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Article

Structural characterization of zinc-deficient human superoxide dismutase and implications for ALS.

Journal of molecular biology - 2 Nov 2007

Roberts Blaine R, Tainer John A, Getzoff Elizabeth D, Malencik Dean A, Anderson Sonia R, Bomben Valerie C, Meyers Kathrin R, Karplus P Andrew, Beckman Joseph S

Abstract excerpt

Over 130 mutations to copper, zinc superoxide dismutase (SOD) are implicated in the selective death of motor neurons found in 25% of patients with familial amyotrophic lateral sclerosis (ALS). Despite their widespread distribution, ALS mutations appear positioned to cause structural and misfolding defects. Such defects decrease SOD's affinity for zinc, and loss of zinc from SOD is sufficient to induce apoptosis...

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

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Identifiers

PMID: 17888947
DOI: 10.1016/j.jmb.2007.07.043
PMCID: PMC2175016

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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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