Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant - Test2 - elhamkhani - TriplyDB

Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

http://www.wikidata.org/entity/Q24306788

about

GTPase activity and neuronal toxicity of Parkinson's disease-associated LRRK2 is regulated by ArfGAP1 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 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 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 Functional interaction of Parkinson's disease-associated LRRK2 with members of the dynamin GTPase superfamily GTP binding to the ROC domain of DAP-kinase regulates its function through intramolecular signalling 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 The G2385R variant of leucine-rich repeat kinase 2 associated with Parkinson's disease is a partial loss-of-function mutation 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?LRRK2 at the interface of autophagosomes, endosomes and lysosomes Pathogenic Parkinson's disease mutations across the functional domains of LRRK2 alter the autophagic/lysosomal response to starvation Inhibition of LRRK2 kinase activity stimulates macroautophagy Leucine-rich repeat kinase 2 interacts with p21-activated kinase 6 to control neurite complexity in mammalian brain Protective LRRK2 R1398H Variant Enhances GTPase and Wnt Signaling Activity.Increasing microtubule acetylation rescues axonal transport and locomotor deficits caused by LRRK2 Roc-COR domain mutations.Mechanisms of Parkinson's disease-related proteins in mediating secondary brain damage after cerebral ischemia.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.Role of LRRK2 kinase dysfunction in Parkinson disease Role of LRRK2 kinase activity in the pathogenesis of Parkinson's disease.Models for LRRK2-Linked Parkinsonism.Targeting GTPases in Parkinson's disease: comparison to the historic path of kinase drug discovery and perspectives Assaying the kinase activity of LRRK2 in vitro.LRRK2 GTPase dysfunction in the pathogenesis of Parkinson's disease.Phos-tag analysis of Rab10 phosphorylation by LRRK2: a powerful assay for assessing kinase function and inhibitors.Metabolic labeling of leucine rich repeat kinases 1 and 2 with radioactive phosphate.Contribution of GTPase activity to LRRK2-associated Parkinson disease On the road to leucine-rich repeat kinase 2 signalling: evidence from cellular and in vivo studies.Mechanisms of LRRK2-mediated neurodegeneration.The GTPase function of LRRK2.Phosphorylation of LRRK2: from kinase to substrate.Targeting leucine-rich repeat kinase 2 in Parkinson's disease.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).LRRK2 and neuroinflammation: partners in crime in Parkinson's disease?

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P2860

Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

http://www.wikidata.org/entity/Q24306788

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2011 nî lūn-bûn

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2011 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2011 թվականի հունվարին հրատարակված գիտական հոդված

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2011年の論文

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年學術文章

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name

Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

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Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

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Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

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Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

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type

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Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

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Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

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Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

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Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

@nl

prefLabel

Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

@ast

Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

@en

Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

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Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

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J.1471-4159.2010.07105.X

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Journal of Neurochemistry

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Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

@en

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Bernard M H Law

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Evy Lobbestael

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Fangye Gao

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Kirsten Harvey

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Renée Vancraenenbroeck

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Veronique Daniëls

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P2860

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

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

The GDP-GTP exchange factor collybistin: an essential determinant of neuronal gephyrin clustering

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

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

Mutations in the LRRK2 Roc-COR tandem domain link Parkinson's disease to Wnt signalling pathways

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304-15

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4234346

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10.1111/J.1471-4159.2010.07105.X

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2

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116

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Veerle Baekelandt

Jean-Marc Taymans

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2011-01-01T00:00:00Z

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47788906

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21073465

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identical protein binding

Leucine rich repeat kinase 2

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3005098

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