Associated Papers
LRRK2 Phosphorylation, More Than an Epiphenomenon.
Marchand A et al.
Frontiers in Neuroscience, 2020
Lack of correlation between the kinase activity of LRRK2 harboring kinase-modifying mutations and its phosphorylation at Ser910, 935, and Ser955.
Ito G et al.
Plos One, 2014
Reevaluation of phosphorylation sites in the Parkinson disease-associated leucine-rich repeat kinase 2.
Li X et al.
The Journal of Biological Chemistry, 2010
GTPase activity plays a key role in the pathobiology of LRRK2.
Xiong Y et al.
Plos Genetics, 2010
The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation.
Greggio E et al.
The Journal of Biological Chemistry, 2008
Mechanistic insight into the dominant mode of the Parkinson's disease-associated G2019S LRRK2 mutation.
Luzón-Toro B et al.
Human Molecular Genetics, 2007
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