Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
about
Inflammatory and oxidative stress in rotavirus infectionAntioxidant responses and cellular adjustments to oxidative stressOxidative protein folding: selective pressure for prolamin evolution in riceKinetics and mechanisms of thiol-disulfide exchange covering direct substitution and thiol oxidation-mediated pathwaysDisulfide bond formation in the mammalian endoplasmic reticulumPreparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbBStructure of a bacterial homologue of vitamin K epoxide reductaseStructure of the Human Sulfhydryl Oxidase Augmenter of Liver Regeneration and Characterization of a Human Mutation Causing an Autosomal Recessive Myopathy,Steps in reductive activation of the disulfide-generating enzyme Ero1pCrystal 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.Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1pCellular disulfide bond formation in bioactive peptides and proteinsRegulation of signal transduction by reactive oxygen species in the cardiovascular systemSEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal muscle pathology, counteracts hyperoxidation by means of redox-regulating SERCA2 pump activityERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasisFrom structure to redox: The diverse functional roles of disulfides and implications in disease.Molecular characterization of the human Calpha-formylglycine-generating enzyme.Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulumRiboflavin deficiency impairs oxidative folding and secretion of apolipoprotein B-100 in HepG2 cells, triggering stress response systems.A small molecule inhibitor of endoplasmic reticulum oxidation 1 (ERO1) with selectively reversible thiol reactivity.Arsenic(III) species inhibit oxidative protein folding in vitro.Oxidative protein folding and the Quiescin-sulfhydryl oxidase family of flavoproteins.Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB.Proteomic analysis of solid pseudopapillary tumor of the pancreas reveals dysfunction of the endoplasmic reticulum protein processing pathwayTwo conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation 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 Ero1The structure of G4, the poxvirus disulfide oxidoreductase essential for virus maturation and infectivity.Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.Balanced Ero1 activation and inactivation establishes ER redox homeostasisProtein substrate discrimination in the quiescin sulfhydryl oxidase (QSOX) familyVersatility of the endoplasmic reticulum protein folding factory.Molecular Characterization of Endoplasmic Reticulum Oxidoreductin 1 from Bombyx moriAtypical protein disulfide isomerases (PDI): Comparison of the molecular and catalytic properties of poplar PDI-A and PDI-M with PDI-L1A.The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress.Role of tryptophan residues of Erv1: Trp95 and Trp183 are important for its folding and oxidase function.
P2860
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P2860
Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
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
Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
@ast
Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
@en
Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
@nl
type
label
Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
@ast
Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
@en
Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
@nl
prefLabel
Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
@ast
Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
@en
Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
@nl
P2093
P1433
P1476
Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell
@en
P2093
Chris A Kaiser
David B Kastner
Deborah Fass
Einav Gross
P304
P356
10.1016/S0092-8674(04)00418-0
P407
P577
2004-05-28T00:00:00Z