Article
Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis.
The Journal of biological chemistry - 3 May 2002
Hayward Lawrence J, Rodriguez Jorge A, Kim Ji W, Tiwari Ashutosh, Goto Joy J, Cabelli Diane E, Valentine Joan Selverstone, Brown Robert H
Abstract excerpt
Over 90 different mutations in the gene encoding copper/zinc superoxide dismutase (SOD1) cause approximately 2% of amyotrophic lateral sclerosis (ALS) cases by an unknown mechanism. We engineered 14 different human ALS-related SOD1 mutants and obtained high yields of biologically metallated proteins from an Sf21 insect cell expression system. Both the wild type and mutant "as isolated" SOD1 variants were...
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