LRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site status

Frontiers in Molecular Neuroscience

Volumn 7, Issue JUNE, 2014, Pages

  Reynolds, April ^a   Doggett, Elizabeth A ^a   Riddle, Steve M ^b   Lebakken, Connie S ^b   Jeremy Nichols, R ^a  

^a PARKINSON S INSTITUTE   (United States)

^b Thermo Fisher Scientific   (United States)

Author keywords

GTPase; Kinase; Kinase inhibitor; LRRK2; Parkinson's disease; Phosphorylation

Indexed keywords

CALYCULIN A; CYCLIC AMP; LEUCINE RICH REPEAT KINASE 2; MONOCLONAL ANTIBODY; OKADAIC ACID; SERINE; THREONINE;

ARTICLE; AUTOPHOSPHORYLATION; CELL DENSITY; CHEMICAL ANALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME ISOLATION; GENE MUTATION; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; IMMUNOAFFINITY CHROMATOGRAPHY; IMMUNOBLOTTING; IMMUNOPRECIPITATION; LYMPHOBLASTOID CELL; MUTAGENESIS; PARKINSON DISEASE; SIGNAL TRANSDUCTION;

EID: 84940344193     PISSN: 16625099     EISSN: None     Source Type: Journal    
DOI: 10.3389/fnmol.2014.00054     Document Type: Article

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