The Micro Domain Essential for the Ligand-Binding of Guanylyl Cyclase C
スポンサーリンク
概要
- 論文の詳細を見る
- 2003-02-01
著者
-
Shimonishi Yasutsugu
Institute For Protein Research Osaka University
-
Hidaka Yuji
Institute For Protein Research Osaka University
-
Matsumoto Yoshiko
Institute For Protein Research Osaka University
関連論文
- 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)
- Amino Acid Sequence of αk Substance, a Mating Pheromone of Saccharomyces kluyveri
- A Novel Modification of the Lysine Residue at Position 12 of Histone H4 in Starfish Sperm
- 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
- pQVPLPRYamide Isolated from the Clam Meretrix lusoria : a Member of a Novel Molluscan Neuropeptide Family
- Structure and Action of Bioactive Peptides Isolated from the Newt, Cynops pyrrhogaster : I. A. C-type Natriuretic Peptide (CNP)
- Bioactive Peptides Isolated from An African Ancient-type Fish, Polypterus senegalus
- Structure and Action of Bioactive Peptides Isolated from the Newt, Cynops pyrrhogaster : II. Four VIP-Related Peptides and Two Neurotensin-Related Peptides
- 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
- A New Method for the Sequence Determination of a Peptide Mixture through Molecular Weight Measurements by Mass Spectrometry
- A Cystine Motif in A Novel Endogenous Inhibitor of Phenoloxidase
- 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
- Mass Spectrometry of Peptides and Proteins in the Post-Genome Era
- Pretreatment of Silicon Emitter for the Enhancement of Ionization Efficiency in Field Desorption Mass Spectrometry
- Computation of amino acid sequences of polypeptides from masses of their constituent peptide fragments and amino acid residues released in Edman-degradation.
- A new method for carboxyl-terminal sequence analysis of a peptide using carboxypeptidases and field-desorption mass spectrometry.
- Chemical synthesis of a heat-stable enterotoxin produced by enterotoxigenic Escherichia coli strain 18D.
- Structure-activity relationship of a heat-stable enterotoxin produced by Yersinia enterocolitica.
- Regeneration to the native form of hen egg-white lysozyme from its protected derivatives.
- Chemical synthesis of fully active and heat-stable fragments of heat-stable enterotoxin of enterotoxigenic Escherichia coli strain 18D.
- 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.
- Influence of Anhydrous Hydrogen Fluoride on Hen Egg-White Lysozyme. I. Effects on Native Hen Egg-White Lysozyme
- Synthesis of a partial sequence of proinsulin using the A-chain of natural insulin. III. Synthesis of a peptide corresponding to positions 41-81 of bovine proinsulin.
- Structural requirements for the spatial structure and toxicity of heat-stable enterotoxin(STh) of enterotoxigenic Escherichia coli.
- A new method for protein sequence analysis using edman-degradation, field-desorption mass spectrometry and computer calculation. Sequence determination of the N-terminal BrCN fragment of Streptomyces erythraeus lysozyme.
- Synthesis of a heat-stable enterotoxin (STh) produced by a human strain SK-1 of enterotoxigenic Escherichia coli.
- Heat-stable enterotoxin (STh) of human enterotoxigenic Escherichia coli (strain SK-1). Structure-activity relationship.