ATP13A2 (PARK9) protein levels are reduced in brain tissue of cases with Lewy bodies - Wikidata - wikimedia - TriplyDB

ATP13A2 (PARK9) protein levels are reduced in brain tissue of cases with Lewy bodies

ATP13A2 (PARK9) protein levels are reduced in brain tissue of cases with Lewy bodies

http://www.wikidata.org/entity/Q33715666

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Reduced glucocerebrosidase is associated with increased α-synuclein in sporadic Parkinson's disease Emerging preclinical pharmacological targets for Parkinson's disease Parkinson's disease-linked human PARK9/ATP13A2 maintains zinc homeostasis and promotes α-Synuclein externalization via exosomes.Legal but lethal: functional protein aggregation at the verge of toxicity LIMP-2 expression is critical for β-glucocerebrosidase activity and α-synuclein clearance Atp13a2 expression in the periaqueductal gray is decreased in the Pink1 -/- rat model of Parkinson disease.Copy number variability in Parkinson's disease: assembling the puzzle through a systems biology approach Mutations in the ATP13A2 gene and Parkinsonism: a preliminary review.Splicing: is there an alternative contribution to Parkinson's disease?Defective autophagy in Parkinson's disease: lessons from genetics.The role of ATP13A2 in Parkinson's disease: Clinical phenotypes and molecular mechanisms.Therapeutic potential of autophagy-enhancing agents in Parkinson's disease.Altered ceramide acyl chain length and ceramide synthase gene expression in Parkinson’s disease.Mechanisms of Gene-Environment Interactions in Parkinson's Disease.Lysosomal-associated membrane protein 2 isoforms are differentially affected in early Parkinson's disease.Biometal Dyshomeostasis and Toxic Metal Accumulations in the Development of Alzheimer's Disease.Parkinson Disease from Mendelian Forms to Genetic Susceptibility: New Molecular Insights into the Neurodegeneration Process.Pathogenic LRRK2 mutations, through increased kinase activity, produce enlarged lysosomes with reduced degradative capacity and increase ATP13A2 expression.

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P2860

ATP13A2 (PARK9) protein levels are reduced in brain tissue of cases with Lewy bodies

http://www.wikidata.org/entity/Q33715666

description

2013 nî lūn-bûn

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2013 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2013 թվականի մայիսին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

ATP13A2 (PARK9) protein levels are reduced in brain tissue of cases with Lewy bodies

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ATP13A2 (PARK9) protein levels are reduced in brain tissue of cases with Lewy bodies

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type

label

ATP13A2 (PARK9) protein levels are reduced in brain tissue of cases with Lewy bodies

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ATP13A2 (PARK9) protein levels are reduced in brain tissue of cases with Lewy bodies

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prefLabel

ATP13A2 (PARK9) protein levels are reduced in brain tissue of cases with Lewy bodies

@ast

ATP13A2 (PARK9) protein levels are reduced in brain tissue of cases with Lewy bodies

@en

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P1433

Acta neuropathologica communications

P1476

ATP13A2 (PARK9) protein levels are reduced in brain tissue of cases with Lewy bodies

@en

P2093

Amanda M Gysbers

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Antony A Cooper

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Karen E Murphy

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Louise Cottle

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P2860

Pathogenic effects of novel mutations in the P-type ATPase ATP13A2 (PARK9) causing Kufor-Rakeb syndrome, a form of early-onset parkinsonism

Identification of novel ATP13A2 interactors and their role in α-synuclein misfolding and toxicity

Alpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity

Lysosomal dysfunction in Parkinson disease: ATP13A2 gets into the groove

ATP13A2 regulates mitochondrial bioenergetics through macroautophagy

Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase

PARK9-associated ATP13A2 localizes to intracellular acidic vesicles and regulates cation homeostasis and neuronal integrity

Staging of brain pathology related to sporadic Parkinson's disease

The role of the Parkinson's disease gene PARK9 in essential cellular pathways and the manganese homeostasis network in yeast.

Deficiency of ATP13A2 leads to lysosomal dysfunction, α-synuclein accumulation, and neurotoxicity.

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11

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scholarly article

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10.1186/2051-5960-1-11

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1

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Glenda Halliday

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2013-05-09T00:00:00Z

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257885167

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4046687

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