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Article

Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status.

Proceedings of the National Academy of Sciences of the United States of America - 25 May 1999

Aslund F, Zheng M, Beckwith J, Storz G

Abstract excerpt

The Escherichia coli transcription factor OxyR is activated by the formation of an intramolecular disulfide bond and subsequently is deactivated by enzymatic reduction of the disulfide bond. Here we show that OxyR can be activated by two possible pathways. In mutants defective in the cellular dis...

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Identifiers

PMID: 10339558
DOI: 10.1073/pnas.96.11.6161
PMCID: PMC26852

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-10339558-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

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Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status.PMID 10339558Read ↗

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Thiol peroxidases mediate specific genome-wide regulation of gene expression in response to hydrogen peroxide.Semantic proximity Read ↗

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OxyR Is a Convergent Target for Mutations Acquired during Adaptation to Oxidative Stress-Prone Metabolic States.Semantic proximity Read ↗

The redox-regulated SoxR protein acts from a single DNA site as a repressor and an allosteric activator.Semantic proximity Read ↗

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