Dopamine-induced α-synuclein oligomers show self- and cross-propagation properties. - sprookjes - yvandenbroek - TriplyDB

Dopamine-induced α-synuclein oligomers show self- and cross-propagation properties.

Dopamine-induced α-synuclein oligomers show self- and cross-propagation properties.

http://www.wikidata.org/entity/Q30364908

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Manganese-induced Neurotoxicity: From C. elegans to Humans The N-terminal residues 43 to 60 form the interface for dopamine mediated α-synuclein dimerisation.Site-Specific Fluorescence Polarization for Studying the Disaggregation of α-Synuclein Fibrils by Small Molecules.High-Throughput Screening Methodology to Identify Alpha-Synuclein Aggregation Inhibitors.Acidic Ca2+ stores in neurodegeneration.Structural and functional properties of prefibrillar α-synuclein oligomers Is Parkinson's disease truly a prion-like disorder? An appraisal of current evidence.A hyperbranched dopamine-containing PEG-based polymer for the inhibition of α-synuclein fibrillation Extracellular ATP induces intracellular alpha-synuclein accumulation via P2X1 receptor-mediated lysosomal dysfunction.

P2860

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P2860

Dopamine-induced α-synuclein oligomers show self- and cross-propagation properties.

http://www.wikidata.org/entity/Q30364908

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

Dopamine-induced α-synuclein oligomers show self- and cross-propagation properties.

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Dopamine-induced α-synuclein oligomers show self- and cross-propagation properties.

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type

label

Dopamine-induced α-synuclein oligomers show self- and cross-propagation properties.

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Dopamine-induced α-synuclein oligomers show self- and cross-propagation properties.

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Dopamine-induced α-synuclein oligomers show self- and cross-propagation properties.

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Dopamine-induced α-synuclein oligomers show self- and cross-propagation properties.

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Protein Science

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Dopamine-induced α-synuclein oligomers show self- and cross-propagation properties.

@en

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Matthew S Planchard

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Sarah E Exley

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Sarah E Morgan

http://www.w3.org/2001/XMLSchema#string

Vijayaraghavan Rangachari

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P2860

Autoproteolytic fragments are intermediates in the oligomerization/aggregation of the Parkinson's disease protein alpha-synuclein as revealed by ion mobility mass spectrometry

Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders

Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host

Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct.

Mechanisms of hybrid oligomer formation in the pathogenesis of combined Alzheimer's and Parkinson's diseases.

Formation of dopamine-mediated alpha-synuclein-soluble oligomers requires methionine oxidation.

Atomistic simulations of the effects of polyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerization

Non-esterified fatty acids generate distinct low-molecular weight amyloid-β (Aβ42) oligomers along pathway different from fibril formation

Assessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptides

Cross-seeding effects of amyloid β-protein and α-synuclein.

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1369-1379

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scholarly article

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10.1002/PRO.2521

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10

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23

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2014-08-01T00:00:00Z

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