Pathogenic LRRK2 mutations, through increased kinase activity, produce enlarged lysosomes with reduced degradative capacity and increase ATP13A2 expression. - Wikidata - awgldk - TriplyDB

Pathogenic LRRK2 mutations, through increased kinase activity, produce enlarged lysosomes with reduced degradative capacity and increase ATP13A2 expression.

Pathogenic LRRK2 mutations, through increased kinase activity, produce enlarged lysosomes with reduced degradative capacity and increase ATP13A2 expression.

http://www.wikidata.org/entity/Q53387936

about

mTOR independent regulation of macroautophagy by Leucine Rich Repeat Kinase 2 via Beclin-1 Additional rare variant analysis in Parkinson's disease cases with and without known pathogenic mutations: evidence for oligogenic inheritance.Acidic Ca2+ stores in neurodegeneration.G2019S-LRRK2 Expression Augments α-Synuclein Sequestration into Inclusions in Neurons.Endocytic membrane trafficking and neurodegenerative disease.Disorders of lysosomal acidification-The emerging role of v-ATPase in aging and neurodegenerative disease.Prelysosomal Compartments in the Unconventional Secretion of Amyloidogenic Seeds.The LRRK2-macroautophagy axis and its relevance to Parkinson's disease LRRK2 and the Immune System.The Role of Astrocyte Dysfunction in Parkinson's Disease Pathogenesis.Protection against Mitochondrial and Metal Toxicity Depends on Functional Lipid Binding Sites in ATP13A2.68 and FX2149 Attenuate Mutant LRRK2-R1441C-Induced Neural Transport Impairment.Connecting Ca2+ and lysosomes to Parkinson disease.Taking out the garbage: cathepsin D and calcineurin in neurodegeneration.Elevated LRRK2 autophosphorylation in brain-derived and peripheral exosomes in LRRK2 mutation carriers.Reduced LRRK2 in association with retromer dysfunction in post-mortem brain tissue from LRRK2 mutation carriers.Familial knockin mutation of LRRK2 causes lysosomal dysfunction and accumulation of endogenous insoluble α-synuclein in neurons.Autophagy impairment in Parkinson's disease.Convergent pathways in Parkinson's disease.Achieving neuroprotection with LRRK2 kinase inhibitors in Parkinson disease.Regulation of LRRK2 by Phosphatases.Alteration of endosomal trafficking is associated with early-onset parkinsonism caused by SYNJ1 mutations.Astrocytes in a dish: Using pluripotent stem cells to model neurodegenerative and neurodevelopmental disorders.Two-pore channels and disease.LRRK2 activity does not dramatically alter α-synuclein pathology in primary neurons.LRRK2 kinase regulates α-synuclein propagation via RAB35 phosphorylation A new hypothesis for Parkinson's disease pathogenesis: GTPase-p38 MAPK signaling and autophagy as convergence points of etiology and genomics

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P2860

Pathogenic LRRK2 mutations, through increased kinase activity, produce enlarged lysosomes with reduced degradative capacity and increase ATP13A2 expression.

http://www.wikidata.org/entity/Q53387936

description

2015 nî lūn-bûn

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2015年の論文

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年学术文章

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name

Pathogenic LRRK2 mutations, th ...... d increase ATP13A2 expression.

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Pathogenic LRRK2 mutations, th ...... d increase ATP13A2 expression.

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type

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Pathogenic LRRK2 mutations, th ...... d increase ATP13A2 expression.

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Pathogenic LRRK2 mutations, th ...... d increase ATP13A2 expression.

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Pathogenic LRRK2 mutations, th ...... d increase ATP13A2 expression.

@en

Pathogenic LRRK2 mutations, th ...... d increase ATP13A2 expression.

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Human Molecular Genetics

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Pathogenic LRRK2 mutations, th ...... d increase ATP13A2 expression.

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P2093

Anastasia G Henry

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Elie Needle

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Harry Samaroo

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Kewa Mou

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Soheil Aghamohammadzadeh

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Warren D Hirst

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Yi Chen

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P2860

CLN3 protein regulates lysosomal pH and alters intracellular processing of Alzheimer's amyloid-beta protein precursor and cathepsin D in human cells

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

LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool

Leucine-rich repeat kinase 2 regulates autophagy through a calcium-dependent pathway involving NAADP

LRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site status

The R1441C mutation of LRRK2 disrupts GTP hydrolysis

Kinase activity of mutant LRRK2 mediates neuronal toxicity

Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant

Dysregulation of lysosomal morphology by pathogenic LRRK2 is corrected by TPC2 inhibition

RAB7L1 interacts with LRRK2 to modify intraneuronal protein sorting and Parkinson's disease risk

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6013-6028

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scholarly article

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10.1093/HMG/DDV314

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21

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24

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2015-08-06T00:00:00Z

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P698

26251043

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