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

Pyruvate protects motor neurons expressing mutant superoxide dismutase 1 against copper toxicity.

Neuroreport - 25 Apr 2005

Kim Hyun-Jung, Kim Jong-Min, Park Jong-Ha, Sung Jung-Joon, Kim Manho, Lee Kwang-Woo

Abstract excerpt

Mutations in the copper/zinc superoxide dismutase (SOD1) gene are known to be responsible for familial amyotrophic lateral sclerosis. Alteration of metal binding properties of mutant SOD1 has been proposed to play a role in the pathogenesis of amyotrophic lateral sclerosis. We investigated the toxic effects of excess extracellular copper on motor neuronal cells expressing human mutant SOD1 (G93A), and evaluated...

Read the complete abstract on PubMed

Topics

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

Share to Copper
Share to Free Radical Scavengers
Share to Hybrid Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Neuroblastoma

Share to Neuroprotective Agents

Share to Pyruvic Acid

Share to Superoxide Dismutase-1

Share to Thiamine

Source

Identifiers

PMID: 15812313
DOI: 10.1097/00001756-200504250-00014

Genes

SOD1

Variants

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

Pyruvate protects motor neurons expressing mutant superoxide dismutase 1 against copper toxicity.PMID 15812313Read ↗

Copper Homeostasis as a Therapeutic Target in Amyotrophic Lateral Sclerosis with SOD1 Mutations.Semantic proximity Read ↗

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

Mutant Superoxide Dismutase-1-Linked Familial Amyotrophic Lateral Sclerosis: Molecular Mechanisms of Neuronal Death and ProtectionSemantic proximity Read ↗

Mitochondrial defects in transgenic mice expressing Cu,Zn superoxide dismutase mutations: the role of copper chaperone for SOD1.Semantic proximity Read ↗

Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis.Semantic proximity Read ↗

Mitochondrial dysfunction due to mutant copper/zinc superoxide dismutase associated with amyotrophic lateral sclerosis is reversed by N-acetylcysteine.Semantic proximity Read ↗

Glutamate carboxypeptidase II inhibition protects motor neurons from death in familial amyotrophic lateral sclerosis modelsSemantic proximity Read ↗

Overexpression of metallothionein protects cultured motor neurons against oxidative stress, but not mutant Cu/Zn-superoxide dismutase toxicity.Semantic proximity Read ↗

Altered MAM function shifts mitochondrial metabolism in SOD1-mutant models of ALSSemantic proximity Read ↗

Metabolic Dysfunction in Familial, but Not Sporadic, Amyotrophic Lateral SclerosisSemantic proximity Read ↗

Disrupted copper availability in sporadic ALS: Implications for Cu <sup>II</sup> (atsm) as a treatment optionSemantic proximity Read ↗

Mutant SOD1 causes motor neuron disease independent of copper chaperone-mediated copper loading.Semantic proximity Read ↗

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