Ser1292 Autophosphorylation Is an Indicator of LRRK2 Kinase Activity and Contributes to the Cellular Effects of PD Mutations
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K. Scearce-Levie | M. P. van der Brug | Xingrong Liu | John G. Moffat | Haitao Zhu | Z. Yue | D. Kirkpatrick | Huifen Chen | Xianting Li | Fang Cai | Marcel P. van der Brug | D. Burdick | Z. Sweeney | Daisy J. Bustos | Anthony A. Estrada | T. Kleinheinz | Sara L. Dominguez | Jason Drummond | Janet Gunzner-Toste | Zejuan Sheng | Shuo Zhang | Xiaolin Zhang | Hilda Solanoy | Claire E. Le Pichon | Xiao Ding | K. Scearce‐Levie | Qinghua Song | Tracy Kleinheinz | Zhenyu Yue
[1] J. Yates,et al. Progressive degeneration of human neural stem cells caused by pathogenic LRRK2 , 2012, Nature.
[2] Jason Drummond,et al. Discovery of selective LRRK2 inhibitors guided by computational analysis and molecular modeling. , 2012, Journal of medicinal chemistry.
[3] Mark Ellisman,et al. LRRK2 Parkinson disease mutations enhance its microtubule association. , 2011, Human molecular genetics.
[4] Jing Zhao,et al. Phosphorylation of LRRK2 serines 955 and 973 is disrupted by Parkinson’s disease mutations and LRRK2 pharmacological inhibition , 2012, Journal of neurochemistry.
[5] J. Sanders,et al. Leucine-Rich Repeat Kinase 2 (LRRK2) Cellular Biology: A Review of Recent Advances in Identifying Physiological Substrates and Cellular Functions , 2011, Journal of neurogenetics.
[6] Masaaki Komatsu,et al. Autophagy: Renovation of Cells and Tissues , 2011, Cell.
[7] G. Drewes,et al. Chemoproteomics-based design of potent LRRK2-selective lead compounds that attenuate Parkinson's disease-related toxicity in human neurons. , 2011, ACS chemical biology.
[8] G. Churchill,et al. Leucine-rich repeat kinase 2 regulates autophagy through a calcium-dependent pathway involving NAADP , 2011, Human molecular genetics.
[9] A. West,et al. Autophosphorylation in the leucine-rich repeat kinase 2 (LRRK2) GTPase domain modifies kinase and GTP-binding activities. , 2011, Journal of molecular biology.
[10] M. Cookson,et al. LRRK2 Kinase Activity Is Dependent on LRRK2 GTP Binding Capacity but Independent of LRRK2 GTP Binding , 2011, PloS one.
[11] C. Schnell,et al. LRRK2 protein levels are determined by kinase function and are crucial for kidney and lung homeostasis in mice , 2011, Human molecular genetics.
[12] M. L. Lachenmayer,et al. Genetic LRRK2 models of Parkinson's disease: Dissecting the pathogenic pathway and exploring clinical applications , 2011, Movement disorders : official journal of the Movement Disorder Society.
[13] Paola Piccini,et al. Priorities in Parkinson's disease research , 2011, Nature Reviews Drug Discovery.
[14] Y. Liu,et al. Dopaminergic Neuronal Loss, Reduced Neurite Complexity and Autophagic Abnormalities in Transgenic Mice Expressing G2019S Mutant LRRK2 , 2011, PloS one.
[15] N. Gray,et al. Characterization of a selective inhibitor of the Parkinson’s disease kinase LRRK2 , 2011, Nature chemical biology.
[16] V. Baekelandt,et al. Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant , 2011, Journal of neurochemistry.
[17] Edward L. Huttlin,et al. A Tissue-Specific Atlas of Mouse Protein Phosphorylation and Expression , 2010, Cell.
[18] Mark R. Cookson,et al. The role of leucine-rich repeat kinase 2 (LRRK2) in Parkinson's disease , 2010, Nature Reviews Neuroscience.
[19] R. Kelley,et al. Improved Quantitative Mass Spectrometry Methods for Characterizing Complex Ubiquitin Signals , 2010, Molecular & Cellular Proteomics.
[20] 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.
[21] M. Farrer,et al. LRRK2 and Parkinson disease. , 2010, Archives of neurology.
