Amyloid oligomerization of the Parkinson's disease related protein α‐synuclein impacts on its curvature‐membrane sensitivity

The amyloid aggregation of the presynaptic protein α‐synuclein (AS) is pathognomonic of Parkinson's disease and other neurodegenerative disorders. Physiologically, AS contributes to synaptic homeostasis by participating in vesicle maintenance, trafficking, and release. Its avidity for highly cu...

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Veröffentlicht in:	Journal of neurochemistry 2018-11, Vol.147 (4), p.541-556
Hauptverfasser:	Gallea, José Ignacio, Ambroggio, Ernesto E., Vilcaes, Aldo Alejandro, James, Nicholas G., Jameson, David M., Celej, María Soledad
Format:	Artikel
Sprache:	eng
Schlagworte:	Amyloid Avidity Binding Composition Curvature FCS Fibrils Fluorescence Fluorescence spectroscopy Freeze drying Homeostasis Interfaces Lipids lipid‐protein interaction Membrane composition Membranes Movement disorders Neurodegeneration Neurodegenerative diseases Neurotoxicity Oligomerization Oligomers Organic chemistry Parkinson's disease protein aggregation Proteins Rehydration Sensitivity Species Synuclein synucleinopathies toxic oligomers
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