SOD1 aggregation and ALS: role of metallation states and disulfide status.

doi:10.2174/1568026611212220010

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Article

SOD1 aggregation and ALS: role of metallation states and disulfide status.

Current topics in medicinal chemistry - 1 Jan 2012

Sheng Yuewei, Chattopadhyay Madhuri, Whitelegge Julian, Valentine Joan Selverstone

Abstract excerpt

Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease characterized by the death of motor neurons. About 10% of ALS cases are inherited (familial), and a large subset of them are caused by mutations in the gene encoding the copper-zinc superoxide dismutase (SOD1). The detection of SOD1-positive inclusions in familial ALS patients suggests the role of SOD1 aggregation underlying the pathology of...

Topics

Amyotrophic Lateral Sclerosis
Animals
Disulfides
Humans
Mutation
Protein Folding
Protein Processing, Post-Translational
Superoxide Dismutase
Superoxide Dismutase-1

Source

Open in PubMed

Identifiers

PMID: 23339308
DOI: 10.2174/1568026611212220010

Genes

SOD1

Provenance

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

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