Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
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The foxa2 gene controls the birth and spontaneous degeneration of dopamine neurons in old agePhosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of ParkinsonismPlant and animal pathogen recognition receptors signal through non-RD kinasesDopaminergic neuronal loss, reduced neurite complexity and autophagic abnormalities in transgenic mice expressing G2019S mutant LRRK2.Web-based genome-wide association study identifies two novel loci and a substantial genetic component for Parkinson's diseaseThe dictyostelium kinome--analysis of the protein kinases from a simple model organism.Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: a mutation updateParkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activityThe genetic epidemiology of neurodegenerative disease.The Parkinson disease-linked LRRK2 protein mutation I2020T stabilizes an active state conformation leading to increased kinase activityPathogenic LRRK2 negatively regulates microRNA-mediated translational repressionLeucine-rich repeat kinase 2 regulates autophagy through a calcium-dependent pathway involving NAADPRibosomal protein s15 phosphorylation mediates LRRK2 neurodegeneration in Parkinson's diseaseExpression of leucine-rich repeat kinase 2 (LRRK2) inhibits the processing of uMtCK to induce cell death in a cell culture model systemMKK6 binds and regulates expression of Parkinson's disease-related protein LRRK2Parkinson disease protein DJ-1 binds metals and protects against metal-induced cytotoxicityInhibition of excessive mitochondrial fission reduced aberrant autophagy and neuronal damage caused by LRRK2 G2019S mutationBiochemical characterization of highly purified leucine-rich repeat kinases 1 and 2 demonstrates formation of homodimersLeucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration.LRRK2 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 statusIdentification of new kinase clusters required for neurite outgrowth and retraction by a loss-of-function RNA interference screenLRRK2 regulates mitochondrial dynamics and function through direct interaction with DLP1Synaptic vesicle trafficking and Parkinson's diseaseThe R1441C mutation of LRRK2 disrupts GTP hydrolysisLeucine-rich repeat kinase 2 regulates Sec16A at ER exit sites to allow ER-Golgi exportLRRK2 phosphorylates tubulin-associated tau but not the free molecule: LRRK2-mediated regulation of the tau-tubulin association and neurite outgrowthARHGEF7 (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 mutationsInteraction of DJ-1 with Daxx inhibits apoptosis signal-regulating kinase 1 activity and cell deathDysregulation of lysosomal morphology by pathogenic LRRK2 is corrected by TPC2 inhibitionLRRK2 expression in idiopathic and G2019S positive Parkinson's disease subjects: a morphological and quantitative studyArfGAP1 is a GTPase activating protein for LRRK2: reciprocal regulation of ArfGAP1 by LRRK2Threonine 56 phosphorylation of Bcl-2 is required for LRRK2 G2019S-induced mitochondrial depolarization and autophagyThe role of oxidative stress in Parkinson's diseaseA direct interaction between leucine-rich repeat kinase 2 and specific β-tubulin isoforms regulates tubulin acetylationParkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation
P2860
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P2860
Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
description
2004 nî lūn-bûn
@nan
2004 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
@ast
Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
@en
Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
@nl
type
label
Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
@ast
Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
@en
Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
@nl
prefLabel
Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
@ast
Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
@en
Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
@nl
P2093
P50
P3181
P1433
P1476
Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
@en
P2093
Iria Carballo Carbajal
Jennifer Kachergus
Mary Hulihan
Nadja Patenge
Peter Vieregge
Petra Leitner
Ronald F Pfeiffer
Sarah Lincoln
Saskia Biskup
Tim M Strom
P356
10.1016/J.NEURON.2004.11.005
P407
P50
P577
2004-11-18T00:00:00Z