α-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease

Nature Neuroscience

Volumn 8, Issue 5, 2005, Pages 657-663

  Chen, Li ^a   Feany, Mel B ^a  

^a BRIGHAM AND WOMEN S HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ALPHA SYNUCLEIN; ASPARTIC ACID; G PROTEIN COUPLED RECEPTOR KINASE 2; SERINE;

AMINO ACID SUBSTITUTION; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CELL INCLUSION; CONTROLLED STUDY; CORRELATION ANALYSIS; DISEASE MODEL; DOPAMINERGIC NERVE CELL; DROSOPHILA; IN VIVO STUDY; LEWY BODY; NERVE DEGENERATION; NEUROPROTECTION; NEUROTOXICITY; NONHUMAN; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; SITE DIRECTED MUTAGENESIS;

ALPHA-SYNUCLEIN; AMINO ACID SUBSTITUTION; ANIMALS; ANIMALS, GENETICALLY MODIFIED; ASPARTIC ACID; BETA-ADRENERGIC RECEPTOR KINASE; BRAIN; CENTRAL NERVOUS SYSTEM; CYCLIC AMP-DEPENDENT PROTEIN KINASES; DISEASE MODELS, ANIMAL; DOPAMINE; DROSOPHILA; DROSOPHILA PROTEINS; INCLUSION BODIES; NERVE DEGENERATION; NERVE TISSUE PROTEINS; NEURONS; PARKINSON DISEASE; PHOSPHORYLATION; POINT MUTATION; RETINA; SERINE; SYNUCLEINS;

EID: 17844406856     PISSN: 10976256     EISSN: None     Source Type: Journal    
DOI: 10.1038/nn1443     Document Type: Article

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