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

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

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

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Ku-0063794 is a specific inhibitor of the mammalian target of rapamycin (mTOR)

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

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Identification of the Autophosphorylation Sites of LRRK2

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LRRK2 regulates autophagic activity and localizes to specific membrane microdomains in a novel human genomic reporter cellular model

(2009) Javier Alegre-Abarrategui et al.   HUMAN MOLECULAR GENETICS

Characterization of Rictor Phosphorylation Sites Reveals Direct Regulation of mTOR Complex 2 by S6K1

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Biological properties of potent inhibitors of class I phosphatidylinositide 3-kinases: from PI-103 through PI-540, PI-620 to the oral agent GDC-0941

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Identification of compounds that inhibit the kinase activity of leucine-rich repeat kinase 2

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

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The discovery of the benzhydroxamate MEK inhibitors CI-1040 and PD 0325901

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Investigation of leucine-rich repeat kinase 2

(2008) Vasanti S. Anand et al.   FEBS Journal

Solid Tumor Proteome and Phosphoproteome Analysis by High Resolution Mass Spectrometry

(2008) Sara Zanivan et al.   JOURNAL OF PROTEOME RESEARCH

LRRK2 Gly2019Ser penetrance in Arab–Berber patients from Tunisia: a case-control genetic study

(2008) Mary M Hulihan et al.   LANCET NEUROLOGY

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

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Identification of RIP1 kinase as a specific cellular target of necrostatins

(2008) Alexei Degterev et al.   Nature Chemical Biology