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Article

FALS mutations in Cu, Zn superoxide dismutase destabilize the dimer and increase dimer dissociation propensity: a large-scale thermodynamic analysis.

Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis - 1 Dec 2006

Khare Sagar D, Caplow Michael, Dokholyan Nikolay V

Abstract excerpt

Mutations in the dimeric enzyme Cu, Zn superoxide dismutase (SOD1) leading to its aggregation are implicated in the toxicity in familial amyotrophic lateral sclerosis (FALS). We and others have previously shown that aggregation occurs by a pathway involving dimer dissociation, metal-loss from monomers and multimeric assembly of apo-SOD1 monomers. We postulate that FALS mutations cause enhanced aggregation by...

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Source

Identifiers

PMID: 17107883
DOI: 10.1080/13506120600960486

Genes

SOD1

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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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