Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1
about
Steps in reductive activation of the disulfide-generating enzyme Ero1pThioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase. An intersubunit disulfide bond serves as a redox switch for activationQuiescin sulfhydryl oxidase from Trypanosoma brucei: catalytic activity and mechanism of a QSOX family member with a single thioredoxin domain.Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulumMutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1beta.Activity-dependent reversible inactivation of the general amino acid permease.Balanced Ero1 activation and inactivation establishes ER redox homeostasisMolecular Characterization of Endoplasmic Reticulum Oxidoreductin 1 from Bombyx moriHyperactivity of the Ero1α oxidase elicits endoplasmic reticulum stress but no broad antioxidant response.Divergence of Erv1-associated mitochondrial import and export pathways in trypanosomes and anaerobic protists.Generating disulfides with the Quiescin-sulfhydryl oxidases.Different ubiquitin signals act at the Golgi and plasma membrane to direct GAP1 trafficking.Novel Roles of the Non-catalytic Elements of Yeast Protein-disulfide Isomerase in Its Interplay with Endoplasmic Reticulum Oxidoreductin 1Oxidative protein-folding systems in plant cells.ER membrane-localized oxidoreductase Ero1 is required for disulfide bond formation in the rice endosperm.Biochemical evidence that regulation of Ero1β activity in human cells does not involve the isoform-specific cysteine 262.Intermolecular disulfide bond to modulate protein function as a redox-sensing switch.An unexpected role for the yeast nucleotide exchange factor Sil1 as a reductant acting on the molecular chaperone BiP.Endoplasmic reticulum protein quality control and its relationship to environmental stress responses in plants.Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulumA CHO cell line engineered to express XBP1 and ERO1-Lα has increased levels of transient protein expression.Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation.Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum.Deciphering structural and functional roles of individual disulfide bonds of the mitochondrial sulfhydryl oxidase Erv1p.Functional and structural characterization of protein disulfide oxidoreductase from Thermus thermophilus HB27.Polyamine Metabolism and Oxidative Protein Folding in the ER as ROS-Producing Systems Neglected in Virology.
P2860
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P2860
Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1
description
2006 nî lūn-bûn
@nan
2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2006年の論文
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2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Disulfide transfer between two ...... y to protein oxidation by Ero1
@ast
Disulfide transfer between two ...... y to protein oxidation by Ero1
@en
Disulfide transfer between two ...... y to protein oxidation by Ero1
@nl
type
label
Disulfide transfer between two ...... y to protein oxidation by Ero1
@ast
Disulfide transfer between two ...... y to protein oxidation by Ero1
@en
Disulfide transfer between two ...... y to protein oxidation by Ero1
@nl
prefLabel
Disulfide transfer between two ...... y to protein oxidation by Ero1
@ast
Disulfide transfer between two ...... y to protein oxidation by Ero1
@en
Disulfide transfer between two ...... y to protein oxidation by Ero1
@nl
P2860
P356
P1476
Disulfide transfer between two ...... y to protein oxidation by Ero1
@en
P2093
Chris A Kaiser
P2860
P304
P356
10.1091/MBC.E05-05-0417
P577
2006-02-22T00:00:00Z