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Article

Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species.

Journal of molecular biology - 30 Apr 2010

Kayatekin Can, Zitzewitz Jill A, Matthews C Robert

Abstract excerpt

Cu,Zn superoxide dismutase (SOD1) is a dimeric metal-binding enzyme responsible for the dismutation of toxic superoxide to hydrogen peroxide and oxygen in cells. Mutations at dozens of sites in SOD1 induce amyotrophic lateral sclerosis (ALS), a fatal gain-of-function neurodegenerative disease whose molecular basis is unknown. To obtain insights into effects of the mutations on the folded and unfolded populations...

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Source

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Identifiers

PMID: 20184893
DOI: 10.1016/j.jmb.2010.02.034
PMCID: PMC3075925

Genes

SOD1

Provenance

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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Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species.PMID 20184893Read ↗

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 ↗

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

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Denaturational stress induces formation of zinc-deficient monomers of Cu,Zn superoxide dismutase: implications for pathogenesis in amyotrophic lateral sclerosis.Semantic proximity Read ↗

Mechanism and thermodynamics of guanidinium chloride-induced denaturation of ALS-associated mutant Cu,Zn superoxide dismutases.Semantic proximity Read ↗

Cu/Zn Superoxide Dismutase Forms Amyloid Fibrils under Near-Physiological Quiescent Conditions: The Roles of Disulfide Bonds and Effects of Denaturant.Semantic proximity Read ↗

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Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: decreased stability of the apo state.Semantic proximity Read ↗

Mutant SOD1 instability: implications for toxicity in amyotrophic lateral sclerosis.Semantic proximity Read ↗

Structural instability and Cu-dependent pro-oxidant activity acquired by the apo form of mutant SOD1 associated with amyotrophic lateral sclerosis.Semantic proximity Read ↗

Immature ALS-associated mutant superoxide dismutases form variable aggregate structures through distinct oligomerization processes.Semantic proximity Read ↗

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