Identification and characterization of a leucine-rich repeat kinase 2 (LRRK2) consensus phosphorylation motif - Test2 - elhamkhani - TriplyDB

Identification and characterization of a leucine-rich repeat kinase 2 (LRRK2) consensus phosphorylation motif

Identification and characterization of a leucine-rich repeat kinase 2 (LRRK2) consensus phosphorylation motif

http://www.wikidata.org/entity/Q28475942

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Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of Parkinsonism LRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site status LRRK2 interactions with α-synuclein in Parkinson's disease brains and in cell models LRRK2 directly phosphorylates Akt1 as a possible physiological substrate: impairment of the kinase activity by Parkinson's disease-associated mutations Parkinson-related LRRK2 mutation R1441C/G/H impairs PKA phosphorylation of LRRK2 and disrupts its interaction with 14-3-3 An early endosome regulator, Rab5b, is an LRRK2 kinase substrate LRRK2 phosphorylates Snapin and inhibits interaction of Snapin with SNAP-25 LRRK2 G2019S mutation attenuates microglial motility by inhibiting focal adhesion kinase.G2385R and I2020T Mutations Increase LRRK2 GTPase Activity Protective LRRK2 R1398H Variant Enhances GTPase and Wnt Signaling Activity.Arsenite stress down-regulates phosphorylation and 14-3-3 binding of leucine-rich repeat kinase 2 (LRRK2), promoting self-association and cellular redistribution Role of LRRK2 kinase dysfunction in Parkinson disease Role of LRRK2 kinase activity in the pathogenesis of Parkinson's disease.Evaluating LRRK2 genetic variants with unclear pathogenicity.Transcriptional responses to loss or gain of function of the leucine-rich repeat kinase 2 (LRRK2) gene uncover biological processes modulated by LRRK2 activity.Leucine-Rich Repeat Kinase 2 (LRRK2) phosphorylates p53 and induces p21(WAF1/CIP1) expression Activation of FADD-Dependent Neuronal Death Pathways as a Predictor of Pathogenicity for LRRK2 Mutations.Metabolism of peptide reporters in cell lysates and single cells Leucine-rich repeat kinase 2 (LRRK2) as a potential therapeutic target in Parkinson's disease.The GTPase function of LRRK2.Human leucine-rich repeat kinase 1 and 2: intersecting or unrelated functions?Phosphorylation of LRRK2: from kinase to substrate.Pharmacological inhibition of LRRK2 cellular phosphorylation sites provides insight into LRRK2 biology.Prediction of the repeat domain structures and impact of parkinsonism-associated variations on structure and function of all functional domains of leucine-rich repeat kinase 2 (LRRK2).Cellular processes associated with LRRK2 function and dysfunction GTP binding regulates cellular localization of Parkinson's disease-associated LRRK2.Phosphorylation of LRRK2 serines 955 and 973 is disrupted by Parkinson's disease mutations and LRRK2 pharmacological inhibition.Phosphoproteomic evaluation of pharmacological inhibition of leucine-rich repeat kinase 2 reveals significant off-target effects of LRRK-2-IN-1.The LRRK2 G2019S mutant exacerbates basal autophagy through activation of the MEK/ERK pathway.Human R1441C LRRK2 regulates the synaptic vesicle proteome and phosphoproteome in a Drosophila model of Parkinson's disease.Biochemical characterization of the GTP-sensing protein, CodY of Bacillus anthracis.Regulation of LRRK2 by Phosphatases.LRRK2 Phosphorylation.

P2860

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P2860

Identification and characterization of a leucine-rich repeat kinase 2 (LRRK2) consensus phosphorylation motif

http://www.wikidata.org/entity/Q28475942

description

2010 nî lūn-bûn

@nan

2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Identification and characteriz ...... onsensus phosphorylation motif

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Identification and characteriz ...... onsensus phosphorylation motif

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Identification and characteriz ...... onsensus phosphorylation motif

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type

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Identification and characteriz ...... onsensus phosphorylation motif

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Identification and characteriz ...... onsensus phosphorylation motif

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Identification and characteriz ...... onsensus phosphorylation motif

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prefLabel

Identification and characteriz ...... onsensus phosphorylation motif

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Identification and characteriz ...... onsensus phosphorylation motif

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Identification and characteriz ...... onsensus phosphorylation motif

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Identification and characteriz ...... onsensus phosphorylation motif

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Brian Bates

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

Eugene L Brown

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

Kerri Lipinski

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

Peter H Reinhart

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Pooja P Pungaliya

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Saurabh Sen

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

Steven P Braithwaite

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

Vasanti S Anand

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

Warren D Hirst

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

Yuchen Bai

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

P2860

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

GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease

The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity

The R1441C mutation of LRRK2 disrupts GTP hydrolysis

Kinase activity of mutant LRRK2 mediates neuronal toxicity

Homo- and heterodimerization of ROCO kinases: LRRK2 kinase inhibition by the LRRK2 ROCO fragment

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

siRNA screening of the kinome identifies ULK1 as a multidomain modulator of autophagy

The familial Parkinsonism gene LRRK2 regulates neurite process morphology

The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation

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e13672

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10.1371/JOURNAL.PONE.0013672

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10

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2010-10-27T00:00:00Z

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47718617

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21060682

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phosphorylation

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