Clustering of alpha-synuclein on supported lipid bilayers: role of anionic lipid, protein, and divalent ion concentration
about
Biophysical characterization of α-synuclein and its controversial structureStructural Basis of Molecular Recognition of the Leishmania Small Hydrophilic Endoplasmic Reticulum-associated Protein (SHERP) at Membrane SurfacesAlpha-synuclein lipid-dependent membrane binding and translocation through the α-hemolysin channelBiophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Adsorption of α-synuclein to supported lipid bilayers: positioning and role of electrostaticsα-Synuclein-induced tubule formation in lipid bilayersLysosomal function in macromolecular homeostasis and bioenergetics in Parkinson's disease.α-Synuclein-induced membrane remodeling is driven by binding affinity, partition depth, and interleaflet order asymmetry.The lipid-binding domain of wild type and mutant alpha-synuclein: compactness and interconversion between the broken and extended helix forms.Phosphatase CD45 both positively and negatively regulates T cell receptor phosphorylation in reconstituted membrane protein clustersConformational heterogeneity of α-synuclein in membrane.Effects of curvature and composition on α-synuclein binding to lipid vesiclesDirect membrane association drives mitochondrial fission by the Parkinson disease-associated protein alpha-synuclein.Parkinson's disease, cortical dysfunction, and alpha-synuclein.Effects of impaired membrane interactions on α-synuclein aggregation and neurotoxicityInteraction of α-synuclein with vesicles that mimic mitochondrial membranes.Morphological changes of supported lipid bilayers induced by lysozyme: planar domain formation vs. multilayer stacking.Structural intermediates during α-synuclein fibrillogenesis on phospholipid vesicles.On-surface aggregation of α-synuclein at nanomolar concentrations results in two distinct growth mechanismsα-Synuclein and mitochondria: partners in crime?Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicityThe Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson's Disease.Implications of peptide assemblies in amyloid diseases.Adsorption of alpha-synuclein on lipid bilayers: modulating the structure and stability of protein assemblies.Elevated levels of α-synuclein oligomer in the cerebrospinal fluid of drug-naïve patients with Parkinson's disease.Amyloids of alpha-synuclein affect the structure and dynamics of supported lipid bilayers.Two different binding modes of α-synuclein to lipid vesicles depending on its aggregation state.Polyunsaturated chains in asymmetric lipids disorder raft mixtures and preferentially associate with α-Synuclein.
P2860
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P2860
Clustering of alpha-synuclein on supported lipid bilayers: role of anionic lipid, protein, and divalent ion concentration
description
2009 nî lūn-bûn
@nan
2009 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Clustering of alpha-synuclein ...... and divalent ion concentration
@ast
Clustering of alpha-synuclein ...... and divalent ion concentration
@en
type
label
Clustering of alpha-synuclein ...... and divalent ion concentration
@ast
Clustering of alpha-synuclein ...... and divalent ion concentration
@en
prefLabel
Clustering of alpha-synuclein ...... and divalent ion concentration
@ast
Clustering of alpha-synuclein ...... and divalent ion concentration
@en
P2093
P2860
P1433
P1476
Clustering of alpha-synuclein ...... and divalent ion concentration
@en
P2093
Anjan P Pandey
Farzin Haque
Jean-Christophe Rochet
Jennifer S Hovis
P2860
P304
P356
10.1016/J.BPJ.2008.10.011
P407
P577
2009-01-01T00:00:00Z