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Yuji Goto

後藤 祐児

Graduate School of Engineering, Specially Appointed Researcher

gtyj8126 protein.osaka-u.ac.jp

keyword Protien Science

Education

  • - 1982, Osaka University
  • - 1982, Osaka University, Graduate School, Division of Natural Science, Biologieal Chemistry
  • - 1977, Osaka University, School of Science
  • - 1977, Osaka University, Faculty of Science

Research Areas

  • Life sciences, Biophysics
  • Life sciences, Structural biochemistry
  • Nanotechnology/Materials, Nanobioscience
  • Nanotechnology/Materials, Nanomaterials

Professional Memberships

  • 日本蛋白質科学会
  • Protein Society
  • 生物物理学会
  • 生化学会

Papers

  • Mass spectrometry-based proteomic analysis of proteins adsorbed by hexadecyl-immobilized cellulose bead column for the treatment of dialysis-related amyloidosis., Suguru Yamamoto,Keiko Yamamoto,Yoshitoshi Hirao,Keiichi Yamaguchi,Kichitaro Nakajima,Mami Sato,Miho Kawachi,Mio Domon,Kei Goto,Kentaro Omori,Noriaki Iino,Hisaki Shimada,Ryuzi Aoyagi,Isei Ei,Shin Goto,Yuji Goto,Fumitake Gejyo,Tadashi Yamamoto,Ichiei Narita, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, p. 1-11, 2024/02/11
  • Supersaturation, a critical factor underlying proteostasis of amyloid fibril formation., Yuji Goto,Kichitaro Nakajima,Suguru Yamamoto,Keiichi Yamaguchi, Journal of molecular biology, p. 168475-168475, 2024/02/02
  • Ultrastiff Amyloid-Fibril Network of α-Synuclein Formed by Surface Seeding Reaction Confirmed by Multichannel Electrodeless Quartz-Crystal-Microbalance Biosensor, Lianjie Zhou,Touko Hajiri,Kichitaro Nakajima,César Aguirre,Kensuke Ikenaka,Hideki Mochizuki,Keiichi Yamaguchi,Yuji Goto,Hirotsugu Ogi, ACS Sensors, American Chemical Society (ACS), 2023/06/26
  • Phosphatidylinositol-3,4,5-trisphosphate interacts with alpha-synuclein and initiates its aggregation and formation of Parkinson’s disease-related fibril polymorphism, Chi Jing Choong,César Aguirre,Keita Kakuda,Goichi Beck,Hiroki Nakanishi,Yasuyoshi Kimura,Shuichi Shimma,Kei Nabekura,Makoto Hideshima,Junko Doi,Keiichi Yamaguchi,Kichitaro Nakajima,Tomoya Wadayama,Hideki Hayakawa,Kousuke Baba,Kotaro Ogawa,Toshihide Takeuchi,Shaymaa Mohamed,Mohamed Badawy,Shigeo Murayama,Seiichi Nagano,Yuji Goto,Yohei Miyanoiri,Yoshitaka Nagai,Hideki Mochizuki,Kensuke Ikenaka, ACTA NEUROPATHOLOGICA, Vol. 145, No. 5, p. 573-595, 2023/03
  • Mechanisms of polyphosphate-induced amyloid fibril formation triggered by breakdown of supersaturation, Keiichi Yamaguchi,Kichitaro Nakajima,Yuji Goto, Biophysics and Physicobiology, Biophysical Society of Japan, Vol. 20, No. 1, p. n/a-n/a, 2023
  • Supersaturation-Dependent Formation of Amyloid Fibrils, Yuji Goto,Masahiro Noji,Kichitaro Nakajima,Keiichi Yamaguchi, Molecules, MDPI AG, Vol. 27, No. 14, p. 4588-4588, 2022/07/19
  • Pathway Dependence of the Formation and Development of Prefibrillar Aggregates in Insulin B Chain, Yuki Yoshikawa,Keisuke Yuzu,Naoki Yamamoto,Ken Morishima,Rintaro Inoue,Masaaki Sugiyama,Tetsushi Iwasaki,Masatomo So,Yuji Goto,Atsuo Tamura,Eri Chatani, Molecules, MDPI AG, Vol. 27, No. 13, p. 3964-3964, 2022/06/21
  • Conformational change in the monomeric alpha-synuclein imparts fibril polymorphs, Cesar Aguirre,Kensuke Ikenaka,Masatomo So,Takahiro Maruno,Keiichi Yamaguchi,Kichitaro Nakajima,Chi-Jing Choong,Kei Nabekura,Goichi Beck,Kentaro Tomii,Yu Yamamori,Junko Doi,Tomoyasu Matsubara,Maho Morishima,Keita Kakuda,Makoto Hideshima,Yasuyoshi Kimura,Seiichi Nagano,Kousuke Baba,Shigeo Murayama,Hirotsugu Ogi,Yoshitaka Nagai,Yasushi Kawata,Susumu Uchiyama,Yohei Miyanoiri,Yuji Goto,Hideki Mochizuki, bioRxiv, Cold Spring Harbor Laboratory, 2022/02/10
  • Macromolecular crowding and supersaturation protect hemodialysis patients from the onset of dialysis-related amyloidosis, Kichitaro Nakajima,Keiichi Yamaguchi,Masahiro Noji,César Aguirre,Kensuke Ikenaka,Hideki Mochizuki,Lianjie Zhou,Hirotsugu Ogi,Toru Ito,Ichiei Narita,Fumitake Gejyo,Hironobu Naiki,Suguru Yamamoto,Yuji Goto, Cold Spring Harbor Laboratory, 2022/02/04
  • Development of HANABI, an ultrasonication-forced amyloid fibril inducer, Yuji Goto,Kichitaro Nakajima,Keiichi Yamaguchi,Masatomo So,Kensuke Ikenaka,Hideki Mochizuki,Hirotsugu Ogi, Neurochemistry International, Elsevier BV, Vol. 153, p. 105270-105270, 2022/02
  • Two-step screening method to identify α-synuclein aggregation inhibitors for Parkinson's disease., Makoto Hideshima,Yasuyoshi Kimura,César Aguirre,Keita Kakuda,Toshihide Takeuchi,Chi-Jing Choong,Junko Doi,Kei Nabekura,Keiichi Yamaguchi,Kichitaro Nakajima,Kousuke Baba,Seiichi Nagano,Yuji Goto,Yoshitaka Nagai,Hideki Mochizuki,Kensuke Ikenaka, Scientific reports, Vol. 12, No. 1, p. 351-351, 2022/01/10
  • Acceleration of amyloid fibril formation by multichannel sonochemical reactor, Kentaro Noi,Kichitaro Nakajima,Keiichi Yamaguchi,Masatomo So,Kensuke Ikenaka,Hideki Mochizuki,Yuji Goto,Hirotsugu OGI, Japanese Journal of Applied Physics, IOP Publishing, 2021/12/08
  • Strong acids induce amyloid fibril formation of β2-microglobulin via an anion-binding mechanism, Keiichi Yamaguchi,Kenshiro Hasuo,Masatomo So,Kensuke Ikenaka,Hideki Mochizuki,Yuji Goto, Journal of Biological Chemistry, Elsevier BV, Vol. 297, No. 5, p. 101286-101286, 2021/11
  • 1Pa4-5 Accelerating amyloid fibril formation by multi-channel ultrasonic chemical reactor, Noi Kentaro,Nakajima Kichitaro,Yamaguchi Keiichi,So Masatomo,Ikenaka Kensuke,Mochizuki Hideki,Goto Yuji,Ogi Hirotugu, Proceedings of Symposium on Ultrasonic Electronics, Institute for Ultrasonic Elecronics, Vol. 42, 2021/10/25
  • Half-Time Heat Map Reveals Ultrasonic Effects on Morphology and Kinetics of Amyloidogenic Aggregation Reaction, Kichitaro Nakajima,Hajime Toda,Keiichi Yamaguchi,Masatomo So,Kensuke Ikenaka,Hideki Mochizuki,Yuji Goto,Hirotsugu Ogi, ACS Chemical Neuroscience, American Chemical Society (ACS), Vol. 12, No. 18, p. 3456-3466, 2021/09/15
  • Disaggregation Behavior of Amyloid β Fibrils by Anthocyanins Studied by Total-Internal-Reflection-Fluorescence Microscopy Coupled with a Wireless Quartz-Crystal Microbalance Biosensor, Kentaro Noi,Kensuke Ikenaka,Hideki Mochizuki,Yuji Goto,Hirotsugu Ogi, Analytical Chemistry, American Chemical Society (ACS), 2021/08/05
  • pHによるウレミックトキシンの蛋白結合能の変化, 山本 卓,山口 圭一,土門 美緒,伊藤 徹,後藤 眞,後藤 祐児,成田 一衛, 日本腎臓学会誌, (一社)日本腎臓学会, Vol. 63, No. 4, p. 481-481, 2021/06
  • Polyphenol-solubility alters amyloid fibril formation of α-synuclein., Masatomo So,Yuto Kimura,Keiichi Yamaguchi,Toshihiko Sugiki,Toshimichi Fujiwara,Cesar Aguirre,Kensuke Ikenaka,Hideki Mochizuki,Yasushi Kawata,Yuji Goto, Protein science : a publication of the Protein Society, Vol. 30, No. 8, p. 1701-1713, 2021/05/27
  • Optimized sonoreactor for accelerative amyloid-fibril assays through enhancement of primary nucleation and fragmentation, Kichitaro Nakajima,Kentaro Noi,Keiichi Yamaguchi,Masatomo So,Kensuke Ikenaka,Hideki Mochizuki,Hirotsugu Ogi,Yuji Goto, Ultrasonics Sonochemistry, Elsevier BV, Vol. 73, p. 105508-105508, 2021/05
  • Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils., Eri Chatani,Keisuke Yuzu,Yumiko Ohhashi,Yuji Goto, International journal of molecular sciences, Vol. 22, No. 9, 2021/04/21
  • Polyphosphates induce amyloid fibril formation of α-synuclein in concentration-dependent distinct manners., Keiichi Yamaguchi,Masatomo So,César Aguirre,Kensuke Ikenaka,Hideki Mochizuki,Yasushi Kawata,Yuji Goto, The Journal of biological chemistry, p. 100510-100510, 2021/03/04
  • pH-Dependent Protein Binding Properties of Uremic Toxins In Vitro., Suguru Yamamoto,Kenichi Sasahara,Mio Domon,Keiichi Yamaguchi,Toru Ito,Shin Goto,Yuji Goto,Ichiei Narita, Toxins, Vol. 13, No. 2, 2021/02/04
  • Multistep Changes in Amyloid Structure Induced by Cross-Seeding on a Rugged Energy Landscape., Keisuke Yuzu,Naoki Yamamoto,Masahiro Noji,Masatomo So,Yuji Goto,Tetsushi Iwasaki,Motonari Tsubaki,Eri Chatani, Biophysical journal, Vol. 120, No. 2, p. 284-295, 2021/01/19
  • Breakdown of supersaturation barrier links protein folding to amyloid formation, Masahiro Noji,Tatsushi Samejima,Keiichi Yamaguchi,Masatomo So,Keisuke Yuzu,Eri Chatani,Yoko Akazawa-Ogawa,Yoshihisa Hagihara,Yasushi Kawata,Kensuke Ikenaka,Hideki Mochizuki,József Kardos,Daniel E. Otzen,Vittorio Bellotti,Johannes Buchner,Yuji Goto, Communications Biology, Springer Science and Business Media LLC, Vol. 4, No. 120, 2021/01
  • 光技術の認知症研究への応用の可能性 放射光を用いたレビー小体の微細構造解析, 荒木 克哉,八木 直人,永井 義隆,後藤 祐児,望月 秀樹, Dementia Japan, (一社)日本認知症学会, Vol. 34, No. 4, p. 464-464, 2020/10
  • Dialysis-related amyloidosis associated with a novel β2-microglobulin variant., Hiroki Mizuno,Junichi Hoshino,Masatomo So,Yuta Kogure,Takeshi Fujii,Yoshifumi Ubara,Kenmei Takaichi,Tetsuko Nakaniwa,Hideaki Tanaka,Genji Kurisu,Fuyuki Kametani,Mayuko Nakagawa,Tsuneaki Yoshinaga,Yoshiki Sekijima,Keiichi Higuchi,Yuji Goto,Masahide Yazaki, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, Vol. 28, No. 1, p. 1-8, 2020/09/02
  • Time-Resolved Observation of Evolution of Amyloid-β Oligomer with Temporary Salt Crystals., Kichitaro Nakajima,Tomoya Yamazaki,Yuki Kimura,Masatomo So,Yuji Goto,Hirotsugu Ogi, The journal of physical chemistry letters, Vol. 11, No. 15, p. 6176-6184, 2020/08/06
  • Distinct residual and disordered structures of alpha-synuclein analyzed by amide-proton exchange and NMR signal intensity., Rina Okuwaki,Iori Shinmura,Shiki Morita,Akimasa Matsugami,Fumiaki Hayashi,Yuji Goto,Chiaki Nishimura, Biochimica et biophysica acta. Proteins and proteomics, p. 140464-140464, 2020/06/01
  • Amyloid Formation of α-Synuclein Based on the Solubility- and Supersaturation-Dependent Mechanism, Maya Sawada,Keiichi Yamaguchi,Miki Hirano,Masahiro Noji,Masatomo So,Daniel Otzen,Yasushi Kawata,Yuji Goto, Langmuir, American Chemical Society (ACS), Vol. 36, No. 17, p. 4671-4681, 2020/05/05
  • Isoelectric point-amyloid formation of α-synuclein extends the generality of the solubility and supersaturation-limited mechanism, Koki Furukawa,Cesar Aguirre,Masatomo So,Kenji Sasahara,Yohei Miyanoiri,Kazumasa Sakurai,Keiichi Yamaguchi,Kensuke Ikenaka,Hideki Mochizuki,Jozsef Kardos,Yasushi Kawata,Yuji Goto, Current Research in Structural Biology, Elsevier BV, Vol. 2, p. 35-44, 2020/04/05
  • Inorganic polyphosphate potentiates lipopolysaccharide-induced macrophage inflammatory response, Toru Ito,Suguru Yamamoto,Keiichi Yamaguchi,Mami Sato,Yoshikatsu Kaneko,Shin Goto,Yuji Goto,Ichiei Narita, Journal of Biological Chemistry, American Society for Biochemistry & Molecular Biology (ASBMB), Vol. 295, No. 12, p. 4014-4023, 2020/03/20
  • The Route from the Folded to the Amyloid State: Exploring the Potential Energy Surface of a Drug-Like Miniprotein., Nóra Taricska,Dániel Horváth,Dóra K Menyhárd,Hanna Ákontz-Kiss,Masahiro Noji,Masatomo So,Yuji Goto,Toshimichi Fujiwara,András Perczel, Chemistry (Weinheim an der Bergstrasse, Germany), Vol. 26, No. 9, p. 1893-1893, 2020/02/11
  • Amyloid Formation under Complicated Conditions in Which β2-Microglobulin Coexists with Its Proteolytic Fragments, Hiroya Muta,Masatomo So,Kazumasa Sakurai,Jozsef Kardos,Hironobu Naiki,Yuji Goto, Biochemistry, American Chemical Society, 2019/11
  • Polyphosphates diminish solubility of a globular protein and thereby promote amyloid aggregation, Kenji Sasahara,Keiichi Yamaguchi,Masatomo So,Yuji Goto, Journal of Biological Chemistry, Elsevier BV, Vol. 294, No. 42, p. 15318-15329, 2019/10
  • Parkinson's disease is a type of amyloidosis featuring accumulation of amyloid fibrils of α-synuclein., Katsuya Araki,Naoto Yagi,Koki Aoyama,Chi-Jing Choong,Hideki Hayakawa,Harutoshi Fujimura,Yoshitaka Nagai,Yuji Goto,Hideki Mochizuki, Proceedings of the National Academy of Sciences of the United States of America, Vol. 116, No. 36, p. 17963-17969, 2019/09/03
  • Heating during agitation of β2-microglobulin reveals that supersaturation breakdown is required for amyloid fibril formation at neutral pH., Noji M,Sasahara K,Yamaguchi K,So M,Sakurai K,Kardos J,Naiki H,Goto Y, The Journal of biological chemistry, Vol. in press, 2019/09
  • Possible mechanisms of polyphosphate-induced amyloid fibril formation of β<sub>2</sub>-microglobulin., Zhang CM,Yamaguchi K,So M,Sasahara K,Ito T,Yamamoto S,Narita I,Kardos J,Naiki H,Goto Y, Proceedings of the National Academy of Sciences of the United States of America, Proceedings of the National Academy of Sciences, Vol. 116, No. 26, p. 12833-12838, 2019/06
  • Ultrasonication-based rapid amplification of α-synuclein aggregates in cerebrospinal fluid., Keita Kakuda,Kensuke Ikenaka,Katsuya Araki,Masatomo So,César Aguirre,Yuta Kajiyama,Kuni Konaka,Kentaro Noi,Kousuke Baba,Hiroshi Tsuda,Seiichi Nagano,Takuma Ohmichi,Yoshitaka Nagai,Takahiko Tokuda,Omar M A El-Agnaf,Hirotsugu Ogi,Yuji Goto,Hideki Mochizuki, Scientific reports, Vol. 9, No. 1, p. 6001-6001, 2019/04/12
  • Aggregation-phase diagrams of β<sub>2</sub>-microglobulin reveal temperature and salt effects on competitive formation of amyloids <i>versus</i> amorphous aggregates., Adachi M,Noji M,So M,Sasahara K,Kardos J,Naiki H,Goto Y, The Journal of biological chemistry, Vol. 293, No. 38, p. 14775-14785, 2018/09
  • Heat-Induced Aggregation of Hen Ovalbumin Suggests a Key Factor Responsible for Serpin Polymerization., Noji M,So M,Yamaguchi K,Hojo H,Onda M,Akazawa-Ogawa Y,Hagihara Y,Goto Y, Biochemistry, American Chemical Society (ACS), Vol. 57, No. 37, p. 5415-5426, 2018/08
  • Structural basis of the correct subunit assembly, aggregation, and intracellular degradation of nylon hydrolase., Seiji Negoro,Naoki Shibata,Young-Ho Lee,Ikki Takehara,Ryo Kinugasa,Keisuke Nagai,Yusuke Tanaka,Dai-Ichiro Kato,Masahiro Takeo,Yuji Goto,Yoshiki Higuchi, Scientific reports, Vol. 8, No. 1, p. 9725-9725, 2018/06/27
  • Salt-induced formations of partially folded intermediates and amyloid fibrils suggests a common underlying mechanism, Yuji Goto,Masayuki Adachi,Hiroya Muta,Masatomo So, Biophysical Reviews, Springer Verlag, Vol. 10, No. 2, p. 493-502, 2018/04/01
  • Membrane-induced initial structure of α-synuclein control its amyloidogenesis on model membranes., Terakawa MS,Lee YH,Kinoshita M,Lin Y,Sugiki T,Fukui N,Ikenoue T,Kawata Y,Goto Y, Biochimica et biophysica acta. Biomembranes, Elsevier BV, Vol. 1860, No. 3, p. 757-766, 2018/03
  • A new look at an old view of denaturant induced protein unfolding, Damien Hall,Akira Kinjo,Yuji Goto, Analytical Biochemistry, Academic Press Inc., Vol. 542, p. 40-57, 2018/02/01
  • Nanoscale Dynamics of Protein Assembly Networks in Supersaturated Solutions, Y. Matsushita,H. Sekiguchi,C. Jae Wong,M. Nishijima,K. Ikezaki,D. Hamada,Y. Goto,Y. C. Sasaki, Scientific Reports, Nature Publishing Group, Vol. 7, No. 1, 2017/12/01
  • Role of An Intramolecular Disulfide Bond in Stability of Lipocalin-Type Prostaglandin D Synthase, Yoshiaki Teraoka,Yoshiaki Teraoka,Shogo Atsuji,Young-Ho Lee,Yuji Goto,Takashi Inui, PROTEIN SCIENCE, WILEY, Vol. 26, p. 107-107, 2017/12
  • Heparin-dependent aggregation of hen egg white lysozyme reveals two distinct mechanisms of amyloid fibrillation, Ayame Nitani,Hiroya Muta,Masayuki Adachi,Masatomo So,Kenji Sasahara,Kazumasa Sakurai,Eri Chatani,Kazumitsu Naoe,Hirotsugu Ogi,Damien Hall,Yuji Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 292, No. 52, p. 21219-21230, 2017/12
  • Non-Native α-Helices in the Initial Folding Intermediate Facilitate the Ordered Assembly of the β-Barrel in β-Lactoglobulin., Sakurai K,Yagi M,Konuma T,Takahashi S,Nishimura C,Goto Y, Biochemistry, Vol. 56, No. 36, p. 4799-4807, 2017/09
  • マイクロ秒 過飽和 状態の ダイナミクス観察, 松下 祐福,関口 博史,太田 昇,一柳 光平,池崎 圭吾,後藤 祐児,佐々木 裕次, 日本結晶成長学会誌, Vol. 44, 2017/08
  • Non-Native alpha-Helices in the Initial Folding Intermediate Facilitate the Ordered Assembly of the beta-Barrel in beta-Lactoglobulin, Sakurai, K,Yagi, M,Konuma, T,Takahashi, S,Nishimura, C,Goto, Y, Biochemistry, 2017/08
  • Model membrane size-dependent amyloidogenesis of Alzheimer's amyloid-beta peptides, Misaki Kinoshita,Erina Kakimoto,Mayu S. Terakawa,Yuxi Lin,Tatsuya Ikenoue,Masatomo So,Toshihiko Sugiki,Ayyalusamy Ramamoorthy,Yuji Goto,Young-Ho Lee, PHYSICAL CHEMISTRY CHEMICAL PHYSICS, ROYAL SOC CHEMISTRY, Vol. 19, No. 24, p. 16257-16266, 2017/06
