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

Water-soluble triarylphosphines as biomarkers for protein S-nitrosation.

ACS chemical biology - 16 Apr 2010

Bechtold Erika, Reisz Julie A, Klomsiri Chananat, Tsang Allen W, Wright Marcus W, Poole Leslie B, Furdui Cristina M, King S Bruce

Abstract excerpt

S-Nitrosothiols (RSNOs) represent an important class of post-translational modifications that preserve and amplify the actions of nitric oxide and regulate enzyme activity. Several regulatory proteins are now verified targets of cellular S-nitrosation, and the direct detection of S-nitrosated res...

Read the complete abstract on PubMed

Topics

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

Share to Cysteine
Share to Mutation
Share to Peroxiredoxins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Salmonella typhimurium

Source

Open in PubMed Open full text

Identifiers

PMID: 20146502
DOI: 10.1021/cb900302u
PMCID: PMC2863053

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20146502-2026-09-02.2. 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

Water-soluble triarylphosphines as biomarkers for protein S-nitrosation.PMID 20146502Read ↗

A substrate trapping approach identifies proteins regulated by reversible S-nitrosylation.Semantic proximity Read ↗

Computational Structural Biology of S-nitrosylation of Cancer TargetsSemantic proximity Read ↗

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

Disruption of Redox Homeostasis by Enzymatic Activation of a Triakylphosphine Probe in MitochondriaSemantic proximity Read ↗

Supersulfides: A Promising Therapeutic Approach for Autoinflammatory DiseasesSemantic proximity Read ↗

S-nitrosoglutathione reductase deficiency causes aberrant placental S-nitrosylation and preeclampsiaSemantic proximity Read ↗

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

Aberrant Protein S-Nitrosylation Mimics the Effect of Rare Genetic Mutations in Neurodegenerative Diseases.Semantic proximity Read ↗

1H, 15N and 13C backbone and side-chain assignments of reduced and S-nitrosated C62only mutant of human thioredoxin.Semantic proximity Read ↗

Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2.Semantic proximity Read ↗

S-nitrosothiols signaling in cystic fibrosis airways.Semantic proximity Read ↗

Ninhydrin as a covalent warhead for chemical proteomic-enabled discovery and selective engagement of reactive argininesSemantic proximity Read ↗

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