Discover Community Create You

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

OxyR: a molecular code for redox-related signaling.

Cell - 3 May 2002

Kim Sung Oog, Merchant Kunal, Nudelman Raphael, Beyer Wayne F, Keng Teresa, DeAngelo Joseph, Hausladen Alfred, Stamler Jonathan S

Abstract excerpt

Redox regulation has been perceived as a simple on-off switch in proteins (corresponding to reduced and oxidized states). Using the transcription factor OxyR as a model, we have generated, in vitro, several stable, posttranslational modifications of the single regulatory thiol (SH), including S-NO, S-OH, and S-SG, and shown that each occurs in vivo. These modified forms of OxyR are transcriptionally active but...

Read the complete abstract on PubMed

Topics

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

Share to In Vitro Techniques
Share to Allosteric Regulation
Share to Cysteine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Disulfides

Share to Hydrogen Bonding

Share to Protein Processing, Post-Translational

Share to Sulfhydryl Compounds

Share to Transcriptional Activation

Source

Identifiers

PMID: 12015987
DOI: 10.1016/s0092-8674(02)00723-7

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

OxyR: a molecular code for redox-related signaling.PMID 12015987Read ↗

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

How to flip the (redox) switch.Semantic proximity Read ↗

Oxidation of a single active site suffices for the functional inactivation of the dimeric Bacillus subtilis OhrR repressor in vitro.Semantic proximity Read ↗

SelR reverses Mical-mediated oxidation of actin to regulate F-actin dynamics.Semantic proximity Read ↗

NOS and SONOS redox switches in proteinsSemantic 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 ↗

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

Real-time monitoring of peroxiredoxin oligomerization dynamics in living cells.Semantic proximity Read ↗

PRDX4, an endoplasmic reticulum-localized peroxiredoxin at the crossroads between enzymatic oxidative protein folding and nonenzymatic protein oxidation.Semantic proximity Read ↗

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

OxyR tightly regulates catalase expression in Neisseria meningitidis through both repression and activation mechanisms.Semantic proximity Read ↗

Ultra-fast genetically encoded sensor for precise real-time monitoring of physiological and pathophysiological peroxide dynamicsSemantic proximity Read ↗

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