  • Drastic acceleration of fibrillation of insulin by transient cavitation bubble, Kichitaro Nakajima,Daisuke Nishioka,Masahiko Hirao,Masatomo So,Yuji Goto,Hirotsugu Ogi, Ultrasonics Sonochemistry, Vol. 36, p. 206-211, 2017/05/01
  • Heparin-induced amyloid fibrillation of (2)-microglobulin explained by solubility and a supersaturation-dependent conformational phase diagram, Masatomo So,Yasuko Hata,Hironobu Naiki,Yuji Goto, PROTEIN SCIENCE, WILEY, Vol. 26, No. 5, p. 1024-1036, 2017/05
  • Optimized Ultrasonic Irradiation Finds Out Ultrastable A beta(1-40) Oligomers, Kichitaro Nakajima,Masatomo So,Kazuma Takahashi,Yoh-ichi Tagawa,Masahiko Hirao,Yuji Goto,Hirotsugu Ogi, JOURNAL OF PHYSICAL CHEMISTRY B, AMER CHEMICAL SOC, Vol. 121, No. 12, p. 2603-2613, 2017/03
  • Variation of Free-Energy Landscape of the p53 C-Terminal Domain Induced by Acetylation: Enhanced Conformational Sampling, Shinji Iida,Tadaaki Mashimo,Takashi Kurosawa,Hironobu Hojo,Hiroya Muta,Yuji Goto,Yoshifumi Fukunishi,Haruki Nakamura,Junichi Higo, JOURNAL OF COMPUTATIONAL CHEMISTRY, WILEY-BLACKWELL, Vol. 37, No. 31, p. 2687-2700, 2016/12
  • Non-covalent forces tune the electron transfer complex between ferredoxin and sulfite reductase to optimize enzymatic activity., Kim JY,Kinoshita M,Kume S,Gt H,Sugiki T,Ladbury JE,Kojima C,Ikegami T,Kurisu G,Goto Y,Hase T,Lee YH, The Biochemical journal, Vol. 473, No. 21, p. 3837-3854, 2016/11
  • Recognizing and analyzing variability in amyloid formation kinetics: Simulation and statistical methods, Damien Hall,Ran Zhao,Masatomo So,Masayuki Adachi,German Rivas,John A. Carver,Yuji Goto, ANALYTICAL BIOCHEMISTRY, ACADEMIC PRESS INC ELSEVIER SCIENCE, Vol. 510, p. 56-71, 2016/10
  • A small-angle X-ray scattering study of alpha-synuclein from human red blood cells., Katsuya Araki,Naoto Yagi,Rie Nakatani,Hiroshi Sekiguchi,Masatomo So,Hisashi Yagi,Noboru Ohta,Yoshitaka Nagai,Yuji Goto,Hideki Mochizuki, Scientific reports, Vol. 6, p. 30473-30473, 2016/07/29
  • Thioflavin T-Silent Denaturation Intermediates Support the Main-Chain-Dominated Architecture of Amyloid Fibrils, Sayaka Noda,Masatomo So,Masayuki Adachi,Jozsef Kardos,Yoko Akazawa-Ogawa,Yoshihisa Hagihara,Yuji Goto, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 55, No. 28, p. 3937-3948, 2016/07
  • Protein aggregate turbidity: Simulation of turbidity profiles for mixed-aggregation reactions, Damien Hall,Ran Zhao,Ian Dehlsen,Nathaniel Bloomfield,Steven R. Williams,Fumio Arisaka,Yuji Goto,John A. Carver, Analytical Biochemistry, Vol. 498, p. 78-94, 2016/04
  • A Stable Mutant Predisposes Antibody Domains to Amyloid Formation through Specific Non-Native Interactions, Cardine N. Nokwe,Manuel Hora,Martin Zacharias,Hisashi Yagi,Jirka Peschek,Bernd Reif,Yuji Goto,Johannes Buchner, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, Vol. 428, No. 6, p. 1315-1332, 2016/03
  • Amorphous Aggregation of Cytochrome c with Inherently Low Amyloidogenicity Is Characterized by the Metastability of Supersaturation and the Phase Diagram, Yuxi Lin,Jozsef Kardos,Mizue Imai,Tatsuya Ikenoue,Misaki Kinoshita,Toshihiko Sugiki,Koichiro Ishimori,Yuji Goto,Young-Ho Lee, LANGMUIR, AMER CHEMICAL SOC, Vol. 32, No. 8, p. 2010-2022, 2016/03
  • Amorphous Aggregation of Cytochrome C with Inherently low Amyloidogenicity is Characterized by the Metastability of Supersaturation and the Phase Diagram, Yuxi Lin,Jozsef Kardos,Koichiro Ishimori,Yuji Goto,Young-Ho Lee, BIOPHYSICAL JOURNAL, CELL PRESS, Vol. 110, No. 3, p. 399A-399A, 2016/02
  • Revisiting supersaturation as a factor determining amyloid fibrillation, Masatomo So,Damien Hall,Yuji Goto, CURRENT OPINION IN STRUCTURAL BIOLOGY, CURRENT BIOLOGY LTD, Vol. 36, p. 32-39, 2016/02
  • Nucleus factory on cavitation bubble for amyloid beta fibril, Kichitaro Nakajima,Hirotsugu Ogi,Kanta Adachi,Kentaro Noi,Masahiko Hirao,Hisashi Yagi,Yuji Goto, SCIENTIFIC REPORTS, NATURE PUBLISHING GROUP, Vol. 6, 2016/02
  • A14 Rapid aggregate reaction of prion protein under the continuous ultrasonication, Yamaguchi Keiichi,Goto Yuji,Kuwata Kazuo, Proceedings of the Annual Meeting of the Japan Society of Sonochemistry, Japan Society of Sonochemistry, Vol. 25, p. 97-98, 2016
  • A15 The effects of ultrasonication on amyloid fibrils, So Masatomo,Goto Yuji, Proceedings of the Annual Meeting of the Japan Society of Sonochemistry, Japan Society of Sonochemistry, Vol. 25, p. 99-100, 2016
  • P28 Ultrasonic power-dependent competitive formation of amyloid fibrils and amorphous aggregates, Adachi Masayuki,So Masatomo,Sakurai Kazumasa,Kardos Jozef,Goto Yuji, Proceedings of the Annual Meeting of the Japan Society of Sonochemistry, Japan Society of Sonochemistry, Vol. 25, p. 87-88, 2016
  • P27 Supersaturation-limited amyloid fibrillation revealed by ultrasonication, Muta Hiroya,Lee Young-Ho,Kardos Jozef,Lin Yuxi,Yagi Hisashi,So Masatomo,Sakurai Kazumasa,Goto Yuji, Proceedings of the Annual Meeting of the Japan Society of Sonochemistry, Japan Society of Sonochemistry, Vol. 25, p. 85-86, 2016
  • P29 Amyloid fibrillation of hen egg white lysozyme accelerated by ultrasonication, Nitani Ayame,Muta Hiroya,Adachi Masayuki,So Masatomo,Goto Yuji, Proceedings of the Annual Meeting of the Japan Society of Sonochemistry, Japan Society of Sonochemistry, Vol. 25, p. 89-90, 2016
  • Measurement of amyloid formation by turbidity assay-seeing through the cloud., Ran Zhao,Masatomo So,Hendrik Maat,Nicholas J Ray,Fumio Arisaka,Yuji Goto,John A Carver,Damien Hall, Biophysical reviews, Vol. 8, No. 4, p. 445-471, 2016
  • Thermal and chemical unfolding pathways of PaSdsA1 sulfatase, a homo-dimer with topologically interlinked chains, Cesar Aguirre,Yuji Goto,Miguel Costas, FEBS LETTERS, WILEY-BLACKWELL, Vol. 590, No. 2, p. 202-214, 2016/01
  • Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson's disease patients., Katsuya Araki,Naoto Yagi,Yuka Ikemoto,Hisashi Yagi,Chi-Jing Choong,Hideki Hayakawa,Goichi Beck,Hisae Sumi,Harutoshi Fujimura,Taro Moriwaki,Yoshitaka Nagai,Yuji Goto,Hideki Mochizuki, Scientific reports, Vol. 5, p. 17625-17625, 2015/12/01
  • The Antibody Light-Chain Linker Is Important for Domain Stability and Amyloid Formation, Cardine N. Nokwe,Manuel Hora,Martin Zacharias,Hisashi Yagi,Christine John,Bernd Reif,Yuji Goto,Johannes Buchner, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, Vol. 427, No. 22, p. 3572-3586, 2015/11
  • Cold Denaturation of Alpha-Synuclein Amyloid Fibrils, Young-Ho Lee,Tatsuya Ikenoue,Yasushi Kawata,Yuji Goto, PROTEIN SCIENCE, WILEY-BLACKWELL, Vol. 24, p. 91-91, 2015/10
  • Delicate Balance of Noncovalent Forces Control the Electron Transfer Complex between Ferredoxin and Sulfite Reductase to Optimize Enzymatic Activity, Juyaen Kim,Misaki Kinoshita,Takahisa Ikegami,Genji Kurisu,Yuji Goto,Toshiharu Hase,Young-Ho Lee, PROTEIN SCIENCE, WILEY-BLACKWELL, Vol. 24, p. 64-65, 2015/10
  • Effects of a reduced disulfide bond on aggregation properties of the human IgG1 CH3 domain., Sakurai K,Nakahata R,Lee YH,Kardos J,Ikegami T,Goto Y, Biochimica et biophysica acta, Vol. 1854, No. 10,Pt.A, p. 1526-1535, 2015/10
  • Supersaturation-Limited and Unlimited Phase Spaces Compete to Produce Maximal Amyloid Fibrillation near the Critical Micelle Concentration of Sodium Dodecyl Sulfate, Masatomo So,Akira Ishii,Yasuko Hata,Hisashi Yagi,Hironobu Naiki,Yuji Goto, LANGMUIR, AMER CHEMICAL SOC, Vol. 31, No. 36, p. 9973-9982, 2015/09
  • Highly Collapsed Conformation of the Initial Folding Intermediates of β-Lactoglobulin with Non-Native α-Helix, Tsuyoshi Konuma,Kazumasa Sakurai,Masanori Yagi,Yuji Goto,Teturo Fujisawa,Satoshi Takahashi, Journal of Molecular Biology, Elsevier BV, Vol. 427, No. 19, p. 3158-3165, 2015/09
  • Supersaturation-limited and Unlimited Phase Transitions Compete to Produce the Pathway Complexity in Amyloid Fibrillation., Adachi M,So M,Sakurai K,Kardos J,Goto Y, The Journal of biological chemistry, Vol. 290, No. 29, p. 18134-18145, 2015/07/17
  • Nucleation-fibrillation dynamics of A beta(1-40) peptides on liquid-solid surface studied by total-internal-reflection fluorescence microscopy coupled with quartz-crystal microbalance biosensor, Hiroki Hamada,Hirotsugu Ogi,Kentaro Noi,Hisashi Yagi,Yuji Goto,Masahiko Hirao, JAPANESE JOURNAL OF APPLIED PHYSICS, IOP PUBLISHING LTD, Vol. 54, No. 7, 2015/07
  • Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy, Andras Micsonai,Frank Wien,Linda Kernya,Young-Ho Lee,Yuji Goto,Matthieu Refregiers,Jozsef Kardos, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, NATL ACAD SCIENCES, Vol. 112, No. 24, p. E3095-E3103, 2015/06
  • Nucleation–fibrillation dynamics of Aβ, Hamada Hiroki,Ogi Hirotsugu,Noi Kentaro,Yagi Hisashi,Goto Yuji,Hirao Masahiko, Jpn. J. Appl. Phys., Institute of Physics, Vol. 54, No. 7, 2015/05/12
  • A multi-pathway perspective on protein aggregation: implications for control of the rate and extent of amyloid formation., Damien Hall,József Kardos,Herman Edskes,John A Carver,Yuji Goto, FEBS letters, Vol. 589, No. 6, p. 672-9, 2015/03/12
  • Ultrasonication-dependent formation and degradation of alpha-synuclein amyloid fibrils, Hisashi Yagi,Aiko Mizuno,Masatomo So,Miki Hirano,Masayuki Adachi,Yoko Akazawa-Ogawa,Yoshihisa Hagihara,Tatsuya Ikenoue,Young-Ho Lee,Yasushi Kawata,Yuji Goto, BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, ELSEVIER SCIENCE BV, Vol. 1854, No. 3, p. 209-217, 2015/03
  • Ultrasonication-dependent formation and degradation of α-synuclein amyloid fibrils., Yagi H,Mizuno A,So M,Hirano M,Adachi M,Akazawa-Ogawa Y,Hagihara Y,Ikenoue T,Lee YH,Kawata Y,Goto Y, Biochimica et biophysica acta, Vol. 1854, No. 3, p. 209-217, 2015/03
  • Investigation of Protein-Protein Interactions of Ferredoxin and Sulfite Reductase Under Different Sodium Chloride Concentrations by NMR Spectroscopy and Isothermal Titration Calorimetry, Ju Yaen Kim,Takahisa Ikegami,Yuji Goto,Toshiharu Hase,Young-Ho Lee, MOLECULAR PHYSIOLOGY AND ECOPHYSIOLOGY OF SULFUR, SPRINGER, p. 169-177, 2015
  • Small Liposomes Accelerate the Fibrillation of Amyloid beta (1-40), Mayu S. Terakawa,Hisashi Yagi,Masayuki Adachi,Young-Ho Lee,Yuji Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 290, No. 2, p. 815-826, 2015/01
  • Ultrafast propagation of beta-amyloid fibrils in oligomeric cloud, Hirotsugu Ogi,Masahiko Fukukshima,Hiroki Hamada,Kentaro Noi,Masahiko Hirao,Hisashi Yagi,Yuji Goto, SCIENTIFIC REPORTS, NATURE PUBLISHING GROUP, Vol. 4, 2014/11
  • Elongation of amyloid fibrils through lateral binding of monomers revealed by total internal reflection fluorescence microscopy, Hisashi Yagi,Yuki Abe,Naoto Takayanagi,Yuji Goto, BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, ELSEVIER SCIENCE BV, Vol. 1844, No. 10, p. 1881-1888, 2014/10
  • A Residue-specific Shift in Stability and Amyloidogenicity of Antibody Variable Domains, Cardine N. Nokwe,Martin Zacharias,Hisashi Yagi,Manuel Hora,Bernd Reif,Yuji Goto,Johannes Buchner, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 289, No. 39, p. 26829-26846, 2014/09
  • High-throughput Analysis of Ultrasonication-forced Amyloid Fibrillation Reveals the Mechanism Underlying the Large Fluctuation in the Lag Time, Ayaka Umemoto,Hisashi Yagi,Masatomo So,Yuji Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 289, No. 39, p. 27290-27299, 2014/09
  • Self-assembly of the chaperonin GroEL nanocage induced at submicellar detergent, Jin Chen,Hisashi Yagi,Yuji Furutani,Takashi Nakamura,Asumi Inaguma,Hao Guo,Yan Kong,Yuji Goto, SCIENTIFIC REPORTS, NATURE PUBLISHING GROUP, Vol. 4, 2014/07
  • Cold denaturation of α-synuclein amyloid fibrils., Ikenoue T,Lee YH,Kardos J,Saiki M,Yagi H,Kawata Y,Goto Y, Angewandte Chemie (International ed. in English), Wiley, Vol. 53, No. 30, p. 7799-7804, 2014/07
  • Supersaturation-limited Amyloid Fibrillation of Insulin Revealed by Ultrasonication, Hiroya Muta,Young-Ho Lee,Jozsef Kardos,Yuxi Lin,Hisashi Yagi,Yuji Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 289, No. 26, p. 18228-18238, 2014/06
  • Heat-induced Irreversible Denaturation of the Camelid Single Domain VHH Antibody Is Governed by Chemical Modifications, Yoko Akazawa-Ogawa,Mizuki Takashima,Young-Ho Lee,Takahisa Ikegami,Yuji Goto,Koichi Uegaki,Yoshihisa Hagihara, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 289, No. 22, p. 15666-15679, 2014/05
  • Heat of supersaturation-limited amyloid burst directly monitored by isothermal titration calorimetry, Tatsuya Ikenoue,Young-Ho Lee,Jozsef Kardos,Hisashi Yagi,Takahisa Ikegami,Hironobu Naiki,Yuji Goto, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, NATL ACAD SCIENCES, Vol. 111, No. 18, p. 6654-6659, 2014/05
  • Fine-tuned broad binding capability of human lipocalin-type prostaglandin D synthase for various small lipophilic ligands, Satoshi Kume,Young-Ho Lee,Masatoshi Nakatsuji,Yoshiaki Teraoka,Keisuke Yamaguchi,Yuji Goto,Takashi Inui, FEBS LETTERS, ELSEVIER SCIENCE BV, Vol. 588, No. 6, p. 962-969, 2014/03
  • Solubility and Supersaturation-Dependent Protein Misfolding Revealed by Ultrasonication, Yuxi Lin,Young-Ho Lee,Yuichi Yoshimura,Hisashi Yagi,Yuji Goto, LANGMUIR, AMER CHEMICAL SOC, Vol. 30, No. 7, p. 1845-1854, 2014/02
  • X線1分子追跡法を用いた結晶化前駆体クラスター動体観察とその界面物性評価, 松下 祐福,関口 博史,太田 昇,池崎 圭吾,後藤 祐児,佐々木 裕次, 表面科学学術講演会要旨集, 公益社団法人 日本表面科学会, Vol. 34, p. 185-185, 2014
  • Acceleration of the depolymerization of amyloid 13 fibrils by ultrasonication, Hisashi Yagi,Kyohei Hasegawa,Yuichi Yoshimura,Yuji Goto, BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, ELSEVIER SCIENCE BV, Vol. 1834, No. 12, p. 2480-2485, 2013/12
  • A common mechanism underlying amyloid fibrillation and protein crystallization revealed by the effects of ultrasonication, Hiroki Kitayama,Yuichi Yoshimura,Masatomo So,Kazumasa Sakurai,Hisashi Yagi,Yuji Goto, BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, ELSEVIER SCIENCE BV, Vol. 1834, No. 12, p. 2640-2646, 2013/12
  • Acceleration of the depolymerization of amyloid β fibrils by ultrasonication., Yagi H,Hasegawa K,Yoshimura Y,Goto Y, Biochimica et biophysica acta, Vol. 1834, No. 12, p. 2480-2485, 2013/12
  • A common mechanism underlying amyloid fibrillation and protein crystallization revealed by the effects of ultrasonication., Kitayama H,Yoshimura Y,So M,Sakurai K,Yagi H,Goto Y, Biochimica et biophysica acta, Vol. 1834, No. 12, p. 2640-2646, 2013/12
  • Remaining structures at the N- and C-terminal regions of alpha-synuclein accurately elucidated by amide-proton exchange NMR with fitting., Okazaki H,Ohori Y,Komoto M,Lee YH,Goto Y,Tochio N,Nishimura C, FEBS letters, Vol. 587, No. 22, p. 3709-3714, 2013/11
  • Structure, folding dynamics, and amyloidogenesis of D76N β2-microglobulin roles of shear flow, hydrophobic surfaces, and α-crystallin, P. Patrizia Mangione,Gennaro Esposito,Annalisa Relini,Sara Raimondi,Riccardo Porcari,Sofia Giorgetti,Alessandra Corazza,Federico Fogolari,Amanda Penco,Yuji Goto,Young-Ho Lee,Hisashi Yagi,Ciro Cecconi,Mohsin M. Naqvi,Julian D. Gillmore,Philip N. Hawkins,Fabrizio Chiti,Ranieri Rolandi,Graham W. Taylor,Mark B. Pepys,Monica Stoppini,Vittorio Bellotti, Journal of Biological Chemistry, Vol. 288, No. 43, p. 30917-30930, 2013/10/25
  • Benzalkonium Chloride Accelerates the Formation of the Amyloid Fibrils of Corneal Dystrophy-associated Peptides, Yusuke Kato,Hisashi Yagi,Yuichi Kaji,Tetsuro Oshika,Yuji Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 288, No. 35, p. 25109-25118, 2013/08
  • Ultrasonication: An Efficient Agitation for Accelerating the Supersaturation-Limited Amyloid Fibrillation of Proteins, Yoshimura Yuichi,So Masatomo,Yagi Hisashi,Goto Yuji, Jpn J Appl Phys, The Japan Society of Applied Physics, Vol. 52, No. 7, p. 07HA01-07HA01-8, 2013/07/25
  • Mechanisms of ultrasonically induced fibrillation of amyloid β<inf>1-40</inf> peptides, Kentaro Uesugi,Hirotsugu Ogi,Masahiko Fukushima,Masatomo So,Hisashi Yagi,Yuji Goto,Masahiko Hirao, Japanese Journal of Applied Physics, Vol. 52, No. 7 PART 2, 2013/07
