Parkinson disease-associated mutation R1441H in LRRK2 prolongs the "active state" of its GTPase domain - Test2 - elhamkhani - TriplyDB

Parkinson disease-associated mutation R1441H in LRRK2 prolongs the "active state" of its GTPase domain

Parkinson disease-associated mutation R1441H in LRRK2 prolongs the "active state" of its GTPase domain

http://www.wikidata.org/entity/Q24338665

about

LRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site status An early endosome regulator, Rab5b, is an LRRK2 kinase substrate Activation Mechanism of LRRK2 and Its Cellular Functions in Parkinson's Disease Ten years and counting: moving leucine-rich repeat kinase 2 inhibitors to the clinic 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 Revisiting the Roco G-protein cycle Protein Kinases and Parkinson's Disease LRRK2 at the interface of autophagosomes, endosomes and lysosomes A novel GTP-binding inhibitor, FX2149, attenuates LRRK2 toxicity in Parkinson's disease models G2385R and I2020T Mutations Increase LRRK2 GTPase Activity Protective LRRK2 R1398H Variant Enhances GTPase and Wnt Signaling Activity.Parkinson's disease-implicated kinases in the brain; insights into disease pathogenesis.Unique functional and structural properties of the LRRK2 protein ATP-binding pocket.Parkinson-Related LRRK2 Mutation R1628P Enables Cdk5 Phosphorylation of LRRK2 and Upregulates Its Kinase Activity LRRK2 autophosphorylation enhances its GTPase activity Structure, function, and leucine-rich repeat kinase 2: On the importance of reproducibility in understanding Parkinson's disease.Oncogenic Mutations Differentially Affect Bax Monomer, Dimer, and Oligomeric Pore Formation in the Membrane.Structural biology of the LRRK2 GTPase and kinase domains: implications for regulation.Genetic, structural, and molecular insights into the function of ras of complex proteins domains.LRRK2 pathobiology in Parkinson's disease.Cellular processes associated with LRRK2 function and dysfunction LRRK2 Pathways Leading to Neurodegeneration.GTP binding regulates cellular localization of Parkinson's disease-associated LRRK2.Mechanisms of LRRK2-dependent neurodegeneration: role of enzymatic activity and protein aggregation.Novel LRRK2 GTP-binding inhibitors reduced degeneration in Parkinson's disease cell and mouse models.Understanding the GTPase Activity of LRRK2: Regulation, Function, and Neurotoxicity.Regulation of LRRK2 promoter activity and gene expression by Sp1.Conformational heterogeneity of the Roc domains in C. tepidum Roc-COR and implications for human LRRK2 Parkinson mutations.The discovery of LRRK2 p.R1441S, a novel mutation for Parkinson's disease, adds to the complexity of a mutational hotspot 68 and FX2149 Attenuate Mutant LRRK2-R1441C-Induced Neural Transport Impairment.Combating Parkinson's disease-associated toxicity by modulating proteostasis.A homologue of the Parkinson's disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover.Rab29 activation of the Parkinson's disease-associated LRRK2 kinase.Mechanisms of Mutant LRRK2 Neurodegeneration.Human R1441C LRRK2 regulates the synaptic vesicle proteome and phosphoproteome in a Drosophila model of Parkinson's disease.Molecular Insights and Functional Implication of LRRK2 Dimerization.LRRK2 Phosphorylation.In Vitro Modeling of Leucine-Rich Repeat Kinase 2 (LRRK2) G2019S-Mediated Parkinson's Disease Pathology.LRRK 2 gene mutations in the pathophysiology of the ROCO domain and therapeutic targets for Parkinson's disease: a review.

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P2860

Parkinson disease-associated mutation R1441H in LRRK2 prolongs the "active state" of its GTPase domain

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description

2014 nî lūn-bûn

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2014 թվականի մարտին հրատարակված գիտական հոդված

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Christopher Burlak

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Chun-Xiang Wu

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Heather Sahm

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Jingling Liao

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Kurt W Vogel

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Mark Federici

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Mu Wang

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Quyen Q Hoang

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R Jeremy Nichols

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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

Kinase activity of mutant LRRK2 mediates neuronal toxicity

Regulation of small GTPases by GEFs, GAPs, and GDIs

Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPase

Structure of the Roc–COR domain tandem of C. tepidum, a prokaryotic homologue of the human LRRK2 Parkinson kinase

Crystal structure of nucleotide-free dynamin

The crystal structure of dynamin

Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology

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

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trisodium guanosine 5'-[beta,gamma-imido]triphosphate

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