[22] Yichin Liu,et al. Differential effects of divalent manganese and magnesium on the kinase activity of leucine-rich repeat kinase 2 (LRRK2). , 2010, Biochemistry.
[23] M. Glicksman,et al. Kinetic mechanistic studies of wild-type leucine-rich repeat kinase 2: characterization of the kinase and GTPase activities. , 2010, Biochemistry.
[24] M. Ueffing,et al. 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, Journal of proteome research.
[25] J. Buxbaum,et al. Enhanced Striatal Dopamine Transmission and Motor Performance with LRRK2 Overexpression in Mice Is Eliminated by Familial Parkinson's Disease Mutation G2019S , 2010, The Journal of Neuroscience.
[26] Yusuke Nakamura,et al. Genome-wide association study identifies common variants at four loci as genetic risk factors for Parkinson's disease , 2009, Nature Genetics.
[27] M. Cookson,et al. The Parkinson's disease kinase LRRK2 autophosphorylates its GTPase domain at multiple sites. , 2009, Biochemical and biophysical research communications.
[28] L. Cantley,et al. Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's disease. , 2009, The Biochemical journal.
[29] 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.
[30] T. Iwatsubo,et al. Identification of the autophosphorylation sites of LRRK2. , 2009, Biochemistry.
[31] Sonja W. Scholz,et al. Genome-Wide Association Study reveals genetic risk underlying Parkinson’s disease , 2009, Nature Genetics.
[32] M. Cookson,et al. Leucine-rich repeat kinase 2 mutations and Parkinson’s disease: three questions , 2009, ASN neuro.
[33] C. Chu,et al. Role of autophagy in G2019S‐LRRK2‐associated neurite shortening in differentiated SH‐SY5Y cells , 2008, Journal of neurochemistry.
[34] Yuliang Wu,et al. Direct binding of α‐actinin enhances TRPP3 channel activity , 2007 .
[35] C. Olanow,et al. Leucine‐rich repeat kinase 2 (LRRK2)/PARK8 possesses GTPase activity that is altered in familial Parkinson’s disease R1441C/G mutants , 2007, Journal of neurochemistry.
[36] Shu G. Chen,et al. The Parkinson's disease-associated protein, leucine-rich repeat kinase 2 (LRRK2), is an authentic GTPase that stimulates kinase activity. , 2007, Experimental cell research.
[37] R. Nichols,et al. LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity. , 2007, The Biochemical journal.
[38] M. Cookson,et al. The R1441C mutation of LRRK2 disrupts GTP hydrolysis. , 2007, Biochemical and biophysical research communications.
[39] K. Lim,et al. Parkinson's disease-associated mutations in LRRK2 link enhanced GTP-binding and kinase activities to neuronal toxicity. , 2007, Human molecular genetics.
[40] T. Katada,et al. GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease. , 2007, Biochemistry.
[41] A. Singleton,et al. A common genetic factor for Parkinson disease in ethnic Chinese population in Taiwan , 2006, BMC neurology.
[42] A. Abeliovich,et al. The Familial Parkinsonism Gene LRRK2 Regulates Neurite Process Morphology , 2006, Neuron.
[43] C. Ross,et al. Kinase activity of mutant LRRK2 mediates neuronal toxicity , 2006, Nature Neuroscience.
[44] Steven P Gygi,et al. A probability-based approach for high-throughput protein phosphorylation analysis and site localization , 2006, Nature Biotechnology.
[45] David W. Miller,et al. Kinase activity is required for the toxic effects of mutant LRRK2/dardarin , 2006, Neurobiology of Disease.
[46] P. Dyck,et al. Vascular endothelial growth factor and POEMS , 2006, Neurology.
[47] C. Ross,et al. Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[48] S. Gygi,et al. Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[49] A. Jon Stoessl,et al. Etiology of Parkinson's Disease , 2003, Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques.
[50] M. Gossen,et al. Transcriptional activation by tetracyclines in mammalian cells. , 1995, Science.
[51] G. Brewer,et al. Optimized survival of hippocampal neurons in B27‐supplemented neurobasal™, a new serum‐free medium combination , 1993, Journal of neuroscience research.
[52] L. Cantley,et al. Substrate specificity and inhibitors of LRRK 2 , a protein kinase mutated in Parkinson ’ s disease , 2009 .