Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization. - Wikidata - wikimedia - TriplyDB

Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization.

Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization.

http://www.wikidata.org/entity/Q37479332

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GTPase activity and neuronal toxicity of Parkinson's disease-associated LRRK2 is regulated by ArfGAP1 Ribosomal protein s15 phosphorylation mediates LRRK2 neurodegeneration in Parkinson's disease A Parkinson's disease gene regulatory network identifies the signaling protein RGS2 as a modulator of LRRK2 activity and neuronal toxicity 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)Heterodimerization of Lrrk1-Lrrk2: Implications for LRRK2-associated Parkinson disease LRRK2 kinase activity regulates synaptic vesicle trafficking and neurotransmitter release through modulation of LRRK2 macro-molecular complex LRRK2 and the stress response: interaction with MKKs and JNK-interacting proteins ARHGEF7 (Beta-PIX) acts as guanine nucleotide exchange factor for leucine-rich repeat kinase 2 GTPase activity regulates kinase activity and cellular phenotypes of Parkinson's disease-associated LRRK2 Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant Membrane localization of LRRK2 is associated with increased formation of the highly active LRRK2 dimer and changes in its phosphorylation Interplay of LRRK2 with chaperone-mediated autophagy Activation Mechanism of LRRK2 and Its Cellular Functions in Parkinson's Disease Heterogeneity of leucine-rich repeat kinase 2 mutations: genetics, mechanisms and therapeutic implications Progressive dopaminergic alterations and mitochondrial abnormalities in LRRK2 G2019S knock-in mice Parkinson's disease and immune system: is the culprit LRRKing in the periphery?Revisiting the Roco G-protein cycle Structural model of the dimeric Parkinson's protein LRRK2 reveals a compact architecture involving distant interdomain contacts Identification and characterization of a leucine-rich repeat kinase 2 (LRRK2) consensus phosphorylation motif Loss of leucine-rich repeat kinase 2 causes impairment of protein degradation pathways, accumulation of alpha-synuclein, and apoptotic cell death in aged mice Phosphorylation-dependent 14-3-3 binding to LRRK2 is impaired by common mutations of familial Parkinson's disease Microtubule affinity-regulating kinase 2 (MARK2) turns on phosphatase and tensin homolog (PTEN)-induced kinase 1 (PINK1) at Thr-313, a mutation site in Parkinson disease: effects on mitochondrial transport 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 LRRK2 kinase activity is dependent on LRRK2 GTP binding capacity but independent of LRRK2 GTP binding.LRRK2-mediated neurodegeneration and dysfunction of dopaminergic neurons in a Caenorhabditis elegans model of Parkinson's disease Reevaluation of phosphorylation sites in the Parkinson disease-associated leucine-rich repeat kinase 2 Recent advances in the genetics of Parkinson's disease.Role of LRRK2 kinase dysfunction in Parkinson disease Unravelling the role of defective genes.Role of LRRK2 kinase activity in the pathogenesis of Parkinson's disease.Unique functional and structural properties of the LRRK2 protein ATP-binding pocket.Models for LRRK2-Linked Parkinsonism.Autophosphorylation in the leucine-rich repeat kinase 2 (LRRK2) GTPase domain modifies kinase and GTP-binding activities 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 deficiency is protective in rhabdomyolysis-induced kidney injury.The Parkinson's Disease-Associated Protein Kinase LRRK2 Modulates Notch Signaling through the Endosomal Pathway.Number and brightness analysis of LRRK2 oligomerization in live cells.

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P2860

Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization.

http://www.wikidata.org/entity/Q37479332

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 13 October 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization.

@en

Dependence of leucine-rich repeat kinase 2

@nl

type

label

Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization.

@en

Dependence of leucine-rich repeat kinase 2

@nl

prefLabel

Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization.

@en

Dependence of leucine-rich repeat kinase 2

@nl

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JBC.M109.025437

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Journal of Biological Chemistry

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Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization.

@en

P2093

Philip J Webber

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

Saurabh Sen

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

P2860

Dimerization via tandem leucine zippers is essential for the activation of the mitogen-activated protein kinase kinase kinase, MLK-3

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

The kinase activation loop is the key to mixed lineage kinase-3 activation via both autophosphorylation and hematopoietic progenitor kinase 1 phosphorylation

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

Identification of potential protein interactors of Lrrk2

The R1441C mutation of LRRK2 disrupts GTP hydrolysis

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

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

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36346-36356

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scholarly article

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10.1074/JBC.M109.025437

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52

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284

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2009-10-13T00:00:00Z

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19826009

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2794750

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