The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha
about
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 regulatedCrystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDICellular disulfide bond formation in bioactive peptides and proteinsThe cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-LalphaRegulated increase in folding capacity prevents unfolded protein stress in the ER.Large-scale discovery and characterization of protein regulatory motifs in eukaryotesOxidative protein folding in vitro: a study of the cooperation between quiescin-sulfhydryl oxidase and protein disulfide isomeraseConserved cysteine residues in the mammalian lamin A tail are essential for cellular responses to ROS generation.Vitamin 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.PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum.Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta.Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1beta.Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1Ero1-α and PDIs constitute a hierarchical electron transfer network of endoplasmic reticulum oxidoreductasesImexon induces an oxidative endoplasmic reticulum stress response in pancreatic cancer cells.A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cellsVersatility of the endoplasmic reticulum protein folding factory.Hyperactivity of the Ero1α oxidase elicits endoplasmic reticulum stress but no broad antioxidant response.Generating disulfides in multicellular organisms: emerging roles for a new flavoprotein family.Novel Roles of the Non-catalytic Elements of Yeast Protein-disulfide Isomerase in Its Interplay with Endoplasmic Reticulum Oxidoreductin 1Ero1L, a thiol oxidase, is required for Notch signaling through cysteine bridge formation of the Lin12-Notch repeats in Drosophila melanogaster.A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cellsThe subcellular distribution of multigene family 110 proteins of African swine fever virus is determined by differences in C-terminal KDEL endoplasmic reticulum retention motifs.Protein folding includes oligomerization - examples from the endoplasmic reticulum and cytosol.Two phases of disulfide bond formation have differing requirements for oxygen.Overexpression of Endoplasmic Reticulum Oxidoreductin 1-α (ERO1L) Is Associated with Poor Prognosis of Gastric Cancer.Molecular characterization of a Bombyx mori protein disulfide isomerase (bPDI).Oxidative folding in the endoplasmic reticulum: towards a multiple oxidant hypothesis?Sulfhydryl oxidases: sources, properties, production and applications.The oxidative protein folding machinery in plant cells.Human endoplasmic reticulum oxidoreductin 1-α is a novel predictor for poor prognosis of breast cancer.Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum
P2860
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P2860
The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha
description
2000 nî lūn-bûn
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2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված
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2000年の論文
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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
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name
The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha
@ast
The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha
@en
The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha
@nl
type
label
The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha
@ast
The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha
@en
The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha
@nl
prefLabel
The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha
@ast
The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha
@en
The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha
@nl
P2093
P2860
P356
P1433
P1476
The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/19.17.4493
P407
P577
2000-09-01T00:00:00Z