Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation.
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Disulphide production by Ero1α-PDI relay is rapid and effectively regulatedRecycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulumDisulfide bond formation in the mammalian endoplasmic reticulumSteps in reductive activation of the disulfide-generating enzyme Ero1pCrystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDICrystal Structure of Reduced and of Oxidized Peroxiredoxin IV Enzyme Reveals a Stable Oxidized Decamer and a Non-disulfide-bonded Intermediate in the Catalytic CycleSynergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein foldingFormation and Reversibility of BiP Protein Cysteine Oxidation Facilitate Cell Survival during and post Oxidative StressMechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative diseaseLifetime imaging of a fluorescent protein sensor reveals surprising stability of ER thiol redoxERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasisIdentification, characterization and purification of porcine Quiescin Q6-Sulfydryl Oxidase 2 protein.The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1α.Quiescin sulfhydryl oxidase from Trypanosoma brucei: catalytic activity and mechanism of a QSOX family member with a single thioredoxin domain.Oxidative protein folding and the Quiescin-sulfhydryl oxidase family of flavoproteins.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.Oxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space.Ero1-α and PDIs constitute a hierarchical electron transfer network of endoplasmic reticulum oxidoreductasesBalanced Ero1 activation and inactivation establishes ER redox homeostasisMolecular Characterization of Endoplasmic Reticulum Oxidoreductin 1 from Bombyx moriCysteines 208 and 241 in Ero1α are required for maximal catalytic turnoverHyperactivity 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 1Elucidation of thioredoxin target protein networks in mouse.Endoplasmic reticulum oxidoreductin-1α (Ero1α) improves folding and secretion of mutant proinsulin and limits mutant proinsulin-induced endoplasmic reticulum stress.Enzyme activity of phosphatase of regenerating liver is controlled by the redox environment and its C-terminal residues.Disulfide formation in the ER and mitochondria: two solutions to a common process.Glutathione peroxidase 7 utilizes hydrogen peroxide generated by Ero1α to promote oxidative protein folding.Lack of an efficient endoplasmic reticulum-localized recycling system protects peroxiredoxin IV from hyperoxidation.Biochemical evidence that regulation of Ero1β activity in human cells does not involve the isoform-specific cysteine 262.Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals.The oxidative protein folding machinery in plant cells.Regulating the level of intracellular hydrogen peroxide: the role of peroxiredoxin IV.Oxidative protein folding: from thiol-disulfide exchange reactions to the redox poise of the endoplasmic reticulum.Functional in vitro analysis of the ERO1 protein and protein-disulfide isomerase pathway.Interplay between redox and protein homeostasis.Oxidative stress and antibacterial properties of a graphene oxide-cystamine nanohybrid.Proteolytic processing of QSOX1A ensures efficient secretion of a potent disulfide catalyst.
P2860
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P2860
Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Low reduction potential of Ero ...... ontrol of substrate oxidation.
@en
type
label
Low reduction potential of Ero ...... ontrol of substrate oxidation.
@en
prefLabel
Low reduction potential of Ero ...... ontrol of substrate oxidation.
@en
P2093
P2860
P356
P1433
P1476
Low reduction potential of Ero ...... control of substrate oxidation
@en
P2093
Alyson M Sheppard
Karl M Baker
Kevin P Langton
Seema Chakravarthi
P2860
P304
P356
10.1038/EMBOJ.2008.230
P407
P577
2008-10-30T00:00:00Z