  • Acceleration of deposition of A beta(1-40) peptide on ultrasonically formed A beta(1-42) nucleus studied by wireless quartz-crystal-microbalance biosensor, Hirotsugu Ogi,Masahiko Fukushima,Kentaro Uesugi,Hisashi Yagi,Yuji Goto,Masahiko Hirao, BIOSENSORS & BIOELECTRONICS, ELSEVIER ADVANCED TECHNOLOGY, Vol. 40, No. 1, p. 200-205, 2013/02
  • Effect of liposome membranes on disaggregation of amyloid beta fibrils by dopamine, Huong Thi Vu,Toshinori Shimanouchi,Daisuke Ishikawa,Tadaharu Matsumoto,Hisashi Yagi,Yuji Goto,Hiroshi Umakoshi,Ryoichi Kuboi, BIOCHEMICAL ENGINEERING JOURNAL, ELSEVIER SCIENCE SA, Vol. 71, p. 118-126, 2013/02
  • A12 Ultrasonication-dependent breakdown of protein supersaturation and formation of amyloid fibrils, Goto Yuji, Proceedings of the Annual Meeting of the Japan Society of Sonochemistry, The Japan Society of Sonochemistry, Vol. 22, p. 107-108, 2013
  • 2P071 Direct observation of burst of amyloid fibril formation by calorimetry(01C. Protein: Property), Ikenoue Tatsuya,Lee Young-Ho,Kardos Jozef,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 53, No. 1, 2013
  • 2P066 The effects of the hydrophobic area of vesicles on the fibrillation of Aβ(01C. Protein: Property), Suzuki Mayu,Yagi Hisashi,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 53, No. 1, 2013
  • 2P068 The properties of the residual structure of amyloid precursor state of β2-microglobulin(01C. Protein: Property), Sakurai Kazumasa,Maeno Akihiro,Naiki Hironobu,Goto Yuji,Akasaka Kazuyuki, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 53, No. 1, 2013
  • 2P067 Effects of various fatty acids on the amyloid fibrillation of β_2-microglobulin(01C. Protein: Property), Ishii Akira,So Masatomo,Yagi Hisashi,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 53, No. 1, 2013
  • 2P070 Solubility and Supersaturation-Dependent Protein Misfolding Revealed by Ultrasonication(01C. Protein: Property), Lin Yuxi,Lee Young-Ho,Yoshimura Yuichi,Yagi Hisashi,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 53, No. 1, 2013
  • 2P069 The mechanism of ultrasonication-induced amyloid fibril formation(01C. Protein: Property), So Masatomo,Yoshimura Yuichi,Yagi Hisashi,Ogi Hirotsugu,Uesugi Kentaro,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 53, No. 1, 2013
  • Application and use of differential scanning calorimetry in studies of thermal fluctuation associated with amyloid fibril formation, Kenji Sasahara,Yuji Goto, Biophysical Reviews, Springer Verlag, Vol. 5, No. 3, p. 259-269, 2013
  • Principal component analysis of chemical shift perturbation data of a multiple-ligand-binding system for elucidation of respective binding mechanism, Tsuyoshi Konuma,Young-Ho Lee,Yuji Goto,Kazumasa Sakurai, PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, WILEY, Vol. 81, No. 1, p. 107-118, 2013/01
  • The Molten Globule of beta(2)-Microglobulin Accumulated at pH 4 and Its Role in Protein Folding, Atsushi Mukaiyama,Takashi Nakamura,Koki Makabe,Kosuke Maki,Yuji Goto,Kunihiro Kuwajima, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, Vol. 425, No. 2, p. 273-291, 2013/01
  • Native-State Heterogeneity of beta(2)-Microglobulin as Revealed by Kinetic Folding and Real-Time NMR Experiments, Atsushi Mukaiyama,Takashi Nakamura,Koki Makabe,Kosuke Maki,Yuji Goto,Kunihiro Kuwajima, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, Vol. 425, No. 2, p. 257-272, 2013/01
  • Kinetic intermediates of amyloid fibrillation studied by hydrogen exchange methods with nuclear magnetic resonance, Young-Ho Lee,Yuji Goto, BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, ELSEVIER SCIENCE BV, Vol. 1824, No. 12, p. 1307-1323, 2012/12
  • Formation of spherulitic amyloid β aggregate by anionic liposomes, Toshinori Shimanouchi,Naoya Shimauchi,Ryo Ohnishi,Nachi Kitaura,Hisashi Yagi,Yuji Goto,Hiroshi Umakoshi,Ryoichi Kuboi, Biochemical and Biophysical Research Communications, Vol. 426, No. 2, p. 165-171, 2012/09/21
  • Systematic interaction analysis of human lipocalin-type prostaglandin D synthase with small lipophilic ligands, Satoshi Kume,Young-Ho Lee,Yuya Miyamoto,Harumi Fukada,Yuji Goto,Takashi Inui, BIOCHEMICAL JOURNAL, PORTLAND PRESS LTD, Vol. 446, p. 279-289, 2012/09
  • The monomer-seed interaction mechanism in the formation of the β2-microglobulin amyloid fibril clarified by solution NMR techniques., Yanagi K,Sakurai K,Yoshimura Y,Konuma T,Lee YH,Sugase K,Ikegami T,Naiki H,Goto Y, Journal of molecular biology, Elsevier BV, Vol. 422, No. 3, p. 390-402, 2012/09
  • Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation., Yoshimura Y,Lin Y,Yagi H,Lee YH,Kitayama H,Sakurai K,So M,Ogi H,Naiki H,Goto Y, Proceedings of the National Academy of Sciences of the United States of America, Vol. 109, No. 36, p. 14446-14451, 2012/09
  • The monomer-seed interaction mechanism in the formation of the β2-microglobulin amyloid fibril clarified by solution NMR techniques., Yanagi K,Sakurai K,Yoshimura Y,Konuma T,Lee YH,Sugase K,Ikegami T,Naiki H,Goto Y, J Mol Biol, Elsevier BV, Vol. 422, No. 3, p. 390-402, 2012/09
  • Long-term observation of fluorescence of free single molecules to explore protein-folding energy landscapes., Kamagata K,Kawaguchi T,Iwahashi Y,Baba A,Fujimoto K,Komatsuzaki T,Sambongi Y,Goto Y,Takahashi S, Journal of the American Chemical Society, 28, Vol. 134, No. 28, p. 11525-11532, 2012/07/18
  • A back hydrogen exchange procedure via the acid-unfolded state for a large protein., Suzuki M,Sakurai K,Lee YH,Ikegami T,Yokoyama K,Goto Y, Biochemistry, Vol. 51, No. 28, p. 5564-5570, 2012/07
  • Polymorphism of β2-microglobulin amyloid fibrils manifested by ultrasonication-enhanced fibril formation in trifluoroethanol., Chatani E,Yagi H,Naiki H,Goto Y, The Journal of biological chemistry, Vol. 287, No. 27, p. 22827-22837, 2012/06
  • Kinetic Intermediate of β_2-microglobulin Fibril Elongation Probed by Tryptophan Fluorescence Spectroscopy and H/D Exchange-NMR, CHATANI Eri,KONUMA Tsuyoshi,GOTO Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 52, No. 3, p. 148-149, 2012/05/25
  • Fibrillogenic propensity of the GroEL apical domain: A Janus-faced minichaperone, Jin Chen,Hisashi Yagi,Pietro Sormanni,Michele Vendruscolo,Koki Makabe,Takashi Nakamura,Yuji Goto,Kunihiro Kuwajima, FEBS Letters, Vol. 586, No. 8, p. 1120-1127, 2012/04/24
  • Drug delivery system for poorly water-soluble compounds using lipocalin-type prostaglandin D synthase, Ayano Fukuhara,Hidemitsu Nakajima,Yuya Miyamoto,Katsuaki Inoue,Satoshi Kume,Young-Ho Lee,Masanori Noda,Susumu Uchiyama,Shigeru Shimamoto,Shigenori Nishimura,Tadayasu Ohkubo,Yuji Goto,Tadayoshi Takeuchi,Takashi Inui, JOURNAL OF CONTROLLED RELEASE, ELSEVIER SCIENCE BV, Vol. 159, No. 1, p. 143-150, 2012/04
  • Three-dimensional structure of nylon hydrolase and mechanism of nylon-6 hydrolysis., Negoro S,Shibata N,Tanaka Y,Yasuhira K,Shibata H,Hashimoto H,Lee YH,Oshima S,Santa R,Oshima S,Mochiji K,Goto Y,Ikegami T,Nagai K,Kato D,Takeo M,Higuchi Y, The Journal of biological chemistry, Vol. 287, No. 7, p. 5079-5090, 2012/02
  • A13 Ultrasonication-dependent breakdown of protein supersaturations, Goto Yuji, Proceedings of the Annual Meeting of the Japan Society of Sonochemistry, The Japan Society of Sonochemistry, Vol. 21, p. 83-84, 2012
  • 1E1436 Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation(Proteins: Property I,Oral Presentation,The 50th Annual Meeting of the Biophysical Society of Japan), Yoshimura Yuichi,Lin Yuxi,Yagi Hisashi,Lee Young-Ho,Kitayama Hiroki,Sakurai Kazumasa,So Masatomo,Ogi Hirotsugu,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 52, 2012
  • 1PT145 Correlation of the dynamics of β_2-microglobulin fragments with their amyloidogenicity(The 50th Annual Meeting of the Biophysical Society of Japan), Takeda Mahoshi,Sakurai Kazumasa,Ikegami Takahisa,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 52, 2012
  • A Two-Step Refolding of Acid-Denatured Microbial Transglutaminase Escaping from the Aggregation-Prone Intermediate, Mototaka Suzuki,Kei-ichi Yokoyama,Young-Ho Lee,Yuji Goto, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 50, No. 47, p. 10390-10398, 2011/11
  • Chiral Superstructures of Insulin Amyloid Fibrils, Viktoria Babenko,Takunori Harada,Hisashi Yagi,Yuji Goto,Reiko Kuroda,Wojciech Dzwolak, CHIRALITY, WILEY, Vol. 23, No. 8, p. 638-646, 2011/09
  • Binding Energetics of Ferredoxin-NADP(+) Reductase with Ferredoxin and Its Relation to Function, Young-Ho Lee,Takahisa Ikegami,Daron M. Standley,Kazumasa Sakurai,Toshiharu Hase,Yuji Goto, CHEMBIOCHEM, WILEY-BLACKWELL, Vol. 12, No. 13, p. 2062-2070, 2011/09
  • Ultrasonication-dependent acceleration of amyloid fibril formation., So M,Yagi H,Sakurai K,Ogi H,Naiki H,Goto Y, Journal of molecular biology, Vol. 412, No. 4, p. 568-577, 2011/09
  • Characterization of DNA-binding activity in the N-terminal domain of the DNA methyltransferase Dnmt3a, Isao Suetake,Yuichi Mishima,Hironobu Kimura,Young-Ho Lee,Yuji Goto,Hideyuki Takeshima,Takahisa Ikegami,Shoji Tajima, BIOCHEMICAL JOURNAL, PORTLAND PRESS LTD, Vol. 437, No. 1, p. 141-148, 2011/07
  • Hexafluoroisopropanol Induces Amyloid Fibrils of Islet Amyloid Polypeptide by Enhancing Both Hydrophobic and Electrostatic Interactions, Kotaro Yanagi,Mizue Ashizaki,Hisashi Yagi,Kazumasa Sakurai,Young-Ho Lee,Yuji Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 286, No. 27, p. 23959-23966, 2011/07
  • A circumventing role for the non-native intermediate in the folding of β-lactoglobulin., Sakurai K,Fujioka S,Konuma T,Yagi M,Goto Y, Biochemistry, Vol. 50, No. 29, p. 6498-6507, 2011/07
  • Seed-Dependent Deposition Behavior of A beta Peptides Studied with Wireless Quartz-Crystal-Microbalance Biosensor, Hirotsugu Ogi,Yuji Fukunishi,Taiji Yanagida,Hisashi Yagi,Yuji Goto,Masahiko Fukushima,Kentaro Uesugi,Masahiko Hirao, ANALYTICAL CHEMISTRY, AMER CHEMICAL SOC, Vol. 83, No. 12, p. 4982-4988, 2011/06
  • Reversible Heat-Induced Dissociation of beta(2)-Microglobulin Amyloid Fibrils, Jozsef Kardos,Andras Micsonai,Henriett Pal-Gabor,Eva Petrik,Laszlo Graf,Janos Kovacs,Young-Ho Lee,Hironobu Naiki,Yuji Goto, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 50, No. 15, p. 3211-3220, 2011/04
  • Destruction of Amyloid Fibrils of Keratoepithelin Peptides by Laser Irradiation Coupled with Amyloid-specific Thioflavin, Daisaku Ozawa,Yuichi Kaji,Hisashi Yagi,Kazumasa Sakurai,Toru Kawakami,Hironobu Naiki,Yuji Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 286, No. 12, p. 10856-10863, 2011/03
  • Inhibition of beta2-microglobulin amyloid fibril formation by alpha2-macroglobulin., Ozawa D,Hasegawa K,Lee YH,Sakurai K,Yanagi K,Ookoshi T,Goto Y,Naiki H, The Journal of biological chemistry, Vol. 286, No. 11, p. 9668-9676, 2011/03
  • Time-Resolved Small-Angle X-ray Scattering Study of the Folding Dynamics of Barnase, Tsuyoshi Konuma,Tetsunari Kimura,Shuzo Matsumoto,Yuji Goto,Tetsuro Fujisawa,Alan R.Fersht,Satoshi Takahashi, Journal of Molecular Biology, Elsevier BV, Vol. 405, No. 5, p. 1284-1294, 2011/02
  • 1D1648 Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions(Protein: Property 1,The 49th Annual Meeting of the Biophysical Society of Japan), Yanagi Kotaro,Ashizaki Mizue,Yagi Hisashi,Sakurai Kazumasa,Lee Young-Ho,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 51, 2011
  • 3D0948 Application of CS-PCA (Chemical shift-principle component analysis) to the NMR data on a multiple-ligand-binding system(3D Protein: Structure & Function 2,The 49th Annual Meeting of the Biophysical Society of Japan), Sakurai Kazumasa,Konuma Tsuyoshi,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 51, 2011
  • Visualization of polymorphism in apolipoprotein C-II amyloid fibrils, Chai L. Teoh,Hisashi Yagi,Michael D. W. Griffin,Yuji Goto,Geoffrey J. Howlett, JOURNAL OF BIOCHEMISTRY, OXFORD UNIV PRESS, Vol. 149, No. 1, p. 67-74, 2011/01
  • Kinetic intermediates of β(2)-microglobulin fibril elongation probed by pulse-labeling H/D exchange combined with NMR analysis., Konuma T,Chatani E,Yagi M,Sakurai K,Ikegami T,Naiki H,Goto Y, Journal of molecular biology, Elsevier BV, Vol. 405, No. 3, p. 851-862, 2011/01
  • Direct observation of minimum-sized amyloid fibrils using solution NMR spectroscopy., Yoshimura Y,Sakurai K,Lee YH,Ikegami T,Chatani E,Naiki H,Goto Y, Protein science : a publication of the Protein Society, WILEY, Vol. 19, No. 12, p. 2347-2355, 2010/12
  • A Disulfide-Linked Amyloid-beta Peptide Dimer Forms a Protofibril-like Oligomer through a Distinct Pathway from Amyloid Fibril Formation, Takahiro Yamaguchi,Hisashi Yagi,Yuji Goto,Katsumi Matsuzaki,Masaru Hoshino, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 49, No. 33, p. 7100-7107, 2010/08
  • The amyloid fibrils of the constant domain of immunoglobulin light chain., Yamamoto K,Yagi H,Lee YH,Kardos J,Hagihara Y,Naiki H,Goto Y, FEBS letters, Vol. 584, No. 15, p. 3348-3353, 2010/08
  • Real-Time Observation of Amyloid-β Fibril Growth by Total Internal Reflection Fluorescence Microscopy, Tadato Ban,Yuji Goto, Protein Misfolding Diseases: Current and Emerging Principles and Therapies, John Wiley and Sons, p. 699-709, 2010/07/02
  • Stop-and-go kinetics in amyloid fibrillation, Jesper Ferkinghoff-Borg,Jesper Fonslet,Christian Beyschau Andersen,Sandeep Krishna,Simone Pigolotti,Hisashi Yagi,Yuji Goto,Daniel Otzen,Mogens H. Jensen, PHYSICAL REVIEW E, AMER PHYSICAL SOC, Vol. 82, No. 1, 2010/07
  • Pre-steady-state kinetic analysis of the elongation of amyloid fibrils of beta(2)-microglobulin with tryptophan mutagenesis., Chatani E,Ohnishi R,Konuma T,Sakurai K,Naiki H,Goto Y, Journal of molecular biology, Elsevier BV, Vol. 400(5):1057-66., No. 5, p. 1057-1066, 2010/07
  • Laser-induced propagation and destruction of amyloid β fibrils, Hisashi Yagi,Daisaku Ozawa,Kazumasa Sakurai,Toru Kawakami,Hiroki Kuyama,Osamu Nishimura,Toshinori Shimanouchi,Ryoichi Kuboi,Hironobu Naiki,Yuji Goto, Journal of Biological Chemistry, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 285, No. 25, p. 19660-19667, 2010/06/18
  • Catechol derivatives inhibit the fibril formation of amyloid-β peptides, Vu Thi Huong,Toshinori Shimanouchi,Naoya Shimauchi,Hisashi Yagi,Hiroshi Umakoshi,Yuji Goto,Ryoichi Kuboi, Journal of Bioscience and Bioengineering, SOC BIOSCIENCE BIOENGINEERING JAPAN, Vol. 109, No. 6, p. 629-634, 2010/06/01
  • The beta-Sheet Structure pH Dependence of the Core Fragments of beta(2)-Microglobulin Amyloid Fibrils, Hirotsugu Hiramatsu,Ming Lu,Yuji Goto,Teizo Kitagawa, BULLETIN OF THE CHEMICAL SOCIETY OF JAPAN, CHEMICAL SOC JAPAN, Vol. 83, No. 5, p. 495-504, 2010/05
  • Critical role of interfaces and agitation on the nucleation of Abeta amyloid fibrils at low concentrations of Abeta monomers., Morinaga A,Hasegawa K,Nomura R,Ookoshi T,Ozawa D,Goto Y,Yamada M,Naiki H, Biochimica et biophysica acta, Vol. 1804, No. 4, p. 986-995, 2010/04
  • Critical role of interfaces and agitation on the nucleation of A beta amyloid fibrils at low concentrations of A beta monomers, Akiyoshi Morinaga,Kazuhiro Hasegawa,Ryo Nomura,Tadakazu Ookoshi,Daisaku Ozawa,Yuji Goto,Masahito Yamada,Hironobu Naiki, BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, ELSEVIER SCIENCE BV, Vol. 1804, No. 4, p. 986-995, 2010/04
  • Lysophospholipids and non-esterified fatty acids induce the extension of beta 2-microglobulin-related amyloid fibrils at neutral pH, K. Hasegawa,T. Ookoshi,H. Kimura,N. Takahashi,H. Yoshida,R. Miyazaki,Y. Goto,H. Naiki, AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS, INFORMA HEALTHCARE, Vol. 17, p. 91-91, 2010/04
  • Differences in the Molecular Structure of beta(2)-Microglobulin between Two Morphologically Different Amyloid Fibrils, Hirotsugu Hiramatsu,Ming Lu,Koichi Matsuo,Kunihiko Gekko,Yuji Goto,Teizo Kitagawa, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 49, No. 4, p. 742-751, 2010/02
  • 1P063 1YA0930 Identification of transient intermediates of the formation of the β2-microglobulin amyloid fibril by heteronuclear NMR techniques.(Protein:Property,Early Research in Biophysics Award Candidate Presentations,Early Research in Biophysics Award,The 48th Annual Meeting of the Biophysical Society of Japan), SAKURAI Kazumasa,YANAGI Kotaro,YOSHIMURA Yuichi,KONUMA Tsuyoshi,IKEGAMI Takahisa,NAIKI Hironobu,GOTO Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 50, No. 2, 2010
