine dinucleotide-depleted ferredoxin-NADP-reductase with residual NADP binding domain. J. Biol. Chem. 277, 17101-17107.
  36. Thelma A. Pertinhez, Daizo Hamada, Lorna J. Smith, Fabrizio Chiti, Niccol? Taddei, Massimo Stefani & Christopher M. Dobson. (2000) Initial denaturing conditions influence the slow folding phase of acylphosphatase associated with proline isomerization. Protein Sci. 9, 1466-1473.
  37. Daizo Hamada, Fabrizio Chiti, J. I?aki Guijarro, Mikio Kataoka, Niccol? Taddei & Christopher M. Dobson. (2000) Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol. Nat. Struct. Biol. 7, 58-61.
  38. Fabrizio Chiti, Niccol? Taddei, Paul Webster, Daizo Hamada, Tania Fiaschi, Giampietro Ramponi & Christopher M. Dobson. (1999) Acceleration of the folding of acylphosphatase by stabilization of local secondary structure. Nat. Struct. Biol. 6, 380-387.
  39. Yoshihisa Hagihara, Masaru Hoshino, Daizo Hamada, Mikio Kataoka & Yuji Goto. (1998) Chain-like conformation of heat-denatured ribonuclease and cytochrome c as evidenced by solution X-ray scattering. Folding & Design, 3, 195-201.
  40. Masaru Hoshino, Yoshihisa Hagihara, Daizo Hamada, Mikio Kataoka & Yuji Goto. (1997) Trifluoroethanol-induced conformational transition of hen egg-white lysozyme studied by small-angle X-ray scattering. FEBS Letters, 416, 72-76.
  41. Daizo Hamada & Yuji Goto. (1997) The equilibrium intermediate of β-lactoglobulin with non-native helical structure. J. Mol. Biol. 269, 479-487.
  42. Daizo Hamada, Shin-ichi Segawa & Yuji Goto. (1996) Non-native helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. Nat. Struct. Biol. 3, 868-873.
  43. Yutaka Kuroda, Daizo Hamada & Yuji Goto. (1996) High helical peptide fragments corresponding to -strand regions of β-lactoglobulin observed by 2D-NMR spectroscopy. Folding & Design, 1, 255-263.
  44. Daizo Hamada, Yutaka Kuroda, Mikio Kataoka, Saburo Aimoto, Tetsuro Yoshimura & Yuji Goto. (1996) Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c. J. Mol. Biol. 256, 172-186.
  45. Daizo Hamada, Yutaka Kuroda, Toshiki Tanaka & Yuji Goto. (1995) High helical propensity of the peptide fragments derived from β-lactoglobulin. J. Mol. Biol. 254, 737-746.
  46. Daizo Hamada, Harumi Fukada, Katsutada Takahashi & Yuji Goto. (1995) Salt-induced formation of the molten globule state of apomyoglobin studied by isothermal titration calorimetry. Thermochemica Acta, 266, 385-400.
  47. Daizo Hamada, Shun-ichi Kidokoro, Harumi Fukada, Katsutada Takahashi & Yuji Goto. (1994) Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry. Proc. Natl. Acad. Sci. USA, 91, 10325-10329.
  48. Yuji Goto, Yoshihisa Hagihara, Daizo Hamada, Masaru Hoshino & Ichiro Nishii. (1993) Acid-induced unfolding and refolding transitions of cytochrome c: A three-state mechanism in H2O and D2O. Biochemistry, 32, 11878-11885.
  49. Daizo Hamada, Hoshino Masaru, Mikio Kataoka, Anthony L. Fink & Yuji Goto. (1993) Intermediate conformational state of apocytochrome c. Biochemistry, 32, 10351-10358.

著書

  1. Cao, Y., Hamada D., Kong, Y., Cao, P. & Chen J. (2012) "Probing dynamic fibril-formation by an integrated microscopic approach" In Current Microscopy Contributions to Advances in Science and Technology, Formatex. Vol. 1 pp668-677.
  2. 濵田大三.改訂 タンパク質実験ハンドブック.竹縄忠臣、伊藤俊樹 編.(2010) 羊土社 第3章 タンパク質精製法 2. カラムクロマトグラフィーによる精製 Ⅰ)クロマトグラフィー総論、Ⅱ)イオン交換クロマトグラフィー、Ⅷ)逆相HPLC、3. タンパク質の巻き戻し.)
  3. Daizo Hamada & Yuji Goto. (2005). "Salt- and alcohol-induced partially folded intermediates" In Protein Folding Handbook (J. Buchner, T. Kiefhaber, eds.) Wiley-VCH, Germany, pp. 884-915.

