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Increased affinity for copper mediated by cysteine 111 in forms of mutant superoxide dismutase 1 linked to amyotrophic lateral sclerosis.

Free radical biology & medicine - 15 May 2007

Watanabe Shohei, Nagano Seiichi, Duce James, Kiaei Mahmoud, Li Qiao-Xin, Tucker Stephanie M, Tiwari Ashutosh, Brown Robert H, Beal M Flint, Hayward Lawrence J, Culotta Valeria C, Yoshihara Satoshi, Sakoda Saburo, Bush Ashley I

Abstract excerpt

Mutations in Cu,Zn-superoxide dismutase (SOD1) cause familial amyotrophic lateral sclerosis (ALS). It has been proposed that neuronal cell death might occur due to inappropriately increased Cu interaction with mutant SOD1. Using Cu immobilized metal-affinity chromatography (IMAC), we showed that mutant SOD1 (A4V, G85R, and G93A) expressed in transfected COS7 cells, transgenic mouse spinal cord tissue, and...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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PMID: 17448900
DOI: 10.1016/j.freeradbiomed.2007.02.004

Genes

SOD1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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