D. Hamada

发表

Direct Observation of Aβ Amyloid Fibril Growth and Inhibition

Satoshi Takahashi, M. Hoshino, T. Ban, 2004 .

Conserved signature proposed for folding in the lipocalin superfamily

Keith Brew, Lesley H Greene, K. Brew, 2003, FEBS letters.

Expression and purification of recombinant human annexin A2 in Pichia pastoris and utility of expression product for detecting annexin A2 antibody.

E. Fukusaki, D. Hamada, Fumihiko Namba, 2006, Journal of bioscience and bioengineering.

Probing dynamic fibril-formation by an integrated microscopic approach

P. Cao, D. Hamada, Y. Kong, 2012 .

Binding of islet amyloid polypeptide to supported lipid bilayers and amyloid aggregation at the membranes.

D. Hamada, K. Morigaki, K. Sasahara, 2012, Biochemistry.

Structure and Functional Characterization of Vibrio parahaemolyticus Thermostable Direct Hemolysin*

T. Ikegami, T. Yamane, M. Ikeguchi, 2010, The Journal of Biological Chemistry.

Tetrameric structure of thermostable direct hemolysin from vibrio parahaemolyticus revealed by ultracentrifugation, small-angle X-ray scattering and electron microscopy.

T. Honda, D. Hamada, I. Yanagihara, 2007, Journal of molecular biology.

Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein

D. Hamada, Y. Goto, S. Segawa, 1996, Nature Structural Biology.

Cutting Edge: Class II–like Structural Features and Strong Receptor Binding of the Nonclassical HLA-G2 Isoform Homodimer

M. Kikkawa, D. Hamada, K. Mio, 2017, The Journal of Immunology.

Nonclassical HLA-G 2 Isoform Homodimer Features and Strong Receptor Binding of the like Structural − Cutting Edge : Class II

M. Kuroki, D. Hamada, K. Mio, 2017 .

Molecular basis of actin reorganization promoted by binding of enterohaemorrhagic Escherichia coli EspB to α‐catenin

I. Sakata, D. Hamada, I. Yanagihara, 2008, The FEBS journal.

High helicity of peptide fragments corresponding to β-strand regions of β-lactoglobulin observed by 2D-NMR spectroscopy

D. Hamada, Y. Goto, Toshiki Tanaka, 1996 .

Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry.

H. Fukada, K. Takahashi, S. Kidokoro, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Effect of lipid type on the binding of lipid vesicles to islet amyloid polypeptide amyloid fibrils.

D. Hall, D. Hamada, K. Sasahara, 2010, Biochemistry.

Folding intermediate of β-lactoglobulin with non-native α-helical conformation

D. Hamada, Y. Goto, S. Segawa, 2002 .

Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c.

M. Kataoka, T. Yoshimura, D. Hamada, 1996, Journal of molecular biology.

Direct observation of Abeta amyloid fibril growth and inhibition.

Satoshi Takahashi, M. Hoshino, T. Ban, 2004, Journal of molecular biology.

Amyloid fibril formation and chaperone-like activity of peptides from alphaA-crystallin.

D. Hamada, S. Kunugi, N. Tanaka, 2008, Biochemistry.

Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol

C. Dobson, F. Chiti, N. Taddei, 2000, Nature Structural Biology.

Acceleration of the folding of acylphosphatase by stabilization of local secondary structure

C. Dobson, F. Chiti, N. Taddei, 1999, Nature Structural Biology.

High helical propensity of the peptide fragments derived from beta-lactoglobulin, a predominantly beta-sheet protein.

T. Tanaka, D. Hamada, Y. Goto, 1995, Journal of molecular biology.

Salt-induced formation of the molten globule state of apomyoglobin studied by isothermal titration calorimetry

H. Fukada, D. Hamada, Y. Goto, 1995 .

The equilibrium intermediate of beta-lactoglobulin with non-native alpha-helical structure.

D. Hamada, Y. Goto, Y Goto, 1997, Journal of molecular biology.

Effect of Ca2+ on the microtubule‐severing enzyme p60‐katanin. Insight into the substrate‐dependent activation mechanism

M. Shirakawa, T. Ikura, H. Hiroaki, 2012, The FEBS journal.

Insight into the substrate-dependent activation mechanism

M. Shirakawa, T. Ikura, H. Hiroaki, 2012 .

Molecular dissection of IZUMO1, a sperm protein essential for sperm-egg fusion

K. Hirata, M. Ikawa, M. Okabe, 2013, Development.

N-Terminal Phosphorylation of HP1α Promotes Its Chromatin Binding

S. Fujiwara, J. Nakayama, D. Hamada, 2011, Molecular and Cellular Biology.

Direct Observation of Amyloid Fibril Growth Monitored by Thioflavin T Fluorescence* 210

T. Ban, D. Hamada, K. Hasegawa, 2003, The Journal of Biological Chemistry.

Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein.

