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

Accelerated s-nitrosothiol breakdown by amyotrophic lateral sclerosis mutant copper,zinc-superoxide dismutase.

The Journal of biological chemistry - 26 Oct 2001

Johnson M A, Macdonald T L, Mannick J B, Conaway M R, Gaston B

Abstract excerpt

Mutations in copper,zinc-superoxide dismutase (SOD) have been implicated in familial amyotrophic lateral sclerosis (FALS). We have investigated the breakdown of S-nitrosothiols by wild-type (WT) SOD and two common FALS mutants, alanine-4 valine (A4V) SOD and glycine-37 arginine (G37R) SOD. In the presence of glutathione, A4V SOD and G37R SOD catalyzed S-nitrosoglutathione breakdown three times more efficiently...

Read the complete abstract on PubMed

Topics

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

Share to Amyotrophic Lateral Sclerosis
Share to Ascorbic Acid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Copper

Share to Mutation

Share to Serum Albumin, Bovine

Share to Superoxide Dismutase

Source

Identifiers

PMID: 11518706
DOI: 10.1074/jbc.M102781200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Accelerated s-nitrosothiol breakdown by amyotrophic lateral sclerosis mutant copper,zinc-superoxide dismutase.PMID 11518706Read ↗

Loss of oxidation-reduction specificity in amyotrophic lateral sclerosis-associated CuZnSOD mutants.Semantic proximity Read ↗

Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite.Semantic proximity Read ↗

Enhanced oxidative damage by the familial amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutants.Semantic proximity Read ↗

Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis.Semantic proximity Read ↗

S-nitrosothiol depletion in amyotrophic lateral sclerosis.Semantic proximity Read ↗

Putative denitrosylase activity of Cu,Zn-superoxide dismutase.Semantic proximity Read ↗

SOD1 mutants linked to amyotrophic lateral sclerosis selectively inactivate a glial glutamate transporter.Semantic proximity Read ↗

Homocysteine induces oxidative cytotoxicity in Cu,Zn-superoxide dismutase mutant motor neuronal cell.Semantic proximity Read ↗

Oral treatment with Cu(II)(atsm) increases mutant SOD1 in vivo but protects motor neurons and improves the phenotype of a transgenic mouse model of amyotrophic lateral sclerosis.Semantic proximity Read ↗

Endogenous Cu in the central nervous system fails to satiate the elevated requirement for Cu in a mutant SOD1 mouse model of ALS.Semantic proximity Read ↗

Release of copper ions from the familial amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutants.Semantic proximity Read ↗

A gain-of-function of an amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutant: An enhancement of free radical formation due to a decrease in Km for hydrogen peroxide.Semantic proximity Read ↗

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