Parkinson-related LRRK2 mutation R1441C/G/H impairs PKA phosphorylation of LRRK2 and disrupts its interaction with 14-3-3
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Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of ParkinsonismLRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site statusLRRK2 transport is regulated by its novel interacting partner Rab32The complex relationships between microglia, alpha-synuclein, and LRRK2 in Parkinson's diseaseLRRK2 inhibitors and their potential in the treatment of Parkinson's disease: current perspectivesLRRK2 phosphorylation level correlates with abnormal motor behaviour in an experimental model of levodopa-induced dyskinesiasA visual review of the interactome of LRRK2: Using deep-curated molecular interaction data to represent biology.Genetic and pharmacological evidence that G2019S LRRK2 confers a hyperkinetic phenotype, resistant to motor decline associated with aging.A genome-wide copy number variant study of suicidal behavior.14-3-3 Proteins regulate mutant LRRK2 kinase activity and neurite shortening.Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR.Mutations in LRRK2 impair NF-κB pathway in iPSC-derived neurons.Identification of chaperones in a MPP+-induced and ATRA/TPA-differentiated SH-SY5Y cell PD model.Drug-induced Parkinson's disease modulates protein kinase A and Olfactory Marker Protein in the mouse olfactory bulb.Interaction of LRRK2 with kinase and GTPase signaling cascadesAlterations in late endocytic trafficking related to the pathobiology of LRRK2-linked Parkinson's disease.A dual phosphorylation switch controls 14-3-3-dependent cell surface expression of TASK-1GTP binding regulates cellular localization of Parkinson's disease-associated LRRK2.Understanding the GTPase Activity of LRRK2: Regulation, Function, and Neurotoxicity.Parkinson disease-associated LRRK2 G2019S transgene disrupts marrow myelopoiesis and peripheral Th17 response.The complex of TRIP-Br1 and XIAP ubiquitinates and degrades multiple adenylyl cyclase isoformsPharmacological LRRK2 kinase inhibition induces LRRK2 protein destabilization and proteasomal degradationCyclic nucleotide signaling changes associated with normal aging and age-related diseases of the brain.Rab29 activation of the Parkinson's disease-associated LRRK2 kinase.PAK6 Phosphorylates 14-3-3γ to Regulate Steady State Phosphorylation of LRRK2.LRRK2 Phosphorylation.Molecular Cloning and Effects of -Silencing on Larval Survivability Against and inA thermodynamic model for multivalency in 14-3-3 protein-protein interactionsLeucine-rich repeat kinase 2 controls protein kinase A activation state through phosphodiesterase 4
P2860
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P2860
Parkinson-related LRRK2 mutation R1441C/G/H impairs PKA phosphorylation of LRRK2 and disrupts its interaction with 14-3-3
description
2014 nî lūn-bûn
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2014 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Parkinson-related LRRK2 mutati ...... ts its interaction with 14-3-3
@ast
Parkinson-related LRRK2 mutati ...... ts its interaction with 14-3-3
@en
Parkinson-related LRRK2 mutati ...... ts its interaction with 14-3-3
@en-gb
Parkinson-related LRRK2 mutati ...... ts its interaction with 14-3-3
@nl
type
label
Parkinson-related LRRK2 mutati ...... ts its interaction with 14-3-3
@ast
Parkinson-related LRRK2 mutati ...... ts its interaction with 14-3-3
@en
Parkinson-related LRRK2 mutati ...... ts its interaction with 14-3-3
@en-gb
Parkinson-related LRRK2 mutati ...... ts its interaction with 14-3-3
@nl
prefLabel
Parkinson-related LRRK2 mutati ...... ts its interaction with 14-3-3
@ast
Parkinson-related LRRK2 mutati ...... ts its interaction with 14-3-3
@en
Parkinson-related LRRK2 mutati ...... ts its interaction with 14-3-3
@en-gb
Parkinson-related LRRK2 mutati ...... ts its interaction with 14-3-3
@nl
P2093
P2860
P50
P3181
P356
P1476
Parkinson-related LRRK2 mutati ...... ts its interaction with 14-3-3
@en
P2093
Anette Jacob
Felix von Zweydorf
Frank Gesellchen
Jennifer Sarah Hermann
Kathrin Muda
P2860
P304
P3181
P356
10.1073/PNAS.1312701111
P407
P577
2014-01-07T00:00:00Z