Associated Papers
LRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site status.
Reynolds A et al.
Frontiers in Molecular Neuroscience, 2014
25009464 (PubMed )
Supplement: DataSheet1.PDF
Differential effects of familial parkinson mutations in LRRK2 revealed by a systematic analysis of autophosphorylation.
Kamikawaji S et al.
Biochemistry, 2013
Deep sequencing of the LRRK2 gene in 14,002 individuals reveals evidence of purifying selection and independent origin of the p.Arg1628Pro mutation in Europe.
Rubio JP et al.
Human Mutation, 2012
Phosphorylation of LRRK2 serines 955 and 973 is disrupted by Parkinson's disease mutations and LRRK2 pharmacological inhibition.
Doggett EA et al.
Journal of Neurochemistry, 2012
Identification of the autophosphorylation sites of LRRK2.
Kamikawaji S et al.
Biochemistry, 2009
The Parkinson's disease kinase LRRK2 autophosphorylates its GTPase domain at multiple sites.
Greggio E et al.
Biochemical and Biophysical Research Communications, 2009
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