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

Development (Cambridge), 2013-08, Vol.140 (15), p.3221-3229

2013

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

The Journal of immunology (1950), 2017-05, Vol.198 (9), p.3399-3403

2017

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

Biochimica et biophysica acta, 2016-10, Vol.1864 (10), p.1464-1472

2016

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Binding of Islet Amyloid Polypeptide to Supported Lipid Bilayers and Amyloid Aggregation at the Membranes

Biochemistry (Easton), 2012-09, Vol.51 (35), p.6908-6919

2012

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N-Terminal Phosphorylation of HP1α Promotes Its Chromatin Binding

Molecular and Cellular Biology, 2011-03, Vol.31 (6), p.1186-1200

2011

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Direct Observation of Amyloid Fibril Growth Monitored by Thioflavin T Fluorescence

The Journal of biological chemistry, 2003-05, Vol.278 (19), p.16462-16465

2003

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

Molecules (Basel, Switzerland), 2018-09, Vol.23 (10), p.2465

2018

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

The FEBS journal, 2017-09, Vol.284 (18), p.3114-3127

2017

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Effect of Lipid Type on the Binding of Lipid Vesicles to Islet Amyloid Polypeptide Amyloid Fibrils

Biochemistry (Easton), 2010-04, Vol.49 (14), p.3040-3048

2010

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Crystal Structure of Human Herpesvirus 6B Tegument Protein U14

PLoS pathogens, 2016-05, Vol.12 (5), p.e1005594-e1005594

2016

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Structure and Functional Characterization of Vibrio parahaemolyticus Thermostable Direct Hemolysin

The Journal of biological chemistry, 2010-05, Vol.285 (21), p.16267-16274

2010

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Decreased Amyloidogenicity Caused by Mutational Modulation of Surface Properties of the Immunoglobulin Light Chain BRE Variable Domain

Biochemistry (Easton), 2014-08, Vol.53 (31), p.5162-5173

2014

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

Journal of biochemistry (Tokyo), 2013-05, Vol.153 (5), p.473-481

2013

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Structural basis of α-catenin recognition by EspB from enterohaemorrhagic E. coli based on hybrid strategy using low-resolution structural and protein dissection

PloS one, 2013-08, Vol.8 (8), p.e71618-e71618

2013

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

The FEBS journal, 2010-06, Vol.277 (11), p.2409-2415

2010

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Effect of an amyloidogenic sequence attached to yellow fluorescent protein

Proteins, structure, function, and bioinformatics, 2008-08, Vol.72 (3), p.811-821

2008

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Tetrameric Structure of Thermostable Direct Hemolysin from Vibrio parahaemolyticus Revealed by Ultracentrifugation, Small-angle X-ray Scattering and Electron Microscopy

Journal of molecular biology, 2007-01, Vol.365 (1), p.187-195

2007

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2P049 平衡条件下において形成される二つの天然変性蛋白質融合蛋白質のフォールディング中間状態(01C. 蛋白質:物性,ポスター,第52回日本生物物理学会年会(2014年度))

生物物理, 2014/08/20, Vol.54(supplement1-2), pp.S203

2014

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2P049 Folding intermediates formed by the fusion protein of two intrisically disordered proteins under equilibrium condition(01C. Protein: Property,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))

Seibutsu Butsuri, 2014/08/20, Vol.54(supplement1-2), pp.S203

Hamada, Daizo

2014

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Thermostable Direct Hemolysin of Vibrio parahaemolyticus Is a Bacterial Reversible Amyloid Toxin

Biochemistry (Easton), 2005-07, Vol.44 (29), p.9825-9832

2005

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3SEA-05 Toward understanding the mechanism of cytotoxicity of amyloidogenic variable domain of immunoglobulin light chains(3SEA Roles of Membrane Interface in amyloidogenesis,Symposium)

Seibutsu Butsuri, 2013/09/13, Vol.53(supplement1-2), pp.S105

Hamada, Daizo

2013

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1PT159 STABILITY OF FOLDING INTERMEDIATE AFFECTS THE AMYLOIDOGENIC PROPENSITY OF IMMUNOGLOBULIN LIGHT CHAIN VARIABLE DOMAIN(The 50th Annual Meeting of the Biophysical Society of Japan)

Seibutsu Butsuri, 2012/08/15, Vol.52(supplement), pp.S96

2012

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EspB from enterohaemorrhagic Escherichia coli is a natively partially folded protein

The FEBS journal, 2005-02, Vol.272 (3), p.756-768

2005

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

Protein science, 2002-10, Vol.11 (10), p.2417-2426

2002

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Direct Observation of Aβ Amyloid Fibril Growth and Inhibition

Journal of molecular biology, 2004-11, Vol.344 (3), p.757-767

2004

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

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

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

Binding of Islet Amyloid Polypeptide to Supported Lipid Bilayers and Amyloid Aggregation at the Membranes

N-Terminal Phosphorylation of HP1α Promotes Its Chromatin Binding

Direct Observation of Amyloid Fibril Growth Monitored by Thioflavin T Fluorescence

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

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

Effect of Lipid Type on the Binding of Lipid Vesicles to Islet Amyloid Polypeptide Amyloid Fibrils

Crystal Structure of Human Herpesvirus 6B Tegument Protein U14

Structure and Functional Characterization of Vibrio parahaemolyticus Thermostable Direct Hemolysin

Decreased Amyloidogenicity Caused by Mutational Modulation of Surface Properties of the Immunoglobulin Light Chain BRE Variable Domain

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

Structural basis of α-catenin recognition by EspB from enterohaemorrhagic E. coli based on hybrid strategy using low-resolution structural and protein dissection

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

Effect of an amyloidogenic sequence attached to yellow fluorescent protein

Tetrameric Structure of Thermostable Direct Hemolysin from Vibrio parahaemolyticus Revealed by Ultracentrifugation, Small-angle X-ray Scattering and Electron Microscopy

2P049 平衡条件下において形成される二つの天然変性蛋白質融合蛋白質のフォールディング中間状態(01C. 蛋白質:物性,ポスター,第52回日本生物物理学会年会(2014年度))

2P049 Folding intermediates formed by the fusion protein of two intrisically disordered proteins under equilibrium condition(01C. Protein: Property,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))

Thermostable Direct Hemolysin of Vibrio parahaemolyticus Is a Bacterial Reversible Amyloid Toxin

3SEA-05 Toward understanding the mechanism of cytotoxicity of amyloidogenic variable domain of immunoglobulin light chains(3SEA Roles of Membrane Interface in amyloidogenesis,Symposium)

1PT159 STABILITY OF FOLDING INTERMEDIATE AFFECTS THE AMYLOIDOGENIC PROPENSITY OF IMMUNOGLOBULIN LIGHT CHAIN VARIABLE DOMAIN(The 50th Annual Meeting of the Biophysical Society of Japan)

EspB from enterohaemorrhagic Escherichia coli is a natively partially folded protein

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

Direct Observation of Aβ Amyloid Fibril Growth and Inhibition

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