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Article

Characterization of the activity, aggregation, and toxicity of heterodimers of WT and ALS-associated mutant Sod1.

Proceedings of the National Academy of Sciences of the United States of America - 17 Dec 2019

Brasil Aline de Araújo, de Carvalho Mariana Dias Castela, Gerhardt Ellen, Queiroz Daniela Dias, Pereira Marcos Dias, Outeiro Tiago Fleming, Eleutherio Elis Cristina Araujo

Abstract excerpt

Mutations in Cu/Zn superoxide dismutase (Sod1) have been reported in both familial and sporadic amyotrophic lateral sclerosis (ALS). In this study, we investigated the behavior of heteromeric combinations of wild-type (WT) and mutant Sod1 proteins A4V, L38V, G93A, and G93C in human cells. We showed that both WT and mutant Sod1 formed dimers and oligomers, but only mutant Sod1 accumulated in intracellular...

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Identifiers

PMID: 31796595
DOI: 10.1073/pnas.1902483116
PMCID: PMC6926019

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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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