Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant
about
GTPase activity and neuronal toxicity of Parkinson's disease-associated LRRK2 is regulated by ArfGAP1A Parkinson's disease gene regulatory network identifies the signaling protein RGS2 as a modulator of LRRK2 activity and neuronal toxicityBiochemical 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 ARHGEF7A direct interaction between leucine-rich repeat kinase 2 and specific β-tubulin isoforms regulates tubulin acetylationFunctional interaction of Parkinson's disease-associated LRRK2 with members of the dynamin GTPase superfamilyGTP binding to the ROC domain of DAP-kinase regulates its function through intramolecular signallingParkinson-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 cycleThe G2385R variant of leucine-rich repeat kinase 2 associated with Parkinson's disease is a partial loss-of-function mutationHeterogeneity of leucine-rich repeat kinase 2 mutations: genetics, mechanisms and therapeutic implicationsIs inhibition of kinase activity the only therapeutic strategy for LRRK2-associated Parkinson's disease?Parkinson's disease and immune system: is the culprit LRRKing in the periphery?LRRK2 at the interface of autophagosomes, endosomes and lysosomesPathogenic Parkinson's disease mutations across the functional domains of LRRK2 alter the autophagic/lysosomal response to starvationInhibition of LRRK2 kinase activity stimulates macroautophagyLeucine-rich repeat kinase 2 interacts with p21-activated kinase 6 to control neurite complexity in mammalian brainProtective LRRK2 R1398H Variant Enhances GTPase and Wnt Signaling Activity.Increasing microtubule acetylation rescues axonal transport and locomotor deficits caused by LRRK2 Roc-COR domain mutations.Mechanisms of Parkinson's disease-related proteins in mediating secondary brain damage after cerebral ischemia.Arsenite stress down-regulates phosphorylation and 14-3-3 binding of leucine-rich repeat kinase 2 (LRRK2), promoting self-association and cellular redistributionLRRK2 kinase activity is dependent on LRRK2 GTP binding capacity but independent of LRRK2 GTP binding.Role of LRRK2 kinase dysfunction in Parkinson diseaseRole of LRRK2 kinase activity in the pathogenesis of Parkinson's disease.Models for LRRK2-Linked Parkinsonism.Targeting GTPases in Parkinson's disease: comparison to the historic path of kinase drug discovery and perspectivesAssaying the kinase activity of LRRK2 in vitro.LRRK2 GTPase dysfunction in the pathogenesis of Parkinson's disease.Phos-tag analysis of Rab10 phosphorylation by LRRK2: a powerful assay for assessing kinase function and inhibitors.Metabolic labeling of leucine rich repeat kinases 1 and 2 with radioactive phosphate.Contribution of GTPase activity to LRRK2-associated Parkinson diseaseOn the road to leucine-rich repeat kinase 2 signalling: evidence from cellular and in vivo studies.Mechanisms of LRRK2-mediated neurodegeneration.The GTPase function of LRRK2.Phosphorylation of LRRK2: from kinase to substrate.Targeting leucine-rich repeat kinase 2 in Parkinson's disease.Prediction of the repeat domain structures and impact of parkinsonism-associated variations on structure and function of all functional domains of leucine-rich repeat kinase 2 (LRRK2).LRRK2 and neuroinflammation: partners in crime in Parkinson's disease?
P2860
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P2860
Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant
description
2011 nî lūn-bûn
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2011 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
name
Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant
@ast
Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant
@en
Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant
@en-gb
Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant
@nl
type
label
Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant
@ast
Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant
@en
Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant
@en-gb
Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant
@nl
prefLabel
Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant
@ast
Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant
@en
Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant
@en-gb
Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant
@nl
P2093
P2860
P50
P3181
P1476
Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant
@en
P2093
Bernard M H Law
Evy Lobbestael
Fangye Gao
Kirsten Harvey
Renée Vancraenenbroeck
Veronique Daniëls
P2860
P304
P3181
P356
10.1111/J.1471-4159.2010.07105.X
P407
P577
2011-01-01T00:00:00Z