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

Wild-type superoxide dismutase acquires binding and toxic properties of ALS-linked mutant forms through oxidation.

Journal of neurochemistry - 1 Jul 2007

Ezzi Samer Abou, Urushitani Makoto, Julien Jean-Pierre

Abstract excerpt

Recent studies suggest that superoxide dismutase (SOD1) may represent a major target of oxidative damage in neurodegenerative diseases. To test the possibility that oxidized species of wild-type (WT) SOD1 might be involved in pathogenic processes, we analyzed the properties of the WT human SOD1 protein after its oxidation in vivo or in vitro by hydrogen peroxide (H2O2) treatment. Using transfected Neuro2a cells...

Read the complete abstract on PubMed

Topics

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

Share to Cell Death
Share to Immunoprecipitation
Share to Motor Neurons

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Spinal Cord

Share to Subcellular Fractions

Share to Superoxide Dismutase

Share to Superoxide Dismutase-1

Share to Ubiquinone

Source

Identifiers

PMID: 17394546
DOI: 10.1111/j.1471-4159.2007.04531.x

Genes

SOD1

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

Wild-type superoxide dismutase acquires binding and toxic properties of ALS-linked mutant forms through oxidation.PMID 17394546Read ↗

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

SOD1 mutations disrupt redox-sensitive Rac regulation of NADPH oxidase in a familial ALS model.Semantic proximity Read ↗

An emerging role for misfolded wild-type SOD1 in sporadic ALS pathogenesisSemantic proximity Read ↗

Oxidation-induced misfolding and aggregation of superoxide dismutase and its implications for amyotrophic lateral sclerosis.Semantic proximity Read ↗

Oxidized/misfolded superoxide dismutase-1: the cause of all amyotrophic lateral sclerosis?Semantic proximity Read ↗

Mutant SOD1 from spinal cord of G93A rats is destabilized and binds to inner mitochondrial membrane.Semantic proximity Read ↗

Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis.Semantic proximity Read ↗

Characterization of the activity, aggregation, and toxicity of heterodimers of WT and ALS-associated mutant Sod1.Semantic proximity Read ↗

The molecular pathogenesis of superoxide dismutase 1-linked ALS is promoted by low oxygen tensionSemantic proximity Read ↗

The structure, redox chemistry and motor neuron toxicity of heterodimeric zinc-deficient SOD1-implications for the toxic gain of function observed in ALS.Semantic proximity Read ↗

Do oxidatively modified proteins cause ALS?Semantic proximity Read ↗

Gain in functions of mutant Cu,Zn-superoxide dismutases as a causative factor in familial amyotrophic lateral sclerosis: less reactive oxidant formation but high spontaneous aggregation and precipitation.Semantic proximity Read ↗

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