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

Tyrosine modifications and inactivation of active site manganese superoxide dismutase mutant (Y34F) by peroxynitrite.

Archives of biochemistry and biophysics - 1 Jun 1999

MacMillan-Crow L A, Thompson J A

Abstract excerpt

Recent studies from this laboratory have demonstrated that human manganese superoxide dismutase (MnSOD) is a target for tyrosine nitration in several chronic inflammatory diseases including chronic organ rejection, arthritis, and tumorigenesis. Furthermore, we demonstrated that peroxynitrite (ONOO-) is the only known biological oxidant competent to inactivate enzymatic activity, nitrate critical tyrosine...

Read the complete abstract on PubMed

Topics

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

Share to Catalytic Domain
Share to Mutation
Share to Nitrates

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Recombinant Proteins

Share to Superoxide Dismutase

Share to Tyrosine

Source

Identifiers

PMID: 10334867
DOI: 10.1006/abbi.1999.1202

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Tyrosine modifications and inactivation of active site manganese superoxide dismutase mutant (Y34F) by peroxynitrite.PMID 10334867Read ↗

Exploring the molecular basis of human manganese superoxide dismutase inactivation mediated by tyrosine 34 nitration.Semantic proximity Read ↗

A novel superoxide dismutase-based trap for peroxynitrite used to detect entry of peroxynitrite into erythrocyte ghosts.Semantic proximity Read ↗

Peroxynitrous acid-modified extracellular matrix alters gene and protein expression in human coronary artery smooth muscle cells and induces a pro-inflammatory phenotype.Semantic proximity Read ↗

Proteomic method identifies proteins nitrated <i>in vivo</i> during inflammatory challengeSemantic proximity Read ↗

Genetically encoding protein oxidative damage.Semantic proximity Read ↗

Peroxynitrite-induced nitration of tyrosine hydroxylase: identification of tyrosines 423, 428, and 432 as sites of modification by matrix-assisted laser desorption ionization time-of-flight mass spectrometry and tyrosine-scanning mutagenesis.Semantic proximity Read ↗

Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant.Semantic proximity Read ↗

Endothelial PHD2 Deficiency Induces Nitrative Stress via Suppression of Caveolin-1 in Pulmonary Arterial HypertensionSemantic proximity Read ↗

Thioredoxin and lipoic acid catalyze the denitrosation of low molecular weight and protein S-nitrosothiols.Semantic proximity Read ↗

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

Potent anti-tumor effects of an active site mutant of human manganese-superoxide dismutase. Evolutionary conservation of product inhibition.Semantic proximity Read ↗

Nitrosative stress leads to protein glutathiolation, increased s-nitrosation, and up-regulation of peroxiredoxins in the heart.Semantic proximity Read ↗

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