Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

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...

Topics

Amyotrophic Lateral Sclerosis
Crystallography, X-Ray
Disulfides
Enzyme Stability
Humans
Mutation
Oxidation-Reduction
Protein Folding
Protein Multimerization
Ribosomes
Superoxide Dismutase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Superoxide Dismutase-1

Zinc

Source

Open in PubMed Open full text

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 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

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 ↗

ALS-causing SOD1 mutations promote production of copper-deficient misfolded species.Semantic proximity Read ↗

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 ↗

SOD1 aggregation and ALS: role of metallation states and disulfide status.Semantic proximity Read ↗

The effects of glutaredoxin and copper activation pathways on the disulfide and stability of Cu,Zn superoxide dismutase.Semantic proximity Read ↗

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 ↗

⌁Select a neighboring publication to make it the new centre.