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Article

Mutations in SOD1 associated with amyotrophic lateral sclerosis cause novel protein interactions.

Nature genetics - 1 Jan 1997

Kunst C B, Mezey E, Brownstein M J, Patterson D

Abstract excerpt

A subset of familial and sporadic amyotrophic lateral sclerosis (ALS-a fatal disorder characterised by progressive motor neuron degeneration) cases are due to mutations in the gene encoding Cu,Zn superoxide dismutase (SOD1). Two mutations which have been successfully used to generate transgenic mice that develop an ALS-like syndrome are glycine 85 to arginine (G85R) and glycine 93 to alanine (G93A) with the...

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Identifiers

PMID: 8988176
DOI: 10.1038/ng0197-91

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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Mutations in SOD1 associated with amyotrophic lateral sclerosis cause novel protein interactions.PMID 8988176Read ↗

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

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Yeast Models of Prion-Like Proteins That Cause Amyotrophic Lateral Sclerosis Reveal Pathogenic MechanismsSemantic proximity Read ↗

Interaction of amyotrophic lateral sclerosis (ALS)-related mutant copper-zinc superoxide dismutase with the dynein-dynactin complex contributes to inclusion formation.Semantic proximity Read ↗

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