  • 1P041 Interaction Analysis of Human Lipocalin-type Prostaglandin D Synthase for Small Lipophilic Ligands(Protein:Structure & Function,The 48th Annual Meeting of the Biophysical Society of Japan), Kume Satoshi,Lee Young-Ho,Miyamoto Yuya,Nishimura Shigenori,Fukuda Harumi,Goto Yuji,Inui Takashi, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 50, No. 2, 2010
  • 2P051 High Speed Amyloid Fibrilization Induced by Ultrasonication(The 48th Annual Meeting of the Biophysical Society of Japan), So Masatomo,Yagi Hisashi,Sakurai Kazumasa,Ogi Hirotsugu,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 50, No. 2, 2010
  • 1P064 Analysis of the intermediate state of the formation of the β2-microglobulin amyloid fibril using paramagnetic relaxation enhancement(Protein:Property,The 48th Annual Meeting of the Biophysical Society of Japan), Fujiwara Kensuke,Sakurai Kazumasa,Yagi Hisashi,So Masatomo,Yoshimura Yuichi,Ikegami Takahisa,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 50, No. 2, 2010
  • Characterization of Amyloid beta Fibrils with An Aqueous Two-Phase System: Implications of Fibril Formation, Toshinori Shimanouchi,Naoya Shimauchi,Keiichi Nishiyama,Huong Thi Vu,Hisashi Yagi,Yuji Goto,Hiroshi Umakoshi,Ryoichi Kuboi, SOLVENT EXTRACTION RESEARCH AND DEVELOPMENT-JAPAN, JAPAN ASSOC SOLVENT EXTRACTION, Vol. 17, p. 121-128, 2010
  • Isolation of short peptide fragments from α-synuclein fibril core identifies a residue important for fibril nucleation: A possible implication for diagnostic applications, Hisashi Yagi,Hideki Takeuchi,Shiho Ogawa,Naomi Ito,Isao Sakane,Kunihiro Hongo,Tomohiro Mizobata,Yuji Goto,Yasushi Kawata, Biochim. Biophys. Acta/Proteins and Proteomics, Vol. 1804, No. 10, p. 2077-2087, 2010
  • Introduction to the Special Issue, Paul F. Cook,Yuji Goto,Friedrich Lottspeich, Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1794, No. 9, p. 1277-1279, 2009/09
  • NMR-based characterization of a refolding intermediate of beta2-microglobulin labeled using a wheat germ cell-free system., Kameda A,Morita EH,Sakurai K,Naiki H,Goto Y, Protein science : a publication of the Protein Society, Vol. 18(8):1592-601, No. 8, p. 1592-1601, 2009/08
  • Mechanism of Lysophosphatidic Acid-Induced Amyloid Fibril Formation of beta(2)-Microglobulin in Vitro under Physiological Conditions, Henriett Pal-Gabor,Linda Gombos,Andras Micsonai,Erika Kovacs,Eva Petrik,Janos Kovacs,Laszlo Graf,Judit Fidy,Hironobu Naiki,Yuji Goto,Karoly Liliom,Jozsef Kardos, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 48, No. 24, p. 5689-5699, 2009/06
  • Structural dynamics and folding of beta-lactoglobulin probed by heteronuclear NMR, Kazumasa Sakurai,Tsuyoshi Konuma,Masanori Yagi,Yuji Goto, BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, ELSEVIER SCIENCE BV, Vol. 1790, No. 6, p. 527-537, 2009/06
  • Structural dynamics and folding of beta-lactoglobulin probed by heteronuclear NMR., Sakurai K,Konuma T,Yagi M,Goto Y, Biochimica et biophysica acta, Vol. 1790(6):527-37, No. 6, p. 527-537, 2009/06
  • Thermal response with exothermic effects of beta2-microglobulin amyloid fibrils and fibrillation., Sasahara K,Yagi H,Naiki H,Goto Y, Journal of molecular biology, Vol. 389, No. 3, p. 584-594, 2009/06
  • Branching in Amyloid Fibril Growth, Christian Beyschau Andersen,Hisashi Yagi,Mauro Manno,Vincenzo Martorana,Tadato Ban,Gunna Christiansen,Daniel Erik Otzen,Yuji Goto,Christian Rischel, BIOPHYSICAL JOURNAL, CELL PRESS, Vol. 96, No. 4, p. 1529-1536, 2009/02
  • 3P-042 Microsecond-resolved single-molecule time traces of protein folding by a line-illuminated confocal microscopy(Protein:Property,The 47th Annual Meeting of the Biophysical Society of Japan), Oikawa Hiroyuki,Kamagata Kiyoto,Goto Yuji,Takahashi Satoshi, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 49, 2009
  • 1P-057 Long-time observation of a single molecule trapped in a capillary cell : application for protein folding(Protein:Property, The 47th Annual Meeting of the Biophysical Society of Japan), Kamagata Kiyoto,Goto Yuji,Takahashi Satoshi, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 49, 2009
  • 1YP1-02 Long-time observation of a single molecule trapped in a capillary cell : application for protein folding(1YP1 Early Research in Biophysics Award Candidate Presentations,The 47th Annual Meeting of the Biophysical Society of Japan), Kamagata Kiyoto,Goto Yuji,Takahashi Satoshi, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 49, 2009
  • 1TP3-01 A channeling role of the non-native intermediate in the folding of β-lactoglobulin(The 47th Annual Meeting of the Biophysical Society of Japan), Fujioka Shunsuke,Sakurai Kazumasa,Konuma Tsuyoshi,Yagi Masanori,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 49, 2009
  • 2P-052 Site directed spin labeling - electron spin resonance analysis of the structure of amyloid fibrils(Protein:Property,The 47th Annual Meeting of the Biophysical Society of Japan), So Masatomo,Yagi Hisashi,Sakurai kazumasa,Naiki Hironobu,Arata Toshiaki,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 49, p. S114-S115, 2009
  • 2P-048 Analysis of the mechanism of the amyloid fiber extension using H/D exchange(Protein:Property,The 47th Annual Meeting of the Biophysical Society of Japan), Yanagi Kotaro,Sakurai Kazumasa,Lee Young-Ho,Ikegami Takahisa,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 49, 2009
  • 2P-050 Single molecule observation of the folding of bovine β-lactoglobulin(Protein:Property,The 47th Annual Meeting of the Biophysical Society of Japan), Kadota Takayuki,Kamagata Kiyoto,Oikawa Hiroyuki,Sakurai Kazumasa,Goto Yuji,Takahashi Satoshi, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 49, 2009
  • 2P-038 Direct Observation of β_2-microglubulin amyloid fibrils using solution NMR(Protein:Property,The 47th Annual Meeting of the Biophysical Society of Japan), Yoshimura Yuichi,Sakurai Kazumasa,Chatani Eri,Lee Young-Ho,Ikegami Takahisa,Kameda Atsushi,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 49, 2009
  • Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils, Eri Chatani,Young-Ho Lee,Hisashi Yagi,Yuichi Yoshimura,Hironobu Naiki,Yuji Goto, Proc. Natl. Acad. Sci. USA, Vol. 106, No. 27, p. 11119-11124, 2009
  • A Comprehensive Model for Packing and Hydration for Amyloid Fibrils of beta(2)-Microglobulin, Young-Ho Lee,Eri Chatani,Kenji Sasahara,Hironobu Naiki,Yuji Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 284, No. 4, p. 2169-2175, 2009/01
  • Destruction of Amyloid Fibrils of a beta(2)-Microglobulin Fragment by Laser Beam Irradiation, Daisaku Ozawa,Hisashi Yagi,Tadato Ban,Atsushi Kameda,Toru Kawakami,Hironobu Naiki,Yuji Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 284, No. 2, p. 1009-1017, 2009/01
  • Growth of beta(2)-microglobulin-related amyloid fibrils by non-esterified fatty acids at a neutral pH, Kazuhiro Hasegawa,Shinobu Tsutsumi-Yasuhara,Tadakazu Ookoshi,Yumiko Ohhashi,Hideki Kimura,Naoki Takahashi,Haruyoshi Yoshida,Ryoichi Miyazaki,Yuji Goto,Hironobu Naiki, BIOCHEMICAL JOURNAL, PORTLAND PRESS LTD, Vol. 416, p. 307-315, 2008/12
  • Lysophospholipids induce the nucleation and extension of beta 2-microglobulin-related amyloid fibrils at a neutral pH, Tadakazu Ookoshi,Kazuhiro Hasegawa,Yumiko Ohhashi,Hideki Kimura,Naoki Takahashi,Haruyoshi Yoshida,Ryoichi Miyazaki,Yuji Goto,Hironobu Naiki, NEPHROLOGY DIALYSIS TRANSPLANTATION, OXFORD UNIV PRESS, Vol. 23, No. 10, p. 3247-3255, 2008/10
  • Kinetic Coupling of Folding and Prolyl Isomerization of beta(2)-Microglobulin Studied by Mutational Analysis, Michiko Sakata,Eri Chatani,Atsushi Kameda,Kazumasa Sakurai,Hironobu Naiki,Yuji Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, Vol. 382, No. 5, p. 1242-1255, 2008/10
  • Structure, Formation and Propagation of Amyloid Fibrils, Yuji Goto,Hisashi Yagi,Keiichi Yamaguchi,Eri Chatani,Tadato Ban, CURRENT PHARMACEUTICAL DESIGN, BENTHAM SCIENCE PUBL LTD, Vol. 14, No. 30, p. 3205-3218, 2008/10
  • Differential rate constants of racemization of aspartyl and asparaginyl residues in human alpha A-crystallin mutants, Tooru Nakamura,Miyo Sakai,Yutaka Sadakane,Tatsuya Haga,Yuji Goto,Tadatoshi Kinouchi,Takeshi Saito,Noriko Fujii, BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, ELSEVIER SCIENCE BV, Vol. 1784, No. 9, p. 1192-1199, 2008/09
  • Dehydration of main-chain amides in the final folding step of single-chain monellin revealed by time-resolved infrared spectroscopy, Tetsunari Kimura,Akio Maeda,Shingo Nishiguchi,Koichiro Ishimori,Isao Morishima,Takashi Konno,Yuji Goto,Satoshi Takahashi, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, NATL ACAD SCIENCES, Vol. 105, No. 36, p. 13391-13396, 2008/09
  • Disulfide-linked bovine beta-lactoglobulin dimers fold slowly, navigating a glassy folding landscape, Masanori Yagi,Atsushi Kameda,Kazumasa Sakurai,Chiaki Nishimura,Yuji Goto, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 47, No. 22, p. 5996-6006, 2008/06
  • Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: Structure of the active catalytic region of C1r, József Kardos,Veronika Harmat,Anna Palló,Orsolya Barabás,Katalin Szilágyi,László Gráf,Gábor Náray-Szabó,Yuji Goto,Péter Závodszky,Péter Gál, Molecular Immunology, Vol. 45, No. 6, p. 1752-1760, 2008/03
  • Amyloid nucleation triggered by agitation of beta(2)-microglobulin under acidic and neutral pH conditions, Kenji Sasahara,Hisashi Yagi,Miyo Sakai,Hironobu Naiki,Yuji Goto, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 47, No. 8, p. 2650-2660, 2008/02
  • Thiol compounds inhibit the formation of amyloid fibrils by beta(2)-microglobulin at neutral pH, Kaori Yamamoto,Hisashi Yagi,Daisaku Ozawa,Kenji Sasahara,Hironobu Naiki,Yuji Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, Vol. 376, No. 1, p. 258-268, 2008/02
  • Alcohol- and Salt-induced Partially Folded Intermediates, Daizo Hamada,Yuji Goto, Protein Folding Handbook, Wiley-VCH Verlag GmbH, Vol. 2, p. 884-915, 2008/01/31
  • 2P-098 Direct observation of single-molecule trajectories of protein folding using a new sheath flow cell(The 46th Annual Meeting of the Biophysical Society of Japan), Kamagata Kiyoto,Kinoshita Masahito,Goto Yuji,Takahashi Satoshi, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 48, 2008
  • 3P-022 Denatured state dynamics of Cytochrome c551 observed by single molecule fluorescence intensity measurements(The 46th Annual Meeting of the Biophysical Society of Japan), Fujimoto Kazuya,Kinoshita Masahito,Kamagata Kiyoto,Goto Yuji,Sambongi Yoshihiro,Baba Akinori,Komatsuzaki Tamiki,Takahashi Satoshi, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 48, 2008
  • 3P-008 The ability of fibril formation of the constant domain of immunoglobulin light chain in comparison with β2-microglobulin(The 46th Annual Meeting of the Biophysical Society of Japan), Yamamoto Kaori,Yagi Hisashi,Hagihara Yoshihisa,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 48, 2008
  • 3P-010 Analysis of the amyloid fiber extension mechanism using H/D exchange(The 46th Annual Meeting of the Biophysical Society of Japan), Yanagi Kotaro,Sakurai Kazumasa,Chatani Eri,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 48, 2008
  • 3P-013 Analysis of native-state prolyl isomerization of β2-microglobulin(The 46th Annual Meeting of the Biophysical Society of Japan), Mukaiyama Atsushi,Nakamura Takashi,Maki Kosuke,Goto Yuji,Kuwajima Kunihiro, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 48, 2008
  • 3P-007 A study of contributions of the α-helix intermediate of β-Lactoglobulin to its folding process(The 46th Annual Meeting of the Biophysical Society of Japan), Fujioka Shunsuke,Konuma Tsuyoshi,Yagi Masanori,Sakurai Kazumasa,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 48, p. S128-S129, 2008
  • 3P-005 The effect of the intermolecular disulfide bond in IgG C_H3 domain to its stability(The 46th Annual Meeting of the Biophysical Society of Japan), Sakurai Kazumasa,Nakahata Ryosuke,Matsumura Masazumi,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 48, 2008
  • 2P-083 Monitoring the fibrillation intermediate of β2-microglobulin by Trp fluorescence and H/D exchange-NMR(The 46th Annual Meeting of the Biophysical Society of Japan), Chatani Eri,Onishi Reina,Konuma Tsuyoshi,Sakurai Kazumasa,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 48, 2008
  • 2P-008 Structural Analysis of Amyloid Fibrils of β2-Microglobulin by Solid-State NMR(The 46th Annual Meeting of the Biophysical Society of Japan), Saeka Miwako,Todokoro Yasuto,Egawa Ayako,Kameda Atsushi,Chatani Eri,Yagi Hisashi,Akutsu Hideo,Naiki Hironobu,Fujiwara Toshimichi,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 48, 2008
  • 1P-087 Structural analysis of the amyloid fibril formed by the fragment of β2-microglobulin(The 46th Annual Meeting of the Biophysical Society of Japan), Yoshimura Yuichi,Sakurai Kazumasa,Chatana Eri,Kameda Atsushi,Sakai Miyo,Yamaguchi Kei-ichi,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 48, 2008
  • A cytotoxic conformer of the polyglutamine protein: Exposed beta-sheet hypothesis, Yoshitaka Nagai,Takashi Inui,Akiko Popiel,Nobuhiro Fujikake,Yuji Goto,Hironobu Naiki,Tatsushi Toda, NEUROSCIENCE RESEARCH, ELSEVIER IRELAND LTD, Vol. 61, p. S44-S44, 2008
  • β_2-ミクログロブリンアミロイド線維形成・沈着の分子機構 : 第50回日本透析医学会シンポジウムより, 山本 卓,長谷川 一浩,山口 格,風間 順一郎,丸山 弘樹,成田 一衛,後藤 祐児,内木 宏延,下条 文武, 日本透析医学会雑誌 = Journal of Japanese Society for Dialysis Therapy, The Japanese Society for Dialysis Therapy, Vol. 40, No. 12, p. 1028-1030, 2007/12/28
  • Visualization and classification of amyloid β supramolecular assemblies, Hisashi Yagi,Tadato Ban,Kenichi Morigaki,Hironobu Naiki,Yuji Goto, Biochemistry, Vol. 46, No. 51, p. 15009-15017, 2007/12/25
  • Seed-dependent accelerated fibrillation of alpha-synuclein induced by periodic ultrasonication treatment, Hyun Jin Kim,Eri Chatani,Yuji Goto,Seung R. Paik, JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY, Vol. 17, No. 12, p. 2027-2032, 2007/12
  • 蛋白質の折り畳み運動を観測するための一分子測定手法の開発(Development of a technique for the investigation of folding dynamics of single proteins for extended time periods), 木下 雅仁,鎌形 清人,前田 晃央,後藤 祐児,小松崎 民樹,高橋 聡, 生物物理, (一社)日本生物物理学会, Vol. 47, No. Suppl.1, p. S139-S139, 2007/11
  • [Rise of amyloid structural biology]., Yagi H,Sakurai K,Goto Y, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, Vol. 52, No. 12, p. 1445-1453, 2007/10
  • Solvation and desolvation dynamics in apomyoglobin folding monitored by time-resolved infrared spectroscopy, Shingo Nishiguchi,Yuji Goto,Satoshi Takahashi, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD, Vol. 373, No. 2, p. 491-502, 2007/10
  • High-resolution crystal structure of beta2-microglobulin formed at pH 7.0., Iwata K,Matsuura T,Sakurai K,Nakagawa A,Goto Y, Journal of biochemistry, 3, Vol. 142, No. 3, p. 413-419, 2007/09
  • Heat-induced conversion of beta(2)-Microglobulin and hen egg-white lysozyme into amyloid fibrils, Kenji Sasahara,Hisashi Yagi,Hironobu Naiki,Yuji Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, Vol. 372, No. 4, p. 981-991, 2007/09
  • Dimethylsulfoxide-quenched hydrogen/deuterium exchange method to study amyloid fibril structure, Masaru Hoshino,Hidenori Katou,Kei-Ichi Yamaguchi,Yuji Goto, BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, ELSEVIER SCIENCE BV, Vol. 1768, No. 8, p. 1886-1899, 2007/08
  • Conformational indeterminism in protein misfolding: Chiral amplification on amyloidogenic pathway of insulin, Wojciech Dzwolak,Anna Loksztejn,Agnieszka Galinska-Rakoczy,Rumi Adachi,Yuji Goto,Leszek Rupnicki, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, AMER CHEMICAL SOC, Vol. 129, No. 24, p. 7517-7522, 2007/06
  • Development of a technique for the investigation of folding dynamics of single proteins for extended time periods, Masahito Kinoshita,Kiyoto Kamagata,Akio Maeda,Yuji Goto,Tamiki Komatsuzaki,Satoshi Takahashi, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, NATL ACAD SCIENCES, Vol. 104, No. 25, p. 10453-10458, 2007/06
