A novel, high-efficiency cellular model of fibrillar alpha-synuclein inclusions and the examination of mutations that inhibit amyloid formation
about
The chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicityAlpha-synuclein cell-to-cell transfer and seeding in grafted dopaminergic neurons in vivoPropagation of alpha-synuclein pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies.More than a Rumor Spreads in Parkinson's DiseaseAlpha-synuclein spreading in Parkinson's diseaseAntibodies against alpha-synuclein reduce oligomerization in living cellsIntramuscular injection of α-synuclein induces CNS α-synuclein pathology and a rapid-onset motor phenotype in transgenic mice.Quantifying prefibrillar amyloids in vitro by using a "thioflavin-like" spectroscopic method.Intrastriatal injection of α-synuclein can lead to widespread synucleinopathy independent of neuroanatomic connectivity.Multiple system atrophy: current and future approaches to managementp62/SQSTM1-dependent autophagy of Lewy body-like α-synuclein inclusionsAugmentation of phenotype in a transgenic Parkinson mouse heterozygous for a Gaucher mutationTransfer of human α-synuclein from the olfactory bulb to interconnected brain regions in mice.Induction of intracellular tau aggregation is promoted by α-synuclein seeds and provides novel insights into the hyperphosphorylation of tau.Alpha-synuclein transfers from neurons to oligodendrocytes.E46K human alpha-synuclein transgenic mice develop Lewy-like and tau pathology associated with age-dependent, detrimental motor impairmentCharacterization of kinases involved in the phosphorylation of aggregated α-synuclein.Studies of lipopolysaccharide effects on the induction of α-synuclein pathology by exogenous fibrils in transgenic mice.Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice.Direct Observation of α-Synuclein Amyloid Aggregates in Endocytic Vesicles of Neuroblastoma Cells.Amyloidogenic α-synuclein seeds do not invariably induce rapid, widespread pathology in mice.Novel antibodies to phosphorylated α-synuclein serine 129 and NFL serine 473 demonstrate the close molecular homology of these epitopesInduction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synucleinInflammatory pre-conditioning restricts the seeded induction of α-synuclein pathology in wild type mice.Robust Central Nervous System Pathology in Transgenic Mice following Peripheral Injection of α-Synuclein Fibrils.Leucine-rich repeat kinase 2 and alpha-synuclein: intersecting pathways in the pathogenesis of Parkinson's disease?A deadly spread: cellular mechanisms of α-synuclein transfer.Protein aggregate spreading in neurodegenerative diseases: problems and perspectivesAggregation of amyloids in a cellular context: modelling and experiment.α-Synuclein in Parkinson's disease.Intercellular (mis)communication in neurodegenerative disease.Targeting intracellular and extracellular alpha-synuclein as a therapeutic strategy in Parkinson's disease and other synucleinopathies.Does a prion-like mechanism play a major role in the apparent spread of α-synuclein pathology?α-Synuclein: the long distance runner.In vitro recapitulation of aberrant protein inclusions in neurodegenerative diseases: New cellular models of neurodegenerative diseases.Cerebrospinal fluid biomarkers in Alzheimer's and Parkinson's diseases-From pathophysiology to clinical practice.Conformational templating of α-synuclein aggregates in neuronal-glial cultures.Lipid peroxidation product 4-hydroxy-2-nonenal promotes seeding-capable oligomer formation and cell-to-cell transfer of α-synuclein.Proteolysis of α-synuclein fibrils in the lysosomal pathway limits induction of inclusion pathology.UV-induced selective oxidation of Met5 to Met-sulfoxide leads to the formation of neurotoxic fibril-incompetent α-synuclein oligomers.
P2860
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P2860
A novel, high-efficiency cellular model of fibrillar alpha-synuclein inclusions and the examination of mutations that inhibit amyloid formation
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
A novel, high-efficiency cellu ...... that inhibit amyloid formation
@ast
A novel, high-efficiency cellu ...... that inhibit amyloid formation
@en
A novel, high-efficiency cellu ...... that inhibit amyloid formation
@nl
type
label
A novel, high-efficiency cellu ...... that inhibit amyloid formation
@ast
A novel, high-efficiency cellu ...... that inhibit amyloid formation
@en
A novel, high-efficiency cellu ...... that inhibit amyloid formation
@nl
prefLabel
A novel, high-efficiency cellu ...... that inhibit amyloid formation
@ast
A novel, high-efficiency cellu ...... that inhibit amyloid formation
@en
A novel, high-efficiency cellu ...... that inhibit amyloid formation
@nl
P2860
P1476
A novel, high-efficiency cellu ...... that inhibit amyloid formation
@en
P2093
Benoit I Giasson
Elisa A Waxman
P2860
P304
P356
10.1111/J.1471-4159.2010.06592.X
P407
P577
2010-02-02T00:00:00Z