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Article

Identification of a protein required for disulfide bond formation in vivo.

Cell - 1 Nov 1991

Bardwell J C, McGovern K, Beckwith J

Abstract excerpt

We describe a mutation (dsbA) that renders Escherichia coli severely defective in disulfide bond formation. In dsbA mutant cells, pulse-labeled beta-lactamase, alkaline phosphatase, and OmpA are secreted but largely lack disulfide bonds. These disulfideless proteins may represent in vivo folding intermediates, since they are protease sensitive and chase slowly into stable oxidized forms. The dsbA gene codes for a...

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PMID: 1934062
DOI: 10.1016/0092-8674(91)90532-4

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

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Identification of a protein required for disulfide bond formation in vivo.PMID 1934062Read ↗

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Converting a Sulfenic Acid Reductase into a Disulfide Bond Isomerase.Semantic proximity Read ↗

Functional analysis of paralogous thiol-disulfide oxidoreductases in Bacillus subtilis.Semantic proximity Read ↗

The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.Semantic proximity Read ↗

Snapshots of DsbA in action: detection of proteins in the process of oxidative folding.Semantic proximity Read ↗

Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions.Semantic proximity Read ↗

Nonconsecutive disulfide bond formation in an essential integral outer membrane protein.Semantic proximity Read ↗

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