Seeded aggregation and toxicity of {alpha}-synuclein and tau: cellular models of neurodegenerative diseases.
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The chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicityMolecular Mechanisms in the Pathogenesis of Alzheimer's disease and Tauopathies-Prion-Like Seeded Aggregation and PhosphorylationKilling Me Softly: Connotations to Unfolded Protein Response and Oxidative Stress in Alzheimer's DiseaseTranscriptional mutagenesis by 8-oxodG in α-synuclein aggregation and the pathogenesis of Parkinson's diseaseThe role of tau in neurodegenerative diseases and its potential as a therapeutic targetAlpha-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.Spreading of pathology in neurodegenerative diseases: a focus on human studiesAlpha-synuclein spreading in Parkinson's diseaseRole of Different Alpha-Synuclein Strains in Synucleinopathies, Similarities with other Neurodegenerative DiseasesAmyloid oligomer neurotoxicity, calcium dysregulation, and lipid raftsLysine-Specific Molecular Tweezers Are Broad-Spectrum Inhibitors of Assembly and Toxicity of Amyloid ProteinsAlzheimer disease: a tale of two prionsBiophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.P301S mutant human tau transgenic mice manifest early symptoms of human tauopathies with dementia and altered sensorimotor gatingPropagation of tau pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies.Single cell imaging and quantification of TDP-43 and α-synuclein intercellular propagation.Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis.Acetylation: a new key to unlock tau's role in neurodegenerationSingle mutations in tau modulate the populations of fibril conformers through seed selection.Pathological alpha-synuclein propagates through neural networksIs there a risk of prion-like disease transmission by Alzheimer- or Parkinson-associated protein particles?Frequent and symmetric deposition of misfolded tau oligomers within presynaptic and postsynaptic terminals in Alzheimer's disease.p62/SQSTM1-dependent autophagy of Lewy body-like α-synuclein inclusionsSeeding of normal Tau by pathological Tau conformers drives pathogenesis of Alzheimer-like tangles.Transfer of human α-synuclein from the olfactory bulb to interconnected brain regions in mice.The many faces of α-synuclein: from structure and toxicity to therapeutic target.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.Direct evidence of Parkinson pathology spread from the gastrointestinal tract to the brain in rats.Mechanisms of protein oligomerization: inhibitor of functional amyloids templates α-synuclein fibrillation.Cross-seeding and conformational selection between three- and four-repeat human Tau proteins.Prion-like spread of protein aggregates in neurodegenerationDirect Observation of α-Synuclein Amyloid Aggregates in Endocytic Vesicles of Neuroblastoma Cells.Conformational basis for asymmetric seeding barrier in filaments of three- and four-repeat tau.Suppression of dynamin GTPase decreases α-synuclein uptake by neuronal and oligodendroglial cells: a potent therapeutic target for synucleinopathy.Biochemical classification of tauopathies by immunoblot, protein sequence and mass spectrometric analyses of sarkosyl-insoluble and trypsin-resistant tauDiverging patterns of amyloid deposition and hypometabolism in clinical variants of probable Alzheimer's diseaseKinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading.Axonal transport and secretion of fibrillar forms of α-synuclein, Aβ42 peptide and HTTExon 1
P2860
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P2860
Seeded aggregation and toxicity of {alpha}-synuclein and tau: cellular models of neurodegenerative diseases.
description
2010 nî lūn-bûn
@nan
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
2010年论文
@zh
2010年论文
@zh-cn
name
Seeded aggregation and toxicit ...... of neurodegenerative diseases.
@en
Seeded aggregation and toxicit ...... of neurodegenerative diseases.
@nl
type
label
Seeded aggregation and toxicit ...... of neurodegenerative diseases.
@en
Seeded aggregation and toxicit ...... of neurodegenerative diseases.
@nl
prefLabel
Seeded aggregation and toxicit ...... of neurodegenerative diseases.
@en
Seeded aggregation and toxicit ...... of neurodegenerative diseases.
@nl
P2093
P2860
P356
P1476
Seeded aggregation and toxicit ...... of neurodegenerative diseases.
@en
P2093
Masato Hasegawa
Sayuri T Watanabe
Takeshi Iwatsubo
P2860
P304
34885-34898
P356
10.1074/JBC.M110.148460
P407
P577
2010-08-30T00:00:00Z