How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?

doi:10.1016/j.tibs.2006.12.005

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Article

How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?

Trends in biochemical sciences - 1 Feb 2007

Shaw Bryan F, Valentine Joan Selverstone

Abstract excerpt

More than 100 different mutations in the gene encoding copper-zinc superoxide dismutase (SOD1) cause familial forms of amyotrophic lateral sclerosis (ALS)--a fatal neurodegenerative disease in which aggregation of the SOD1 protein is considered to be the primary mode of pathogenesis. Recent results show that these mutations have remarkably diverse and unexpected effects on the structure, activity and native state...

Topics

Amyotrophic Lateral Sclerosis
Animals
Enzyme Stability
Humans
Mutation
Superoxide Dismutase
Superoxide Dismutase-1

Source

Open in PubMed

Identifiers

PMID: 17208444
DOI: 10.1016/j.tibs.2006.12.005

Genes

SOD1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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