Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2.
about
Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of ParkinsonismRibosomal protein s15 phosphorylation mediates LRRK2 neurodegeneration in Parkinson's diseaseLRRK2 functions as a Wnt signaling scaffold, bridging cytosolic proteins and membrane-localized LRP6Biochemical characterization of highly purified leucine-rich repeat kinases 1 and 2 demonstrates formation of homodimersLRRK2 kinase activity regulates synaptic vesicle trafficking and neurotransmitter release through modulation of LRRK2 macro-molecular complexDifferential protein-protein interactions of LRRK1 and LRRK2 indicate roles in distinct cellular signaling pathwaysLRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site statusProgressive degeneration of human neural stem cells caused by pathogenic LRRK2Dysregulation of lysosomal morphology by pathogenic LRRK2 is corrected by TPC2 inhibitionArfGAP1 is a GTPase activating protein for LRRK2: reciprocal regulation of ArfGAP1 by LRRK2Phosphorylation of LRRK2 by casein kinase 1α regulates trans-Golgi clustering via differential interaction with ARHGEF7A direct interaction between leucine-rich repeat kinase 2 and specific β-tubulin isoforms regulates tubulin acetylationIdentification of protein phosphatase 1 as a regulator of the LRRK2 phosphorylation cycleMutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodiesLRRK2 regulates synaptogenesis and dopamine receptor activation through modulation of PKA activityThe G2385R variant of leucine-rich repeat kinase 2 associated with Parkinson's disease is a partial loss-of-function mutationG2019S leucine-rich repeat kinase 2 causes uncoupling protein-mediated mitochondrial depolarizationActivation Mechanism of LRRK2 and Its Cellular Functions in Parkinson's DiseaseCurrent understanding of LRRK2 in Parkinson's disease: biochemical and structural features and inhibitor designThe complex relationships between microglia, alpha-synuclein, and LRRK2 in Parkinson's diseaseTen years and counting: moving leucine-rich repeat kinase 2 inhibitors to the clinicHeterogeneity of leucine-rich repeat kinase 2 mutations: genetics, mechanisms and therapeutic implicationsThe role of the LRRK2 gene in ParkinsonismIs inhibition of kinase activity the only therapeutic strategy for LRRK2-associated Parkinson's disease?No dopamine cell loss or changes in cytoskeleton function in transgenic mice expressing physiological levels of wild type or G2019S mutant LRRK2 and in human fibroblastsLeucine-rich repeat kinase 2 (LRRK2)-deficient rats exhibit renal tubule injury and perturbations in metabolic and immunological homeostasisLRRK2 G2019S mutation attenuates microglial motility by inhibiting focal adhesion kinase.Selective Aurora Kinase Inhibitors Identified Using a Taxol-Induced Checkpoint Sensitivity ScreenX-ray Crystal Structure of ERK5 (MAPK7) in Complex with a Specific InhibitorRoco kinase structures give insights into the mechanism of Parkinson disease-related leucine-rich-repeat kinase 2 mutationsParkinson's disease and immune system: is the culprit LRRKing in the periphery?LRRK2 inhibitors and their potential in the treatment of Parkinson's disease: current perspectivesInhibition of LRRK2 kinase activity stimulates macroautophagyThe IkappaB kinase family phosphorylates the Parkinson's disease kinase LRRK2 at Ser935 and Ser910 during Toll-like receptor signalingScreening for novel LRRK2 inhibitors using a high-throughput TR-FRET cellular assay for LRRK2 Ser935 phosphorylationA novel GTP-binding inhibitor, FX2149, attenuates LRRK2 toxicity in Parkinson's disease modelsLRRK2 phosphorylation level correlates with abnormal motor behaviour in an experimental model of levodopa-induced dyskinesiasRegulation of LRRK2 expression points to a functional role in human monocyte maturationmTOR independent regulation of macroautophagy by Leucine Rich Repeat Kinase 2 via Beclin-1Harnessing Connectivity in a Large-Scale Small-Molecule Sensitivity Dataset.
P2860
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P2860
Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2.
@ast
Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2.
@en
type
label
Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2.
@ast
Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2.
@en
prefLabel
Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2.
@ast
Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2.
@en
P2093
P2860
P50
P356
P1476
Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2.
@en
P2093
Jiing-Dwan Lee
Matthew P Patricelli
Nathanael S Gray
Paul Davies
Tyzoon K Nomanbhoy
Xianming Deng
P2860
P2888
P304
P356
10.1038/NCHEMBIO.538
P577
2011-03-06T00:00:00Z