Characterization of a selective inhibitor of the Parkinson’s disease kinase LRRK2
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N. Gray | Qingsong Liu | Xianming Deng | A. Prescott | D. Alessi | Jiing-Dwan Lee | M. Patricelli | T. Nomanbhoy | N. Dzamko | Qingkai Yang | Paul Davies | Nicolas Dzamko
[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.