  • A toxic monomeric conformer of the polyglutamine protein., Yoshitaka Nagai,Takashi Inui,H Akiko Popiel,Nobuhiro Fujikake,Kazuhiro Hasegawa,Yoshihiro Urade,Yuji Goto,Hironobu Naiki,Tatsushi Toda, Nature structural & molecular biology, Vol. 14, No. 4, p. 332-40, 2007/04
  • Promiscuous binding of ligands by beta-lactoglobulin involves hydrophobic interactions and plasticity., Konuma T,Sakurai K,Goto Y, Journal of molecular biology, Elsevier BV, Vol. 368, No. 1, p. 209-218, 2007/04
  • A rapid flow mixer with 11-mu s mixing time microfabricated by a pulsed-laser ablation technique: Observation of a barrier-limited collapse in cytochrome c folding, Shuzo Matsumoto,Akira Yane,Satoru Nakashima,Masaki Hashida,Masayuki Fujita,Yuji Goto,Satoshi Takahashi, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, AMER CHEMICAL SOC, Vol. 129, No. 13, p. 3840-+, 2007/04
  • Lipocalin-type prostaglandin D synthase/beta-trace is a major amyloid beta-chaperone in human cerebrospinal fluid, Takahisa Kanekiyo,Tadato Ban,Kosuke Aritake,Zhi-Li Huang,Wei-Min Qu,Issay Okazaki,Ikuko Mohri,Shigeo Murayama,Keiichi Ozono,Masako Taniike,Yuji Goto,Yoshihiro Urade, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, NATL ACAD SCIENCES, Vol. 104, No. 15, p. 6412-6417, 2007/04
  • Heat-triggered conversion of protofibrils into mature amyloid fibrils of beta(2)-microglobulin, Kenji Sasahara,Hisashi Yagi,Hironobu Naiki,Yuji Goto, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 46, No. 11, p. 3286-3293, 2007/03
  • Flow-induced alignment of amyloid protofilaments revealed by linear dichroism, Rumi Adachi,Kei-ichi Yamaguchi,Hisashi Yagi,Kazumasa Sakurai,Hironobu Naiki,Yuji Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 282, No. 12, p. 8978-8983, 2007/03
  • Cores and pH-dependent dynamics of ferredoxin-NADP(+) reductase revealed by hydrogen/deuterium exchange, Young-Ho Lee,Kosuke Tamura,Masahiro Maeda,Masaru Hoshino,Kazumasa Sakurai,Satoshi Takahashi,Takahisa Ikegami,Toshiharu Hase,Yuji Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 282, No. 8, p. 5959-5967, 2007/02
  • 2P100 Observation of the initial collapse in apomyoglobin folding by ultra-rapid mixing(Proteins-stability, folding, and other physicochemical properties,Poster Presentations), Tatsumi Tetsuma,Kinoshita Masahito,Goto Yuji,Takahashi Satoshi, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 47, 2007
  • 2P104 Development of a technique for the investigation of folding dynamics of single proteins for extended time periods(Proteins-stability, folding, and other physicochemical properties,Poster Presentations), Kinoshita Masahito,Kamagata Kiyoto,Maeda Akio,Goto Yuji,Komatsuzaki Tamiki,Takahashi Satoshi, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 47, 2007
  • 2P092 Equilibrium and kinetics of β_2-Microglobulin from the acid-unfolded state(Proteins-stability, folding, and other physicochemical properties,Oral Presentations), Mukaiyama Atsushi,Maki Kosuke,Goto Yuji,Kuwajima Kunihiro, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 47, 2007
  • 2P094 Direct observation of single-molecule trajectories of protein folding under non-equilibrium condition(Proteins-stability, folding, and other physicochemical properties,Oral Presentations), Kamagata Kiyoto,Kinoshita Masahito,Goto Yuji,Takahashi Satoshi, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 47, 2007
  • 3P048 Packing density of amiloid-like and amyloid fibrils(Proteins-stability, folding, and other physicochemical properties,Poster Presentations), Lee Young-Ho,Chatani Eri,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 47, 2007
  • 3P052 The effects of reductant on the amyloid fibril formation of β2-microglobulin(Proteins-stability, folding, and other physicochemical properties,Poster Presentations), Yamamoto Kaori,Ozawa Daisaku,Yagi Hisashi,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 47, 2007
  • 3P055 Uniforming the Molecular Weigh of Amyloid Fibrils by Ultrasonication(Proteins-stability, folding, and other physicochemical properties,Oral Presentations), Chatani Eri,Adachi Rumi,Sakai Miyo,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 47, 2007
  • 2P078 Time-resolved small angle x-ray scattering study on the burst phase intermediate in the folding of bamase(Proteins-stability, folding, and other physicochemical properties,Poster Presentations), Konuma Tsuyoshi,Kimura Tetsunari,Matsumoto Shuzo,Goto Yuji,Fujisawa Tetsuro,Takahashi Satoshi, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 47, 2007
  • 1P058 Principal component analysis of the pH-dependent conformational transitions of bovine β-lactoglobulin monitored by heteronuclear NMR(Proteins-functions, methodology, and protein enigineering,Oral Presentations), Sakurai Kazumasa,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 47, 2007
  • Principal component analysis of the pH-dependent conformational transitions of bovine beta-lactoglobulin monitored by heteronuclear NMR., Proc. Natl. Acad. Sci. USA, Vol. 104 (39), 15346-15351, 2007
  • Age-related changes of alpha-crystallin aggregate in human lens, N. Fujii,Y. Shimmyo,M. Sakai,Y. Sadakane,T. Nakamura,Y. Morimoto,T. Kinouchi,Y. Goto,K. Lampi, AMINO ACIDS, SPRINGER, Vol. 32, No. 1, p. 87-94, 2007/01
  • Dynamics and mechanism of the ligand binding of bovine beta-lactoglobulin studied using heteronuclear NMR spectroscopy., J. Mol. Biol., Vol. 368 (1), 209-218, 2007
  • High-resolution crystal structure of beta2-microglobulin formed under physiological conditions., J. Biochem., Vol. 142 (3), 413-419, 2007
  • 3D structure of amyloid protofilaments of β2-microglobulin fragment probed by solid-state NMR, Kentaro Iwata,Toshimichi Fujiwara,Yoh Matsuki,Hideo Akutsu,Satoshi Takahashi,Hironobu Naiki,Yuji Goto, Proceedings of the National Academy of Sciences of the United States of America, Vol. 103, No. 48, p. 18119-18124, 2006/11/28
  • Real-time and single fibril observation of the formation of amyloid beta spherulitic structures, Tadato Ban,Kenichi Morigaki,Hisashi Yagi,Takashi Kawasaki,Atsuko Kobayashi,Shunsuke Yuba,Hironobu Naiki,Yuji Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 281, No. 44, p. 33677-33683, 2006/11
  • Flexible docking of an amyloid-forming peptide from beta(2)-microglobulin, Daron M. Standley,Yasushige Yonezawa,Yuji Goto,Haruki Nakamura, FEBS LETTERS, ELSEVIER SCIENCE BV, Vol. 580, No. 26, p. 6199-6205, 2006/11
  • Conformation of amyloid fibrils of beta(2)-microglobulin probed by tryptophan mutagenesis, Miho Kihara,Eri Chatani,Kentaro Iwata,Kaori Yamamoto,Takanori Matsuura,Atsushi Nakagawa,Hironobu Naiki,Yuji Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 281, No. 41, p. 31061-31069, 2006/10
  • Mechanism by which the amyloid-like fibrils of a beta(2)-microglobulin fragment are induced by fluorine-substituted alcohols, Kei-ichi Yamaguchi,Hironobu Naiki,Yuji Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, Vol. 363, No. 1, p. 279-288, 2006/10
  • Direct observation of amyloid fibril growth, propagation, and adaptation, Tadato Ban,Keiichi Yamaguchi,Yuji Goto, ACCOUNTS OF CHEMICAL RESEARCH, AMER CHEMICAL SOC, Vol. 39, No. 9, p. 663-670, 2006/09
  • Structure of interacting segments in the growing amyloid fibril of beta(2)-microglobulin probed with IR Spectroscopy, Ming Lu,Hirotsugu Hiramatsu,Yuji Goto,Teizo Kitagawa, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD, Vol. 362, No. 2, p. 355-364, 2006/09
  • Exothermic effects observed upon heating of beta(2)-microglobulin monomers in the presence of amyloid seeds, Kenji Sasahara,Hironobu Naiki,Yuji Goto, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 45, No. 29, p. 8760-8769, 2006/07
  • Seeding-dependent propagation and maturation of beta(2)-microglobulin amyloid fibrils under high pressure, Eri Chatani,Hironobu Naiki,Yuji Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, Vol. 359, No. 4, p. 1086-1096, 2006/06
  • Dynamics and mechanism of the Tanford transition of bovine beta-lactoglobulin studied using Heteronuclear NMR Spectroscopy, K Sakurai,Y Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD, Vol. 356, No. 2, p. 483-496, 2006/02
  • 1P112 Multiple time scales in the folding dynamics of single chain monellin revealed by single molecule measurements(3. Protein folding and misfolding (1),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006), Maeda Akio,Kinoshita Masahito,Kamagata Kiyoto,Konno Takashi,Goto Yuji,Takahashi Satoshi, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 46, No. 2, 2006
  • 1P108 Development of sheath-flow system to observe protein folding events at a single-molecule level(3. Protein folding and misfolding (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006), Kamagata Kiyoto,Kinoshita Masahito,Goto Yuji,Takahashi Satoshi, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 46, No. 2, 2006
  • 2P277 Promiscuous ligand binding of β-lactoglobulin allowed by hydrophobic interactions and structural variability(40. Membrane structure,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006), Konuma Tsuyoshi,Sakurai Kazumasa,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 46, No. 2, 2006
  • 2P125 Relationship between pH-dependent conformational and stability changes of bovine β-lactoglobulin studied using NMR spectroscopy(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006), Sakurai Kazumasa,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 46, No. 2, 2006
  • 2P109 Folding and Unfolding Kinetics of β2-Microglobulin as Probed by Tryptophan Fluorescence(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006), Sakata Michiko,Chatani Eri,Kameda Atsushi,Sakurai Kazumasa,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 46, No. 2, 2006
  • 2P119 Reduction of disulfide bridge inhibits the amyloid fibril formation of β2-microglobulin(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006), Yamamoto Kaori,Yagi Hisashi,Hasegawa Kazuhiro,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 46, No. 2, 2006
  • 2P112 Heat Capacity Change Associated with Structural Conversion into Amyloid Fibril(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006), Sasahara Kenji,Yagi Hisashi,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 46, No. 2, 2006
  • 2P105 Structural polymorphism of β_2-microglobulin amyloid fibrils induced by the addition of trifluoroethanol(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006), Chatani Eri,Yagi Hisashi,Naiki Hironobu,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 46, No. 2, 2006
  • alpha B-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta 2-microglobulin, B Raman,T Ban,M Sakai,SY Pasta,T Ramakrishna,H Naiki,Y Goto,CM Rao, BIOCHEMICAL JOURNAL, PORTLAND PRESS LTD, Vol. 392, p. 573-581, 2005/12
  • Dialysis-related amyloidosis: From molecular mechanism to therapies, Yuji Goto,Vittorio Bellotti,Rino Esposito, Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1753, No. 1, p. 1-3, 2005/11/10
  • Structural stability of amyloid fibrils of β2-microglobulin in comparison with its native fold, Eri Chatani,Yuji Goto, Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1753, No. 1, p. 64-75, 2005/11/10
  • Kinetic analysis of the polymerization and depolymerization of beta(2)-microglobulin-related amyloid fibrils in vitro., Yamamoto S,Hasegawa K,Yamaguchi I,Goto Y,Gejyo F,Naiki H, Biochimica et biophysica acta, Vol. 1753, No. 1, p. 34-43, 2005/11
  • Structural studies reveal that the diverse morphology of beta(2)-microglobulin aggregates is a reflection of different molecular architectures, J Kardos,D Okuno,T Kawai,Y Hagihara,N Yumoto,T Kitagawa,P Zavodszky,H Naiki,Y Goto, BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, ELSEVIER SCIENCE BV, Vol. 1753, No. 1, p. 108-120, 2005/11
  • Kinetic analysis of the polymerization and depolymerization of beta2-microglobulin-related amyloid fibrils in vitro, S Yamamoto,K Hasegawa,Yamaguchi, I,Y Goto,F Gejyo,H Naiki, BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, ELSEVIER SCIENCE BV, Vol. 1753, No. 1, p. 34-43, 2005/11
  • Seeding-dependent propagation and maturation of amyloid fibril conformation, Kei-Ichi Yamaguchi,Satoshi Takahashi,Tomoji Kawai,Hironobu Naiki,Yuji Goto, Journal of Molecular Biology, Vol. 352, No. 4, p. 952-960, 2005/09/30
  • Ultrasonication-induced amyloid fibril formation of beta(2)-microglobulin, Y Ohhashi,M Kihara,H Naiki,Y Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 280, No. 38, p. 32843-32848, 2005/09
  • Main-chain dominated amyloid structures demonstrated by the effect of high pressure, E Chatani,M Kato,T Kawai,H Naiki,Y Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, Vol. 352, No. 4, p. 941-951, 2005/09
  • Kinetically controlled thermal response of beta(2)-microglobulin amyloid fibrils, K Sasahara,H Naiki,Y Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, Vol. 352, No. 3, p. 700-711, 2005/09
  • Identification of the n- and c-terminal substrate binding segments of Ferredoxin-NADP plus reductase by NMR, M Maeda,YH Lee,T Ikegami,K Tamura,M Hoshino,T Yamazaki,M Nakayama,T Hase,Y Goto, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 44, No. 31, p. 10644-10653, 2005/08
  • Direct calorimetric measurement of the thermodynamic parameters of amyloid formation, J Kardos,K Yamamoto,K Hasegawa,H Naiki,L Graf,Y Goto, FEBS JOURNAL, WILEY-BLACKWELL, Vol. 272, p. 379-379, 2005/07
  • Structural model of the amyloid fibril formed by beta(2)-microglobulin #21-31 fragment based on vibrational spectroscopy, H Hiramatsu,Y Goto,H Naiki,T Kitagawa, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, AMER CHEMICAL SOC, Vol. 127, No. 22, p. 7988-7989, 2005/06
  • Metal ion-dependent effects of clioquinol on the fibril growth of an amyloid beta peptide, B Raman,T Ban,K Yamaguchi,M Sakai,T Kawai,H Naiki,Y Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 280, No. 16, p. 16157-16162, 2005/04
  • Nuclear magnetic resonance characterization of the refolding intermediate of beta(2)-microglobulin trapped by non-native prolyl peptide bond, A Kameda,M Hoshino,T Higurashi,S Takahashi,H Naiki,Y Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, Vol. 348, No. 2, p. 383-397, 2005/04
  • Molecular interactions in the formation and deposition of beta(2)-microglobuhn-related amyloid fibrils, H Naiki,S Yamamoto,K Hasegawa,Yamaguchi, I,Y Goto,F Gejyo, AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS, INFORMA HEALTHCARE, Vol. 12, No. 1, p. 15-25, 2005/03
  • Seeding-dependent maturation of ss(2)-microglobulin amyloid fibrils at neutral pH, M Kihara,E Chatani,M Sakai,K Hasegawa,H Naiki,Y Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 280, No. 12, p. 12012-12018, 2005/03
  • Association of thin filaments into thick filaments revealing the structural hierarchy of amyloid fibrils, Takashi Kanno,Keiichi Yamaguchi,Hironobu Naiki,Yuji Goto,Tomoji Kawai, Journal of Structural Biology, Vol. 149, No. 2, p. 213-218, 2005/02
  • Electron transfer reaction in a single protein molecule observed by total internal reflection fluorescence microscopy, Y Furukawa,T Ban,D Hamada,K Ishimori,Y Goto,Morishima, I, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, AMER CHEMICAL SOC, Vol. 127, No. 7, p. 2098-2103, 2005/02
  • Critical balance of electrostatic and hydrophobic interactions is required for beta(2)-microglobulin amyloid fibril growth and stability, B Raman,E Chatani,M Kihara,T Ban,M Sakai,K Hasegawa,H Naiki,CM Rao,Y Goto, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 44, No. 4, p. 1288-1299, 2005/02
  • 1P012 pH dependence of amyloid fibril structures of b2-microglobulin fragment peptides investigated by IR spectroscopy, Lu M.,Hiramatsu H.,Goto Y.,Kitagawa T., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 45, 2005
  • 2P074 The Structual Model for the Amyloid Fibril Formed by β_2-microglobulin Fragment Based on Solid-state NMR, Iwata K.,Fujiwara T.,Matsuki Y.,Akutsu H.,Naiki H.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 45, 2005
