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

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

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

http://www.wikidata.org/entity/Q24298689

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Dopaminergic neuronal loss, reduced neurite complexity and autophagic abnormalities in transgenic mice expressing G2019S mutant LRRK2.GTPase activity and neuronal toxicity of Parkinson's disease-associated LRRK2 is regulated by ArfGAP1 MKK6 binds and regulates expression of Parkinson's disease-related protein LRRK2 Rac1 protein rescues neurite retraction caused by G2019S leucine-rich repeat kinase 2 (LRRK2)LRRK2 and the stress response: interaction with MKKs and JNK-interacting proteins Identification of new kinase clusters required for neurite outgrowth and retraction by a loss-of-function RNA interference screen 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 LRRK2 directly phosphorylates Akt1 as a possible physiological substrate: impairment of the kinase activity by Parkinson's disease-associated mutations LRRK2 transport is regulated by its novel interacting partner Rab32 LRRK2 expression in idiopathic and G2019S positive Parkinson's disease subjects: a morphological and quantitative study ArfGAP1 is a GTPase activating protein for LRRK2: reciprocal regulation of ArfGAP1 by LRRK2 Functional interaction of Parkinson's disease-associated LRRK2 with members of the dynamin GTPase superfamily Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation Parkin is an E3 ubiquitin-ligase for normal and mutant ataxin-2 and prevents ataxin-2-induced cell death LRRK2 phosphorylates Snapin and inhibits interaction of Snapin with SNAP-25 Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies PINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neurons Leucine-Rich Repeat Kinase 2 interacts with Parkin, DJ-1 and PINK-1 in a Drosophila melanogaster model of Parkinson's disease 14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization Role of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cells Intrabody and Parkinson's disease Current understanding of LRRK2 in Parkinson's disease: biochemical and structural features and inhibitor design RBR E3 ubiquitin ligases: new structures, new insights, new questions LRRK2 G2019S mutation attenuates microglial motility by inhibiting focal adhesion kinase.Structure of the Parkin in-between-ring domain provides insights for E3-ligase dysfunction in autosomal recessive Parkinson's disease Structure of the Roc–COR domain tandem of C. tepidum, a prokaryotic homologue of the human LRRK2 Parkinson kinase Parkinson's disease genes VPS35 and EIF4G1 interact genetically and converge on α-synuclein Parkin occurs in a stable, non-covalent, approximately 110-kDa complex in brain Enhanced striatal dopamine transmission and motor performance with LRRK2 overexpression in mice is eliminated by familial Parkinson's disease mutation G2019S Disease-toxicant interactions in Parkinson's disease neuropathology R1441C mutation in LRRK2 impairs dopaminergic neurotransmission in mice.Conditional expression of Parkinson's disease-related R1441C LRRK2 in midbrain dopaminergic neurons of mice causes nuclear abnormalities without neurodegeneration Solving the puzzle of Parkinson's disease using induced pluripotent stem cells.Proteome profiling of human cerebrospinal fluid: exploring the potential of capillary electrophoresis with surface modified capillaries for analysis of complex biological samples.Mitochondrial DNA and primary mitochondrial dysfunction in Parkinson's disease.Regulation of LRRK2 stability by the E3 ubiquitin ligase CHIP GTPase activity plays a key role in the pathobiology of LRRK2.Development of a mechanism-based high-throughput screen assay for leucine-rich repeat kinase 2--discovery of LRRK2 inhibitors.Leucine-rich repeat kinase 2-linked Parkinson's disease: clinical and molecular findings.

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P2860

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

http://www.wikidata.org/entity/Q24298689

description

2005 nî lūn-bûn

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2005 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2005年の論文

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2005年論文

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2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

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2005年論文

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2005年论文

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name

Leucine-rich repeat kinase 2 ( ...... induces neuronal degeneration

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Leucine-rich repeat kinase 2 ( ...... induces neuronal degeneration.

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Leucine-rich repeat kinase 2 ( ...... induces neuronal degeneration.

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type

label

Leucine-rich repeat kinase 2 ( ...... induces neuronal degeneration

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Leucine-rich repeat kinase 2 ( ...... induces neuronal degeneration.

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Leucine-rich repeat kinase 2 ( ...... induces neuronal degeneration.

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prefLabel

Leucine-rich repeat kinase 2 ( ...... induces neuronal degeneration

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Leucine-rich repeat kinase 2 ( ...... induces neuronal degeneration.

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Leucine-rich repeat kinase 2 ( ...... induces neuronal degeneration.

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PNAS.0508052102

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Proceedings of the National Academy of Sciences of the United States of America

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Leucine-rich repeat kinase 2 ( ...... induces neuronal degeneration.

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P2093

Darren J Moore

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

Haibing Jiang

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Wanli W Smith

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Yideng Liang

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Zhong Pei

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P2860

Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions

Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase

Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease

Parkin accumulation in aggresomes due to proteasome impairment

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

BAG5 inhibits parkin and enhances dopaminergic neuron degeneration

Mutation in the alpha-synuclein gene identified in families with Parkinson's disease

Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology

Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective

Autosomal recessive early onset parkinsonism is linked to three loci: PARK2, PARK6, and PARK7

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51

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102

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Valina L. Dawson

Christopher A Ross

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7416752

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16352719

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positive regulation of protein autoubiquitination

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1317945

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