D. Hamada, Y. Goto, S. Segawa, 1996, Nature structural biology.

A kinetic study of β‐lactoglobulin amyloid fibril formation promoted by urea

C. Dobson, D. Hamada, 2002 .

Engineering amyloidogenicity towards the development of nanofibrillar materials.

K. Tsumoto, D. Hamada, I. Yanagihara, 2004, Trends in biotechnology.

Thermostable direct hemolysin of Vibrio parahaemolyticus is a bacterial reversible amyloid toxin.

E. Fukusaki, S. Fujiwara, T. Imanaka, 2005, Biochemistry.

Nanoscale Dynamics of Protein Assembly Networks in Supersaturated Solutions

H. Sekiguchi, Y. Sasaki, D. Hamada, 2017, Scientific Reports.

Spatial Overlap of Claudin- and Phosphatidylinositol Phosphate-Binding Sites on the First PDZ Domain of Zonula Occludens 1 Studied by NMR

T. Ikegami, H. Hiroaki, D. Hamada, 2018, Molecules.

Decreased amyloidogenicity caused by mutational modulation of surface properties of the immunoglobulin light chain BRE variable domain.

H. Kamikubo, M. Kataoka, S. Unzai, 2014, Biochemistry.

Pharmacological induction of heat shock proteins ameliorates toxicity of mutant PKCγ in spinocerebellar ataxia type 14

N. Saito, D. Hamada, T. Seki, 2018, The Journal of Biological Chemistry.

Identification and characterization of PKCγ, a kinase associated with SCA14, as an amyloidogenic protein.

M. Vendruscolo, H. Hirai, N. Saito, 2015, Human molecular genetics.

Chain-like conformation of heat-denatured ribonuclease A and cytochrome c as evidenced by solution X-ray scattering.

M. Kataoka, M. Hoshino, D. Hamada, 1998, Folding & design.

Residual structures in the unfolded state of starch-binding domain of glucoamylase revealed by near-UV circular dichroism and protein engineering techniques.

D. Hamada, A. Tanaka, M. Ikeguchi, 2016, Biochimica et biophysica acta.

Competition between folding, native-state dimerisation and amyloid aggregation in beta-lactoglobulin.

C. Dobson, A. Tamura, M. Vendruscolo, 2009, Journal of molecular biology.

MIT domain of Vps4 is a Ca2+-dependent phosphoinositide-binding domain.

M. Shirakawa, H. Hiroaki, D. Hamada, 2013, Journal of biochemistry.

A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea.

C. Dobson, D. Hamada, 2002, Protein science : a publication of the Protein Society.

Cytoskeleton‐modulating effectors of enteropathogenic and enterohemorrhagic Escherichia coli: a case for EspB as an intrinsically less‐ordered effector

I. Sakata, D. Hamada, I. Yanagihara, 2010, The FEBS journal.

Effect of an amyloidogenic sequence attached to yellow fluorescent protein

K. Tsumoto, K. Shiraki, D. Hamada, 2008, Proteins.

Cytoskeleton‐modulating effectors of enteropathogenic and enterohemorrhagic Escherichia coli

D. Hamada, 2010, The FEBS journal.

Structural Basis of α-Catenin Recognition by EspB from Enterohaemorrhagic E. coli Based on Hybrid Strategy Using Low-Resolution Structural and Protein Dissection

H. Kamikubo, M. Kataoka, I. Sakata, 2013, PloS one.

EspB from enterohaemorrhagic Escherichia coli is a natively partially folded protein

T. Ikegami, T. Honda, M. Hayashi, 2005, The FEBS journal.

Heat‐induced native dimerization prevents amyloid formation by variable domain from immunoglobulin light‐chain REI

H. Kamikubo, M. Kataoka, Tsutomu Nakamura, 2017, The FEBS journal.

Crystal Structure of Human Herpesvirus 6B Tegument Protein U14

Huamin Tang, Y. Mori, Z. Khanlari, 2016, PLoS pathogens.

Initial denaturing conditions influence the slow folding phase of acylphosphatase associated with proline isomerization

C. Dobson, F. Chiti, N. Taddei, 2000, Protein science : a publication of the Protein Society.

A pH‐dependent conformational change in EspA, a component of the Escherichia coli O157:H7 type III secretion system

T. Honda, M. Hayashi, Tomoaki Kato, 2005, The FEBS journal.

Decreased amyloidogenicity caused by mutational modulation of surface properties of the immunoglobulin light chain BRE variable domain.

H. Kamikubo, M. Kataoka, S. Unzai, 2014, Biochemistry.

Trifluoroethanol‐induced conformational transition of hen egg‐white lysozyme studied by small‐angle X‐ray scattering

M. Kataoka, M. Hoshino, D. Hamada, 1997, FEBS letters.

Acid-induced unfolding and refolding transitions of cytochrome c: a three-state mechanism in H2O and D2O.

I. Nishii, M. Hoshino, D. Hamada, 1993, Biochemistry.

Analysis of recombinant human saposin A expressed by Pichia pastoris.

K. Ozono, D. Hamada, K. Inui, 2004, Biochemical and biophysical research communications.