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

Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD.

Science (New York, N.Y.) - 23 Apr 2004

Budanov Andrei V, Sablina Anna A, Feinstein Elena, Koonin Eugene V, Chumakov Peter M

Abstract excerpt

Acting as a signal, hydrogen peroxide circumvents antioxidant defense by overoxidizing peroxiredoxins (Prxs), the enzymes that metabolize peroxides. We show that sestrins, a family of proteins whose expression is modulated by p53, are required for regeneration of Prxs containing Cys-SO(2)H, thus reestablishing the antioxidant firewall. Sestrins contain a predicted redox-active domain homologous to AhpD, the...

Read the complete abstract on PubMed

Topics

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

Share to Heat-Shock Proteins
Share to Hydrogen Peroxide
Share to Oxidation-Reduction

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oxidoreductases

Share to Peroxidases

Share to Peroxiredoxins

Share to Reactive Oxygen Species

Share to RNA, Small Interfering

Source

Identifiers

PMID: 15105503
DOI: 10.1126/science.1095569

Provenance

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

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

Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD.PMID 15105503Read ↗

Microbial 2-Cys Peroxiredoxins: Insights into Their Complex Physiological Roles.Semantic proximity Read ↗

Emerging Roles of Sestrins in Neurodegenerative Diseases: Counteracting Oxidative Stress and BeyondSemantic proximity Read ↗

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

Sestrins at the Interface of ROS Control and Autophagy Regulation in Health and DiseaseSemantic proximity Read ↗

A Peroxiredoxin-P38 MAPK scaffold increases MAPK activity by MAP3K-independent mechanismsSemantic proximity Read ↗

The Gasotransmitter Trio (NO, CO, H₂S) in Cardiovascular Health and Disease: From Molecular Crosstalk to Precision Gas MedicineSemantic proximity Read ↗

Sestrin-2, a repressor of PDGFRβ signalling, promotes cigarette-smoke-induced pulmonary emphysema in mice and is upregulated in individuals with COPDSemantic proximity Read ↗

Nox Enzymes and New Thinking on Reactive Oxygen: A Double-Edged Sword RevisitedSemantic proximity Read ↗

Identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin.Semantic proximity Read ↗

The 1 -Cys peroxiredoxin, PRDX-6, suppresses an NHR-49-dependent pro-survival response, including the Flavin monooxygenase, FMO-2, that protects against fungal and bacterial infection.Semantic proximity Read ↗

Sohlh2 promotes pulmonary fibrosis via repression of p62/Keap1/Nrf2 mediated anti-oxidative signaling pathwaySemantic proximity Read ↗

PRDX6 contributes to selenocysteine metabolism and ferroptosis resistanceSemantic proximity Read ↗

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