Membrane disruption by oligomeric alpha-synuclein (alphaS) is considered a likely mechanism of cytotoxicity in Parkinson's disease (PD). However, the mechanism of oligomer binding and the relation between binding and membrane disruption is not known. We have visualized alphaS oligomer-lipid binding by fluorescence microscopy and have measured membrane disruption using a dye release assay. The data reveal that oligomeric alphaS selectively binds to membranes containing anionic lipids and preferentially accumulates into liquid disordered (Ld) domains. Furthermore, we show that binding of oligomers to the membrane and disruption of the membrane require different lipid properties. Thus membrane-bound oligomeric alphaS does not always cause bila...
A key feature of Parkinson disease is the aggregation of α-synuclein and its intracellular depositio...
The question of how the aggregation of the neuronal protein α-synuclein contributes to neuronal toxi...
Previous studies indicate that binding of alpha-synuclein to membranes is critical for its physiolog...
Membrane disruption by oligomeric α-synuclein (αS) is considered a likely mechanism of cytotoxicity ...
AbstractMembrane disruption by oligomeric α-synuclein (αS) is considered a likely mechanism of cytot...
Soluble oligomeric aggregates of alpha-synuclein have been implicated to play a central role in the ...
alpha-Synuclein oligomers are increasingly considered to be responsible for the death of dopaminergi...
Item does not contain fulltextInteractions of oligomeric aggregates of the intrinsically disordered ...
Alpha-synuclein (aS) oligomers are increasingly considered to be responsible for the death of dopami...
Interactions of oligomeric aggregates of the intrinsically disordered protein α-synuclein with lipid...
AbstractSoluble oligomeric aggregates of α-synuclein have been implicated to play a central role in ...
This thesis gives insights into the biophysical mechanisms of α-synuclein (αS) oligomer-membrane int...
Interactions of oligomeric aggregates of the intrinsically disordered protein α-synuclein with lipid...
α-Synuclein oligomers are increasingly considered to be responsible for the death of dopaminergic ne...
The question of how the aggregation of the neuronal protein α-synuclein contributes to neuronal toxi...
A key feature of Parkinson disease is the aggregation of α-synuclein and its intracellular depositio...
The question of how the aggregation of the neuronal protein α-synuclein contributes to neuronal toxi...
Previous studies indicate that binding of alpha-synuclein to membranes is critical for its physiolog...
Membrane disruption by oligomeric α-synuclein (αS) is considered a likely mechanism of cytotoxicity ...
AbstractMembrane disruption by oligomeric α-synuclein (αS) is considered a likely mechanism of cytot...
Soluble oligomeric aggregates of alpha-synuclein have been implicated to play a central role in the ...
alpha-Synuclein oligomers are increasingly considered to be responsible for the death of dopaminergi...
Item does not contain fulltextInteractions of oligomeric aggregates of the intrinsically disordered ...
Alpha-synuclein (aS) oligomers are increasingly considered to be responsible for the death of dopami...
Interactions of oligomeric aggregates of the intrinsically disordered protein α-synuclein with lipid...
AbstractSoluble oligomeric aggregates of α-synuclein have been implicated to play a central role in ...
This thesis gives insights into the biophysical mechanisms of α-synuclein (αS) oligomer-membrane int...
Interactions of oligomeric aggregates of the intrinsically disordered protein α-synuclein with lipid...
α-Synuclein oligomers are increasingly considered to be responsible for the death of dopaminergic ne...
The question of how the aggregation of the neuronal protein α-synuclein contributes to neuronal toxi...
A key feature of Parkinson disease is the aggregation of α-synuclein and its intracellular depositio...
The question of how the aggregation of the neuronal protein α-synuclein contributes to neuronal toxi...
Previous studies indicate that binding of alpha-synuclein to membranes is critical for its physiolog...