About: Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase

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scientific article published in Nature

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rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) article publié dans la revue scientifique Nature (fr) im September 1993 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Nature (en) наукова стаття, опублікована в Nature у вересні 1993 (uk)
publication date	wds:Q60066033-868F1A33-F87A-4B38-B348-280E91E74AB2
publication date	1993-09-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q60066033-F37D094F-411D-41BF-9DEF-E7BF8163285F
language of work or name	English
exact match	wds:Q60066033-D76A09D8-919A-4644-9A93-9AB3147EE99A
exact match	https://scigraph.springernature.com/pub.10.1038/365185a0
cites work	wds:Q60066033-046657A3-E17E-468B-9489-32F7944E8D3B wds:Q60066033-114C9D6F-5D6D-4711-A7CB-4F81323816FF wds:Q60066033-1534CB63-0D68-494B-A337-F0A46C28AC02 wds:Q60066033-1C36416D-B2E0-4731-A8AF-F9396A59E17B wds:Q60066033-1FB39E9F-D688-4EAD-BECC-2B1CC34D68D0 wds:Q60066033-21C64447-2F29-4D4A-BC81-C85D4E17F4CB wds:Q60066033-2AAF8C74-9387-473E-926A-5573DA918364 wds:Q60066033-35038C1A-AEB6-469F-A21D-8A8637CABA33 wds:Q60066033-4FBDA238-E494-421E-9CBD-2F17D49E1DF3 wds:Q60066033-53725C6F-6ADF-499C-AD62-97137611A26B wds:Q60066033-5F5B1722-EF4F-4B24-8803-96B06EC10DC8 wds:Q60066033-6AF8A9C6-830F-440C-9505-32BB6733B844 wds:Q60066033-7A4027BD-D187-4C7D-9535-7AF1513F5951 wds:Q60066033-82735B70-C752-45AD-B948-5504359A735A wds:Q60066033-A639AF5F-648C-44AF-9DE8-18E7B269B259 wds:Q60066033-AB6E8B2F-9394-4DDD-B9CF-F226D3F35826 wds:Q60066033-C7FB9962-9DBD-496E-B8D1-C72A8E04B573 wds:Q60066033-CC3DF7B1-6A13-4AA4-A920-C64A645D9B45 wds:Q60066033-CF341108-66DD-4FDF-8401-D7F1A030E8FA wds:Q60066033-F8166056-308A-42F9-8FEB-B6169E60E4C5
cites work	Structure of bovine pancreatic trypsin inhibitor. Results of joint neutron and X-ray refinement of crystal form II The interpretation of protein structures: Estimation of static accessibility Oxidized redox state of glutathione in the endoplasmic reticulum Conformational restrictions on the pathway of folding and unfolding of the pancreatic trypsin inhibitor Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at l.5 Å resolution Peptide binding and release by proteins implicated as catalysts of protein assembly Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer Catalysis by protein-disulphide isomerase of the unfolding and refolding of proteins with disulphide bonds Guanidine hydrochloride stabilization of a partially unfolded intermediate during the reversible denaturation of protein disulfide isomerase. Reexamination of the folding of BPTI: predominance of native intermediates. The pro region of BPTI facilitates folding Two-dimensional 1H NMR of two chemically modified analogs of the basic pancreatic trypsin inhibitor. Sequence-specific resonance assignments and sequence location of conformation changes relative to the native protein (14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance study Structural effects induced by removal of a disulfide-bridge: the X-ray structure of the C30A/C51A mutant of basic pancreatic trypsin inhibitor at 1.6 A. Kinetic role of a meta-stable native-like two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitor A new two-disulphide intermediate in the refolding of reduced bovine pancreatic trypsin inhibitor Effect of protein and peptide inhibitors on the activity of protein disulfide isomerase. Sequences of the genes and polypeptide precursors for two bovine protease inhibitors. Folding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulum Kinetic role of nonnative species in the folding of bovine pancreatic trypsin inhibitor
author name string	wds:Q60066033-14D4B9AB-5227-4943-9583-AA0BF8A4A89F wds:Q60066033-DD2DC381-B5CD-43C3-AC6A-D3C425547EF4
author name string	Weissman JS Kim PS
rdfs:label	Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase (en) Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase (nl)
skos:prefLabel	Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase (en) Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase (nl)
name	Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase (en) Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase (nl)
title	wds:Q60066033-720F236C-1F96-47B0-B940-18A0CFF9FCED
title	Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase (en)
page(s)	wds:Q60066033-A821A862-39ED-4171-953D-928A90DBE86F
page(s)	185-188
instance of	wds:Q60066033-0C51DFEC-D4F3-4CAD-9B4A-87CD4FD446DB
instance of	scholarly article
PubMed ID	wds:Q60066033-D0A6864C-9158-45E3-84AE-C2B762A95845
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7690463
PubMed ID	7690463
published in	wds:Q60066033-6BCAEE0B-11C5-4ED8-8278-4DECF374BED3
published in	Nature
issue	wds:Q60066033-1F6477BB-2B0F-440E-B594-AA8F8B6D2300
volume	wds:Q60066033-876E3F81-03E6-41C4-BA58-A8A21F1EE299
issue	6442
volume	365
DOI	wds:Q60066033-702BD6DA-5DE6-4AB3-8AAB-6B2097B1269E
DOI	http://dx.doi.org/10.1038/365185A0
DOI	10.1038/365185A0
Dimensions Publication ID	wds:Q60066033-FFFB616A-C34C-4048-9283-864AD0621C95
Dimensions Publication ID	1024959388
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q60066033
is cites work of	ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum Protein disulfide isomerase isomerizes non-native disulfide bonds in human proinsulin independent of its peptide-binding activity Congenital hypothyroid goiter with deficient thyroglobulin. Identification of an endoplasmic reticulum storage disease with induction of molecular chaperones Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells Folding and association of oligomeric and multimeric proteins Protein disulfide isomerase and newly synthesized procollagen chains form higher-order structures in the lumen of the endoplasmic reticulum The protein disulphide-isomerase family: unravelling a string of folds Structural determinants of oxidative folding in proteins Pre-expression of a sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E.coli An endoplasmic reticulum storage disease causing congenital goiter with hypothyroidism The Crystal Structure of the Protein-Disulfide Isomerase Family Member ERp27 Provides Insights into Its Substrate Binding Capabilities Elevated expression of PDI family proteins during differentiation of mouse F9 teratocarcinoma cells Catalysis of Protein Folding by Protein Disulfide Isomerase and Small-Molecule Mimics The eS-Sence of -SH in the ER. Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation

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