Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence* 210 T Ban, D Hamada, K Hasegawa, H Naiki, Y Goto Journal of Biological Chemistry 278 (19), 16462-16465, 2003 | 442 | 2003 |
Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein D Hamada, S Segawa, Y Goto Nature structural biology 3 (10), 868-873, 1996 | 323 | 1996 |
A kinetic study of β‐lactoglobulin amyloid fibril formation promoted by urea D Hamada, CM Dobson Protein Science 11 (10), 2417-2426, 2002 | 312 | 2002 |
Direct observation of Aβ amyloid fibril growth and inhibition T Ban, M Hoshino, S Takahashi, D Hamada, K Hasegawa, H Naiki, ... Journal of molecular biology 344 (3), 757-767, 2004 | 277 | 2004 |
High helical propensity of the peptide fragments derived from β-lactoglobulin, a predominantly β-sheet protein D Hamada, Y Kuroda, T Tanaka, Y Goto Journal of molecular biology 254 (4), 737-746, 1995 | 221 | 1995 |
The equilibrium intermediate of β-lactoglobulin with non-native α-helical structure D Hamada, Y Goto Journal of molecular biology 269 (4), 479-487, 1997 | 158 | 1997 |
Acid-induced unfolding and refolding transitions of cytochrome c: A three-state mechanism in water and deuterium oxide Y Goto, Y Hagihara, D Hamada, M Hoshino, I Nishii Biochemistry 32 (44), 11878-11885, 1993 | 153 | 1993 |
Molecular dissection of IZUMO1, a sperm protein essential for sperm-egg fusion N Inoue, D Hamada, H Kamikubo, K Hirata, M Kataoka, M Yamamoto, ... Development 140 (15), 3221-3229, 2013 | 135 | 2013 |
Engineering amyloidogenicity towards the development of nanofibrillar materials D Hamada, I Yanagihara, K Tsumoto Trends in biotechnology 22 (2), 93-97, 2004 | 133 | 2004 |
Acceleration of the folding of acylphosphatase by stabilization of local secondary structure F Chiti, N Taddei, P Webster, D Hamada, T Fiaschi, G Ramponi, ... nature structural biology 6 (4), 380-387, 1999 | 123 | 1999 |
Intermediate conformational states of apocytochrome c D Hamada, M Hoshino, M Kataoka, AL Fink, Y Goto Biochemistry 32 (39), 10351-10358, 1993 | 113 | 1993 |
N-terminal phosphorylation of HP1α promotes its chromatin binding K Hiragami-Hamada, K Shinmyozu, D Hamada, Y Tatsu, K Uegaki, ... Molecular and cellular biology 31 (6), 1186-1200, 2011 | 110 | 2011 |
Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry. D Hamada, S Kidokoro, H Fukada, K Takahashi, Y Goto Proceedings of the National Academy of Sciences 91 (22), 10325-10329, 1994 | 109 | 1994 |
Role of Heme Axial Ligands in the Conformational Stability of the Native and Molten Globule States of Horse Cytochromec D Hamada, Y Kuroda, M Kataoka, S Aimoto, T Yoshimura, Y Goto Journal of molecular biology 256 (1), 172-186, 1996 | 107 | 1996 |
On risk and plant-based biopharmaceuticals RKD Peterson, CJ Arntzen TRENDS in Biotechnology 22 (2), 64-66, 2004 | 102 | 2004 |
Competition between folding, native-state dimerisation and amyloid aggregation in β-lactoglobulin D Hamada, T Tanaka, GG Tartaglia, A Pawar, M Vendruscolo, ... Journal of molecular biology 386 (3), 878-890, 2009 | 97 | 2009 |
Structure and functional characterization of Vibrio parahaemolyticus thermostable direct hemolysin I Yanagihara, K Nakahira, T Yamane, S Kaieda, K Mayanagi, D Hamada, ... Journal of biological chemistry 285 (21), 16267-16274, 2010 | 96 | 2010 |
High helicity of peptide fragments corresponding to β-strand regions of β-lactoglobulin observed by 2D-NMR spectroscopy Y Kuroda, D Hamada, T Tanaka, Y Goto Folding and Design 1 (4), 255-263, 1996 | 95 | 1996 |
Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol D Hamada, F Chiti, JI Guijarro, M Kataoka, N Taddei, CM Dobson Nature structural biology 7 (1), 58-61, 2000 | 89 | 2000 |
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 416 (1), 72-76, 1997 | 73 | 1997 |