  • 2P076 Effects of surface interaction on the Aβ(1-40) amyloid fibril formation and growth, Ban T.,Morigaki K.,Naiki H.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 45, 2005
  • 2P089 Time-resolved fluorescence and resonance raman measurements of the initial collapse in cytochrome c folding, Matsumoto S.,Yane A.,Goto Y.,Hashida M.,Fujita M.,Nakashima S.,Takahashi S., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 45, 2005
  • 2P085 Development of the fluorescence detection device to observe single molecule dynamics of protein folding for extended periods, Maeda A.,Kinoshita M.,Konno T.,Goto Y.,Takahashi S., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 45, 2005
  • 2P075 Ultrasonication-induced amyloid fibril formation of beta_2-microglobulin, Ohhashi Y.,Kihara M.,Naiki H.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 45, 2005
  • 3P046 Structural analysis of amyloid fibrils ofβ2-microglobulin using tryptophan fluorescence probe, Kihara M.,Yamamoto K.,Iwata K.,Chatani E.,Hasegawa K.,Naiki H.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 45, 2005
  • 3P067 Study of dynamics and mechanism of Tanford transition of bovine β-lactoglobulin, Sakurai K.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 45, 2005
  • 3P045 Direct observation ofβ_2-microglobulin amyloid fibril formation at neutral pH, Ozawa D.,Ban T.,Kameda A.,Naiki H.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 45, 2005
  • 1P087 Iso-1-Cytochrome c Folding Studied by a New Method of Single Molecule Detection, Kinoshita M.,Goto Y.,Takahashi S., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 45, 2005
  • 1P097 Transition from non-amyloidogenic aggregates to amyloid fibrils, Sasahara K.,Naiki H.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 45, 2005
  • 1P095 Analyses of the folding reaction of the bovine β-lactoglobulin mutant using pulse-labeling H/D exchange, Yagi M.,Kameda A.,Sakurai K.,Nishimura C.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 45, 2005
  • Characterization of alpha-crystallin aggregate of lens from elderly donors, Noriko Fujii,Yoshiari Shimmyo,Miyo Sakai,Yutaka Sadakane,Tooru Nakamura,Tadatoshi Kinouchi,Yuji Goto,Yukio Morimoto,Kirsten Lampi, 第78回日本生化学会大会, 2005
  • Stereospecific amyloid-like fibril formation by a peptide fragment of beta(2)-microglobulin, H Wadai,K Yamaguchi,S Takahashi,T Kanno,T Kawai,H Naiki,Y Goto, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 44, No. 1, p. 157-164, 2005/01
  • Direct observation of A beta amyloid fibril growth and inhibition, T Ban,M Hoshino,S Takahashi,D Hamada,K Hasegawa,H Naiki,Y Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, Vol. 344, No. 3, p. 757-767, 2004/11
  • Conformational stability of amyloid fibrils of beta-microglobulin probed by guanidine-hydrochloride-induced unfolding, T Narimoto,K Sakurai,A Okamoto,E Chatani,M Hoshino,K Hasegawa,H Naiki,Y Goto, FEBS LETTERS, ELSEVIER SCIENCE BV, Vol. 576, No. 3, p. 313-319, 2004/10
  • Structure and Formation of Amyloid Fibrils of β_2-Microglobulin, YAMAGUCHI Keiichi,GOTO Yuji, Biophysics, The Biophysical Society of Japan General Incorporated Association, Vol. 44, No. 5, p. 212-217, 2004/09/25
  • Low concentrations of sodium dodecyl sulfate induce the extension of beta(2)-microglobulin-related amyloid fibrils at a neutral pH, S Yamamoto,K Hasegawa,Yamaguchi, I,S Tsutsumi,J Kardos,Y Goto,F Gejyo,H Naiki, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 43, No. 34, p. 11075-11082, 2004/08
  • Core and heterogeneity of beta(2)-microglobulin amyloid fibrils as revealed by H/D exchange, KI Yamaguchi,H Katou,M Hoshino,K Hasegawa,H Naiki,Y Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD, Vol. 338, No. 3, p. 559-571, 2004/04
  • Core structure of amyloid fibril proposed from IR-microscope linear dichroism, H Hiramatsu,Y Goto,H Naiki,T Kitagawa, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, AMER CHEMICAL SOC, Vol. 126, No. 10, p. 3008-3009, 2004/03
  • Increase in the conformational flexibility of beta(2)-microglobulin upon copper binding: A possible role for copper in dialysis-related amyloidosis, J Villanueva,M Hoshino,H Katou,J Kardos,K Hasegawa,H Naiki,Y Goto, PROTEIN SCIENCE, COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT, Vol. 13, No. 3, p. 797-809, 2004/03
  • 3P019 Development of the rapid mixing apparatus by laser processing and elucidation of the initial collapse in the cytochrome c folding, Matsumoto S.,Yane A.,Goto Y.,Takahashi S.,Hashida M.,Fujita M.,Nakashima S., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 44, 2004
  • 2P023 The structure of the interaction part of the amyloid fibril of beta 2 microglobulin elucidated by IR microscope, Lu M.,Hiramatsu H.,Goto Y.,Naiki H.,Kitagawa T., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 44, 2004
  • 2P022 Amyloid fibril structure proposed from IR-microscope linear dichroism, Hiramatsu H.,Goto Y.,Naiki H.,Kitagawa T., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 44, 2004
  • 3P022 Helix environment in the early folding intermediate of apomyoglobin detected by time-resolved IR spectroscopy, Nishiguchi S.,Goto Y.,Takahashi S., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 44, 2004
  • 3P057 Calorimetric analysis of amyloid fibril formation of beta-2-microglobulin, Yamamoto K.,Kardos Jozsef,Hasegawa K.,Naiki H.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 44, 2004
  • 3P020 Iso-1-Cytochrome c Folding Studied by a New Method of Single Molecule Detection, Kinoshita M.,Goto Y.,Takahashi S., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 44, 2004
  • 1P008 Structual Analysis of Amyloid Fibril of Fragment, Iwata K.,Fujiwara T.,Matsuki Y.,Naiki H.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 44, 2004
  • Amyloid fibril structure of beta2-microglobulin #21-31 peptide elucidated by IR-microscope linear dichroism, H Hiramatsu,Y Goto,H Naiki,T Kitagawa, BIOPHYSICAL JOURNAL, BIOPHYSICAL SOCIETY, Vol. 86, No. 1, p. 505A-505A, 2004/01
  • Glycosaminoglycans enhance the trifluoroethanol-induced extensionof beta(2)-microglobulin-related amyloid fibrils at a neutral pH, S Yamamoto,Yamaguchi, I,K Hasegawa,S Tsutsumi,Y Goto,F Gejyo,H Naiki, JOURNAL OF THE AMERICAN SOCIETY OF NEPHROLOGY, AMER SOC NEPHROLOGY, Vol. 15, No. 1, p. 126-133, 2004/01
  • Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry, Kardos, J,Yamamoto, K,Hasegawa, K,Naiki, H,Goto, Y, J. Biol. Chem, Vol. 279(53), p. 55308-55314, 2004
  • Optimum amyloid fibril formation of a peptide fragment suggests the amyloidogenic preference of β<SUB>2</SUB>-microglobulin under physiological conditions, Ohhashi, Y,Hasegawa, K,Naiki, H,Goto, Y, J Biol. Chem, Vol. 279(11), p. 10814-10821, 2004
  • Protein folding by the effects of macromolecular crowding, N Tokuriki,M Kinjo,S Negi,M Hoshino,Y Goto,Urabe, I,T Yomo, PROTEIN SCIENCE, COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT, Vol. 13, No. 1, p. 125-133, 2004/01
  • Reversible unfolding of bovine beta-lactoglobulin mutants without a free thiol group, M Yagi,K Sakurai,C Kalidas,CA Batt,Y Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 278, No. 47, p. 47009-47015, 2003/11
  • Amyloid fibril formation in the context of full-length protein - Effects of proline mutations on the amyloid fibril formation of beta(2)-microglobulin, T Chiba,Y Hagihara,T Higurashi,K Hasegawa,H Naiki,Y Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 278, No. 47, p. 47016-47024, 2003/11
  • Dissolution of beta(2)-microglobulin amyloid fibrils by dimethylsulfoxide, N Hirota-Nakaoka,K Hasegawa,H Naiki,Y Goto, JOURNAL OF BIOCHEMISTRY, JAPANESE BIOCHEMICAL SOC, Vol. 134, No. 1, p. 159-164, 2003/07
  • Conformational dynamics of beta(2)-microglobulin analyzed by reduction and reoxidation of the disulfide bond, M Gozu,YH Lee,Y Ohhashi,M Hoshino,H Naiki,Y Goto, JOURNAL OF BIOCHEMISTRY, JAPANESE BIOCHEMICAL SOC, Vol. 133, No. 6, p. 731-736, 2003/06
  • Structural defects and the diagnosis of amyloidogenic propensity, A Fernandez,J Kardos,LR Scott,Y Goto,RS Berry, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, NATL ACAD SCIENCES, Vol. 100, No. 11, p. 6446-6451, 2003/05
  • Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence, T Ban,D Hamada,K Hasegawa,H Naiki,Y Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 278, No. 19, p. 16462-16465, 2003/05
  • Amyloidogenic synthetic peptides of beta 2-microglobulin - a role of the disulfide bond, K Hasegawa,Y Ohhashi,Yamaguchi, I,N Takahashi,S Tsutsumi,Y Goto,F Gejyo,H Naiki, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, ACADEMIC PRESS INC ELSEVIER SCIENCE, Vol. 304, No. 1, p. 101-106, 2003/04
  • Real time observation of individual beta(2)-microglobulin unfolding and refolding equilibrium using X-ray diffraction, T Higurashi,YC Sasaki,H Naiki,Y Goto, BIOPHYSICAL JOURNAL, BIOPHYSICAL SOCIETY, Vol. 84, No. 2, p. 166A-166A, 2003/02
  • Protein folding: could hydrophobic collapse be coupled with hydrogen-bond formation?, A Fernandez,J Kardos,Y Goto, FEBS LETTERS, ELSEVIER SCIENCE BV, Vol. 536, No. 1-3, p. 187-192, 2003/02
  • NMR analysis of the native and acid denatured β2-microglobulin proline mutants, Kameda A.,Hoshino M.,Higurashi T.,Hagihara Y.,Naiki H.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 43, 2003
  • Urea unfolding of ferredoxin-NADP^+ reductase, Tamura K.,Maeda M.,Hoshino M.,Ikegami T.,Yamazaki T.,Hase T.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 43, 2003
  • Inhibition of amyloid β peptide (25-35) amyloid fibril extension using L/D isomer chimera peptide, Ban T.,Goto Y.,Naiki H., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 43, 2003
  • Various stability of amyloid fibrils formed under different conditions, Okamoto A.,Narimoto T.,Chatani E.,Hoshino M.,Hasegawa K.,Naiki H.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 43, 2003
  • Amyloidogenic synthetic peptides of beta2-microglobulin, Hasegawa K.,Ohhashi Y.,Yamaguchi I.,Takahashi N.,Tsutsumi S.,Goto Y.,Gejyo F.,Naiki H., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 43, 2003
  • Amyloid fibril formation and Structural Stability of β2-microgloblin mutants, Kihara M.,Hagihara Y.,Hasegawa K.,Naiki H.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 43, 2003
  • Effect of Enantiomeric Fragment for Amyloid Fibril Formation, Wadai H.,Yamaguchi K.,Kanno T.,Nakamura T.,T. Tomoji,Hasagawa K.,Naiki H.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 43, 2003
  • Formation of molten globule-like state of cytochrome c induced by n-alkyl sulfates at low concentrations., J. Biochem., Vol. 133, No. 1, p. 93-102, 2003
  • The interaction of beta(2)-glycoprotein I domain V with chaperonin GroEL: The similarity with the domain V and membrane interaction, M Gozu,M Hoshino,T Higurashi,H Kato,Y Goto, PROTEIN SCIENCE, COLD SPRING HARBOR LAB PRESS, Vol. 11, No. 12, p. 2792-2803, 2002/12
  • The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR, H Katou,T Kanno,M Hoshino,Y Hagihara,H Tanaka,T Kawai,K Hasegawa,H Naiki,Y Goto, PROTEIN SCIENCE, COLD SPRING HARBOR LAB PRESS, Vol. 11, No. 9, p. 2218-2229, 2002/09
  • Manipulating monomer-dimer equilibrium of bovine beta-lactoglobulin by amino acid substitution, K Sakurai,Y Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 277, No. 28, p. 25735-25740, 2002/07
  • Conformation of beta(2)-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond, DP Hong,M Gozu,K Hasegawa,H Naiki,Y Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 277, No. 24, p. 21554-21560, 2002/06
  • Amyloid fibril formation of beta 2-microglobulin, Y. Goto,M. Hoshino, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, Vol. 47, No. 6, p. 663-669, 2002/05
  • Mapping the core of the beta(2)-microglobulin amyloid fibril by H/D exchange, M Hoshino,H Katou,Y Hagihara,K Hasegawa,H Naiki,Y Goto, NATURE STRUCTURAL BIOLOGY, NATURE AMERICA INC, Vol. 9, No. 5, p. 332-336, 2002/05
  • Partially folded structure of flavin adenine dinucleotide-depleted ferredoxin-NADP(+) reductase with residual NADP(+) binding domain, M Maeda,D Hamada,M Hoshino,Y Onda,T Hase,Y Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 277, No. 19, p. 17101-17107, 2002/05
  • Amyloid fibril formation of the mouse V-L domain at acidic pH, SP Martsev,AP Dubnovitsky,AP Vlasov,M Hoshino,K Hasegawa,H Naiki,Y Goto, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 41, No. 10, p. 3389-3395, 2002/03
  • 3M1445 Real time observation of individual beta2-microglobulin folding reaction using X-ray diffraction, Higurashi T.,Sasaki Y.C.,Naiki H.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 42, No. 2, 2002
  • 2I615 Conformation of anyloid fibrils studied by nuclear magnetic resonance, Hoshino M.,Katou H.,Ohhashi Y.,Hagihara Y.,Hasegawa K.,Naiki H.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 42, No. 2, 2002
  • 2I1630 Amyloid fibril formation of beta2-Microglobulin proline mutants, Chiba T.,Hagihara Y.,Higurashi T.,Hasegawa K.,Naiki H.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 42, No. 2, 2002
  • 2I1645 Analysis of Structural Stability of beta2-Microglobulin Amyloid Fibris, Narimoto T.,Hoshino M.,Kardos Jozsef,Hasegawa K.,Naiki H.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 42, No. 2, 2002
  • 2R1615 H/D exchange reaction of ferredoxin-NADP^+ reductase analyzed by NMR, Tamura K.,Maeda M.,Hoshino M.,Yamazaki T.,Hase T.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 42, No. 2, 2002
  • Single molecular observation of conformational change of beta2-microglobulin using FRET and DXT, T Higurashi,YC Sasaki,H Naiki,Y Goto, BIOPHYSICAL JOURNAL, BIOPHYSICAL SOCIETY, Vol. 82, No. 1, p. 46A-46A, 2002/01
  • Structural analysis of ferredoxin-NADP(+) reductase and substrate complex by nuclear magnetic resonance, M Maeda,M Hoshino,T Yamazaki,T Hase,Y Goto, PLANT AND CELL PHYSIOLOGY, OXFORD UNIV PRESS, Vol. 43, p. S24-S24, 2002
  • Aggregation of beta(2)-glycoprotein I induced by sodium lauryl sulfate and lysophospholipids, Y Hagihara,DP Hong,M Hoshino,K Enjyoji,H Kato,Y Goto, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 41, No. 3, p. 1020-1026, 2002/01
  • Investigation of a peptide responsible for amyloid fibril formation of beta(2)-microglobulin by Achromobacter protease I, GV Kozhukh,Y Hagihara,T Kawakami,K Hasegawa,H Naiki,Y Goto, JOURNAL OF BIOLOGICAL CHEMISTRY, AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, Vol. 277, No. 2, p. 1310-1315, 2002/01
  • The intrachain disulfide bond of beta(2)-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pH, Y Ohhashi,Y Hagihara,G Kozhukh,M Hoshino,K Hasegawa,Yamaguchi, I,H Naiki,Y Goto, JOURNAL OF BIOCHEMISTRY, JAPANESE BIOCHEMICAL SOC, Vol. 131, No. 1, p. 45-52, 2002/01
  • Salt-dependent monomer-dimer equilibrium of bovine beta-lactoglobulin at pH 3, K Sakurai,M Oobatake,Y Goto, PROTEIN SCIENCE, COLD SPRING HARBOR LAB PRESS, Vol. 10, No. 11, p. 2325-2335, 2001/11
  • A two-process model describes the hydrogen exchange behavior of cytochrome c in the molten globule state with various extents of acetylation, Z Szewczuk,Y Konishi,Y Goto, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 40, No. 32, p. 9623-9630, 2001/08
  • Flexible loop of beta(2)-glycoprotein I domain V specifically interacts with hydrophobic ligands, DP Hong,Y Hagihara,H Kato,Y Goto, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 40, No. 27, p. 8092-8100, 2001/07
  • Native-like beta-hairpin retained in the cold-denatured state of bovine beta-lactoglobulin, H Katou,M Hoshino,H Kamikubo,CA Batt,Y Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD, Vol. 310, No. 2, p. 471-484, 2001/07
  • Structural and kinetic characterization of early folding events in beta-lactoglobulin, K Kuwata,R Shastry,H Cheng,M Hoshino,CA Batt,Y Goto,H Roder, NATURE STRUCTURAL BIOLOGY, NATURE AMERICA INC, Vol. 8, No. 2, p. 151-155, 2001/02
  • High pressure NMR reveals a variety of fluctuating conformers in beta-lactoglobulin, K Kuwata,H Li,H Yamada,CA Batt,Y Goto,K Akasaka, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD, Vol. 305, No. 5, p. 1073-1083, 2001/02
  • Folding of b-lactoglobulin : nonhierarchic or hierarchic?, Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 41, 2001
