Ser1292 autophosphorylation is an indicator of LRRK2 kinase activity and contributes to the cellular effects of PD mutations.
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Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of ParkinsonismThe Parkinson disease-linked LRRK2 protein mutation I2020T stabilizes an active state conformation leading to increased kinase activityLRRK2 kinase activity regulates synaptic vesicle trafficking and neurotransmitter release through modulation of LRRK2 macro-molecular complexLRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site statusPhosphorylation 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 acetylationParkinson-related LRRK2 mutation R1441C/G/H impairs PKA phosphorylation of LRRK2 and disrupts its interaction with 14-3-3The regulation and deregulation of Wnt signaling by PARK genes in health and 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 implicationsProtein Kinases and Parkinson's DiseaseLRRK2 inhibitors and their potential in the treatment of Parkinson's disease: current perspectivesPhosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPasesLeucine-rich repeat kinase 2 interacts with p21-activated kinase 6 to control neurite complexity in mammalian brainParkinson's disease-implicated kinases in the brain; insights into disease pathogenesis.Membrane recruitment of endogenous LRRK2 precedes its potent regulation of autophagy.Arsenite stress down-regulates phosphorylation and 14-3-3 binding of leucine-rich repeat kinase 2 (LRRK2), promoting self-association and cellular redistributionGenetic and pharmacological evidence that G2019S LRRK2 confers a hyperkinetic phenotype, resistant to motor decline associated with aging.Unique functional and structural properties of the LRRK2 protein ATP-binding pocket.Targeted quantitation of proteins by mass spectrometry.Short- and long-term effects of LRRK2 on axon and dendrite growthLack of correlation between the kinase activity of LRRK2 harboring kinase-modifying mutations and its phosphorylation at Ser910, 935, and Ser955.A novel reaction mediated by human aldehyde oxidase: amide hydrolysis of GDC-0834Leucine-rich repeat kinase 2 deficiency is protective in rhabdomyolysis-induced kidney injury.The Parkinson's Disease-Associated Mutation LRRK2-G2019S Impairs Synaptic Plasticity in Mouse Hippocampus.Leucine-Rich Repeat Kinase 2 Influences Fate Decision of Human Monocytes Differentiated from Induced Pluripotent Stem CellsLRRK2 and ubiquitination: implications for kinase inhibitor therapyActivation of FADD-Dependent Neuronal Death Pathways as a Predictor of Pathogenicity for LRRK2 Mutations.LRRK2 autophosphorylation enhances its GTPase activity14-3-3 Proteins regulate mutant LRRK2 kinase activity and neurite shortening.Urinary LRRK2 phosphorylation predicts parkinsonian phenotypes in G2019S LRRK2 carriers.LRRK2: an éminence grise of Wnt-mediated neurogenesis?Comprehensive characterization and optimization of anti-LRRK2 (leucine-rich repeat kinase 2) monoclonal antibodies.Decoding Parkinson's Disease Pathogenesis: The Role of Deregulated mRNA Translation.G2019S-LRRK2 Expression Augments α-Synuclein Sequestration into Inclusions in Neurons.Structure, function, and leucine-rich repeat kinase 2: On the importance of reproducibility in understanding Parkinson's disease.Phos-tag analysis of Rab10 phosphorylation by LRRK2: a powerful assay for assessing kinase function and inhibitors.Development of inducible leucine-rich repeat kinase 2 (LRRK2) cell lines for therapeutics development in Parkinson's disease.Mutations in LRRK2 impair NF-κB pathway in iPSC-derived neurons.Metabolic labeling of leucine rich repeat kinases 1 and 2 with radioactive phosphate.
P2860
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P2860
Ser1292 autophosphorylation is an indicator of LRRK2 kinase activity and contributes to the cellular effects of PD mutations.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh-hant
name
Ser1292 autophosphorylation is ...... lular effects of PD mutations.
@en
Ser1292 autophosphorylation is ...... lular effects of PD mutations.
@nl
type
label
Ser1292 autophosphorylation is ...... lular effects of PD mutations.
@en
Ser1292 autophosphorylation is ...... lular effects of PD mutations.
@nl
prefLabel
Ser1292 autophosphorylation is ...... lular effects of PD mutations.
@en
Ser1292 autophosphorylation is ...... lular effects of PD mutations.
@nl
P2093
P1476
Ser1292 autophosphorylation is ...... lular effects of PD mutations.
@en
P2093
Anthony A Estrada
Claire E Le Pichon
Daisy Bustos
Daniel J Burdick
Haitao Zhu
Hilda O Solanoy
Huifen Chen
Janet Gunzner-Toste
Jason Drummond
P304
P356
10.1126/SCITRANSLMED.3004485
P407
P577
2012-12-01T00:00:00Z