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

Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae.

BMC biochemistry - 14 Jan 2010

Greetham Darren, Vickerstaff Jill, Shenton Daniel, Perrone Gabriel G, Dawes Ian W, Grant Chris M

Abstract excerpt

BACKGROUND: Protein-SH groups are amongst the most easily oxidized residues in proteins, but irreversible oxidation can be prevented by protein glutathionylation, in which protein-SH groups form mixed disulphides with glutathione. Glutaredoxins and thioredoxins are key oxidoreductases which have been implicated in regulating glutathionylation/deglutathionylation in diverse organisms. Glutaredoxins have been...

Read the complete abstract on PubMed

Topics

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

Share to Glutaredoxins
Share to Glutathione
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oxidation-Reduction

Share to Reactive Oxygen Species

Share to Recombinant Proteins

Share to Saccharomyces cerevisiae

Share to Thioredoxins

Source

Open in PubMed Open full text

Identifiers

PMID: 20074363
DOI: 10.1186/1471-2091-11-3
PMCID: PMC2836980

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

Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae.PMID 20074363Read ↗

Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system.Semantic proximity Read ↗

Thioredoxins are required for protection against a reductive stress in the yeast Saccharomyces cerevisiae.Semantic proximity Read ↗

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

Role of yeast glutaredoxins as glutathione S-transferases.Semantic proximity Read ↗

Nuclear monothiol glutaredoxins of Saccharomyces cerevisiae can function as mitochondrial glutaredoxins.Semantic proximity Read ↗

AtGRXcp, an Arabidopsis chloroplastic glutaredoxin, is critical for protection against protein oxidative damage.Semantic proximity Read ↗

A single glutaredoxin or thioredoxin gene is essential for viability in the yeast Saccharomyces cerevisiae.Semantic proximity Read ↗

The mitochondrial thioredoxin system.Semantic proximity Read ↗

Quantitative assessment of the determinant structural differences between redox-active and inactive glutaredoxins.Semantic proximity Read ↗

The roles of thiol oxidoreductases in yeast replicative aging.Semantic proximity Read ↗

Differential expression and role of two dithiol glutaredoxins Grx1 and Grx2 in Schizosaccharomyces pombe.Semantic proximity Read ↗

Glutaredoxin catalysis requires two distinct glutathione interaction sites.Semantic proximity Read ↗

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