  • Stability of beta2-Microgloblin Amyloid Fibrils Analyzed by Depolymerization and Reduction of the Disulfide Bond, Hong D.-P,Hasegawa K,Naiki H,Goto Y, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 41, 2001
  • Role of the intrachain disulfide bond of beta2-microglobulin on its amyloid fibril formation., Ohashi Y,Hagihara Y,Gennadiy Kozhukh,Hoshino M,Hasegawa K,Yamaguchi I,Naiki H,Kanno T,Kawai T,Goto Y, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 41, 2001
  • The Effect of Alcohol on beta2-Microglobulin Amyloid Fibrils, Hirota-Nakaoka N,Hasegawa K,Naiki H,Goto Y, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 41, 2001
  • Role of disulfide bond in the amyloid fibril formation of beta2-microglobulin by NMR, Katou H,Hoshino M,Gennadiy Kozhukh,Hasegawa K,Naiki H,Goto Y, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 41, 2001
  • Dimerization Interaction of Bovine beta-Lactoglobulin Studied by Amino Acid Substitution., Sakurai K,Hoshino M,Goto Y, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 41, 2001
  • Real Time Obsevation of beta2-microglobulin Amylolid Fibril Extension, Ban T.,Hamada D.,Hagihara Y.,Chiba T.,Hasegawa K.,Naiki H.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 41, 2001
  • Kinetic evidence for non-native A-helix at the N-terminus of B-lactoglobulin, RMC Shastry,H Roder,K Kuwata,Y Goto, BIOPHYSICAL JOURNAL, BIOPHYSICAL SOCIETY, Vol. 80, No. 1, p. 186A-186A, 2001/01
  • Direct observation of dynamics in cytochrome c by single molecule fluorometry., T Wazawa,Y Ishii,T Nishida,D Hamada,Y Goto,T Yanagida, BIOPHYSICAL JOURNAL, BIOPHYSICAL SOCIETY, Vol. 80, No. 1, p. 406A-406A, 2001/01
  • Identification of the phospholipid-binding site of human beta(2)-glycoprotein I domain V by heteronuclear magnetic resonance, M Hoshino,Y Hagihara,Nishii, I,T Yamazaki,H Kato,Y Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD, Vol. 304, No. 5, p. 927-939, 2000/12
  • Control of antibody-antigen interaction using anion-induced conformational change in antigen peptide, Y Katakura,T Miyazaki,H Wada,T Omasa,M Kishimoto,Y Goto,K Suga, PROTEIN ENGINEERING, OXFORD UNIV PRESS, Vol. 13, No. 10, p. 719-724, 2000/10
  • Conformation and stability of thiol-modified bovine beta-lactoglobulin, K Sakai,K Sakurai,M Sakai,M Hoshino,Y Goto, PROTEIN SCIENCE, CAMBRIDGE UNIV PRESS, Vol. 9, No. 9, p. 1719-1729, 2000/09
  • Is folding of beta-Lactoglobulin non-hierarchic? Intermediate with native-like beta-sheet and non-native alpha-helix, Forge, V,M Hoshino,K Kuwata,M Arai,K Kuwajima,CA Batt,Y Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD, Vol. 296, No. 4, p. 1039-1051, 2000/03
  • The Conformational Stability of Maize Ferredoxin-NADP^+ Reductase Associated with FAD, Maeda M.,Hamada D.,Onda Y.,Hase T.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 40, 2000
  • Expression of human bete2-microglobulin by Pichia pastoris, Ohhash Y.,Hagihara Y.,Hoshino I.,Yamaguchi I.,Hasegawa K.,Naiki H.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 40, 2000
  • Analysis of reversible self-assocciation of bovine beta-Lactoglobulin : Salt effect and temperature dependency, Sakurai K.,Sakai M.,Aimoto S.,Obatake M.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 40, 2000
  • High Pressure NMR measurement of prion and beta-lactoglobulin, Kuwata K.,Hua L.,Goto Y.,Akasaka K.,James Thomas, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 40, 2000
  • Structural analysis of thiol modified beta-lactoglobulin by using NMR, Kashiwai H.,Sakai K.,Sakurai K.,Hoshino M.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 40, 2000
  • Interaction of labeled beta-Lactoglobulin with chaperonin GroEL, Sakai K.,Yamasaki R.,Hoshino H.,Kawata Y.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 40, 2000
  • Transition in cytochrome c conformation observed by single-molecule fluorometry, Wazawa T.,Nishida T.,Ishii Y.,Goto Y.,Yanagida T., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 40, 2000
  • Structural characterization of the cold-denatured state of beta-lactoglobulin, Katou H.,Hoshino M.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 40, 2000
  • Folding intermediate of beta-lactoglobulin, Kuwata K.,Goto Y.,Hoshino M.,Heinrich Roder, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 40, 2000
  • Stability and conformation of beta-lactoglobulin detected by SH titration, Hirota-Nakaoka Nami,Goto Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 40, 2000
  • High mobility of the phospholipid binding loop of human β2-glycoprotein I domain V revealed by heteronuclear NMR., J.Mol.Biol., Vol. 304, No. 5, p. 927-940, 2000
  • Solution structure and dynamics of bovine beta-lactoglobulin A, K Kuwata,M Hoshino,Forge, V,S Era,CA Batt,Y Goto, PROTEIN SCIENCE, CAMBRIDGE UNIV PRESS, Vol. 8, No. 11, p. 2541-2545, 1999/11
  • Single molecular observation of the interaction of GroEL with substrate proteins, R Yamasaki,M Hoshino,T Wazawa,Y Ishii,T Yanagida,Y Kawata,T Higurashi,K Sakai,J Nagai,Y Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD, Vol. 292, No. 5, p. 965-972, 1999/10
  • Clustering of fluorine-substituted alcohols as a factor responsible for their marked effects on proteins and peptides, DP Hong,M Hoshino,R Kuboi,Y Goto, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, AMER CHEMICAL SOC, Vol. 121, No. 37, p. 8427-8433, 1999/09
  • Folding process of β-lactoglobulin, Kuwata K.,Li H.,Yamada H.,Hoshino M.,Era S.,Goto Y.,Akasaka K.,Batt C. A.,Roder H., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 39, 1999
  • SH titration as a tool for understanding the effect of alcohols, Hirota-Nakaoka N.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 39, 1999
  • Interaction of DTNB Labeled β-Lactoglobulin with Chaperonin GroEL., Sakai K.,Yamasaki R.,Hoshino M.,Kawata Y.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 39, 1999
  • Ligand binding mechanism of β-lactoglobulin, Taguchi M.,Hoshino M,Aimoto S.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 39, 1999
  • An Analysis of Reversible Self-Association Reactions of β-Lactoglobulin by Isothemal Titration Calorimeter, Sakurai K.,Aimoto S.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 39, 1999
  • Single molecular observation of the interaction of GroEL with substrate proteins, Yamasaki T.,Sakai K.,Hoshino M.,Wasawa T.,Ishi Y.,Kawata Y.,Yanagida T.,Goto Y., Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 39, 1999
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  • Folding of beta-lactoglobulin analyzed by NMR, Hoshino Masaru,Forge Vincent,Kuwata Kazuo,Goto Yuii, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 39, 1999
  • Folding of beta-lactoglobulin, a case of the inconsistency of local and non-local interactions, Y Goto,M Hoshino,K Kuwata,CA Batt, OLD AND NEW VIEWS OF PROTEIN FOLDING, ELSEVIER SCIENCE BV, Vol. 1194, p. 3-11, 1999
  • Dynamic stability of bovine beta-lactoglobulin studied by hydrogen/deuterium exchange, Forge, V,M Hoshino,K Kuwata,CA Batt,Y Goto, OLD AND NEW VIEWS OF PROTEIN FOLDING, ELSEVIER SCIENCE BV, Vol. 1194, p. 13-19, 1999
  • Alcohol-induced denaturation of beta-lactoglobulin: A close correlation to the alcohol-induced alpha-helix formation of melittin, N Hirota-Nakaoka,Y Goto, BIOORGANIC & MEDICINAL CHEMISTRY, PERGAMON-ELSEVIER SCIENCE LTD, Vol. 7, No. 1, p. 67-73, 1999/01
  • alpha -&gt;beta transition of beta-lactoglobulin as evidenced by heteronuclear NMR, K Kuwata,M Hoshino,S Era,CA Batt,Y Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD, Vol. 283, No. 4, p. 731-739, 1998/11
  • Plasmin can reduce the function of human beta(2) glycoprotein I by cleaving domain V into a nicked form, N Ohkura,Y Hagihara,T Yoshimura,Y Goto,H Kato, BLOOD, W B SAUNDERS CO, Vol. 91, No. 11, p. 4173-4179, 1998/06
  • Folding intermediate of beta-lactoglobulin with non-native alpha-helical conformation, Y Goto,D Hamada,S Segawa, PEPTIDES, SPRINGER, p. 96-97, 1998
  • Chain-like conformation of heat-denatured ribonuclease A and cytochrome c as evidenced by solution X-ray scattering, Y Hagihara,M Hoshino,D Hamada,M Kataoka,Y Goto, FOLDING & DESIGN, CURRENT BIOLOGY LTD, Vol. 3, No. 3, p. 195-201, 1998
  • Group additive contributions to the alcohol-induced alpha-helix formation of melittin: Implication for the mechanism of the alcohol effects on proteins, N Hirota,K Mizuno,Y Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD, Vol. 275, No. 2, p. 365-378, 1998/01
  • High-level expression of bovine beta-lactoglobulin in Pichia pastoris and characterization of its physical properties, TR Kim,Y Goto,N Hirota,K Kuwata,H Denton,SY Wu,L Sawyer,CA Batt, PROTEIN ENGINEERING, OXFORD UNIV PRESS, Vol. 10, No. 11, p. 1339-1345, 1997/11
  • Trifluoroethanol-induced conformational transition of hen egg-white lysozyme studied by small-angle X-ray scattering, M Hoshino,Y Hagihara,D Hamada,M Kataoka,Y Goto, FEBS LETTERS, ELSEVIER SCIENCE BV, Vol. 416, No. 1, p. 72-76, 1997/10
  • Design and characterization of the anion-sensitive coiled-coil peptide, M Hoshino,N Yumoto,S Yoshikawa,Y Goto, PROTEIN SCIENCE, CAMBRIDGE UNIV PRESS, Vol. 6, No. 7, p. 1396-1404, 1997/07
  • The equilibrium intermediate of beta-lactoglobulin with non-native alpha-helical structure, D Hamada,Y Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD, Vol. 269, No. 4, p. 479-487, 1997/06
  • Cooperative alpha-helix formation of beta-lactoglobulin and melittin induced by hexafluoroisopropanol, N Hirota,K Mizuno,Y Goto, PROTEIN SCIENCE, CAMBRIDGE UNIV PRESS, Vol. 6, No. 2, p. 416-421, 1997/02
  • Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering, M Kataoka,K Kuwajima,F Tokunaga,Y Goto, PROTEIN SCIENCE, CAMBRIDGE UNIV PRESS, Vol. 6, No. 2, p. 422-430, 1997/02
  • Formation of protein and peptide-membrane assemblies and membrane fusion, T Yoshimura,K Kameyama,S Aimoto,T Takagi,Y Goto,S Takahashi, FORMATION AND DYNAMICS OF SELF-ORGANIZED STRUCTURES IN SURFACTANTS AND POLYMER SOLUTIONS, STEINKOPFF DARMSTADT, Vol. 106, p. 219-222, 1997
  • Structure and function of the recombinant fifth domain of human beta(2)-glycoprotein I: Effects of specific cleavage between Lys77 and Thr78, Y Hagihara,K Enjyoji,T Omasa,Y Katakura,K Suga,M Igarashi,E Matsuura,H Kato,T Yoshimura,Y Goto, JOURNAL OF BIOCHEMISTRY, JAPANESE BIOCHEMICAL SOC, Vol. 121, No. 1, p. 128-137, 1997/01
  • Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein, D Hamada,S Segawa,Y Goto, NATURE STRUCTURAL BIOLOGY, NATURE PUBLISHING CO, Vol. 3, No. 10, p. 868-873, 1996/10
  • Interaction of GroEL with conformational states of horse cytochrome c, M Hoshino,Y Kawata,Y Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD, Vol. 262, No. 4, p. 575-587, 1996/10
  • Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c, D Hamada,Y Kuroda,M Kataoka,S Aimoto,T Yoshimura,Y Goto, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD, Vol. 256, No. 1, p. 172-186, 1996/02
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  • HIGH HELICAL PROPENSITY OF THE PEPTIDE-FRAGMENTS DERIVED FROM BETA-LACTOGLOBULIN, A PREDOMINANTLY BETA-SHEET PROTEIN, D HAMADA,Y KURODA,T TANAKA,Y GOTO, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS (LONDON) LTD, Vol. 254, No. 4, p. 737-746, 1995/12
  • Salt-induced formation of the molten globule state of apomyoglobin studied by isothermal titration calorimetry, D Hamada,H Fukada,K Takahashi,Y Goto, THERMOCHIMICA ACTA, ELSEVIER SCIENCE BV, Vol. 266, p. 385-400, 1995/11
  • ROLE OF THE N-TERMINAL AND C-TERMINAL DOMAINS OF BOVINE BETA(2)-GLYCOPROTEIN-I IN ITS INTERACTION WITH CARDIOLIPIN, Y HAGIHARA,Y GOTO,H KATO,T YOSHIMURA, JOURNAL OF BIOCHEMISTRY, JAPAN BIOCHEMICAL SOC, Vol. 118, No. 1, p. 129-136, 1995/07
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  • Structural characterization of the molten globule and native states of apomyoglobin by solution x-ray scattering, Mikio Kataoka,Ichiro Nishii,Tetsuro Fujisawa,Tatzuo Ueki,Fumio Tokunaga,Yuji Goto, Journal of Molecular Biology, Vol. 249, No. 1, p. 215-228, 1995/05/26
  • High helical propensity of the peptide fragments derived from ?-lactoglobulin, a predominantlyβ-sheet protein, D. Hamada,Y. Kuroda,T. Tanaka,Y. Goto, Jour. Mol. Biol., Vol. 270, p. 1422-1428, 1995/04
  • STRUCTURE AND FUNCTION OF BETA(2)-GLYCOPROTEIN-I - WITH SPECIAL REFERENCE TO THE INTERACTION WITH PHOSPHOLIPID, Y HAGIHARA,Y GOTO,H KATO,T YOSHIMURA, LUPUS, STOCKTON PRESS, Vol. 4, p. S3-S5, 1995/02
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  • SALT-INDUCED FORMATION OF THE MOLTEN GLOBULE STATE OF CYTOCHROME-C STUDIED BY ISOTHERMAL TITRATION CALORIMETRY, D HAMADA,SI KIDOKORO,H FUKADA,K TAKAHASHI,Y GOTO, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, NATL ACAD SCIENCES, Vol. 91, No. 22, p. 10325-10329, 1994/10
  • THERMAL UNFOLDING OF TETRAMERIC MELITTIN - COMPARISON WITH THE MOLTEN GLOBULE STATE OF CYTOCHROME-C, Y HAGIHARA,M OOBATAKE,Y GOTO, PROTEIN SCIENCE, CAMBRIDGE UNIV PRESS, Vol. 3, No. 9, p. 1418-1429, 1994/09
  • COLD DENATURATION OF THE MOLTEN GLOBULE STATES OF APOMYOGLOBIN AND A PROFILE FOR PROTEIN-FOLDING, NISHII, I,M KATAOKA,F TOKUNAGA,Y GOTO, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 33, No. 16, p. 4903-4909, 1994/04
  • COMPARISON OF THE CONFORMATIONAL STABILITY OF THE MOLTEN GLOBULE AND NATIVE STATES OF HORSE CYTOCHROME-C - EFFECTS OF ACETYLATION, HEAT, UREA AND GUANIDINE-HYDROCHLORIDE, Y HAGIHARA,Y TAN,Y GOTO, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD, Vol. 237, No. 3, p. 336-348, 1994/04
  • ACID-INDUCED FOLDING OF HEME-PROTEINS, Y GOTO,AL FINK, HEMOGLOBINS, PT C, ACADEMIC PRESS INC, Vol. 232, p. 3-15, 1994
  • ACID-INDUCED UNFOLDING AND REFOLDING TRANSITIONS OF CYTOCHROME-C - A 3-STATE MECHANISM IN H2O AND D2O, Y GOTO,Y HAGIHARA,D HAMADA,M HOSHINO,NISHII, I, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 32, No. 44, p. 11878-11885, 1993/11
  • INTERMEDIATE CONFORMATIONAL STATES OF APOCYTOCHROME-C, D HAMADA,M HOSHINO,M KATAOKA,AL FINK,Y GOTO, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 32, No. 39, p. 10351-10358, 1993/10
  • CHARACTERIZATION OF THE STABLE, ACID-INDUCED, MOLTEN GLOBULE-LIKE STATE OF STAPHYLOCOCCAL NUCLEASE, AL FINK,LJ CALCIANO,Y GOTO,M NISHIMURA,SA SWEDBERG, PROTEIN SCIENCE, CAMBRIDGE UNIV PRESS, Vol. 2, No. 7, p. 1155-1160, 1993/07
  • GUANIDINE HYDROCHLORIDE-INDUCED FOLDING OF PROTEINS, Y HAGIHARA,S AIMOTO,AL FINK,Y GOTO, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD, Vol. 231, No. 2, p. 180-184, 1993/05
  • MOLTEN GLOBULE OF CYTOCHROME-C STUDIED BY SMALL-ANGLE X-RAY-SCATTERING, M KATAOKA,Y HAGIHARA,K MIHARA,Y GOTO, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD, Vol. 229, No. 3, p. 591-596, 1993/02
  • Molecular conformation of porcine amelogenin in solution: Three folding units at the N-terminal, central, and C-terminal regions, Yuji Goto,Eiichi Kogure,Toshio Takagi,Saburo Aimoto,Takaaki Aobo, Journal of Biochemistry, Oxford University Press, Vol. 113, No. 1, p. 55-60, 1993
  • FUSION OF PHOSPHOLIPID-VESICLES INDUCED BY AN AMPHIPHILIC MODEL PEPTIDE - CLOSE CORRELATION BETWEEN FUSOGENICITY AND HYDROPHOBICITY OF THE PEPTIDE IN AN ALPHA-HELIX, T YOSHIMURA,Y GOTO,S AIMOTO, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 31, No. 26, p. 6119-6126, 1992/07
  • Charge Repulsion in the Conformational Stability of Melittin, Yoshihisa Hagihara,Mikio Kataoka,Yuji Goto,Saburo Aimoto, Biochemistry, Vol. 31, No. 47, p. 11908-11914, 1992/02/01
  • MECHANISM OF THE CONFORMATIONAL TRANSITION OF MELITTIN, Y GOTO,Y HAGIHARA, BIOCHEMISTRY, AMER CHEMICAL SOC, Vol. 31, No. 3, p. 732-738, 1992/01
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  • ATP-INDUCED CONFORMATIONAL TRANSITION OF DENATURED PROTEINS, Y GOTO,N OKAMURA,S AIMOTO, JOURNAL OF BIOCHEMISTRY, JAPAN BIOCHEMICAL SOC, Vol. 109, No. 5, p. 746-750, 1991/05
  • ANION AND PH-DEPENDENT CONFORMATIONAL TRANSITION OF AN AMPHIPHILIC POLYPEPTIDE, Y GOTO,S AIMOTO, JOURNAL OF MOLECULAR BIOLOGY, ACADEMIC PRESS LTD, Vol. 218, No. 2, p. 387-396, 1991/03
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Misc.

