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Article

Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS.

Proceedings of the National Academy of Sciences of the United States of America - 12 May 2009

Karch Celeste M, Prudencio Mercedes, Winkler Duane D, Hart P John, Borchelt David R

Abstract excerpt

Transgenic mice that model familial (f)ALS, caused by mutations in superoxide dismutase (SOD)1, develop paralysis with pathology that includes the accumulation of aggregated forms of the mutant protein. Using a highly sensitive detergent extraction assay, we traced the appearance and abundance of detergent-insoluble and disulfide cross-linked aggregates of SOD1 throughout the disease course of SOD1-fALS mice...

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Source

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Identifiers

PMID: 19416874
DOI: 10.1073/pnas.0902505106
PMCID: PMC2675570

Genes

SOD1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS.PMID 19416874Read ↗

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