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

Peroxiredoxin-mediated redox regulation of the nuclear localization of Yap1, a transcription factor in budding yeast.

Antioxidants & redox signaling - 1 Jan 2000

Okazaki Shoko, Naganuma Akira, Kuge Shusuke

Abstract excerpt

A redox reaction involving cysteine thiol-disulfide exchange is crucial for the intracellular monitoring of oxidation status. The yeast transcription factor Yap1 is activated by formation of a disulfide bond, which inhibits nuclear export in response to peroxide stress, with resultant enhancement of the nuclear localization of Yap1. A glutathione peroxidase-like protein, Gpx3, which has peroxiredoxin activity, is...

Read the complete abstract on PubMed

Topics

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

Share to Adaptor Proteins, Signal Transducing
Share to Cell Nucleus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glutathione Peroxidase

Share to Hydrogen Peroxide

Share to Oxidation-Reduction

Share to Peroxidases

Share to Peroxiredoxins

Share to Saccharomyces cerevisiae Proteins

Source

Identifiers

PMID: 15706081
DOI: 10.1089/ars.2005.7.327

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Peroxiredoxin-mediated redox regulation of the nuclear localization of Yap1, a transcription factor in budding yeast.PMID 15706081Read ↗

Thioredoxin deficiency causes the constitutive activation of Yap1, an AP-1-like transcription factor in Saccharomyces cerevisiae.Semantic proximity Read ↗

Role of thioredoxin reductase in the Yap1p-dependent response to oxidative stress in Saccharomyces cerevisiae.Semantic proximity Read ↗

Genetic analysis of glutathione peroxidase in oxidative stress response of Saccharomyces cerevisiae.Semantic proximity Read ↗

Cooperation of yeast peroxiredoxins Tsa1p and Tsa2p in the cellular defense against oxidative and nitrosative stress.Semantic proximity Read ↗

Loss of yeast peroxiredoxin Tsa1p induces genome instability through activation of the DNA damage checkpoint and elevation of dNTP levels.Semantic proximity Read ↗

Transcriptional regulation of yeast peroxiredoxin gene TSA2 through Hap1p, Rox1p, and Hap2/3/5p.Semantic proximity Read ↗

Nuclear import of the yeast AP-1-like transcription factor Yap1p is mediated by transport receptor Pse1p, and this import step is not affected by oxidative stress.Semantic proximity Read ↗

The thioredoxin system protects ribosomes against stress-induced aggregation.Semantic proximity Read ↗

Yap, a novel family of eight bZIP proteins in Saccharomyces cerevisiae with distinct biological functions.Semantic proximity Read ↗

Analysis of the oxidative stress regulation of the Candida albicans transcription factor, Cap1p.Semantic proximity Read ↗

Activity of the Yap1 transcription factor in Saccharomyces cerevisiae is modulated by methylglyoxal, a metabolite derived from glycolysis.Semantic proximity Read ↗

Regulation of the fission yeast transcription factor Pap1 by oxidative stress: requirement for the nuclear export factor Crm1 (Exportin) and the stress-activated MAP kinase Sty1/Spc1.Semantic proximity Read ↗

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