Neuronal inclusions of α-synuclein contribute to the pathogenesis of Krabbe disease. - Wikidata - awgldk - TriplyDB

Neuronal inclusions of α-synuclein contribute to the pathogenesis of Krabbe disease.

Neuronal inclusions of α-synuclein contribute to the pathogenesis of Krabbe disease.

http://www.wikidata.org/entity/Q37687353

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The Synaptic Function of α-Synuclein Lysosomal Re-acidification Prevents Lysosphingolipid-Induced Lysosomal Impairment and Cellular Toxicity Aberrant production of tenascin-C in globoid cell leukodystrophy alters psychosine-induced microglial functions Mechanism of neuromuscular dysfunction in Krabbe disease.Astrocytes and lysosomal storage diseases.Lysosomal Storage Diseases-Regulating Neurodegeneration.Patient fibroblasts-derived induced neurons demonstrate autonomous neuronal defects in adult-onset Krabbe disease.Lithium improves cell viability in psychosine-treated MO3.13 human oligodendrocyte cell line via autophagy activation.Biochemical, cell biological, pathological, and therapeutic aspects of Krabbe's disease.Axonal pathology in Krabbe's disease: The cytoskeleton as an emerging therapeutic target.Substrate reduction therapy for Krabbe's disease.Perspective on innovative therapies for globoid cell leukodystrophy.Coupling of the non-amyloid-component (NAC) domain and the KTK(E/Q)GV repeats stabilize the α-synuclein fibrils.Beyond Krabbe's disease: The potential contribution of galactosylceramidase deficiency to neuronal vulnerability in late-onset synucleinopathies Long-Term Improvement of Neurological Signs and Metabolic Dysfunction in a Mouse Model of Krabbe's Disease after Global Gene Therapy.Analysis of age-related changes in psychosine metabolism in the human brain.Glycosphingolipid levels and glucocerebrosidase activity are altered in normal aging of the mouse brain.Is Parkinson's disease a lysosomal disorder?α-Synuclein interacts directly but reversibly with psychosine: implications for α-synucleinopathies

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Neuronal inclusions of α-synuclein contribute to the pathogenesis of Krabbe disease.

http://www.wikidata.org/entity/Q37687353

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 20 February 2014

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Neuronal inclusions of α-synuclein contribute to the pathogenesis of Krabbe disease.

@en

Neuronal inclusions of α-synuclein contribute to the pathogenesis of Krabbe disease.

@nl

type

label

Neuronal inclusions of α-synuclein contribute to the pathogenesis of Krabbe disease.

@en

Neuronal inclusions of α-synuclein contribute to the pathogenesis of Krabbe disease.

@nl

prefLabel

Neuronal inclusions of α-synuclein contribute to the pathogenesis of Krabbe disease.

@en

Neuronal inclusions of α-synuclein contribute to the pathogenesis of Krabbe disease.

@nl

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The Journal of Pathology

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Neuronal inclusions of α-synuclein contribute to the pathogenesis of Krabbe disease

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Aurora Lopez-Rosas

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Benjamin R Smith

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Ernesto R Bongarzone

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Jose I Gallea

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Kumiko I Claycomb

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Maria I Givogri

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Marta B Santos

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Stephen J Crocker

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P2860

Alpha-synuclein in Lewy bodies

Brain stem control of swallowing: neuronal network and cellular mechanisms

Molecular genetics of Krabbe disease (globoid cell leukodystrophy): diagnostic and clinical implications

Targeting oligomers in neurodegenerative disorders: lessons from α-synuclein, tau, and amyloid-β peptide

Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking alpha-synuclein

Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein

Molecular cloning and expression of cDNA for murine galactocerebrosidase and mutation analysis of the twitcher mouse, a model of Krabbe's disease

Central neurocircuitry associated with emesis

Molecular genetics of Krabbe disease (globoid cell leukodystrophy): Diagnostic and clinical implications

Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function

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509-521

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scholarly article

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10.1002/PATH.4328

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5

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232

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Richard van Breemen

María Soledad Celej

Michael S Marshall

Ludovico Cantuti

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2014-02-20T00:00:00Z

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24415155

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3977150

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