LRRK2 dephosphorylation increases its ubiquitination

Biochemical Journal

Volumn 469, Issue 1, 2015, Pages 107-120

  Zhao, Jing ^a   Molitor, Tyler P ^a   Langston, J William ^a   Nichols, R Jeremy ^a  

^a PARKINSON S INSTITUTE   (United States)

Author keywords

Kinase; Kinase inhibitor; Parkinson's disease; Phosphatase; Ubiquitin

Indexed keywords

CALYCULIN A; DEUBIQUITINASE; LEUCINE RICH REPEAT KINASE 2; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; ENZYME INHIBITOR; LRRK2 PROTEIN, HUMAN; LRRK2 PROTEIN, MOUSE; OXAZOLE DERIVATIVE; PROTEIN 14 3 3; PROTEIN SERINE THREONINE KINASE;

ANIMAL CELL; ARTICLE; AUTOPHAGY; CONTROLLED STUDY; ENZYME INHIBITION; GENE EXPRESSION SYSTEM; HUMAN; HUMAN CELL; LOSS OF FUNCTION MUTATION; MOUSE; NONHUMAN; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DEPHOSPHORYLATION; PROTEIN STABILITY; UBIQUITINATION; AMINO ACID SUBSTITUTION; ANIMAL; DRUG EFFECTS; GENETICS; HEK293 CELL LINE; METABOLISM; MISSENSE MUTATION; PHOSPHORYLATION; PHYSIOLOGY;

ANIMALIA;

14-3-3 PROTEINS; AMINO ACID SUBSTITUTION; ANIMALS; ENZYME INHIBITORS; HEK293 CELLS; HUMANS; MICE; MUTATION, MISSENSE; OXAZOLES; PHOSPHORYLATION; PROTEIN-SERINE-THREONINE KINASES; UBIQUITINATION;

EID: 84935077167     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20141305     Document Type: Article

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