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Article

Disease-associated mutations at copper ligand histidine residues of superoxide dismutase 1 diminish the binding of copper and compromise dimer stability.

The Journal of biological chemistry - 5 Jan 2007

Wang Jiou, Caruano-Yzermans Amy, Rodriguez Angela, Scheurmann Jonathan P, Slunt Hilda H, Cao Xiaohang, Gitlin Jonathan, Hart P John, Borchelt David R

Abstract excerpt

A subset of superoxide dismutase 1 (Cu/Zn-SOD1) mutants that cause familial amyotrophic lateral sclerosis (FALS) have heightened reactivity with (-)ONOO and H(2)O(2) in vitro. This reactivity requires a copper ion bound in the active site and is a suggested mechanism of motor neuron injury. However, we have found that transgenic mice that express SOD1-H46R/H48Q, which combines natural FALS mutations at ligands...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 17092942
DOI: 10.1074/jbc.M604503200
PMCID: PMC2757151

Genes

SOD1

Variants

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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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