Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Redox signal transduction: mutations shifting [2Fe-2S] centers of the SoxR sensor-regulator to the oxidized form.

Cell - 10 Jan 1997

Hidalgo E, Ding H, Demple B

Abstract excerpt

SoxR is a [2Fe-2S] transcription factor triggered by oxidative stress and activated in vitro by one-electron oxidation or assembly of the iron-sulfur centers. To distinguish which mechanism operates in cells, we studied constitutively active SoxR (SoxRc) proteins. Three SoxRc proteins contained [...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacterial Proteins
Share to DNA
Share to Escherichia coli

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to Mutation

Share to Promoter Regions, Genetic

Share to Signal Transduction

Share to Transcription Factors

Source

Identifiers

PMID: 9019397
DOI: 10.1016/s0092-8674(00)81864-4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-9019397-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

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

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Redox signal transduction: mutations shifting [2Fe-2S] centers of the SoxR sensor-regulator to the oxidized form.PMID 9019397Read ↗

Functional analysis of SoxR residues affecting transduction of oxidative stress signals into gene expression.Semantic proximity Read ↗

Regulation of the soxRS oxidative stress regulon. Reversible oxidation of the Fe-S centers of SoxR in vivo.Semantic proximity Read ↗

Transcription-defective soxR mutants of Escherichia coli: isolation and in vivo characterization.Semantic proximity Read ↗

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

Rational Tuning of Superoxide Sensitivity in SoxR, the [2Fe-2S] Transcription Factor: Implications of Species-Specific Lysine Residues.Semantic proximity Read ↗

A reducing system of the superoxide sensor SoxR in Escherichia coli.Semantic proximity Read ↗

Effects of mutations in active site heme ligands on the spectroscopic and catalytic properties of SoxAX cytochromes.Semantic proximity Read ↗

OxyR: a molecular code for redox-related signaling.Semantic proximity Read ↗

Miscoordination of the iron-sulfur clusters of the anaerobic transcription factor, FNR, allows simple repression but not activation.Semantic proximity Read ↗

Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction.Semantic proximity Read ↗

A cluster of constitutive mutations affecting the C-terminus of the redox-sensitive SoxR transcriptional activator.Semantic proximity Read ↗

Functional Characterization of RseC in the SoxR Reducing System and Its Role in Oxidative Stress Response in Escherichia coli.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.