Single-channel electrophysiology reveals a distinct and uniform pore complex formed by α-synuclein oligomers in lipid membranes - Wikidata - wikimedia - TriplyDB

Single-channel electrophysiology reveals a distinct and uniform pore complex formed by α-synuclein oligomers in lipid membranes

Single-channel electrophysiology reveals a distinct and uniform pore complex formed by α-synuclein oligomers in lipid membranes

http://www.wikidata.org/entity/Q34374310

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Features of alpha-synuclein that could explain the progression and irreversibility of Parkinson's disease Seeking a mechanism for the toxicity of oligomeric α-synuclein Environmental toxins trigger PD-like progression via increased alpha-synuclein release from enteric neurons in mice Anle138b: a novel oligomer modulator for disease-modifying therapy of neurodegenerative diseases such as prion and Parkinson's disease.Modelling Ser129 phosphorylation inhibits membrane binding of pore-forming alpha-synuclein oligomers Seeding and transgenic overexpression of alpha-synuclein triggers dendritic spine pathology in the neocortex Post translational changes to α-synuclein control iron and dopamine trafficking; a concept for neuron vulnerability in Parkinson's disease.Structures formed by a cell membrane-associated arabinogalactan-protein on graphite or mica alone and with Yariv phenylglycosides.Piceatannol and Other Wine Stilbenes: A Pool of Inhibitors against α-Synuclein Aggregation and Cytotoxicity.The Function of the Mitochondrial Calcium Uniporter in Neurodegenerative Disorders.Calcium signaling in Parkinson's disease.Insights on the interaction of alpha-synuclein and metals in the pathophysiology of Parkinson's disease.Structure, function and toxicity of alpha-synuclein: the Bermuda triangle in synucleinopathies.Intracellular soluble α-synuclein oligomers reduce pyramidal cell excitability.Cu(II) promotes amyloid pore formation.Localization of A11-reactive oligomeric species in prion diseases.Single-molecule assays for investigating protein misfolding and aggregation.A Focus on the Beneficial Effects of Alpha Synuclein and a Re-appraisal of Synucleinopathies.Extracellular α-synuclein alters synaptic transmission in brain neurons by perforating the neuronal plasma membrane.Capturing intracellular Ca2+ dynamics in computational models of neurodegenerative diseases.Current perspective of mitochondrial biology in Parkinson's disease.

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Single-channel electrophysiology reveals a distinct and uniform pore complex formed by α-synuclein oligomers in lipid membranes

http://www.wikidata.org/entity/Q34374310

description

2012 nî lūn-bûn

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2012 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի օգոստոսին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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name

Single-channel electrophysiolo ...... n oligomers in lipid membranes

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Single-channel electrophysiolo ...... n oligomers in lipid membranes

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Single-channel electrophysiolo ...... n oligomers in lipid membranes

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Single-channel electrophysiolo ...... n oligomers in lipid membranes

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Single-channel electrophysiolo ...... n oligomers in lipid membranes

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Single-channel electrophysiolo ...... n oligomers in lipid membranes

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Single-channel electrophysiolo ...... n oligomers in lipid membranes

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Single-channel electrophysiolo ...... n oligomers in lipid membranes

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Felix Schmidt

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

Frits Kamp

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Hans Kretzschmar

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Kai Bötzel

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P2860

Protein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseases

Membrane Permeabilization by Oligomeric α-Synuclein: In Search of the Mechanism

Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore

Alpha-synuclein and neurodegenerative diseases

Protein aggregation and neurodegenerative disease

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Dissociation of amyloid fibrils of alpha-synuclein in supercooled water.

Recent advances in the genetics of Parkinson's disease.

Reconstitution of cell membrane structure in vitro and its transformation into an excitable system.

Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis.

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22880029

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electrophysiology

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3411845

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