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

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

The Journal of clinical investigation - 1 Feb 2008

Harraz Maged M, Marden Jennifer J, Zhou Weihong, Zhang Yulong, Williams Aislinn, Sharov Victor S, Nelson Kathryn, Luo Meihui, Paulson Henry, Schöneich Christian, Engelhardt John F

Abstract excerpt

Neurodegeneration in familial amyotrophic lateral sclerosis (ALS) is associated with enhanced redox stress caused by dominant mutations in superoxide dismutase-1 (SOD1). SOD1 is a cytosolic enzyme that facilitates the conversion of superoxide (O(2)(*-)) to H(2)O(2). Here we demonstrate that SOD1 is not just a catabolic enzyme, but can also directly regulate NADPH oxidase-dependent (Nox-dependent) O(2)(*-)...

Read the complete abstract on PubMed

Topics

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

Share to Hydrogen Peroxide
Share to Longevity

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to NADPH Oxidase 2

Share to NADPH Oxidases

Share to Neuropeptides

Share to rac GTP-Binding Proteins

Share to rac1 GTP-Binding Protein

Share to Superoxide Dismutase-1

Source

Open in PubMed Open full text

Identifiers

PMID: 18219391
DOI: 10.1172/JCI34060
PMCID: PMC2213375

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

SOD1 mutations disrupt redox-sensitive Rac regulation of NADPH oxidase in a familial ALS model.PMID 18219391Read ↗

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

Alsin and SOD1(G93A) proteins regulate endosomal reactive oxygen species production by glial cells and proinflammatory pathways responsible for neurotoxicity.Semantic proximity Read ↗

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

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

Highlight Commentary on "Redox proteomics analysis of oxidatively modified proteins in G93A-SOD1 transgenic mice--a model of familial amyotrophic lateral sclerosis".Semantic proximity Read ↗

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

SOD1 Function and Its Implications for Amyotrophic Lateral Sclerosis Pathology: New and Renascent Themes.Semantic proximity Read ↗

Mitochondrial redox signalling by p66Shc mediates ALS-like disease through Rac1 inactivation.Semantic proximity Read ↗

Oxidative stress in ALS: key role in motor neuron injury and therapeutic target.Semantic proximity Read ↗

Late-onset motoneuron disease caused by a functionally modified AMPA receptor subunitSemantic proximity Read ↗

Skeletal Muscle-Restricted Expression of Human SOD1 in Transgenic Mice Causes a Fatal ALS-Like SyndromeSemantic proximity Read ↗

Lessons from models of SOD1-linked familial ALS.Semantic proximity Read ↗

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