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Article

Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis.

Proceedings of the National Academy of Sciences of the United States of America - 14 Dec 2010

Auclair Jared R, Boggio Kristin J, Petsko Gregory A, Ringe Dagmar, Agar Jeffrey N

Abstract excerpt

Amyotrophic lateral sclerosis (ALS) is a disorder characterized by the death of both upper and lower motor neurons and by 3- to 5-yr median survival postdiagnosis. The only US Food and Drug Administration-approved drug for the treatment of ALS, Riluzole, has at best, moderate effect on patient su...

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Identifiers

PMID: 21098299
DOI: 10.1073/pnas.1015463107
PMCID: PMC3003092

Genes

SOD1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-21098299-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

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Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis.PMID 21098299Read ↗

Protein crosslinking as a therapeutic strategy for SOD1-related ALSSemantic proximity Read ↗

Evaluating protein cross-linking as a therapeutic strategy to stabilize SOD1 variants in a mouse model of familial ALS.Semantic proximity Read ↗

An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis.Semantic proximity Read ↗

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Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation.Semantic proximity Read ↗

Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.Semantic proximity Read ↗

Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of 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 ↗

Toxic SOD1 trimers are off-pathway in the formation of amyloid-like fibrils in ALS.Semantic proximity Read ↗

Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the apo- and reduced form of SOD1, leading to unfolding and oxidative aggregation.Semantic proximity Read ↗

Silence superoxide dismutase 1 (SOD1): a promising therapeutic target for amyotrophic lateral sclerosis (ALS).Semantic proximity Read ↗

Nonnative SOD1 trimer is toxic to motor neurons in a model of amyotrophic lateral sclerosis.Semantic proximity Read ↗

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