The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation
about
Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: a mutation updateMKK6 binds and regulates expression of Parkinson's disease-related protein LRRK2Biochemical characterization of highly purified leucine-rich repeat kinases 1 and 2 demonstrates formation of homodimersRac1 protein rescues neurite retraction caused by G2019S leucine-rich repeat kinase 2 (LRRK2)Heterodimerization of Lrrk1-Lrrk2: Implications for LRRK2-associated Parkinson diseaseLRRK2 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 and the stress response: interaction with MKKs and JNK-interacting proteinsLRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site statusARHGEF7 (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 LRRK2Insight into the mode of action of the LRRK2 Y1699C pathogenic mutantGTP 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 sitesMembrane 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 pathwaysInterplay of LRRK2 with chaperone-mediated autophagyThe G2385R variant of leucine-rich repeat kinase 2 associated with Parkinson's disease is a partial loss-of-function mutationThe kinase LRRK2 is a regulator of the transcription factor NFAT that modulates the severity of inflammatory bowel diseaseIntrabody and Parkinson's diseaseActivation 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 implicationsProgressive dopaminergic alterations and mitochondrial abnormalities in LRRK2 G2019S knock-in miceStructure of the Roc–COR domain tandem of C. tepidum, a prokaryotic homologue of the human LRRK2 Parkinson kinaseRoco 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?Revisiting the Roco G-protein cycleLRRK2 at the interface of autophagosomes, endosomes and lysosomesStructural model of the dimeric Parkinson's protein LRRK2 reveals a compact architecture involving distant interdomain contactsGene-environment interactions: key to unraveling the mystery of Parkinson's diseaseIdentification and characterization of a leucine-rich repeat kinase 2 (LRRK2) consensus phosphorylation motifThe nitric oxide-cyclic GMP pathway regulates FoxO and alters dopaminergic neuron survival in DrosophilaLoss of leucine-rich repeat kinase 2 causes impairment of protein degradation pathways, accumulation of alpha-synuclein, and apoptotic cell death in aged miceFunctional and Morphological Correlates in the Drosophila LRRK2 loss-of-function Model of Parkinson's Disease: Drug Effects of Withania somnifera (Dunal) AdministrationPhosphorylation-dependent 14-3-3 binding to LRRK2 is impaired by common mutations of familial Parkinson's diseaseSelective inhibition of the kinase DYRK1A by targeting its folding processThe LRRK2-related Roco kinase Roco2 is regulated by Rab1A and controls the actin cytoskeleton
P2860
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P2860
The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation
description
2008 nî lūn-bûn
@nan
2008 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
name
The Parkinson disease-associat ...... amolecular autophosphorylation
@ast
The Parkinson disease-associat ...... amolecular autophosphorylation
@en
The Parkinson disease-associat ...... amolecular autophosphorylation
@en-gb
The Parkinson disease-associat ...... amolecular autophosphorylation
@nl
type
label
The Parkinson disease-associat ...... amolecular autophosphorylation
@ast
The Parkinson disease-associat ...... amolecular autophosphorylation
@en
The Parkinson disease-associat ...... amolecular autophosphorylation
@en-gb
The Parkinson disease-associat ...... amolecular autophosphorylation
@nl
prefLabel
The Parkinson disease-associat ...... amolecular autophosphorylation
@ast
The Parkinson disease-associat ...... amolecular autophosphorylation
@en
The Parkinson disease-associat ...... amolecular autophosphorylation
@en-gb
The Parkinson disease-associat ...... amolecular autophosphorylation
@nl
P2093
P2860
P50
P921
P3181
P356
P1476
The Parkinson disease-associat ...... amolecular autophosphorylation
@en
P2093
Alice Kaganovich
Ibardo Zambrano
Jinhui Ding
Kelly J Thomas
Shushant Jain
Veronique Daniëls
P2860
P304
P3181
P356
10.1074/JBC.M708718200
P407
P577
2008-06-13T00:00:00Z