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濵田大三(Daizo Hamada)
濵田大三(Daizo Hamada)
BeCellBar, LLC
Verified email at becellbar.co.jp
Title
Cited by
Cited by
Year
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
4392003
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
3231996
A kinetic study of β‐lactoglobulin amyloid fibril formation promoted by urea
D Hamada, CM Dobson
Protein Science 11 (10), 2417-2426, 2002
3122002
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
2742004
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
2211995
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
1581997
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
1531993
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
1332013
Engineering amyloidogenicity towards the development of nanofibrillar materials
D Hamada, I Yanagihara, K Tsumoto
Trends in biotechnology 22 (2), 93-97, 2004
1332004
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
1231999
Intermediate conformational states of apocytochrome c
D Hamada, M Hoshino, M Kataoka, AL Fink, Y Goto
Biochemistry 32 (39), 10351-10358, 1993
1131993
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
1091994
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
1082011
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
1071996
On risk and plant-based biopharmaceuticals
RKD Peterson, CJ Arntzen
TRENDS in Biotechnology 22 (2), 64-66, 2004
1012004
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
972009
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
952010
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
951996
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
892000
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
731997
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Articles 1–20