Addition of exogenous α-synuclein preformed fibrils to primary neuronal cultures to seed recruitment of endogenous α-synuclein to Lewy body and Lewy neurite-like aggregates.
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Transmission of α-synucleinopathy from olfactory structures deep into the temporal lobe.More than a Rumor Spreads in Parkinson's DiseaseLegal but lethal: functional protein aggregation at the verge of toxicityIntrastriatal injection of pre-formed mouse α-synuclein fibrils into rats triggers α-synuclein pathology and bilateral nigrostriatal degenerationFormation of α-synuclein Lewy neurite-like aggregates in axons impedes the transport of distinct endosomes.Toll-like receptor 4 stimulation with monophosphoryl lipid A ameliorates motor deficits and nigral neurodegeneration triggered by extraneuronal α-synucleinopathyGlucocerebrosidase Deficiency in Drosophila Results in α-Synuclein-Independent Protein Aggregation and Neurodegeneration.Direct Observation of α-Synuclein Amyloid Aggregates in Endocytic Vesicles of Neuroblastoma Cells.shRNA-Based Screen Identifies Endocytic Recycling Pathway Components That Act as Genetic Modifiers of Alpha-Synuclein Aggregation, Secretion and Toxicity.microRNA-155 Regulates Alpha-Synuclein-Induced Inflammatory Responses in Models of Parkinson Disease.G2019S-LRRK2 Expression Augments α-Synuclein Sequestration into Inclusions in Neurons.Widespread transneuronal propagation of α-synucleinopathy triggered in olfactory bulb mimics prodromal Parkinson's diseaseProtein kinase Cδ upregulation in microglia drives neuroinflammatory responses and dopaminergic neurodegeneration in experimental models of Parkinson's disease.Environmental and genetic factors support the dissociation between α-synuclein aggregation and toxicity.Increased fibroblast chymase production mediates procollagen autophagic digestion in volume overload.TMEM175 deficiency impairs lysosomal and mitochondrial function and increases α-synuclein aggregation.The Identification of Alpha-Synuclein as the First Parkinson Disease Gene.Neuropathology of multiple system atrophy: new thoughts about pathogenesis.Impaired endo-lysosomal membrane integrity accelerates the seeding progression of α-synuclein aggregates.Review: Spreading the word: precise animal models and validated methods are vital when evaluating prion-like behaviour of alpha-synuclein.Cellular internalization of alpha-synuclein aggregates by cell surface heparan sulfate depends on aggregate conformation and cell typeThe Effect of Fragmented Pathogenic α-Synuclein Seeds on Prion-like Propagation.Endocytic vesicle rupture is a conserved mechanism of cellular invasion by amyloid proteins.How can rAAV-α-synuclein and the fibril α-synuclein models advance our understanding of Parkinson's disease?Novel conformation-selective alpha-synuclein antibodies raised against different in vitro fibril forms show distinct patterns of Lewy pathology in Parkinson's disease.Trehalose does not improve neuronal survival on exposure to alpha-synuclein pre-formed fibrils.Selective neuronal vulnerability in Parkinson disease.Modeling Parkinson's disease pathology by combination of fibril seeds and α-synuclein overexpression in the rat brain.Pathological α-synuclein transmission initiated by binding lymphocyte-activation gene 3.Protein arginylation targets alpha synuclein, facilitates normal brain health, and prevents neurodegenerationSelective imaging of internalized proteopathic α-synuclein seeds in primary neurons reveals mechanistic insight into transmission of synucleinopathies.Amyloid single-cell cytotoxicity assays by nanomotion detection.LRRK2 Antisense Oligonucleotides Ameliorate α-Synuclein Inclusion Formation in a Parkinson's Disease Mouse Model.Molecular and Biological Compatibility with Host Alpha-Synuclein Influences Fibril Pathogenicity.Tunneling nanotubes spread fibrillar α-synuclein by intercellular trafficking of lysosomes.The importance of developing strain-specific models of neurodegenerative disease.The Molecular Physiopathogenesis of Islet Amyloidosis.Intercellular transfer of pathogenic α-synuclein by extracellular vesicles is induced by the lipid peroxidation product 4-hydroxynonenal.Selective lowering of synapsins induced by oligomeric α-synuclein exacerbates memory deficits.Phosphorylated exogenous alpha-synuclein fibrils exacerbate pathology and induce neuronal dysfunction in mice.
P2860
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P2860
Addition of exogenous α-synuclein preformed fibrils to primary neuronal cultures to seed recruitment of endogenous α-synuclein to Lewy body and Lewy neurite-like aggregates.
description
2014 nî lūn-bûn
@nan
2014 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Addition of exogenous α-synucl ...... Lewy neurite-like aggregates.
@ast
Addition of exogenous α-synucl ...... Lewy neurite-like aggregates.
@en
type
label
Addition of exogenous α-synucl ...... Lewy neurite-like aggregates.
@ast
Addition of exogenous α-synucl ...... Lewy neurite-like aggregates.
@en
prefLabel
Addition of exogenous α-synucl ...... Lewy neurite-like aggregates.
@ast
Addition of exogenous α-synucl ...... Lewy neurite-like aggregates.
@en
P2860
P356
P1433
P1476
Addition of exogenous α-synucl ...... d Lewy neurite-like aggregates
@en
P2093
Laura A Volpicelli-Daley
Virginia M-Y Lee
P2860
P2888
P304
P356
10.1038/NPROT.2014.143
P50
P577
2014-08-14T00:00:00Z