Phosphorylation of LRRK2 serines 955 and 973 is disrupted by Parkinson’s disease mutations and LRRK2 pharmacological inhibition

Rac1 Protein Rescues Neurite Retraction Caused by G2019S Leucine-rich Repeat Kinase 2 (LRRK2)

(2011) Diane Chan et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Autophosphorylation in the Leucine-Rich Repeat Kinase 2 (LRRK2) GTPase Domain Modifies Kinase and GTP-Binding Activities

(2011) Philip J. Webber et al.   JOURNAL OF MOLECULAR BIOLOGY

Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2

(2011) Xianming Deng et al.   Nature Chemical Biology

On the Road to Leucine-Rich Repeat Kinase 2 Signalling: Evidence from Cellular and in vivo Studies

(2011) V. Daniëls et al.   NEUROSIGNALS

LRRK2 Kinase Activity Is Dependent on LRRK2 GTP Binding Capacity but Independent of LRRK2 GTP Binding

(2011) Jean-Marc Taymans et al.   PLoS One

LRRK2 signaling pathways: the key to unlocking neurodegeneration?

(2011) Daniel C. Berwick et al.   TRENDS IN CELL BIOLOGY

Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser910/Ser935, disruption of 14-3-3 binding and altered cytoplasmic localization

(2010) Nicolas Dzamko et al.   BIOCHEMICAL JOURNAL

14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization

(2010) R. Jeremy Nichols et al.   BIOCHEMICAL JOURNAL

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

(2010) Jean-Marc Taymans et al.   BIOESSAYS

Leucine-rich repeat kinase 2 induces α-synuclein expression via the extracellular signal-regulated kinase pathway

(2010) Iria Carballo-Carbajal et al.   CELLULAR SIGNALLING

Phosphopeptide Analysis Reveals Two Discrete Clusters of Phosphorylation in the N-Terminus and the Roc Domain of the Parkinson-Disease Associated Protein Kinase LRRK2

(2010) Christian Johannes Gloeckner et al.   JOURNAL OF PROTEOME RESEARCH

Identification and Characterization of a Leucine-Rich Repeat Kinase 2 (LRRK2) Consensus Phosphorylation Motif

(2010) Pooja P. Pungaliya et al.   PLoS One

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

(2009) Elisa Greggio et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's disease

(2009) R. Jeremy Nichols et al.   BIOCHEMICAL JOURNAL

Identification of the Autophosphorylation Sites of LRRK2

(2009) Shogo Kamikawaji et al.   BIOCHEMISTRY

Regulation of LRRK2 Stability by the E3 Ubiquitin Ligase CHIP

(2009) Xiaodong Ding et al.   PLoS One

CHIP regulates leucine-rich repeat kinase-2 ubiquitination, degradation, and toxicity

(2009) Han Seok Ko et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Zeroing in on LRRK2-linked pathogenic mechanisms in Parkinson's disease

(2008) Saskia Biskup et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE

The Chaperone Activity of Heat Shock Protein 90 Is Critical for Maintaining the Stability of Leucine-Rich Repeat Kinase 2

(2008) L. Wang et al.   JOURNAL OF NEUROSCIENCE

Phenotype, genotype, and worldwide genetic penetrance of LRRK2-associated Parkinson's disease: a case-control study

(2008) Daniel G Healy et al.   LANCET NEUROLOGY