Identification of potential protein interactors of Lrrk2 - Test2 - elhamkhani - TriplyDB

Identification of potential protein interactors of Lrrk2

Identification of potential protein interactors of Lrrk2

http://www.wikidata.org/entity/Q24301415

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MKK6 binds and regulates expression of Parkinson's disease-related protein LRRK2 Heterodimerization of Lrrk1-Lrrk2: Implications for LRRK2-associated Parkinson disease LRRK2 phosphorylates tubulin-associated tau but not the free molecule: LRRK2-mediated regulation of the tau-tubulin association and neurite outgrowth Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant LRRK2 phosphorylates Snapin and inhibits interaction of Snapin with SNAP-25 The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylation Role of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cells Neuronal dark matter: the emerging role of microRNAs in neurodegeneration Gene and MicroRNA transcriptome analysis of Parkinson's related LRRK2 mouse models The chaperone activity of heat shock protein 90 is critical for maintaining the stability of leucine-rich repeat kinase 2.Regulation of LRRK2 stability by the E3 ubiquitin ligase CHIP The WD40 domain is required for LRRK2 neurotoxicity.The amyloid precursor protein/protease nexin 2 Kunitz inhibitor domain is a highly specific substrate of mesotrypsin.Leucine-rich repeat kinase 2 (LRRK2): a key player in the pathogenesis of Parkinson's disease The 19-amino acid insertion in the tumor-associated splice isoform Rac1b confers specific binding to p120 catenin.Mesotrypsin promotes malignant growth of breast cancer cells through shedding of CD109 Models for LRRK2-Linked Parkinsonism.Coordinate Regulation of Neurite Outgrowth by LRRK2 and Its Interactor, Rab5.Molecular chaperones in Parkinson's disease--present and future Mechanisms in dominant parkinsonism: The toxic triangle of LRRK2, alpha-synuclein, and tau.Purine-scaffold Hsp90 inhibitors.Kinase inhibitors arrest neurodegeneration in cell and C. elegans models of LRRK2 toxicity The Roc domain of leucine-rich repeat kinase 2 is sufficient for interaction with microtubules Leucine-rich repeat kinase 2 mutations and Parkinson's disease: three questions.Zeroing in on LRRK2-linked pathogenic mechanisms in Parkinson's disease.The function of ROCO proteins in health and disease.Update on the functional biology of Lrrk2.Dependence of leucine-rich repeat kinase 2 (LRRK2) kinase activity on dimerization.LRRK2 in Parkinson's disease: in vivo models and approaches for understanding pathogenic roles.Pharmacological therapy in Parkinson's disease: focus on neuroprotection.Understanding the molecular basis of Parkinson's disease, identification of biomarkers and routes to therapy.Protective role of heat shock proteins in Parkinson's disease.On the road to leucine-rich repeat kinase 2 signalling: evidence from cellular and in vivo studies.Phosphorylation of LRRK2: from kinase to substrate.Cellular processes associated with LRRK2 function and dysfunction LRRK2 Pathways Leading to Neurodegeneration.LRRK2 is a component of granular alpha-synuclein pathology in the brainstem of Parkinson's disease.LRRK2 in Transcription and Translation Regulation: Relevance for Parkinson's Disease.Phosphoproteomic evaluation of pharmacological inhibition of leucine-rich repeat kinase 2 reveals significant off-target effects of LRRK-2-IN-1.Parkinson's disease: leucine-rich repeat kinase 2 and autophagy, intimate enemies.

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P2860

Identification of potential protein interactors of Lrrk2

http://www.wikidata.org/entity/Q24301415

description

2007 nî lūn-bûn

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2007 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2007 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

Identification of potential protein interactors of Lrrk2

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Identification of potential protein interactors of Lrrk2

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Identification of potential protein interactors of Lrrk2

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Identification of potential protein interactors of Lrrk2

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Identification of potential protein interactors of Lrrk2

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Identification of potential protein interactors of Lrrk2

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Identification of potential protein interactors of Lrrk2

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Identification of potential protein interactors of Lrrk2

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Identification of potential protein interactors of Lrrk2

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Identification of potential protein interactors of Lrrk2

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Identification of potential protein interactors of Lrrk2

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Identification of potential protein interactors of Lrrk2

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J.PARKRELDIS.2007.01.008

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Parkinsonism and Related Disorders

P1476

Identification of potential protein interactors of Lrrk2

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P2093

Benjamin Madden

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Jacob H Hines

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Jennifer Szutu

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Julie P Taylor

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Justus C Dächsel

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Kelly M Hinkle

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Matthew J Farrer

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Rachel M Bailey

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Su San Mok

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P2860

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

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

The familial Parkinsonism gene LRRK2 regulates neurite process morphology

Localization of LRRK2 to membranous and vesicular structures in mammalian brain

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

Kinase activity is required for the toxic effects of mutant LRRK2/dardarin

Genetics of Parkinson disease: paradigm shifts and future prospects.

The LRRK2 Gly2385Arg variant is associated with Parkinson's disease: genetic and functional evidence.

Biochemical and pathological characterization of Lrrk2.

LRRK2 expression in normal and pathologic human brain and in human cell lines.

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382-5

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10.1016/J.PARKRELDIS.2007.01.008

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7

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13

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Leonard Petrucelli

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2007-10-01T00:00:00Z

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6416544

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17400507

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2970619

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