The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes
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Seeking a mechanism for the toxicity of oligomeric α-synucleinConformational heterogeneity of α-synuclein in membrane.The Tubular Sheaths Encasing Methanosaeta thermophila Filaments Are Functional Amyloids.Functional amyloids keep quorum-sensing molecules in checkStructural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation.Molecular details of α-synuclein membrane association revealed by neutrons and photons.Phenolic compounds prevent the oligomerization of α-synuclein and reduce synaptic toxicity.Effect of pH on the Aggregation of α-syn12 Dimer in Explicit Water by Replica-Exchange Molecular Dynamics Simulation.The influence of N-terminal acetylation on micelle-induced conformational changes and aggregation of α-Synuclein.Development of Passive Immunotherapies for Synucleinopathies.Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation.Prolyl oligopeptidase enhances α-synuclein dimerization via direct protein-protein interactionHow epigallocatechin gallate can inhibit α-synuclein oligomer toxicity in vitro.The Contribution of α-Synuclein Spreading to Parkinson's Disease Synaptopathy.Direct Visualization of Model Membrane Remodeling by α-Synuclein Fibrillization.Amyloids of alpha-synuclein affect the structure and dynamics of supported lipid bilayers.The Impact of N-terminal Acetylation of α-Synuclein on Phospholipid Membrane Binding and Fibril Structure.Quarterly intrinsic disorder digest (January-February-March, 2014).Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers.Self-Assembled Cyclic d,l-α-Peptides as Generic Conformational Inhibitors of the α-Synuclein Aggregation and Toxicity: In Vitro and Mechanistic Studies.The attachment of α-synuclein to a fiber: A coarse-grain approach.Oligomers of α-synuclein: picking the culprit in the line-up.Membrane-Bound Alpha Synuclein Clusters Induce Impaired Lipid Diffusion and Increased Lipid Packing.Strong interactions with polyethylenimine-coated human serum albumin nanoparticles (PEI-HSA NPs) alter α-synuclein conformation and aggregation kinetics.
P2860
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P2860
The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes
description
2014 nî lūn-bûn
@nan
2014 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հունվարին 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
The N-terminus of α-synuclein ...... ic interactions with membranes
@ast
The N-terminus of α-synuclein ...... ic interactions with membranes
@en
The N-terminus of α-synuclein ...... ic interactions with membranes
@en-gb
The N-terminus of α-synuclein ...... ic interactions with membranes
@nl
type
label
The N-terminus of α-synuclein ...... ic interactions with membranes
@ast
The N-terminus of α-synuclein ...... ic interactions with membranes
@en
The N-terminus of α-synuclein ...... ic interactions with membranes
@en-gb
The N-terminus of α-synuclein ...... ic interactions with membranes
@nl
prefLabel
The N-terminus of α-synuclein ...... ic interactions with membranes
@ast
The N-terminus of α-synuclein ...... ic interactions with membranes
@en
The N-terminus of α-synuclein ...... ic interactions with membranes
@en-gb
The N-terminus of α-synuclein ...... ic interactions with membranes
@nl
P2093
P2860
P921
P3181
P1433
P1476
The N-terminus of α-synuclein ...... ic interactions with membranes
@en
P2093
Lasse Lemminger
Nikolai Lorenzen
Søren Bang Nielsen
P2860
P304
P3181
P356
10.1016/J.FEBSLET.2013.12.015
P407
P577
2014-01-31T00:00:00Z