  • Multi-step conformational changes via intermediate states induced by cross-seeding of human and bovine insulin amyloid fibrils, 柚佳祐,山本直樹,野地真広,宗正智,後藤祐児,岩崎哲史,岩崎哲史,鍔木基成,茶谷絵理, 日本生化学会大会(Web), Vol. 93rd, 2020
  • タンパク質に対する圧力研究の新展開-基本熱力学から,分子構造に基づく理解,アミロイド線維まで, 櫻井一正,茶谷絵理,後藤祐児, 化学, Vol. 75, No. 11, 2020
  • 分子夾雑のタンパク質物理化学:タンパク質凝集研究の進展とこれから, CHATANI ERI,後藤 祐児, 現代化学, 東京化学同人, No. 578, p. 26-30, 2019/05
  • β<sub>2</sub>-microglobulinアミロイド線維のex vivo立体構造解析, 田巻初,宗正智,川本晃大,後藤祐児,藤原敏道,松木陽, Abstracts. Annual Meeting of the NMR Society of Japan, Vol. 58th (CD-ROM), 2019
  • 固体NMRによるβ<sub>2</sub>-microglobulinアミロイド線維の立体構造解析, 田巻初,宗正智,後藤祐児,藤原敏道,松木陽, Abstracts. Annual Meeting of the NMR Society of Japan, Vol. 57th, 2018
  • The structure analysis for alpha-synuclein and Lewy bodies of Parkinson's disease patients with synchrotron radiation, Katsuya Araki,Naoto Yagi,Rie Nakatani,Hideki Hayakawa,Kousuke Baba,Yuji Goto,Hideki Mochizuki, MOVEMENT DISORDERS, WILEY-BLACKWELL, Vol. 31, p. S66-S66, 2016/03
  • X-ray Observation of Novel Nucleation Factor in Protein Supersaturated Solution, Yufuku Matsushita,Hiroshi Sekiguchi,Noboru Ohta,Keigo Ikezaki,Yuji Goto,Yuji C. Sasaki, BIOPHYSICAL JOURNAL, CELL PRESS, Vol. 110, No. 3, p. 223A-223A, 2016/02
  • 1C12 Study on nucleation reaction of amyloid β peptide induced by ultrasonic cavitation, NAKAJIMA Kichitaro,OGI Hirotsugu,HIRAO Masahiko,GOTO Yuji, The Japan Society of Mechanical Engineers, Vol. 2016, No. 28, p. "1C12-1"-"1C12-5", 2016/01/09
  • 2P2-1 Monitoring of dissociation dynamics of Alzheimer-disease aggregates by poly-phenol with TIRFM-QCM system, Yamada Kotaro,Nakajima Kichitaro,Nishioka Daisuke,Ogi Hirotsugu,Goto Yuji,Hirao Masahiko, Proceedings of Symposium on Ultrasonic Electronics, Steering committee of symposium on ultrasonic electronics, Vol. 36, p. "2P2-1-1"-"2P2-1-2", 2015/11/05
  • 2P5-6 Study on aggregation reactions of amyloid β peptides induced by ultrasonic irradiation and stirring agitation, Nakajima Kichitaro,Ogi Hirotsugu,Hirao Masahiko,Goto Yuji, Proceedings of Symposium on Ultrasonic Electronics, Steering committee of symposium on ultrasonic electronics, Vol. 36, p. "2P5-6-1"-"2P5-6-2", 2015/11/05
  • Time-resolved X-ray Observations of Nano-scale Protein Assembly Networks, Yufuku Matsushita,Hiroshi Sekiguchi,Noboru Ohta,Keigo Ikezaki,Yuji Goto,Yuji Sasaki, PROTEIN SCIENCE, WILEY-BLACKWELL, Vol. 24, p. 154-155, 2015/10
  • Ultrasonication-forced amyloid fibrillation of proteins, Masatomo So,Yuichi Yoshimura,Yuji Goto, Advances in Organic Crystal Chemistry: Comprehensive Reviews 2015, p. 15-29, 2015/08/06
  • Observation of High Accuracy Rotational Dynamics and Dissolution Characteristics of Gold Nanocrystals on Sodium Acetate Supersaturated Solution, MATSUSHITA Yufuku,SEKIGUCHI Hiroshi,ICHIYANAGI Kouhei,IKEZAKI Keigo,GOTO Yuji,SASAKI Yuji C, J. Surf. Sci. Soc. Jpn., The Surface Science Society of Japan, Vol. 36, No. 10, p. 539-542, 2015
  • Microsecond X-Ray Dynamics Observation of Nano Supersaturated Protein's Network, Yufuku Matsushita,Hiroshi Sekiguchi,Noboru Ohta,Keigo Ikezaki,Yuji Goto,Yuji C. Sasaki, BIOPHYSICAL JOURNAL, CELL PRESS, Vol. 108, No. 2, p. 220A-220A, 2015/01
  • 3J2-4 Frequency dependence of ultrasonically accelerated fibrillation phenomenon of Alzheimer-disease peptides(Biomedical Ultrasound II), Adachi Kanta,Nakajima Kichitaro,Noi Kentaro,Yagi Hisashi,Goto Yuji,Ogi Hirotsugu,Hirao Masahiko, Proceedings of Symposium on Ultrasonic Electronics, Steering committee of symposium on ultrasonic electronics, Vol. 35, p. 389-390, 2014/12/03
  • 1J4-1 Study on Nucleation-Fibrillation Dynamics of Aβ Peptides by TIRFM-QCM(Measurement techniques), Hamada Hiroki,Noi Kentaro,Ogi Hirotsugu,Yagi Hisashi,Goto Yuji,Hirao Masahiko, Proceedings of Symposium on Ultrasonic Electronics, Steering committee of symposium on ultrasonic electronics, Vol. 35, p. 177-178, 2014/12/03
  • 2E3-2 Study on ultrasonically accelerated aggregation phenomenon of Aβ peptides based on cavitation-bubble dynamics(High Power Ultrasound, Sonochemistry), Nakajima Kichitaro,Adachi Kanta,Noi Kentaro,Yagi Hisashi,Goto Yuji,Ogi Hirotsugu,Hirao Masahiko, Proceedings of Symposium on Ultrasonic Electronics, Steering committee of symposium on ultrasonic electronics, Vol. 35, p. 201-202, 2014/12/03
  • 超音波による蛋白質のアミロイド線維形成・結晶化の促進, 宗 正智,八木 寿梓,後藤 祐児, 日本生物物理学会、生物物理誌, 2014/07
  • ラクダ科動物由来シングルドメイン抗体(VHH抗体)の熱変性は化学修飾による, 赤澤陽子,高島瑞紀,LEE Young-Ho,池上貴久,後藤祐児,上垣浩一,萩原義久, 日本蛋白質科学会年会プログラム・要旨集, Vol. 14th, 2014
  • Function, structure and fibrillation of α-synuclein(PARK1/4), Vol. 247, No. 10, p. 993-998, 2013/12/07
  • 2P5-9 Effect of glycerol on ultrasonically induced aggregation phenomenon of amyloid β peptides(Poster Session), Nakajima Kichitaro,Noi Kentaro,Ogi Hirotsugu,Yagi Hisashi,Goto Yuji,Hirao Masahiko, Proceedings of Symposium on Ultrasonic Electronics, Steering committee of symposium on ultrasonic electronics, Vol. 34, p. 317-318, 2013/11/20
  • 1P2-13 Monitoring of Deposition Reaction of Aβ Peptides on Heterogenous Nuclei by TIRF-QCM(Poster Session), Hamada Hiroki,Noi Kentaro,Ogi Hirotsugu,Yagi Hisashi,Goto Yuji,Hirao Masahiko, Proceedings of Symposium on Ultrasonic Electronics, Steering committee of symposium on ultrasonic electronics, Vol. 34, p. 61-62, 2013/11/20
  • 超音波を用いた蛋白質凝集検出装置HANABIの開発, 八木寿梓,梅本彩香,北山寛貴,吉村優一,宗正智,後藤祐児, 日本生化学会大会(Web), (公社)日本生化学会, Vol. 86th, p. 2T06P-10(2P-094) (WEB ONLY)-10, 2013/09
  • 超音波によるタンパク質のアミロイド線維形成反応の促進, 宗正智,吉村優一,八木寿梓,後藤祐児, ケミカルエンジニヤリング 、 化学工業社, 2013/09
  • 固体NMRによるβ<sub>2</sub>ミクログロブリンのアミロイド線維構造解析, 宗正智,松木陽,江川文子,戸所泰人,佐伯美和子,櫻井一正,藤原敏道,後藤祐児, 日本蛋白質科学会年会プログラム・要旨集, Vol. 13th, 2013
  • ラクダ科動物由来のシングルドメイン抗体(VHH抗体)の熱耐性機構の検証, 赤澤陽子,高島瑞紀,李映昊,池上貴久,後藤祐児,上垣浩一,萩原義久, 日本蛋白質科学会年会プログラム・要旨集, Vol. 13th, 2013
  • フェレドキシンと亜硫酸還元酵素の電子伝達複合体の構造と分子間相互作用の解析(Structure of an electron transfer complex of ferredoxin and sulfite reductase and analysis of their molecular interactions), 金 宙妍,中山 雅登,李 映昊,池上 貴久,後藤 祐児,栗栖 源嗣,長谷 俊治, 日本生化学会大会プログラム・講演要旨集, (公社)日本生化学会, Vol. 85回, p. 2T07-03, 2012/12
  • 2P4-8 Relationship between ultrasonically induced aggregation phenomenon of amyloid β peptides and pressure of ultrasonic harmonics(Poster Session), Uesugi Kentaro,Ogi Hirotsugu,Yagi Hisashi,So Masatomo,Goto Yuji,Hirao Masahiko, Proceedings of Symposium on Ultrasonic Electronics, Steering committee of symposium on ultrasonic electronics, Vol. 33, p. 223-224, 2012/11/13
  • 1I-1 Ultrasonication-triggered Amyloid Fibrillation of Proteins(Invited Talk 1), Goto Yuji, Proceedings of Symposium on Ultrasonic Electronics, Steering committee of symposium on ultrasonic electronics, Vol. 33, p. 17-18, 2012/11/13
  • 1J2-1 Flow-Injection Wireless-Electrodeless QCM System Combined with Total Internal Reflection Fluorescence Microscopy(Measurement Techniques, Imaging, Nondestructive Evaluation), Fukushima Masahiko,Uesugi Kentaro,Ogi Hirotsugu,Yagi Hisashi,Goto Yuji,Hirao Masahiko, Proceedings of Symposium on Ultrasonic Electronics, Steering committee of symposium on ultrasonic electronics, Vol. 33, p. 1-2, 2012/11/13
  • Fibrillogenic propensity of the GroEL apical domain, Jin Chen,Hisashi Yagi,Pietro Sormanni,Michele Vendruscolo,Koki Makabe,Takashi Nakamura,Yuji Goto,Kunihiro Kuwajima, PROTEIN SCIENCE, WILEY-BLACKWELL, Vol. 21, p. 102-102, 2012/08
  • 抗体及び抗体フラグメント(Fab,scFv,VHH)の耐熱性の検証, 萩原義久,赤澤陽子,高島瑞紀,LEE Young-ho,池上貴久,後藤祐児,上垣浩一, 日本分子生物学会年会プログラム・要旨集(Web), Vol. 35th, 2012
  • A14 Ultrasonication-Dependent Acceleration of Amyloid Fibril Formation, So Masatomo,Yoshimura Yuichi,Yagi Hisashi,Sakurai Kazumasa,Goto Yuji,Ogi Hirotsugu,Naiki Hironobu, Proceedings of the Annual Meeting of the Japan Society of Sonochemistry, Japan Society of Sonochemistry, Vol. 21, No. 0, p. 85-86, 2012
  • Stability of prophenol oxidase with alcohol in Drosophila melanogaster, Eri Sato,Kotomi Mita,Hisashi Yagi,Yuji Goto,Nobuhiko Asada, GENES & GENETIC SYSTEMS, GENETICS SOC JAPAN, Vol. 86, No. 6, p. 417-417, 2011/12
  • 2Pb4-13 Acoustic-Pressure Dependence of Ultrasonically-Induced Aggregation Behavior of Amyloid β Peptides(Poster Session), Uesugi Kentaro,Ogi Hirotsugu,Yagi Hisashi,So Masatomo,Goto Yuji,Hirao Masahiko, Proceedings of Symposium on Ultrasonic Electronics, Steering committee of symposium on ultrasonic electronics, Vol. 32, p. 257-258, 2011/11/08
  • 21pRC-5 Unifying Principle of Protein Folding and Amyloid Fibril Formation Institute for Protein Research, Goto Yuji, Meeting abstracts of the Physical Society of Japan, The Physical Society of Japan (JPS), Vol. 66, No. 2, p. 311-311, 2011/08/24
  • 21pRC-5 Unifying Principle of Protein Folding and Amyloid Fibril Formation, Goto Yuji, Meeting abstracts of the Physical Society of Japan, The Physical Society of Japan (JPS), Vol. 66, No. 2, p. 905-905, 2011/08/24
  • Mechanism of the formation of β2-microglobulin amyloid fibrils, Vol. 55, No. 1, p. 19-26, 2011/01
  • アミロイドーシス発症の分子機構解明 (特集 老化と加齢性疾患を科学する), 八木 寿梓,後藤 祐児, メディカルバイオ, オーム社, Vol. 7, No. 5, p. 30-35, 2010/09
  • β2ミクログロブリンのフォールディング機構と天然状態におけるプロリン異性化反応の解析, 向山厚,中村敬,真壁幸樹,真壁幸樹,槇亙介,後藤祐児,桑島邦博,桑島邦博, 日本蛋白質科学会年会プログラム・要旨集, Vol. 10th, 2010
  • 29pVC-2 Folding and amyloid fibril formation of proteins, Goto Yuji, Meeting abstracts of the Physical Society of Japan, The Physical Society of Japan (JPS), Vol. 64, No. 1, p. 382-382, 2009/03/03
  • Amyloid Fibril Formation and Protein Science, GOTO Yuji, Vol. 58, No. 2, p. 92-96, 2009/02/01
  • New world of amyloid science, Young-Ho Lee,Daisaku Ozawa,Yuji Goto, Seikagaku, Vol. 81, No. 8, p. 677-687, 2009
  • Acid denaturation and anion-induced folding of globular proteins: Multitude of equilibrium partially folded intermediates, Vladimir N. Uversky,Yuji Goto, Current Protein and Peptide Science, Vol. 10, No. 5, p. 447-455, 2009
  • アミロイド線維の全反射蛍光顕微鏡による観察法, 伴匡人,八木寿梓,後藤祐児, 蛋白質科学会アーカイブ 、 蛋白質科学会, 2008/08
  • アミロイド構造生物学の台頭, 八木寿梓,櫻井一正,後藤祐児, 蛋白質・核酸・酵素 、 共立出版, 2007/10
  • Recent applications of high pressure to the studies of amyloid fibrils, Eri Chatani,Yuji Goto, Review of High Pressure Science and Technology/Koatsuryoku No Kagaku To Gijutsu, Japan Society of High Pressure Science and Technology, Vol. 17, No. 1, p. 42-49, 2007
  • アミロイドーシス発症の分子機構解明を目指して:現状と展望,夢, 後藤 祐児,桑田 一夫,関島 良樹,田中 元雅,内木 宏延,永井 義隆,松崎 勝巳,樋口 京一, 細胞工学, Vol. 26, No. 2, p. 181-185, 2007
  • Calorimetric Analysis of the Formation and the Thermal Response ofβ2 Microglobulin Amyloid Fibril, SASAHARA Kenji,GOTO Yuji, Calorimetry and thermal analysis., Vol. 33, No. 2, p. 83-88, 2006/03/31
  • Direct observation of amyloid growth monitored by total internal reflection fluorescence microscopy, Methods Enzymol., Vol. 413, 91-102, 2006
  • Direct observation of amyloid growth monitored by total internal reflection fluorescence microscopy, Tadato Ban,Yuji Goto, AMYLOID, PRIONS, AND OTHER PROTEIN AGGREGATES, PT C, ELSEVIER ACADEMIC PRESS INC, Vol. 413, p. 91-102, 2006
  • 透析アミロイドーシス 基礎研究から治療戦略Update β2-ミクログロブリンアミロイド線維・沈着の分子機構, 山本 卓,長谷川 一浩,下條 文武,内木 宏延,風間 順一郎,丸山 弘樹,成田 一衛,山口 格,後藤 祐児, 日本透析医学会雑誌, (一社)日本透析医学会, Vol. 38, No. Suppl.1, p. 601-601, 2005/05
  • in vitroフォールディング (特集 階層別にみるタンパク質のフォールディングと品質管理:in vitroのから細胞・個体レベルまで), 櫻井 一正,後藤 祐児, 細胞工学, 秀潤社, Vol. 23, No. 12, p. 1364-1369, 2004/12
  • タンパク質フォールディングの昼と夜, 後藤 祐児,高橋 聡, 現代化学, 東京化学同人, No. 402, p. 26-33, 2004/09
  • Conformational stability of amyloid fibril: Nanoscale needle, 後藤祐児,伴匡人,星野大, 蛋白質 核酸 酵素, Vol. 49, No. 7, p. 1091-1095, 2004/05/10
  • (総説)アミロイド線維の構造安定性-ナノスケールの針, 蛋白質核酸酵素, 2004
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  • アミロイド線維の構造安定化機構-ナノスケールの針, 化学, 2004
  • in vitroフォールディング, 細胞工学, Vol. 23, 12, 1364-1369., 2004
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  • タンパク質凝集による病気:狂牛病もアルツハイマーも・・・, 後藤 祐児, パリティ, 丸善, Vol. 18, No. 1, p. 49-51, 2003
  • 蛋白質のフォールディングとアミロイド線維形成:蛋白質、昼の顔と夜の顔 後藤祐児, 実験医学, Vol. 21, No. 7, p. 898-902, 2003
  • 蛋白質凝集による病気:アルツハイマーも・・・後藤祐児, パリティ, Vol. 18, No. 1, p. 49-51, 2003
  • 24pYC-3 To understand the molecular basis of bovine spongiform encephalopathy, Goto Y., Meeting abstracts of the Physical Society of Japan, The Physical Society of Japan (JPS), Vol. 57, No. 1, p. 312-312, 2002/03/01
  • タンパク質の低温変性, バイオサイエンスとインダストリー, Vol. 60(4), 235-238/,, 2002
  • β2 ミクログロリンのアミロイド線維形成(共著), 蛋白質核酸酵素, Vol. 47(6), 663-669/,, 2002
  • 蛋白質フォールディングの諸問題(共著), 蛋白質核酸酵素, Vol. 47(6), 653-656/,, 2002
  • β-ラクトグロブリンの低温変性状態の構造 (新世紀における蛋白質科学の進展) -- (第2部 蛋白質の構造・物性・進化), 後藤 祐児,加藤 秀典,星野 大, 蛋白質核酸酵素, 共立出版, Vol. 46, No. 11, p. 1423,1527-1534, 2001/08
  • (訳本)タンパク質フォールディングのキネティクス、Bengt N(]E88D8[)lting著後藤祐児訳, シュプリンガーフェアラーク東京, 2000
  • Three Dimensional Structure of Sushi Domains, GOTO Yuji,HAGIHARA Yoshihisa, Vol. 10, No. 6, p. 457-462, 1999/12/01
  • 蛋白質のフォールディング反応の1分子測定 (シリーズ 蛋白質・核酸・酵素の1分子測定と操作法), 後藤 祐児, 蛋白質核酸酵素, 共立出版, Vol. 44, No. 16, p. 2614-2616, 1999/12
  • α→β transition and structural fluctuation in β lactoglobulin., Kuwata K.,Hoshino M.,Goto Y.,Era S.,Batt C.A., Biophysics, The Biophysical Society of Japan General Incorporated Association, Vol. 38, No. 2, 1998/09/07
  • The folding intermediate state of β-lactoglobulin., Hoshino M.,Forge V.,Kuwata K.,Batt C.A.,Goto Y., Biophysics, The Biophysical Society of Japan General Incorporated Association, Vol. 38, No. 2, 1998/09/07
  • Single molecular measurement of protein of protein folding : Is it possible?, Goto Y., Biophysics, The Biophysical Society of Japan General Incorporated Association, Vol. 38, No. 2, 1998/09/07
  • Molecular Mechanism of Helix Induction by Amphiphilic Alcohols, Hong D.P.,Goto Y.,Kuboi R., Biophysics, The Biophysical Society of Japan General Incorporated Association, Vol. 38, No. 2, 1998/09/07
  • Allosteric control of an antibody-peptide interaction using a conformational change of the peptide, KATAKURA Y.,MIYAZAKI T.,OMASA T.,GOTO Y.,SUGA K., Biophysics, The Biophysical Society of Japan General Incorporated Association, Vol. 37, 1997/10
  • Folding of beta-lactoglobulin and interaction with GroE, HOSHINO M.,HIROTA N.,KUWATA K.,KAWATA Y.,BATT Carl A.,GOTO Y., Biophysics, The Biophysical Society of Japan General Incorporated Association, Vol. 37, 1997/10
  • NMR structure and dynamics of β lactoblobulin, KUWATA K.,HOSHINO M.,GOTO Y.,BATT Carl. A.,ERA S., Biophysics, The Biophysical Society of Japan General Incorporated Association, Vol. 37, 1997/10
  • Toward the understanding of the 3 effects of alcohol on proteins, HIROTA N.,KAWAKAMI T.,AIMOTO S.,GOTO Y., Biophysics, The Biophysical Society of Japan General Incorporated Association, Vol. 37, 1997/10
  • 大腸菌GroELの基質蛋白質認識機構, 後藤 祐児,星野 大, 日本分子生物学会年会プログラム・講演要旨集, Vol. 19, p. 25-25, 1996/08
  • 分子シャペロンは何を認識するのか?, 星野 大,河田 康志,溝端 知宏,永井 純,後藤 祐児, 日本分子生物学会年会プログラム・講演要旨集, Vol. 19, p. 235-235, 1996/08/01
  • Structural features recognized by the molecular chaperone, GroE, HOSHINO Masaru,GOTO Yuji, Bioscience & industry, Vol. 53, No. 12, p. 36-38, 1995/12/01
  • 質量分析法を用いた蛋白質の高次構造の研究(共著), 蛋白質核酸酵素, Vol. 40, p. 534-544, 1994
  • 蛋白質の立体構造形成反応-階層的機構と非階層的機構(単著), 後藤 祐児, 化学と生物, 学会出版センタ-, Vol. 32, No. 10, p. 681-687, 1994
  • Study of Protein Conformation by Mass Spectrometry, Protein, Nucleic Acid and Enzyme, Vol. 40, p. 534-544, 1994
  • Mechanism of Protein Folding-Hierarchical Mechanism and Nonhierarchical Mechanism., Chemistry and Biology, Vol. 32, p. 681-687, 1994
  • (総説)タンパク質の立体構造形成反応-モルテン・グロビュール状態の構造と安定性-, 後藤 祐児, 生化学, 日本生化学会, Vol. 65,321-337/,, No. 5, p. p321-337, 1993
  • Protein Foldin-Conformation and Stability of the Molten Globule State-, Vol. 65,321-337/,, 1993
  • 蛋白質の変性状態, 後藤 祐児, 蛋白質核酸酵素, 共立出版, Vol. 37, No. 8, p. p1442-1444, 1992/06
  • 蛋白質のジスルフィド結合形成反応と立体構造形成反応--クレイトンの提案した機構の危機, 後藤 祐児, 蛋白質核酸酵素, 共立出版, Vol. 37, No. 5, p. p880-885, 1992/04
  • モルテン・グロビュールをめぐって(共著), 蛋白質 核酸 酵素, Vol. 37, No. 4, p. 772-780, 1992
  • What is "Molten Globule"? : Questions and Answers, Protein, Nucleic Acid and Enzyme, Vol. 37, No. 4, p. 772-780, 1992
  • Molten Globule State of Globular Proteins, GOTO Yuji, Seibutsu Butsuri, The Biophysical Society of Japan General Incorporated Association, Vol. 31, No. 4, p. 122-127, 1991
  • Molten Globule State of Globular Proteins, Biphysics, Vol. 31, No. 4, p. 122-127, 1991
  • 硫安による変性蛋白質の巻戻りと結晶化, 後藤 祐児, 蛋白質核酸酵素, 共立出版, Vol. 34, No. 4, p. p365-367, 1989/04
  • 蛋白質の立体構造形成反応-免疫グロブリンのドメインの変性と再生, 後藤 祐児, 蛋白質 核酸 酵素, 共立出版, Vol. 33, No. 6, p. 1083-1097, 1988
  • Folding Process of Proteins-Unfolding and Refolding of the immunoglibulin Fragments, Protein, Nucleic Acid and Enzyme, Vol. 33, No. 6, p. 1083-1097, 1988
  • Unfolding and refolding of the constant fragment of the immunoglobulin light chain containing an intramolecular mercury bridge., GOTO Yuji,HAMAGUCHI Kozo, J Biochem (Tokyo), The Japanese Biochemical Society, Vol. 99, No. 5, p. 1501-1511, 1986
  • プロリン残基のcis-trans異性とタンパク質の構造形成 (1981年の化学), 後藤 祐児, 化学, 化学同人, Vol. 37, No. 1, p. p89-91, 1982/01

Publications

  • タンパク質科学, 化学同人, 2005
  • Protein Science, KAGAKUDOJIN, 2005
  • Molecular chaperones in the life cycle of proteins : Structure, function, and mode of action. (共著), Marcel Dekker, 1997
  • (訳本)タンパク質のフォールディング原理・機構・応用(共著), シュプリンガー・フェアラーク東京, 1995
  • Mechanism of protein folding, 1995
  • 蛋白質はどのようにしてできるか?(単著), 生物物理別冊「蛋白質-この絶妙なる設計物」, 1994
  • How protein folds?, Protein-Sophisticated Architecuture, 1994

Works

  • タンパク質の構造異常性の解析・診断システムの構築, 2004 -

Awards

  • 日本生化学会奨励賞, 1992

Committee Memberships

  • 生物物理学会, 委員, 2003 -
  • 日本蛋白質科学会, 理事, -
  • 生化学会, 評議員, -