Discover Community Create You

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

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

Journal of molecular biology - 7 Nov 2008

Mulligan Vikram Khipple, Kerman Aaron, Ho Sylvia, Chakrabartty Avijit

Abstract excerpt

Mutations in the Cu,Zn superoxide dismutase (SOD1) cause a subset of amyotrophic lateral sclerosis cases. SOD1 is a homodimer in which each monomer binds one copper atom and one zinc atom. Mutation is believed to increase the conformational flexibility of SOD1, giving rise to a misfolded SOD1 population with novel cytotoxic properties. While SOD1's metal ligands affect its stability greatly, little is known about...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amyotrophic Lateral Sclerosis
Share to Copper

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Dimerization

Share to Guanidine

Share to Protein Denaturation

Share to Superoxide Dismutase

Share to Tryptophan

Source

Identifiers

PMID: 18761352
DOI: 10.1016/j.jmb.2008.08.024

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Denaturational stress induces formation of zinc-deficient monomers of Cu,Zn superoxide dismutase: implications for pathogenesis in amyotrophic lateral sclerosis.PMID 18761352Read ↗

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

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

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

Mutations in Superoxide Dismutase 1 (Sod1) Linked to Familial Amyotrophic Lateral Sclerosis Can Disrupt High-Affinity Zinc-Binding Promoted by the Copper Chaperone for Sod1 (Ccs).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 ↗

Pathogenic superoxide dismutase structure, folding, aggregation and turnover.Semantic proximity Read ↗

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

The structure, redox chemistry and motor neuron toxicity of heterodimeric zinc-deficient SOD1-implications for the toxic gain of function observed in ALS.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 ↗

Metal distribution in Cu/Zn-superoxide dismutase revealed by native mass spectrometry.Semantic proximity Read ↗

Metal migration and subunit swapping in ALS-linked SOD1: Zn2+ transfer between mutant and wild-type occurs faster than the rate of heterodimerization.Semantic proximity Read ↗

Voltage-Induced Misfolding of Zinc-Replete ALS Mutant Superoxide Dismutase-1.Semantic proximity Read ↗

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