Oxidation versus aggregation - How do SOD1 mutants cause ALS?

Nature Medicine

Volumn 6, Issue 12, 2000, Pages 1320-1321

  Cleveland, D W ^a   Liu, J ^a  

^a LUDWIG INSTITUTE FOR CANCER RESEARCH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COPPER; MUTANT PROTEIN; NITRIC OXIDE; SUPEROXIDE; SUPEROXIDE DISMUTASE;

AMYOTROPHIC LATERAL SCLEROSIS; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; APOPTOSIS; CHEMICAL MUTAGENESIS; CONTROLLED STUDY; CYTOLOGY; ENZYME CONFORMATION; MOTONEURON; MOUSE; NERVE CELL NECROSIS; NONHUMAN; OXIDATION; PRIORITY JOURNAL; SHORT SURVEY; TRANSGENIC MOUSE;

AMYOTROPHIC LATERAL SCLEROSIS; ANIMALS; CELL DEATH; MICE; MODELS, BIOLOGICAL; MOTOR NEURONS; MUTATION; OXIDATION-REDUCTION; SUPEROXIDE DISMUTASE;

EID: 0034530030     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/82122     Document Type: Short Survey

References (11)

1. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
2. From Charcot to SOD1: Mechanisms ot selective motor neuron death in ALS
3. Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1
4. Induction of nitric oxide-dependent apoptosis in motor neurons by zinc- deficient superoxide dismutase
5. Toxicity of ALS-linked SOD1 mutants
6. The copper chaperone for superoxide dismutase
7. Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase
8. Motor neuron disease is not ameliorated in mutant SOD1 transgenic mice deficient in copper chaperone for SOD1
9. Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis
10. Formation of high molecular weight complexes of mutant Cu,Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis
11. Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS