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Article

Fully metallated S134N Cu,Zn-superoxide dismutase displays abnormal mobility and intermolecular contacts in solution.

The Journal of biological chemistry - 28 Oct 2005

Banci Lucia, Bertini Ivano, D'Amelio Nicola, Gaggelli Elena, Libralesso Elisa, Matecko Irena, Turano Paola, Valentine Joan Selverstone

Abstract excerpt

S134N copper-zinc superoxide dismutase (SOD1) is one of the many mutant SOD1 proteins known to cause familial amyotrophic lateral sclerosis. Earlier studies demonstrated that partially metal-deficient S134N SOD1 crystallized in filament-like arrays with abnormal contacts between the individual protein molecules. Because protein aggregation is implicated in SOD1-linked familial amyotrophic lateral sclerosis,...

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Identifiers

PMID: 16105836
DOI: 10.1074/jbc.M506637200

Genes

SOD1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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