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

[1]  L. Petrucelli,et al.  Inhibitors of Leucine Rich Repeat Kinase 2 (LRRK2) Protect Against LRRK2-Models of Parkinson’s Disease , 2010, Nature Medicine.

[2]  A. Reith,et al.  Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser910/Ser935, disruption of 14-3-3 binding and altered cytoplasmic localization , 2010, The Biochemical journal.

[3]  A. Prescott,et al.  14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization , 2010, The Biochemical journal.

[4]  M. Farrer,et al.  LRRK2 and Parkinson disease. , 2010, Archives of neurology.

[5]  L. Cantley,et al.  Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's disease. , 2009, The Biochemical journal.

[6]  Richard Wade-Martins,et al.  LRRK2 regulates autophagic activity and localizes to specific membrane microdomains in a novel human genomic reporter cellular model. , 2009, Human molecular genetics.

[7]  Shu G. Chen,et al.  Leucine‐rich repeat kinase 2 (LRRK2): A key player in the pathogenesis of Parkinson's disease , 2009, Journal of neuroscience research.

[8]  B. Giasson,et al.  Identification of compounds that inhibit the kinase activity of leucine-rich repeat kinase 2. , 2009, Biochemical and biophysical research communications.

[9]  E. Brown,et al.  Investigation of leucine‐rich repeat kinase 2 , 2009, The FEBS journal.

[10]  M. Cookson,et al.  Leucine-rich repeat kinase 2 mutations and Parkinson’s disease: three questions , 2009, ASN neuro.

[11]  E. Tolosa,et al.  Phenotype, genotype, and worldwide genetic penetrance of LRRK2-associated Parkinson's disease: a case-control study , 2008, The Lancet Neurology.

[12]  P. Zarrinkar,et al.  High-throughput kinase profiling as a platform for drug discovery , 2008, Nature Reviews Drug Discovery.

[13]  Mindy I. Davis,et al.  A quantitative analysis of kinase inhibitor selectivity , 2008, Nature Biotechnology.

[14]  P. Cohen,et al.  The selectivity of protein kinase inhibitors: a further update. , 2007, The Biochemical journal.

[15]  R. Nichols,et al.  LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity. , 2007, The Biochemical journal.

[16]  Péter Lénárt,et al.  BI 2536, a Potent and Selective Inhibitor of Polo-like Kinase 1, Inhibits Tumor Growth In Vivo , 2007, Current Biology.

[17]  J. Peters,et al.  The Small-Molecule Inhibitor BI 2536 Reveals Novel Insights into Mitotic Roles of Polo-like Kinase 1 , 2007, Current Biology.

[18]  Helge Weissig,et al.  Functional interrogation of the kinome using nucleotide acyl phosphates. , 2007, Biochemistry.

[19]  David W. Miller,et al.  Kinase activity is required for the toxic effects of mutant LRRK2/dardarin , 2006, Neurobiology of Disease.

[20]  Acknowledgments , 2006, Molecular and Cellular Endocrinology.

[21]  L. Wodicka,et al.  A small molecule–kinase interaction map for clinical kinase inhibitors , 2005, Nature Biotechnology.

[22]  Thomas Meitinger,et al.  Mutations in LRRK2 Cause Autosomal-Dominant Parkinsonism with Pleomorphic Pathology , 2004, Neuron.

[23]  Andrew Lees,et al.  Cloning of the Gene Containing Mutations that Cause PARK8-Linked Parkinson's Disease , 2004, Neuron.

[24]  Y. Durocher,et al.  High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells. , 2002, Nucleic acids research.

[25]  A Aitken,et al.  Phosphorylation-dependent interactions between enzymes of plant metabolism and 14-3-3 proteins. , 1999, The Plant journal : for cell and molecular biology.

[26]  J. Abe,et al.  Big Mitogen-activated Protein Kinase 1 (BMK1) Is a Redox-sensitive Kinase* , 1996, The Journal of Biological Chemistry.

[27]  Philip R. Cohen,et al.  PD 098059 Is a Specific Inhibitor of the Activation of Mitogen-activated Protein Kinase Kinase in Vitro and in Vivo(*) , 1995, The Journal of Biological Chemistry.

[28]  Philip R. Cohen,et al.  SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin‐1 , 1995, FEBS letters.

[29]  K Y Hui,et al.  A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002). , 1994, The Journal of biological chemistry.