The Parkinson's disease protein LRRK2 impairs proteasome substrate clearance without affecting proteasome catalytic activity.
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Disrupted autophagy leads to dopaminergic axon and dendrite degeneration and promotes presynaptic accumulation of α-synuclein and LRRK2 in the brainProtein degradation pathways in Parkinson's disease: curse or blessingLeucine-rich repeat kinase 2 (LRRK2)-deficient rats exhibit renal tubule injury and perturbations in metabolic and immunological homeostasisDysregulation of autophagy and mitochondrial function in Parkinson's diseaseNeurodegenerative phenotypes in an A53T α-synuclein transgenic mouse model are independent of LRRK2.The ubiquitin-proteasome system in neurodegenerative diseases: precipitating factor, yet part of the solutionMutant LRRK2 enhances glutamatergic synapse activity and evokes excitotoxic dendrite degenerationInterplay between Leucine-Rich Repeat Kinase 2 (LRRK2) and p62/SQSTM-1 in Selective AutophagyP73 and age-related diseases: is there any link with Parkinson Disease?scyllo-Inositol promotes robust mutant Huntingtin protein degradation.Mechanisms of LRRK2-mediated neurodegeneration.LRRK2, a puzzling protein: insights into Parkinson's disease pathogenesisScreening for E3-ubiquitin ligase inhibitors: challenges and opportunities.The Role of α-Synuclein and LRRK2 in Tau Phosphorylation.LRRK2 and Autophagy.Models of LRRK2-Associated Parkinson's Disease.Iron overload causes endolysosomal deficits modulated by NAADP-regulated 2-pore channels and RAB7A.LRRK2 Promotes Tau Accumulation, Aggregation and Release.Chaperone-dependent Neurodegeneration: A Molecular Perspective on Therapeutic Intervention.Analysis of apoptosis methods recently used in Cancer Research and Cell Death & Disease publications.Lack of exacerbation of neurodegeneration in a double transgenic mouse model of mutant LRRK2 and tau.Astrocytes in a dish: Using pluripotent stem cells to model neurodegenerative and neurodevelopmental disorders.Pathogenic LRRK2 mutations, through increased kinase activity, produce enlarged lysosomes with reduced degradative capacity and increase ATP13A2 expression.Dangerous duet: LRRK2 and α-synuclein jam at CMA.Effect of leucine-rich repeat kinase 2 (LRRK2) on protein synthesisA new hypothesis for Parkinson's disease pathogenesis: GTPase-p38 MAPK signaling and autophagy as convergence points of etiology and genomics
P2860
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P2860
The Parkinson's disease protein LRRK2 impairs proteasome substrate clearance without affecting proteasome catalytic activity.
description
2011 nî lūn-bûn
@nan
2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
The Parkinson's disease protei ...... proteasome catalytic activity.
@ast
The Parkinson's disease protei ...... proteasome catalytic activity.
@en
type
label
The Parkinson's disease protei ...... proteasome catalytic activity.
@ast
The Parkinson's disease protei ...... proteasome catalytic activity.
@en
prefLabel
The Parkinson's disease protei ...... proteasome catalytic activity.
@ast
The Parkinson's disease protei ...... proteasome catalytic activity.
@en
P2093
P2860
P356
P1476
The Parkinson's disease protei ...... proteasome catalytic activity.
@en
P2093
A Mansilla
D C Rubinsztein
M Lichtenberg
V R Zecchini
P2860
P356
10.1038/CDDIS.2011.81
P577
2011-08-25T00:00:00Z