招待講演など

  1. 濵田大三. 「免疫グロブリン軽鎖可変 ドメインの構造揺らぎと分子病態」 第三回岐阜構造生物学・医学・論理的創薬研究会シンポジウム 2014年3月18日 岐阜大学
  2. 濵田大三. 「免疫グロブリン関連アミロイドーシス発症の分子病態学 - 構造揺らぎの伝播と不安定化」 立命館大学 R-GIRO研究プログラム「蛋白質のフォールディングおよびフォールディング病発症機構の解明のための統合研究」セミナー 2014年3月14日 立命館大学
  3. 濵田大三. 「タンパク質構造決定 ~各手法の強み・留意点」 文部科学省「地域イノベーション戦略支援プログラム」関西ライフイノベーション戦略プロジェクト「先進技術活用力養成講座(第一回) 構造ベース創薬セミナー」(主催:神戸大学連携創造本部、協賛:(公財)計算科学振興財団、理研 HPCI計算生命科学推進プログラム、理研 播磨研究所放射光科学総合研究センター) 2014年3月7日 計算科学振興財団
  4. 濵田大三. 「免疫グロブリン関連アミロイドーシス発症における分子病態学」 名古屋大学大学院 創薬化学研究科 創薬科学セミナー(共催 理学研究科附属構造生物学研究センター) 2014年1月31日 名古屋大学
  5. 濵田大三. 特別講演 「腸管出血性大腸菌による中毒発生のメカニズム」?構造生物学的・生化学的アプローチ? 第35回 日本中毒学会総会・学術集会 2013年7月19日;大阪
  6. Hamada D. Extracting Structural Fluctuations of Proteins by Combination of Low-and High-resolution Data Sets. Workshop on Innovation and Pioneering Technology. 18-19 February 2013. Kobe, Japan
  7. Hamada D. Regulation of Structural Properties of Higher Order Aggregates by Conformational Fluctuations within a Protein Molecule. Institute for Protein Research Seminar, Osaka University. "Impacts on Supersaturation on Protein Science". 18-19 June 2012. Osaka, Japan
  8. Hamada D. Conformational states of immunoglobulin light chain variable domain. 2010 Christopher Dobson 60th Birthday Symposium "From Neuroscience to Nanoscience" 2010 April 8-9; Cambridge, UK.
  9. 濵田大三. アミロイド線維形成蛋白質の線維化機構とリン脂質膜との相互作用. 神戸大学自然環境論セミナー 2009年7月22日;神戸
  10. 濵田大三. アミロイド形成を抑制するネガティブデザイン. 蛋白研セミナー「蛋白質立体構造を基盤とするプリオン現象の解明と制御」 2009年7月13-14日;吹田
  11. Hamada D. Factors that promote or protect against formation of amyloid fibrils by folded proteins. 2009 BIT Lifesciences' 2nd Annual PepCon-2009, 2009 April 2-4; Seoul, South Korea.
  12. Hamada D. "Negative design principle to avoid the formation of misfolded aggregates as revealed by β-lactoglobulin. The Joint 2nd Pacific Rim International Conference on Protein Science (PRICPS) / 4th Asia-Oceania Human Proteomics Organization meeting. 2008 June 22-26; Carins, Australia.
  13. 濵田大三. 大腸菌O157のIII型分泌機構に関与するEspBの立体構造と機能」 蛋白研セミナー 「疾患関連タンパク質の構造生物学」 2006年3月7-8日;吹田
  14. 濵田大三. 蛋白質の自己組織化現象-折れたたみ反応における局所的相互作用の役割-. 立命館大学理工学振興会研究分科会「水の科学と産業利用」第1回 分科会 2004年12月10日;滋賀県草津市
  15. 濵田大三. βラクトグロブリンのアミロイド形成反応. 立命館大学理工学研究所プロジェクト研究シンポジウム?蛋白質を主とする生体系の化学?生物科学と溶液化学の融合?  2004年1月15日;滋賀県草津市
  16. 濵田大三. 蛋白質のミスフォールディング?アミロイド凝集反応の速度論的解析. 第33回 中部化学関係学協会支部連合秋季大会、2002年10月5-6日;名古屋
  17. 濵田大三,黒田裕,田中俊樹,瀬川新一,後藤祐児 β-蛋白質であるβ-ラクトグロブリンのヘリックス構造を含む、折りたたみ中間状態: 非階層的折れたたみ反応機構. 第47回 タンパク質構造討論会 1996年10月;大阪
inserted by FC2 system