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Article

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

Proceedings of the National Academy of Sciences of the United States of America - 8 Feb 2011

Vassall Kenrick A, Stubbs Helen R, Primmer Heather A, Tong Ming Sze, Sullivan Sarah M, Sobering Ryan, Srinivasan Saipraveen, Briere Lee-Ann K, Dunn Stanley D, Colón Wilfredo, Meiering Elizabeth M

Abstract excerpt

Protein aggregation is a hallmark of many diseases, including amyotrophic lateral sclerosis (ALS), where aggregation of Cu/Zn superoxide dismutase (SOD1) is implicated in causing neurodegeneration. Recent studies have suggested that destabilization and aggregation of the most immature form of SOD1, the disulfide-reduced, unmetallated (apo) protein is particularly important in causing ALS. We report herein in...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 21257910
DOI: 10.1073/pnas.0913021108
PMCID: PMC3038722

Genes

SOD1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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