Jean-Marc Taymans

The Parkinson's disease associated LRRK2 exhibits weaker in vitro phosphorylation of 4E-BP compared to autophosphorylation.

Distribution of PINK1 and LRRK2 in rat and mouse brain.

Comparative analysis of adeno-associated viral vector serotypes 1, 2, 5, 7, and 8 in mouse brain.

The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation.

The Parkinson's disease kinase LRRK2 autophosphorylates its GTPase domain at multiple sites.

Phosphorylation of ezrin/radixin/moesin proteins by LRRK2 promotes the rearrangement of actin cytoskeleton in neuronal morphogenesis.

Mechanisms in dominant parkinsonism: The toxic triangle of LRRK2, alpha-synuclein, and tau.

Inhibition of FK506 binding proteins reduces alpha-synuclein aggregation and Parkinson's disease-like pathology.

Immunohistochemical detection of transgene expression in the brain using small epitope tags.

Automated quantitative gait analysis in animal models of movement disorders.

Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant.

Kinases as targets for Parkinson's disease: from genetics to therapy.

LRRK2 kinase activity is dependent on LRRK2 GTP binding capacity but independent of LRRK2 GTP binding.

Expression, purification and preliminary biochemical and structural characterization of the leucine rich repeat namesake domain of leucine rich repeat kinase 2.

Biochemical characterization of highly purified leucine-rich repeat kinases 1 and 2 demonstrates formation of homodimers.

The GTPase function of LRRK2.

Phosphorylation of LRRK2: from kinase to substrate.

MicroRNA-205 regulates the expression of Parkinson's disease-related leucine-rich repeat kinase 2 protein.

Identification of protein phosphatase 1 as a regulator of the LRRK2 phosphorylation cycle.