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

Mutation in G6PD gene leads to loss of cellular control of protein glutathionylation: mechanism and implication.

Journal of cellular biochemistry - 1 Jan 2008

Ayene Iraimoudi S, Biaglow John E, Kachur Alexander V, Stamato Thomas D, Koch Cameron J

Abstract excerpt

More than 400 million people are susceptible to oxidative stress due to glucose-6-phosphate dehydrogenase (G6PD) deficiency. Protein glutathionylation is believed to be responsible for loss of protein function and/or cellular signaling during oxidative stress. To elucidate the implications of G6P...

Read the complete abstract on PubMed

Topics

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

Share to Chromatography, High Pressure Liquid
Share to Cricetinae
Share to DNA

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Helicases

Share to Glucosephosphate Dehydrogenase

Share to Glutathione

Share to Protein Binding

Source

Identifiers

PMID: 17516514
DOI: 10.1002/jcb.21394

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17516514-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutation in G6PD gene leads to loss of cellular control of protein glutathionylation: mechanism and implication.PMID 17516514Read ↗

Mutation in the glucose-6-phosphate dehydrogenase gene leads to inactivation of Ku DNA end binding during oxidative stress.Semantic proximity Read ↗

Oxidation of cellular thiols by hydroxyethyldisulphide inhibits DNA double-strand-break rejoining in G6PD deficient mammalian cells.Semantic proximity Read ↗

S-Glutathionylation of human inducible Hsp70 reveals a regulatory mechanism involving the C-terminal α-helical lid.Semantic proximity Read ↗

Exploring the role of glucose‑6‑phosphate dehydrogenase in cancer (Review).Semantic proximity Read ↗

Glutathione reductase underlies the stability of mutant p53 by antagonizing protein glutathionylation.Semantic proximity Read ↗

Redox-dependent regulation of end-binding protein 1 activity by glutathionylation.Semantic proximity Read ↗

Activated thiol Sepharose-based proteomic approach to globally quantify protein oxidationSemantic proximity Read ↗

Molecular analysis of Ku redox regulation.Semantic proximity Read ↗

Glyoxal induces DNA-Protein Crosslinking in CellsSemantic proximity Read ↗

SIRT5 promotes IDH2 desuccinylation and G6PD deglutarylation to enhance cellular antioxidant defense.Semantic proximity Read ↗

Glutathionylation of the Bacterial Hsp70 Chaperone DnaK Provides a Link between Oxidative Stress and the Heat Shock Response.Semantic proximity Read ↗

Regulation of Glutathione S-Transferase Omega 1 Mediated by Cysteine Residues Sensing the Redox Environment.Semantic proximity Read ↗

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