GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease
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Dopaminergic neuronal loss, reduced neurite complexity and autophagic abnormalities in transgenic mice expressing G2019S mutant LRRK2.GTPase activity and neuronal toxicity of Parkinson's disease-associated LRRK2 is regulated by ArfGAP1The Parkinson disease-linked LRRK2 protein mutation I2020T stabilizes an active state conformation leading to increased kinase activityMKK6 binds and regulates expression of Parkinson's disease-related protein LRRK2A 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 pathwaysThe R1441C mutation of LRRK2 disrupts GTP hydrolysisARHGEF7 (Beta-PIX) acts as guanine nucleotide exchange factor for leucine-rich repeat kinase 2GTPase activity regulates kinase activity and cellular phenotypes of Parkinson's disease-associated LRRK2LRRK2 directly phosphorylates Akt1 as a possible physiological substrate: impairment of the kinase activity by Parkinson's disease-associated mutationsInsight into the mode of action of the LRRK2 Y1699C pathogenic mutantFunctional interaction of Parkinson's disease-associated LRRK2 with members of the dynamin GTPase superfamilyGTP binding controls complex formation by the human ROCO protein MASL1GTP binding to the ROC domain of DAP-kinase regulates its function through intramolecular signallingThe Parkinson's disease kinase LRRK2 autophosphorylates its GTPase domain at multiple sitesParkinson-related LRRK2 mutation R1441C/G/H impairs PKA phosphorylation of LRRK2 and disrupts its interaction with 14-3-3Membrane localization of LRRK2 is associated with increased formation of the highly active LRRK2 dimer and changes in its phosphorylationMutations in the LRRK2 Roc-COR tandem domain link Parkinson's disease to Wnt signalling pathwaysIdentification of protein phosphatase 1 as a regulator of the LRRK2 phosphorylation cycleThe Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylationParkinson disease-associated mutation R1441H in LRRK2 prolongs the "active state" of its GTPase domainG2019S leucine-rich repeat kinase 2 causes uncoupling protein-mediated mitochondrial depolarizationRole of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cellsActivation Mechanism of LRRK2 and Its Cellular Functions in Parkinson's DiseaseCurrent understanding of LRRK2 in Parkinson's disease: biochemical and structural features and inhibitor designLRRK2 as a Potential Genetic Modifier of Synucleinopathies: Interlacing the Two Major Genetic Factors of Parkinson's DiseaseHeterogeneity of leucine-rich repeat kinase 2 mutations: genetics, mechanisms and therapeutic implicationsGenetics of Parkinson's disease - a clinical perspectiveStructure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPaseStructure of the Roc–COR domain tandem of C. tepidum, a prokaryotic homologue of the human LRRK2 Parkinson kinaseParkinson's disease and immune system: is the culprit LRRKing in the periphery?Revisiting the Roco G-protein cycleIdentification and characterization of a leucine-rich repeat kinase 2 (LRRK2) consensus phosphorylation motifThe IkappaB kinase family phosphorylates the Parkinson's disease kinase LRRK2 at Ser935 and Ser910 during Toll-like receptor signalingPhosphorylation-dependent 14-3-3 binding to LRRK2 is impaired by common mutations of familial Parkinson's diseaseEnhanced striatal dopamine transmission and motor performance with LRRK2 overexpression in mice is eliminated by familial Parkinson's disease mutation G2019SWild-type LRRK2 but not its mutant attenuates stress-induced cell death via ERK pathway.R1441C mutation in LRRK2 impairs dopaminergic neurotransmission in mice.Regulation of LRRK2 stability by the E3 ubiquitin ligase CHIP
P2860
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P2860
GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease
description
2007 nî lūn-bûn
@nan
2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
GTP binding is essential to th ...... r familial Parkinson's disease
@ast
GTP binding is essential to th ...... r familial Parkinson's disease
@en
GTP binding is essential to th ...... r familial Parkinson's disease
@en-gb
GTP binding is essential to th ...... r familial Parkinson's disease
@nl
type
label
GTP binding is essential to th ...... r familial Parkinson's disease
@ast
GTP binding is essential to th ...... r familial Parkinson's disease
@en
GTP binding is essential to th ...... r familial Parkinson's disease
@en-gb
GTP binding is essential to th ...... r familial Parkinson's disease
@nl
prefLabel
GTP binding is essential to th ...... r familial Parkinson's disease
@ast
GTP binding is essential to th ...... r familial Parkinson's disease
@en
GTP binding is essential to th ...... r familial Parkinson's disease
@en-gb
GTP binding is essential to th ...... r familial Parkinson's disease
@nl
P2093
P50
P921
P3181
P356
P1433
P1476
GTP binding is essential to th ...... r familial Parkinson's disease
@en
P2093
Takeshi Iwatsubo
Takuro Okai
Toshiaki Katada
P304
P3181
P356
10.1021/BI061960M
P407
P577
2007-02-06T00:00:00Z