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

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

Journal of the neurological sciences - 15 Jan 2014

Son Marjatta, Elliott Jeffrey L

Abstract excerpt

Several hypotheses have been proposed for the mechanisms underlying mutant Cu,Zn Superoxide Dismutase-related Amyotrophic Lateral Sclerosis. These include aggregation pathology, mitochondrial dysfunctions, oxidative stress, and glutamate-mediated excitotoxicity. Mitochondrial disease may be a primary event in neurodegeneration, contributing to oxidative stress and apoptosis, or it may be caused by other cellular...

Read the complete abstract on PubMed

Topics

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

Share to Mice
Share to Mice, Transgenic
Share to Mitochondrial Diseases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mitochondrial Proteins

Share to Molecular Chaperones

Share to Mutation

Share to Protein Folding

Share to Superoxide Dismutase

Source

Identifiers

PMID: 24269091
DOI: 10.1016/j.jns.2013.11.004

Genes

SOD1

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

Mitochondrial defects in transgenic mice expressing Cu,Zn superoxide dismutase mutations: the role of copper chaperone for SOD1.PMID 24269091Read ↗

Transgenic mouse models of amyotrophic lateral sclerosis.Semantic proximity Read ↗

Transgenic mouse model for familial amyotrophic lateral sclerosis with superoxide dismutase-1 mutationSemantic proximity Read ↗

Mitochondrial dysfunction and amyotrophic lateral sclerosis.Semantic proximity Read ↗

Transgenics, toxicity and therapeutics in rodent models of mutant SOD1-mediated familial ALS.Semantic proximity Read ↗

Amyotrophic lateral sclerosis associated with mutations in the CuZn superoxide dismutase gene.Semantic proximity Read ↗

Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria.Semantic proximity Read ↗

Oligomerization of mutant SOD1 in mitochondria of motoneuronal cells drives mitochondrial damage and cell toxicity.Semantic proximity Read ↗

Dysregulation of intracellular copper homeostasis is common to transgenic mice expressing human mutant superoxide dismutase-1s regardless of their copper-binding abilities.Semantic proximity Read ↗

Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNS.Semantic proximity Read ↗

Mitochondrial dysfunction and its role in motor neuron degeneration in ALS.Semantic proximity Read ↗

Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice.Semantic proximity Read ↗

Neurodegenerative disease. Oxidative stress and motorneuron disease.Semantic proximity Read ↗

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