Article
Toxicity of familial ALS-linked SOD1 mutants from selective recruitment to spinal mitochondria.
Neuron - 8 Jul 2004
Liu Jian, Lillo Concepción, Jonsson P Andreas, Vande Velde Christine, Ward Christopher M, Miller Timothy M, Subramaniam Jamuna R, Rothstein Jeffery D, Marklund Stefan, Andersen Peter M, Brännström Thomas, Gredal Ole, Wong Philip C, Williams David S, Cleveland Don W
Abstract excerpt
One cause of amyotrophic lateral sclerosis (ALS) is mutation in ubiquitously expressed copper/zinc superoxide dismutase (SOD1), but the mechanism of toxicity to motor neurons is unknown. Multiple disease-causing mutants, but not wild-type SOD1, are now demonstrated to be recruited to mitochondria, but only in affected tissues. This is independent of the copper chaperone for SOD1 and dismutase activity. Highly...
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