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Article

Biochemical basis of oxidative protein folding in the endoplasmic reticulum.

Science (New York, N.Y.) - 24 Nov 2000

Tu B P, Ho-Schleyer S C, Travers K J, Weissman J S

Abstract excerpt

The endoplasmic reticulum (ER) supports disulfide bond formation by a poorly understood mechanism requiring protein disulfide isomerase (PDI) and ERO1. In yeast, Ero1p-mediated oxidative folding was shown to depend on cellular flavin adenine dinucleotide (FAD) levels but not on ubiquinone or heme, and Ero1p was shown to be a FAD-binding protein. We reconstituted efficient oxidative folding in vitro using FAD,...

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Identifiers

PMID: 11090354
DOI: 10.1126/science.290.5496.1571

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Biochemical basis of oxidative protein folding in the endoplasmic reticulum.PMID 11090354Read ↗

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

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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 ↗

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

Ero1p oxidizes protein disulfide isomerase in a pathway for 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 ↗

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

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