Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations - Wikidata - awgldk - TriplyDB

Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations

Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations

http://www.wikidata.org/entity/Q33836384

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alpha-Synuclein and neuronal cell death Redistribution of DAT/α-synuclein complexes visualized by "in situ" proximity ligation assay in transgenic mice modelling early Parkinson's disease Dynamic structural flexibility of α-synuclein Immunotherapy in Parkinson's Disease: Micromanaging Alpha-Synuclein Aggregation The Synaptic Function of α-Synuclein The contribution of alpha synuclein to neuronal survival and function - Implications for Parkinson's disease Alpha-Synuclein in Parkinson's Disease: From Pathogenetic Dysfunction to Potential Clinical Application Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications Distinct α-synuclein strains differentially promote tau inclusions in neurons Passive immunization reduces behavioral and neuropathological deficits in an alpha-synuclein transgenic model of Lewy body disease Value of genetic models in understanding the cause and mechanisms of Parkinson's disease Astrocytic expression of Parkinson's disease-related A53T alpha-synuclein causes neurodegeneration in mice.Cathepsin D is the main lysosomal enzyme involved in the degradation of alpha-synuclein and generation of its carboxy-terminally truncated species.GTPase activity plays a key role in the pathobiology of LRRK2.The first N-terminal amino acids of alpha-synuclein are essential for alpha-helical structure formation in vitro and membrane binding in yeast.N-Terminal Extensions Retard Aβ42 Fibril Formation but Allow Cross-Seeding and Coaggregation with Aβ42 Molecular chaperones and protein folding as therapeutic targets in Parkinson's disease and other synucleinopathies Synphilin-1 enhances α-synuclein aggregation in yeast and contributes to cellular stress and cell death in a Sir2-dependent manner The alpha-synuclein 5'untranslated region targeted translation blockers: anti-alpha synuclein efficacy of cardiac glycosides and Posiphen.Metabolic Investigations of the Molecular Mechanisms Associated with Parkinson's Disease Reducing C-terminal-truncated alpha-synuclein by immunotherapy attenuates neurodegeneration and propagation in Parkinson's disease-like models.Critical role of truncated α-synuclein and aggregates in Parkinson's disease and incidental Lewy body disease.Quantitative measurement of intact alpha-synuclein proteoforms from post-mortem control and Parkinson's disease brain tissue by intact protein mass spectrometry.Overexpression of the calpain-specific inhibitor calpastatin reduces human alpha-Synuclein processing, aggregation and synaptic impairment in [A30P]αSyn transgenic mice.Neurodegenerative models in Drosophila: polyglutamine disorders, Parkinson disease, and amyotrophic lateral sclerosis.Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR.Cross dimerization of amyloid-β and αsynuclein proteins in aqueous environment: a molecular dynamics simulations study.Identification of a helical intermediate in trifluoroethanol-induced alpha-synuclein aggregation Abnormal neurites containing C-terminally truncated alpha-synuclein are present in Alzheimer's disease without conventional Lewy body pathology.Quantitative analysis of α-synuclein solubility in living cells using split GFP complementation α-Synuclein Transgenic Drosophila As a Model of Parkinson's Disease and Related Synucleinopathies.A relationship between the transient structure in the monomeric state and the aggregation propensities of α-synuclein and β-synuclein Parkin depletion delays motor decline dose-dependently without overtly affecting neuropathology in α-synuclein transgenic mice.Diagnosis and treatment of Parkinson disease: molecules to medicine Impairment of mitochondria in adult mouse brain overexpressing predominantly full-length, N-terminally acetylated human α-synuclein Role of matrix metalloproteinase 3-mediated alpha-synuclein cleavage in dopaminergic cell death.The many faces of α-synuclein: from structure and toxicity to therapeutic target.Environmental neurotoxic challenge of conditional alpha-synuclein transgenic mice predicts a dopaminergic olfactory-striatal interplay in early PD.Exogenous α-synuclein fibrils induce Lewy body pathology leading to synaptic dysfunction and neuron death Role of α-synuclein in inducing innate and adaptive immunity in Parkinson disease.

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P2860

Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations

http://www.wikidata.org/entity/Q33836384

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2005 nî lūn-bûn

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2005 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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Aggregation promoting C-termin ...... son's disease-linked mutations

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Aggregation promoting C-termin ...... son's disease-linked mutations

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Aggregation promoting C-termin ...... son's disease-linked mutations

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Aggregation promoting C-termin ...... son's disease-linked mutations

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Aggregation promoting C-termin ...... son's disease-linked mutations

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Aggregation promoting C-termin ...... son's disease-linked mutations

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Proceedings of the National Academy of Sciences of the United States of America

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Aggregation promoting C-termin ...... son's disease-linked mutations

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P2093

Donald L Price

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Juan C Troncoso

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Laura Marsh

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Neva West

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Olga Pletnikova

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Pekka Jäkälä

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Wenxue Li

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P2860

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism

Mutation in the alpha-synuclein gene identified in families with Parkinson's disease

alpha-Synuclein locus triplication causes Parkinson's disease

Alpha-synuclein in Lewy bodies

Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders

Human alpha-synuclein-harboring familial Parkinson's disease-linked Ala-53 --> Thr mutation causes neurodegenerative disease with alpha-synuclein aggregation in transgenic mice.

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2162-2167

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6

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102

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Tobias Hartmann

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8048440

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15684072

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Parkinson's disease

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548541

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