Plasticity of human protein disulfide isomerase: evidence for mobility around the X-linker region and its functional significance.
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Compact conformations of human protein disulfide isomeraseA substrate-driven allosteric switch that enhances PDI catalytic activityCrystal 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′Structure analysis of the extracellular domain reveals disulfide bond forming-protein properties of Mycobacterium tuberculosis Rv2969cLemon protein disulfide isomerase: cDNA cloning and biochemical characterization.Machine Learning and Network Analysis of Molecular Dynamics Trajectories Reveal Two Chains of Red/Ox-specific Residue Interactions in Human Protein Disulfide Isomerase.Protein disulfide isomerase in thrombosis and vascular inflammationBacitracin inhibits the reductive activity of protein disulfide isomerase by disulfide bond formation with free cysteines in the substrate-binding domain.Different interaction modes for protein-disulfide isomerase (PDI) as an efficient regulator and a specific substrate of endoplasmic reticulum oxidoreductin-1α (Ero1α).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.Acid-denatured Green Fluorescent Protein (GFP) as model substrate to study the chaperone activity of protein disulfide isomeraseA structural overview of the PDI family of proteins.Functional in vitro analysis of the ERO1 protein and protein-disulfide isomerase pathway.S-nitrosylation of the thioredoxin-like domains of protein disulfide isomerase and its role in neurodegenerative conditions.Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulumThe 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).Protein disulfide isomerase isomerizes non-native disulfide bonds in human proinsulin independent of its peptide-binding activity.Mechanistic insight of photo-induced aggregation of chicken egg white lysozyme: the interplay between hydrophobic interactions and formation of intermolecular disulfide bonds.
P2860
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P2860
Plasticity of human protein disulfide isomerase: evidence for mobility around the X-linker region and its functional significance.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Plasticity of human protein di ...... d its functional significance.
@ast
Plasticity of human protein di ...... d its functional significance.
@en
Plasticity of human protein di ...... d its functional significance.
@nl
type
label
Plasticity of human protein di ...... d its functional significance.
@ast
Plasticity of human protein di ...... d its functional significance.
@en
Plasticity of human protein di ...... d its functional significance.
@nl
prefLabel
Plasticity of human protein di ...... d its functional significance.
@ast
Plasticity of human protein di ...... d its functional significance.
@en
Plasticity of human protein di ...... d its functional significance.
@nl
P2093
P2860
P356
P1476
Plasticity of human protein di ...... d its functional significance.
@en
P2093
A Katrine Wallis
Chih-chen Wang
Robert B Freedman
Sihong Chen
P2860
P304
26788-26797
P356
10.1074/JBC.M110.107839
P407
P50
P577
2010-06-01T00:00:00Z