ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
about
Gene function in early mouse embryonic stem cell differentiation.Manipulation of oxidative protein folding and PDI redox state in mammalian cellsERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin familyDisulphide production by Ero1α-PDI relay is rapid and effectively regulatedTwo pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulumThe CXXCXXC motif determines the folding, structure and stability of human Ero1-LalphaThiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1Oxidative protein folding in eukaryotes: mechanisms and consequencesAntioxidant responses and cellular adjustments to oxidative stressDisulfide bond formation in the mammalian endoplasmic reticulumCrystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDIThe Crystal Structure of the Protein-Disulfide Isomerase Family Member ERp27 Provides Insights into Its Substrate Binding CapabilitiesDomain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum.A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation.ERp57 is a multifunctional thiol-disulfide oxidoreductaseDisulfide bonds in ER protein folding and homeostasisRedox regulation of store-operated Ca2+ entryEndoplasmic reticulum thiol oxidase deficiency leads to ascorbic acid depletion and noncanonical scurvy in miceThe cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-LalphaERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasisPotential role of glutathione in evolution of thiol-based redox signaling sites in proteinsCatalysis of Protein Folding by Protein Disulfide Isomerase and Small-Molecule MimicsProteomic mapping of cytosol-facing outer mitochondrial and ER membranes in living human cells by proximity biotinylationCancer-associated oxidoreductase ERO1-α promotes immune escape through up-regulation of PD-L1 in human breast cancer.Proteome analysis of human Wharton's jelly cells during in vitro expansion.Oxidative protein folding in vitro: a study of the cooperation between quiescin-sulfhydryl oxidase and protein disulfide isomeraseVitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function.Glycoprotein folding in the endoplasmic reticulum.Formation and transfer of disulphide bonds in living cells.Oxidative protein folding and the Quiescin-sulfhydryl oxidase family of flavoproteins.Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum.Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum.Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta.Different interaction modes for protein-disulfide isomerase (PDI) as an efficient regulator and a specific substrate of endoplasmic reticulum oxidoreductin-1α (Ero1α).Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzymeOxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin.Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1beta.
P2860
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P2860
ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
description
2000 nî lūn-bûn
@nan
2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
@ast
ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
@en
ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
@en-gb
ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
@nl
type
label
ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
@ast
ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
@en
ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
@en-gb
ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
@nl
prefLabel
ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
@ast
ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
@en
ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
@en-gb
ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
@nl
P2093
P2860
P50
P921
P356
P1476
ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
@en
P2093
P2860
P304
P356
10.1074/JBC.275.7.4827
P407
P577
2000-02-01T00:00:00Z