Hidaka Yuji | Institute For Protein Research Osaka University

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著作論文

2P054 CHARACTERIZATION OF CONFORMATIONAL CHANGES AND DYNAMICS IN SOLUTION STRUCTURE OF THE EXTRACELLULAR DOMAIN OF AMYLOID PRECURSOR(The 48th Annual Meeting of the Biophysical Society of Japan)
The N-Terminal Region of Prouroguanylin Responsible for the Folding of Uroguanylin
Folding Mechanism of Guanylyl Cyclase-Activating Peptides and its Precursor Protein
The Role of Propeptide in the Folding Pathway of Uroguanylin
Folding of a Peptide Hormone Assisted by a Propeptide : Folding of Hybrid Disulfide Isomers of Uroguanylin and Heat-stable Enterotoxin
Propeptide-Mediated Folding in a Peptide Hormone : Uroguanylin
IDENTIFICATION OF THE BINDING SITE ON THE EXTRACELLULAR DOMAIN OF GUANYLYL CYCLASE C TO HEAT-STABLE ENTEROTOXIN
The Micro Domain Essential for the Ligand-Binding of Guanylyl Cyclase C
Precious Role of Ile^3 of Prouroguanylin in the Folding of the Mature Peptide, Uroguanylin
Folding Mechanism of Prouroguanylin
A Study of the Role of the N-terminal Region of Prouroguanylin in the Folding by Site-directed Mutational Analysis
Structure-activity relationship of a heat-stable enterotoxin produced by Yersinia enterocolitica.
Disulfide linkages in a heat-stable enterotoxin (STP) produced by a porcine strain of enterotoxigenic Escherichia coli.
Structure-activity relationship of Escherichia coli heat-stable enterotoxin: Role of Ala residue at position 14 in toxin-receptor interaction.
Structural requirements for the spatial structure and toxicity of heat-stable enterotoxin(STh) of enterotoxigenic Escherichia coli.

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