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Article

Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase.

Proceedings of the National Academy of Sciences of the United States of America - 12 Jun 2007

Strange Richard W, Yong Chin W, Smith William, Hasnain S Samar

Abstract excerpt

Mutations of the gene encoding Cu-Zn superoxide dismutase (SOD1) cause 20% of the familial cases of the progressive neurodegenerative disease ALS. A growing body of evidence suggests that in familial ALS (FALS) it is the molecular behavior of the metal-depleted SOD1 dimer that leads to a gain of toxic properties by misfolding, unfolding, and aggregation. Structural studies have so far provided static snapshots on...

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Identifiers

PMID: 17548825
DOI: 10.1073/pnas.0703857104
PMCID: PMC1885824

Genes

SOD1

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Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase.PMID 17548825Read ↗

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