S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function

Science

Volumn 304, Issue 5675, 2004, Pages 1328-1331

  Chung, Kenny K K ^a   Thomas, Bobby ^a   Li, Xiaojie ^a   Pletnikova, Olga ^a   Troncoso, Juan C ^a   Marsh, Laura ^a   Dawson, Valina L ^a   Dawson, Ted M ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BRAIN; DISEASE CONTROL; FUNCTIONS; PATIENT MONITORING;

MOUSE MODEL; PARKIN SUBSTRATES;

ENZYMES;

PARKIN; UBIQUITIN PROTEIN LIGASE;

PROTEIN;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BRAIN; CELL SURVIVAL; CONTROLLED STUDY; DOPAMINERGIC NERVE CELL; EMBRYO; ENZYME INHIBITION; HUMAN; HUMAN CELL; HUMAN TISSUE; IN VITRO STUDY; IN VIVO STUDY; LEWY BODY; MOUSE; NERVE DEGENERATION; NEUROPROTECTION; NITROSYLATION; NONHUMAN; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN FUNCTION; UBIQUITINATION;

ALZHEIMER DISEASE; ANIMALS; BRAIN; CARRIER PROTEINS; CATALYTIC DOMAIN; CELL DEATH; CELL LINE; CYSTEINE PROTEINASE INHIBITORS; HUMANS; LEWY BODY DISEASE; MICE; MICE, KNOCKOUT; MPTP POISONING; NERVE TISSUE PROTEINS; NITRIC OXIDE; NITRIC OXIDE DONORS; NITRIC OXIDE SYNTHASE; PARKINSON DISEASE; RECOMBINANT PROTEINS; SYNUCLEINS; TRANSFECTION; UBIQUITIN; UBIQUITIN-PROTEIN LIGASES;

ANIMALIA;

EID: 2542534741     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1093891     Document Type: Article

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34. Supported by U.S. Public Health Service grant NS38377, the Edward D. and Anna Mitchell Family Foundation, and the Mary Lou McIlhaney Scholar Award. We thank H. Ischiropoulos, R. Cole, and C. Lowenstein for helpful comments and advice on detection of S-nitrosylation.