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Article

Role of disulfide cross-linking of mutant SOD1 in the formation of inclusion-body-like structures.

PloS one - 1 Jan 2012

Roberts Brittany L T, Patel Kinaree, Brown Hilda H, Borchelt David R

Abstract excerpt

BACKGROUND: Pathologic aggregates of superoxide dismutase 1 (SOD1) harboring mutations linked to familial amyotrophic lateral sclerosis (fALS) have been shown to contain aberrant intermolecular disulfide cross-links. In prior studies, we observed that intermolecular bonding was not necessary in the formation of detergent- insoluble SOD1 complexes by mutant SOD1, but we were unable to assess whether this type of...

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Identifiers

PMID: 23118898
DOI: 10.1371/journal.pone.0047838
PMCID: PMC3485248

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.

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