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Article

Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization.

Proceedings of the National Academy of Sciences of the United States of America - 27 Oct 2009

Teilum Kaare, Smith Melanie H, Schulz Eike, Christensen Lea C, Solomentsev Gleb, Oliveberg Mikael, Akke Mikael

Abstract excerpt

Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease linked to the misfolding of Cu/Zn superoxide dismutase (SOD1). ALS-related defects in SOD1 result in a gain of toxic function that coincides with aberrant oligomerization. The structural events triggering oligomerization have remained enigmatic, however, as is the case in other protein-misfolding diseases. Here, we target the critical...

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Source

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Identifiers

PMID: 19828437
DOI: 10.1073/pnas.0907387106
PMCID: PMC2775296

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.

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