Phosphorylation-dependent 14-3-3 binding to LRRK2 is impaired by common mutations of familial Parkinson's disease
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Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of ParkinsonismBiochemical characterization of highly purified leucine-rich repeat kinases 1 and 2 demonstrates formation of homodimersDifferential 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 statusPhosphorylation of LRRK2 by casein kinase 1α regulates trans-Golgi clustering via differential interaction with ARHGEF7Parkinson-related LRRK2 mutation R1441C/G/H impairs PKA phosphorylation of LRRK2 and disrupts its interaction with 14-3-3Identification of protein phosphatase 1 as a regulator of the LRRK2 phosphorylation cycleLRRK2 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 mutationUnbiased screen for interactors of leucine-rich repeat kinase 2 supports a common pathway for sporadic and familial Parkinson diseaseMutant LRRK2 elicits calcium imbalance and depletion of dendritic mitochondria in neuronsCurrent 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 diseaseThe 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 phosphorylation14-3-3theta protects against neurotoxicity in a cellular Parkinson's disease model through inhibition of the apoptotic factor BaxThe Role of Interleukin-18, Oxidative Stress and Metabolic Syndrome in Alzheimer's Disease.Interleukin-18 alters protein expressions of neurodegenerative diseases-linked proteins in human SH-SY5Y neuron-like cellsGenetic and pharmacological evidence that G2019S LRRK2 confers a hyperkinetic phenotype, resistant to motor decline associated with aging.Sequences located within the N-terminus of the PD-linked LRRK2 lead to increased aggregation and attenuation of 6-hydroxydopamine-induced cell death.Lack of correlation between the kinase activity of LRRK2 harboring kinase-modifying mutations and its phosphorylation at Ser910, 935, and Ser955.Leucine-rich repeat kinase 2 modulates neuroinflammation and neurotoxicity in models of human immunodeficiency virus 1-associated neurocognitive disordersLRRK2 protein levels are determined by kinase function and are crucial for kidney and lung homeostasis in mice.14-3-3 proteins as potential therapeutic targets.Increased 14-3-3 phosphorylation observed in Parkinson's disease reduces neuroprotective potential of 14-3-3 proteins.α-synuclein, LRRK2 and their interplay in Parkinson's disease.Parkinson-Related LRRK2 Mutation R1628P Enables Cdk5 Phosphorylation of LRRK2 and Upregulates Its Kinase Activity14-3-3 inhibition promotes dopaminergic neuron loss and 14-3-3θ overexpression promotes recovery in the MPTP mouse model of Parkinson's disease.14-3-3 Proteins regulate mutant LRRK2 kinase activity and neurite shortening.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.LRRK2: cause, risk, and mechanism.Leucine-rich repeat kinase 2 (LRRK2) cellular biology: a review of recent advances in identifying physiological substrates and cellular functions.Genetic mouse models for understanding LRRK2 biology, pathology and pre-clinical application.14-3-3 proteins in neurological disorders.Human leucine-rich repeat kinase 1 and 2: intersecting or unrelated functions?Phosphorylation of LRRK2: from kinase to substrate.Pharmacological inhibition of LRRK2 cellular phosphorylation sites provides insight into LRRK2 biology.
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P2860
Phosphorylation-dependent 14-3-3 binding to LRRK2 is impaired by common mutations of familial Parkinson's disease
description
2011 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մարտին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique PLoS ONE
@fr
artículu científicu espublizáu en 2011
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im März 2011 veröffentlichter wissenschaftlicher Artikel
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scientific journal article
@en
vedecký článok (publikovaný 2011/03/01)
@sk
vědecký článek publikovaný v roce 2011
@cs
wetenschappelijk artikel (gepubliceerd op 2011/03/01)
@nl
наукова стаття, опублікована в березні 2011
@uk
name
Phosphorylation-dependent 14-3 ...... f familial Parkinson's disease
@ast
Phosphorylation-dependent 14-3 ...... f familial Parkinson's disease
@en
Phosphorylation-dependent 14-3 ...... f familial Parkinson's disease
@nl
type
label
Phosphorylation-dependent 14-3 ...... f familial Parkinson's disease
@ast
Phosphorylation-dependent 14-3 ...... f familial Parkinson's disease
@en
Phosphorylation-dependent 14-3 ...... f familial Parkinson's disease
@nl
prefLabel
Phosphorylation-dependent 14-3 ...... f familial Parkinson's disease
@ast
Phosphorylation-dependent 14-3 ...... f familial Parkinson's disease
@en
Phosphorylation-dependent 14-3 ...... f familial Parkinson's disease
@nl
P2093
P2860
P921
P3181
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P1476
Phosphorylation-dependent 14-3 ...... f familial Parkinson's disease
@en
P2093
Brian T Chait
Sangkyu Lee
Xianting Li
Yingming Zhao
Zhenyu Yue
P2860
P304
P3181
P356
10.1371/JOURNAL.PONE.0017153
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P50
P577
2011-03-01T00:00:00Z