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Article

Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum.

The Journal of biological chemistry - 16 Jul 2004

Bertoli Gloria, Simmen Thomas, Anelli Tiziana, Molteni Silvia Nerini, Fesce Riccardo, Sitia Roberto

Abstract excerpt

Human Ero1alpha is an endoplasmic reticulum (ER)-resident protein responsible for protein disulfide isomerase (PDI) oxidation. To clarify the molecular mechanisms underlying its function, we generated a panel of cysteine replacement mutants and analyzed their capability of: 1) complementing a temperature-sensitive yeast Ero1 mutant, 2) favoring oxidative folding in mammalian cells, 3) forming mixed disulfides...

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Identifiers

PMID: 15136577
DOI: 10.1074/jbc.M403192200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum.PMID 15136577Read ↗

Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum.Semantic proximity Read ↗

Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1.Semantic proximity Read ↗

Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover.Semantic proximity Read ↗

Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.Semantic proximity Read ↗

Steps in reductive activation of the disulfide-generating enzyme Ero1p.Semantic proximity Read ↗

Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum.Semantic proximity Read ↗

Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum.Semantic proximity Read ↗

Manipulation of oxidative protein folding and PDI redox state in mammalian cells.Semantic proximity Read ↗

Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1beta.Semantic proximity Read ↗

Competition between glutathione and protein thiols for disulphide-bond formation.Semantic proximity Read ↗

Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway.Semantic proximity Read ↗

Deciphering structural and functional roles of individual disulfide bonds of the mitochondrial sulfhydryl oxidase Erv1p.Semantic proximity Read ↗

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