The Catalytic Activity of Protein-disulfide Isomerase Requires a Conformationally Flexible Molecule
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Compact conformations of human protein disulfide isomeraseSolution structure of the bb' domains of human protein disulfide isomeraseCrystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDIHuman Protein-disulfide Isomerase Is a Redox-regulated Chaperone Activated by Oxidation of Domain a′Structural insight into the dimerization of human protein disulfide isomeraseEffects of macromolecular crowding on protein conformational changesThe Redox State Regulates the Conformation of Rv2466c to Activate the Antitubercular Prodrug TP053.Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulumPlasticity of human protein disulfide isomerase: evidence for mobility around the X-linker region and its functional significance.Multivalency in the inhibition of oxidative protein folding by arsenic(III) species.Protein disulfide isomerase interacts with tau protein and inhibits its fibrillization.Substrate-induced unfolding of protein disulfide isomerase displaces the cholera toxin A1 subunit from its holotoxin.Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substratesStructural basis of redox-dependent substrate binding of protein disulfide isomeraseAdverse Outcomes Associated with Cigarette Smoke Radicals Related to Damage to Protein-disulfide IsomeraseMapping the O-Mannose Glycoproteome in Saccharomyces cerevisiaeGenerating an unfoldase from thioredoxin-like domainsOxidative protein-folding systems in plant cells.A structural overview of the PDI family of proteins.Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals.The role of s-nitrosylation and s-glutathionylation of protein disulphide isomerase in protein misfolding and neurodegeneration.Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulumA shape-shifting redox foldase contributes to Proteus mirabilis copper resistance.The ligand-binding b' domain of human protein disulphide-isomerase mediates homodimerization.The flexibility and dynamics of protein disulfide isomerase.Molecular bases of cyclic and specific disulfide interchange between human ERO1alpha protein and protein-disulfide isomerase (PDI).'Something in the way she moves': The functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI).Inhibition of the functional interplay between endoplasmic reticulum (ER) oxidoreduclin-1α (Ero1α) and protein-disulfide isomerase (PDI) by the endocrine disruptor bisphenol A.Ni-CeO2 spherical nanostructures for magnetic and electrochemical supercapacitor applications.Protein folding and disulfide bond formation in the eukaryotic cell: meeting report based on the presentations at the European Network Meeting on Protein Folding and Disulfide Bond Formation 2009 (Elsinore, Denmark).Synthesis and Experimental Validation of New PDI Inhibitors with Antiproliferative Activity
P2860
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P2860
The Catalytic Activity of Protein-disulfide Isomerase Requires a Conformationally Flexible Molecule
description
2008 nî lūn-bûn
@nan
2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
The Catalytic Activity of Prot ...... ormationally Flexible Molecule
@ast
The Catalytic Activity of Prot ...... ormationally Flexible Molecule
@en
The Catalytic Activity of Prot ...... ormationally Flexible Molecule
@nl
type
label
The Catalytic Activity of Prot ...... ormationally Flexible Molecule
@ast
The Catalytic Activity of Prot ...... ormationally Flexible Molecule
@en
The Catalytic Activity of Prot ...... ormationally Flexible Molecule
@nl
prefLabel
The Catalytic Activity of Prot ...... ormationally Flexible Molecule
@ast
The Catalytic Activity of Prot ...... ormationally Flexible Molecule
@en
The Catalytic Activity of Prot ...... ormationally Flexible Molecule
@nl
P2093
P2860
P3181
P356
P1476
The Catalytic Activity of Prot ...... ormationally Flexible Molecule
@en
P2093
Franz-Xaver Kober
Urs Lewandrowski
William J Lennarz
P2860
P304
P3181
P356
10.1074/JBC.M806026200
P407
P577
2008-11-28T00:00:00Z