Anne Stuendl

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Extracellular a-synuclein has been proposed as a crucial mechanism for induction of pathological aggregate formation in previously healthy cells. In vitro, extracellular a-synuclein is partially associated with exosomal vesicles. Recently, we have provided evidence that exosomal a-synuclein is present in the central nervous system in vivo. We hypothesized(More)
Extracellular α-synuclein has been proposed as a crucial mechanism for induction of pathological aggregate formation in previously healthy cells. In vitro, extracellular α-synuclein is partially associated with exosomal vesicles. Recently, we have provided evidence that exosomal α-synuclein is present in the central nervous system in vivo. We hypothesized(More)
Extracellular α-Synuclein has been implicated in interneuronal propagation of disease pathology in Parkinson’s Disease. How α-Synuclein is released into the extracellular space is still unclear. Here, we show that α-Synuclein is present in extracellular vesicles in the central nervous system. We find that sorting of α-Synuclein in extracellular vesicles is(More)
Pathogenesis of Alzheimer's disease (AD) is associated with aggregation of the amyloid-β (Aβ) peptide into oligomeric and fibrillar assemblies; however, little is known about the molecular basis of aggregation of Aβ into distinct assembly states. Here we demonstrate that phosphorylation at serine 26 (S26) impairs Aβ fibrillization while stabilizing its(More)
Extracellular a-synuclein has been proposed as a crucial mechanism for induction of pathological aggregate formation in previously healthy cells. In vitro, extracellular a-synuclein is partially associated with exosomal vesicles. Recently, we have provided evidence that exosomal a-synuclein is present in the central nervous system in vivo. We hypothesized(More)
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