14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization - Wikidata - awgldk - TriplyDB

14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization

14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization

http://www.wikidata.org/entity/Q24339094

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Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of Parkinsonism The Parkinson disease-linked LRRK2 protein mutation I2020T stabilizes an active state conformation leading to increased kinase activity Biochemical characterization of highly purified leucine-rich repeat kinases 1 and 2 demonstrates formation of homodimers Rac1 protein rescues neurite retraction caused by G2019S leucine-rich repeat kinase 2 (LRRK2)The chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicity LRRK2 kinase activity regulates synaptic vesicle trafficking and neurotransmitter release through modulation of LRRK2 macro-molecular complex Differential protein-protein interactions of LRRK1 and LRRK2 indicate roles in distinct cellular signaling pathways LRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site status Progressive degeneration of human neural stem cells caused by pathogenic LRRK2 Phosphorylation of LRRK2 by casein kinase 1α regulates trans-Golgi clustering via differential interaction with ARHGEF7 A direct interaction between leucine-rich repeat kinase 2 and specific β-tubulin isoforms regulates tubulin acetylation Parkinson-related LRRK2 mutation R1441C/G/H impairs PKA phosphorylation of LRRK2 and disrupts its interaction with 14-3-3 Identification of protein phosphatase 1 as a regulator of the LRRK2 phosphorylation cycle Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies The G2385R variant of leucine-rich repeat kinase 2 associated with Parkinson's disease is a partial loss-of-function mutation Unbiased screen for interactors of leucine-rich repeat kinase 2 supports a common pathway for sporadic and familial Parkinson disease G2019S leucine-rich repeat kinase 2 causes uncoupling protein-mediated mitochondrial depolarization Mutant LRRK2 elicits calcium imbalance and depletion of dendritic mitochondria in neurons Activation Mechanism of LRRK2 and Its Cellular Functions in Parkinson's Disease The associations between Parkinson's disease and cancer: the plot thickens Current understanding of LRRK2 in Parkinson's disease: biochemical and structural features and inhibitor design The complex relationships between microglia, alpha-synuclein, and LRRK2 in Parkinson's disease Heterogeneity of leucine-rich repeat kinase 2 mutations: genetics, mechanisms and therapeutic implications Is 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?Genetics in Parkinson disease: Mendelian versus non-Mendelian inheritance LRRK2 inhibitors and their potential in the treatment of Parkinson's disease: current perspectives Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases Leucine-rich repeat kinase 2 interacts with p21-activated kinase 6 to control neurite complexity in mammalian brain The IkappaB kinase family phosphorylates the Parkinson's disease kinase LRRK2 at Ser935 and Ser910 during Toll-like receptor signaling Screening for novel LRRK2 inhibitors using a high-throughput TR-FRET cellular assay for LRRK2 Ser935 phosphorylation Phosphorylation-dependent 14-3-3 binding to LRRK2 is impaired by common mutations of familial Parkinson's disease LRRK2 phosphorylation level correlates with abnormal motor behaviour in an experimental model of levodopa-induced dyskinesias 14-3-3theta protects against neurotoxicity in a cellular Parkinson's disease model through inhibition of the apoptotic factor Bax G2385R and I2020T Mutations Increase LRRK2 GTPase Activity Protective LRRK2 R1398H Variant Enhances GTPase and Wnt Signaling Activity.The LRRK2 G2385R variant is a partial loss-of-function mutation that affects synaptic vesicle trafficking through altered protein interactions.Membrane recruitment of endogenous LRRK2 precedes its potent regulation of autophagy.Efficient allele-specific targeting of LRRK2 R1441 mutations mediated by RNAi.Arsenite stress down-regulates phosphorylation and 14-3-3 binding of leucine-rich repeat kinase 2 (LRRK2), promoting self-association and cellular redistribution

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14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization

http://www.wikidata.org/entity/Q24339094

description

2010 nî lūn-bûn

@nan

2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

14-3-3 binding to LRRK2 is dis ...... lates cytoplasmic localization

@ast

14-3-3 binding to LRRK2 is dis ...... lates cytoplasmic localization

@en

14-3-3 binding to LRRK2 is dis ...... lates cytoplasmic localization

@en-gb

14-3-3 binding to LRRK2 is dis ...... lates cytoplasmic localization

@nl

type

label

14-3-3 binding to LRRK2 is dis ...... lates cytoplasmic localization

@ast

14-3-3 binding to LRRK2 is dis ...... lates cytoplasmic localization

@en

14-3-3 binding to LRRK2 is dis ...... lates cytoplasmic localization

@en-gb

14-3-3 binding to LRRK2 is dis ...... lates cytoplasmic localization

@nl

prefLabel

14-3-3 binding to LRRK2 is dis ...... lates cytoplasmic localization

@ast

14-3-3 binding to LRRK2 is dis ...... lates cytoplasmic localization

@en

14-3-3 binding to LRRK2 is dis ...... lates cytoplasmic localization

@en-gb

14-3-3 binding to LRRK2 is dis ...... lates cytoplasmic localization

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Biochemical Journal

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14-3-3 binding to LRRK2 is dis ...... lates cytoplasmic localization

@en

P2093

Alban Ordureau

http://www.w3.org/2001/XMLSchema#string

David G Campbell

http://www.w3.org/2001/XMLSchema#string

Jie Shen

http://www.w3.org/2001/XMLSchema#string

Nicholas A Morrice

http://www.w3.org/2001/XMLSchema#string

R Jeremy Nichols

http://www.w3.org/2001/XMLSchema#string

Thomas Macartney

http://www.w3.org/2001/XMLSchema#string

Youren Tong

http://www.w3.org/2001/XMLSchema#string

P2860

Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity

Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration.

The Parkinson's disease kinase LRRK2 autophosphorylates its GTPase domain at multiple sites

Differential 14-3-3 affinity capture reveals new downstream targets of phosphatidylinositol 3-kinase signaling

LRRK2 regulates autophagic activity and localizes to specific membrane microdomains in a novel human genomic reporter cellular model

14-3-3eta is a novel regulator of parkin ubiquitin ligase.

Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology

alpha-Synuclein shares physical and functional homology with 14-3-3 proteins

LRRK2 in Parkinson's disease: protein domains and functional insights

Phospho-specific binding of 14-3-3 proteins to phosphatidylinositol 4-kinase III beta protects from dephosphorylation and stabilizes lipid kinase activity

P304

393-404

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scholarly article

P3181

1364133

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10.1042/BJ20100483

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P433

3

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430

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P50

Alan R. Prescott

P577

2010-09-15T00:00:00Z

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P5875

45273677

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P698

20642453

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P921

Parkinson's disease

P932

2932554

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