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Article

Cysteine 111 affects aggregation and cytotoxicity of mutant Cu,Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis.

The Journal of biological chemistry - 11 Jan 2008

Cozzolino Mauro, Amori Ilaria, Pesaresi Maria Grazia, Ferri Alberto, Nencini Monica, Carrì Maria Teresa

Abstract excerpt

Converging evidence indicates that aberrant aggregation of mutant Cu,Zn-superoxide dismutase (mutSOD1) is strongly implicated in familial amyotrophic lateral sclerosis (FALS). MutSOD1 forms high molecular weight oligomers, which disappear under reducing conditions, both in neural tissues of FALS transgenic mice and in transfected cultured cells, indicating a role for aberrant intermolecular disulfide...

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Identifiers

PMID: 18006498
DOI: 10.1074/jbc.M705657200
PMCID: PMC2842925

Genes

SOD1

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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.

Related research

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Cysteine 111 affects aggregation and cytotoxicity of mutant Cu,Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis.PMID 18006498Read ↗

Oligomerization of mutant SOD1 in mitochondria of motoneuronal cells drives mitochondrial damage and cell toxicity.Semantic proximity Read ↗

A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis.Semantic proximity Read ↗

Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria.Semantic proximity Read ↗

Oxidative modification of cysteine 111 promotes disulfide bond-independent aggregation of SOD1.Semantic proximity Read ↗

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

Oxidative modification to cysteine sulfonic acid of Cys111 in human copper-zinc superoxide dismutase.Semantic proximity Read ↗

Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1.Semantic proximity Read ↗

SOD1 gains pro-oxidant activity upon aberrant oligomerization: change in enzymatic activity by intramolecular disulfide bond cleavage.Semantic proximity Read ↗

Glutaredoxin 2 prevents aggregation of mutant SOD1 in mitochondria and abolishes its toxicity.Semantic proximity Read ↗

Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis.Semantic proximity Read ↗

Amyotrophic lateral sclerosis associated with mutations in the CuZn superoxide dismutase gene.Semantic proximity Read ↗

Spinal cord homogenates from SOD1 familial amyotrophic lateral sclerosis induce SOD1 aggregation in living cells.Semantic proximity Read ↗

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