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  1. Article

    Open Access

    Screening of small molecules using the inhibition of oligomer formation in α-synuclein aggregation as a selection parameter

    The aggregation of α-synuclein is a central event in Parkinsons’s disease and related synucleinopathies. Since pharmacologically targeting this process, however, has not yet resulted in approved disease-modify...

    Roxine Staats, Thomas C. T. Michaels, Patrick Flagmeier in Communications Chemistry (2020)

  2. No Access

    Article

    Direct measurement of lipid membrane disruption connects kinetics and toxicity of Aβ42 aggregation

    The formation of amyloid deposits in human tissues is a defining feature of more than 50 medical disorders, including Alzheimer’s disease. Strong genetic and histological evidence links these conditions to the...

    Patrick Flagmeier, Suman De, Thomas C. T. Michaels in Nature Structural & Molecular Biology (2020)

  3. Article

    Open Access

    Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms

    Protein aggregation is a complex process resulting in the formation of heterogeneous mixtures of aggregate populations that are closely linked to neurodegenerative conditions, such as Alzheimer’s disease. Here...

    Suman De, David C. Wirthensohn, Patrick Flagmeier, Craig Hughes in Nature Communications (2019)

  4. Article

    Open Access

    β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces

    α-Synuclein is an intrinsically disordered protein that is associated with the pathogenesis of Parkinson’s disease through the processes involved in the formation of amyloid fibrils. α and β-synuclein are homolog...

    James W. P. Brown, Alexander K. Buell, Thomas C. T. Michaels in Scientific Reports (2016)