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Showing 1–5 of 5 results
Advanced filters: Author: Amberley D. Stephens Clear advanced filters

  • In Parkinson’s disease (PD) the monomeric protein alpha-synuclein (aSyn) misfolds and aggregates into insoluble fibrils. Here the authors use NMR measurements and hydrogen–deuterium exchange mass spectrometry and find that the more solvent exposed the N-terminus of aSyn is, the more aggregation prone its conformation becomes, and further show how PD mutations and post translational modifications influence the extent of the N-terminus solvent exposure.

    • Amberley D. Stephens
    • Maria Zacharopoulou
    • Gabriele S. Kaminski Schierle
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-15

  • Alpha-synuclein is associated with neuronal dysfunction in Parkinson’s disease. This study shows that alpha-synuclein interacts with neuronal synaptic vesicles in a calcium-dependent fashion, and this interaction is important for synaptic vesicle clustering.

    • Janin Lautenschläger
    • Amberley D. Stephens
    • Gabriele S. Kaminski Schierle
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-13

  • α-synuclein, a protein associated to Parkinson's disease, is involved in synaptic vesicle interaction and assembly. Here, the authors use NMR spectroscopy and super-resolution microscopy to unveil the nature and molecular mechanism of α-synuclein-mediated synaptic vesicle clustering.

    • Giuliana Fusco
    • Tillmann Pape
    • Alfonso De Simone
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-12

  • Interaction of alpha-synuclein (aSyn) with physiological lipid membranes leads to the disintegration of membranes, incorporation of lipids by aSyn fibrils, increased aggregation rate of aSyn fibrils, and increased uptake of lipid-associated fibrils compared to aSyn only fibrils into neurons.

    • Amberley D. Stephens
    • Ana Fernandez Villegas
    • Gabriele S. Kaminski Schierle
    ResearchOpen Access
    Communications Biology
    Volume: 6, P: 1-13