Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies
about
Leucine-rich repeat kinase 2 binds to neuronal vesicles through protein interactions mediated by its C-terminal WD40 domainAn early endosome regulator, Rab5b, is an LRRK2 kinase substrateDeconvoluting the complexity of autophagy and Parkinson's disease for potential therapeutic purposeHeterogeneity of leucine-rich repeat kinase 2 mutations: genetics, mechanisms and therapeutic implicationsThe role of the LRRK2 gene in ParkinsonismCell-based screening: extracting meaning from complex data.Progressive dopaminergic alterations and mitochondrial abnormalities in LRRK2 G2019S knock-in miceGenetic and pharmacological evidence that G2019S LRRK2 confers a hyperkinetic phenotype, resistant to motor decline associated with aging.The LRRK2 inhibitor GSK2578215A induces protective autophagy in SH-SY5Y cells: involvement of Drp-1-mediated mitochondrial fission and mitochondrial-derived ROS signaling.LRRK2 and ubiquitination: implications for kinase inhibitor therapyActivation of FADD-Dependent Neuronal Death Pathways as a Predictor of Pathogenicity for LRRK2 Mutations.Parkinson's disease-associated genetic variation is linked to quantitative expression of inflammatory genes.Clinical Trials in a Dish: The Potential of Pluripotent Stem Cells to Develop Therapies for Neurodegenerative Diseases.Altered Development of Synapse Structure and Function in Striatum Caused by Parkinson's Disease-Linked LRRK2-G2019S MutationStructure, function, and leucine-rich repeat kinase 2: On the importance of reproducibility in understanding Parkinson's disease.Mutations in LRRK2 impair NF-κB pathway in iPSC-derived neurons.Overexpression of Parkinson's Disease-Associated Mutation LRRK2 G2019S in Mouse Forebrain Induces Behavioral Deficits and α-Synuclein PathologyLRRK2, a puzzling protein: insights into Parkinson's disease pathogenesisInteraction of LRRK2 with kinase and GTPase signaling cascadesLRRK2 pathobiology in Parkinson's disease.The Role of α-Synuclein and LRRK2 in Tau Phosphorylation.LRRK2 Pathways Leading to Neurodegeneration.Alterations in late endocytic trafficking related to the pathobiology of LRRK2-linked Parkinson's disease.Genes associated with Parkinson's disease: regulation of autophagy and beyond.Targeting the Autophagy/Lysosomal Degradation Pathway in Parkinson's Disease.A proteomic analysis of LRRK2 binding partners reveals interactions with multiple signaling components of the WNT/PCP pathway.Functional Impairment in Miro Degradation and Mitophagy Is a Shared Feature in Familial and Sporadic Parkinson's Disease.Developmental alterations in Huntington's disease neural cells and pharmacological rescue in cells and mice.Neurotrophin Signaling and Stem Cells-Implications for Neurodegenerative Diseases and Stem Cell Therapy.Mechanisms of LRRK2-dependent neurodegeneration: role of enzymatic activity and protein aggregation.Targeting LRRK2 in Parkinson's disease: an update on recent developments.Regulation of LRRK2 promoter activity and gene expression by Sp1.Pharmacological LRRK2 kinase inhibition induces LRRK2 protein destabilization and proteasomal degradationLRRK2 Antisense Oligonucleotides Ameliorate α-Synuclein Inclusion Formation in a Parkinson's Disease Mouse Model.Nrf2 mitigates LRRK2- and α-synuclein-induced neurodegeneration by modulating proteostasis.The G-quadruplex DNA stabilizing drug pyridostatin promotes DNA damage and downregulates transcription of Brca1 in neurons.LRRK2 Expression Is Deregulated in Fibroblasts and Neurons from Parkinson Patients with Mutations in PINK1.Mutations in LRRK2 potentiate age-related impairment of autophagic flux.E46K α-synuclein pathological mutation causes cell-autonomous toxicity without altering protein turnover or aggregation.iPS cells in the study of PD molecular pathogenesis.
P2860
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P2860
Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies
description
2014 nî lūn-bûn
@nan
2014 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Mutant LRRK2 toxicity in neuro ...... e activity or inclusion bodies
@ast
Mutant LRRK2 toxicity in neuro ...... e activity or inclusion bodies
@en
Mutant LRRK2 toxicity in neuro ...... e activity or inclusion bodies
@en-gb
Mutant LRRK2 toxicity in neuro ...... e activity or inclusion bodies
@nl
type
label
Mutant LRRK2 toxicity in neuro ...... e activity or inclusion bodies
@ast
Mutant LRRK2 toxicity in neuro ...... e activity or inclusion bodies
@en
Mutant LRRK2 toxicity in neuro ...... e activity or inclusion bodies
@en-gb
Mutant LRRK2 toxicity in neuro ...... e activity or inclusion bodies
@nl
prefLabel
Mutant LRRK2 toxicity in neuro ...... e activity or inclusion bodies
@ast
Mutant LRRK2 toxicity in neuro ...... e activity or inclusion bodies
@en
Mutant LRRK2 toxicity in neuro ...... e activity or inclusion bodies
@en-gb
Mutant LRRK2 toxicity in neuro ...... e activity or inclusion bodies
@nl
P2093
P2860
P921
P3181
P1476
Mutant LRRK2 toxicity in neuro ...... e activity or inclusion bodies
@en
P2093
Gaia Skibinski
Ken Nakamura
Steven Finkbeiner
P2860
P304
P3181
P356
10.1523/JNEUROSCI.2712-13.2014
P407
P577
2014-01-08T00:00:00Z