About: The Unfolding Pathway and Conformational Stability of Potato Carboxypeptidase Inhibitor

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scientific article published in Journal of Biological Chemistry

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rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) наукова стаття, опублікована в травні 2000 (uk) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im Mai 2000 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Journal of Biological Chemistry (en)
publication date	wds:Q57957058-373A7B63-9B04-4FAC-9FC6-8CF55BC35248
publication date	2000-05-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57957058-A28B8A42-BB85-41D9-AA96-8CDDCF3D5B59
language of work or name	English
cites work	wds:Q57957058-002632F3-CEE8-48F4-937B-42E8141E5056 wds:Q57957058-04B50449-9F92-4640-91D3-69665C15721D wds:Q57957058-04DC8AD9-3D35-4CEB-A294-FD6921E282E3 wds:Q57957058-04FD5892-DC8A-499A-B8FB-9F18ADC1A80F wds:Q57957058-0E98CA2F-82C2-4C13-9D1C-5B1A3608F966 wds:Q57957058-237105C7-2748-425C-BF55-9EAFA3C4EA68 wds:Q57957058-2C66CD80-BDC0-44C5-983C-F54D6E4FAE85 wds:Q57957058-36BA8274-4F9F-4B15-914C-B49434A1FCB2 wds:Q57957058-39201836-6B21-4353-8DA1-61A871F8315E wds:Q57957058-41232091-05E9-4811-B735-DBE127BC4F56 wds:Q57957058-439D2908-0872-484D-B476-9ED2C32E6EE4 wds:Q57957058-4B8F0EF4-5301-4C1F-A7F0-9AF134206478 wds:Q57957058-4F3C7079-D2E6-43F2-8F68-218CDD490752 wds:Q57957058-506416DF-1843-4812-99BF-D38A00795417 wds:Q57957058-5FCE4D2F-1429-4D7E-B8BC-0D66C52EFAA8 wds:Q57957058-795413D2-2BB2-4E86-B8A7-B9A865075525 wds:Q57957058-91AF340C-6876-4A9A-9CF3-18869CA810E5 wds:Q57957058-A843A5ED-FA1A-45A3-948A-D2075DF08C4B wds:Q57957058-AE99661C-3C21-4E3C-9FA0-C591983F94DE wds:Q57957058-B14017FF-EE88-4788-96BF-93A20F7965E7 wds:Q57957058-B2998E5B-EAC0-4ACD-8CB3-6576AE2F0486 wds:Q57957058-B53DC39F-EA4E-4099-B4A1-6B0E8B142606 wds:Q57957058-B6815D67-0A7E-4811-A415-B769B9511571 wds:Q57957058-C147662C-58A3-4F7C-9917-C8A080FEF428 wds:Q57957058-CD87FA0E-876A-44DC-A283-B615C7FFC555 wds:Q57957058-D301CB6F-EE8E-42DC-95C9-8520D83EE47B wds:Q57957058-E244FCEF-1CCF-4B3F-972C-C98CED57E0A4 wds:Q57957058-E4F40100-C138-4894-9B1C-DF4FE1820850 wds:Q57957058-F7CBE7AB-205B-4DBE-80B7-C978AFEED19B
cites work	A disulphide-reinforced structural scaffold shared by small proteins with diverse functions Expression of a synthetic gene encoding potato carboxypeptidase inhibitor using a bacterial secretion vector The new biology of spongiform encephalopathy: infectious amyloidoses with a genetic twist Intramolecular chaperones and protein folding Denatured states of proteins Oxidative refolding of insulin-like growth factor 1 yields two products of similar thermodynamic stability: a bifurcating protein-folding pathway NMR determination of residual structure in a urea-denatured protein, the 434-repressor Extensive nonrandom structure in reduced and unfolded bovine pancreatic trypsin inhibitor Protein Denaturation Refined crystal structure of the potato inhibitor complex of carboxypeptidase A at 2.5 A resolution Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics Determination and analysis of urea and guanidine hydrochloride denaturation curves Potato carboxypeptidase inhibitor, a T-knot protein, is an epidermal growth factor antagonist that inhibits tumor cell growth The concept of a random coil. Residual structure in peptides and denatured proteins Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? The disulfide folding pathway of tick anticoagulant peptide (TAP), a Kunitz-type inhibitor structurally homologous to BPTI pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1. Analysis of the extent of unfolding of denatured insulin-like growth factor Unfolding and Refolding of Cardiotoxin III Elucidated by Reversible Conversion of the Native and Scrambled Species† Controlling the speed of hirudin folding Denatured states of tick anticoagulant peptide. Compositional analysis of unfolded scrambled isomers Protein similarities beyond disulphide bridge topology Characterization of the wound-induced metallocarboxypeptidase inhibitor from potato. cDNA sequence, induction of gene expression, subcellular immunolocalization and potential roles of the C-terminal propeptide. Sulfhydryl-Disulfide Interchange Disulfide exchange folding of insulin-like growth factor I Reduction studies on bacterial recombinant somatomedin C/insulin-like growth factor-1 Location of disulphide bonds in human insulin-like growth factors (IGFs) synthesized by recombinant DNA technology Unfolding of hirudin characterized by the composition of denatured scrambled isomers Quantitative analysis of the composition of the native and scrambled ribonuclease A
author name string	wds:Q57957058-89DA0889-5977-4197-B2F7-CDBED614B3AB wds:Q57957058-DD1A7103-B83A-45E9-A68F-2D796431C2C2 wds:Q57957058-E4039187-3FC0-47CC-8FD7-D3AB280A4B74
author name string	L Li J Y Chang F Canals
rdfs:label	The Unfolding Pathway and Conformational Stability of Potato Carboxypeptidase Inhibitor (en) The Unfolding Pathway and Conformational Stability of Potato Carboxypeptidase Inhibitor (nl)
skos:prefLabel	The Unfolding Pathway and Conformational Stability of Potato Carboxypeptidase Inhibitor (en) The Unfolding Pathway and Conformational Stability of Potato Carboxypeptidase Inhibitor (nl)
name	The Unfolding Pathway and Conformational Stability of Potato Carboxypeptidase Inhibitor (en) The Unfolding Pathway and Conformational Stability of Potato Carboxypeptidase Inhibitor (nl)
author	wds:Q57957058-25C6BBC0-5CA5-4C4F-9EAF-B31F312329A4
author	Francesc Xavier Avilés Puigvert
title	wds:Q57957058-267B4793-F37F-4EED-BF0D-8CFE68962852
title	The unfolding pathway and conformational stability of potato carboxypeptidase inhibitor (en)
page(s)	wds:Q57957058-2FDE70B9-1723-4B12-B5F3-CA1918AB471D
page(s)	14205-14211
instance of	wds:Q57957058-92620936-3E67-48AC-B805-F3D1F9E83DD8
instance of	scholarly article
PubMed ID	wds:Q57957058-6B3CDF91-F627-41B1-8877-0F8D09029720
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10799497
PubMed ID	10799497
published in	wds:Q57957058-DD190843-4607-41D5-BEE6-5952D726B132
published in	Journal of Biological Chemistry
issue	wds:Q57957058-1B2E9049-3107-4941-BDB0-4EA902DECEAF
volume	wds:Q57957058-9A426595-B3BB-4D20-BBDB-CA20CE0CFD56
issue	19
volume	275
DOI	wds:Q57957058-80C1B56B-FD43-4C6D-AB8D-3BA6B39891B0
DOI	http://dx.doi.org/10.1074/JBC.275.19.14205

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