Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum.
about
Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDIEfficient IgM assembly and secretion require the plasma cell induced endoplasmic reticulum protein pERp1Probing mechanisms of axonopathy. Part I: Protein targets of 1,2-diacetylbenzene, the neurotoxic metabolite of aromatic solvent 1,2-diethylbenzeneTissue-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 Ero1Golgi and related vesicle proteomics: simplify to identify.Hyperactivity of the Ero1α oxidase elicits endoplasmic reticulum stress but no broad antioxidant response.Novel Roles of the Non-catalytic Elements of Yeast Protein-disulfide Isomerase in Its Interplay with Endoplasmic Reticulum Oxidoreductin 1A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cellsGlutathione peroxidase 7 utilizes hydrogen peroxide generated by Ero1α to promote oxidative protein folding.Biochemical evidence that regulation of Ero1β activity in human cells does not involve the isoform-specific cysteine 262.The oxidative protein folding machinery in plant cells.Functional in vitro analysis of the ERO1 protein and protein-disulfide isomerase pathway.The Ero1alpha-PDI redox cycle regulates retro-translocation of cholera toxin.Interplays between covalent modifications in the endoplasmic reticulum increase conformational diversity in nascent prion protein.Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation.Molecular bases of cyclic and specific disulfide interchange between human ERO1alpha protein and protein-disulfide isomerase (PDI).Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a' domains of protein-disulfide isomerase.Polyamine Metabolism and Oxidative Protein Folding in the ER as ROS-Producing Systems Neglected in Virology.
P2860
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P2860
Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum.
description
2004 nî lūn-bûn
@nan
2004 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Two conserved cysteine triads ...... in the endoplasmic reticulum.
@ast
Two conserved cysteine triads ...... in the endoplasmic reticulum.
@en
Two conserved cysteine triads ...... in the endoplasmic reticulum.
@nl
type
label
Two conserved cysteine triads ...... in the endoplasmic reticulum.
@ast
Two conserved cysteine triads ...... in the endoplasmic reticulum.
@en
Two conserved cysteine triads ...... in the endoplasmic reticulum.
@nl
prefLabel
Two conserved cysteine triads ...... in the endoplasmic reticulum.
@ast
Two conserved cysteine triads ...... in the endoplasmic reticulum.
@en
Two conserved cysteine triads ...... in the endoplasmic reticulum.
@nl
P2093
P2860
P50
P356
P1476
Two conserved cysteine triads ...... in the endoplasmic reticulum.
@en
P2093
Riccardo Fesce
Silvia Nerini Molteni
Thomas Simmen
P2860
P304
30047-30052
P356
10.1074/JBC.M403192200
P407
P577
2004-05-10T00:00:00Z