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Showing 1–7 of 7 results
Advanced filters: Author: Meine Ramakers Clear advanced filters

  • In this work, using a combination of Cryo-EM, in-cell experiments and biophysical analysis, the authors decoded the aggregation propensity of tau, revealing 5 central hot spots in its primary sequence and identify PAM4 as short segment that determines both the structure, as well as the cellular propagation of tau aggregates extracted from Alzheimer’s disease, corticobasal degeneration, and progressive supranuclear palsy patients.

    • Nikolaos Louros
    • Martin Wilkinson
    • Joost Schymkowitz
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-16

  • Here the authors show that beta-lactamase have an intrinsic aggregation propensity that can be exploited to inactivate these enzymes that mediate antibiotic resistance, using peptides that are based on aggregation prone regions in the sequence of the beta-lactamase.

    • Ladan Khodaparast
    • Laleh Khodaparast
    • Joost Schymkowitz
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-16

  • Some human amyloid proteins have been shown to interact with viral proteins, suggesting that they may have potential as therapeutic agents. Here the authors design synthetic amyloids specific for influenza A and Zika virus proteins, respectively, and show that they can inhibit viral replication.

    • Emiel Michiels
    • Kenny Roose
    • Joost Schymkowitz
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-13

  • Mutations in aggregation prone regions of recombinant proteins often improve their solubility, although they might cause negative effects on their structure and function. Here, the authors identify proteins hot spots that can be exploited to optimize solubility without compromising stability.

    • Ashok Ganesan
    • Aleksandra Siekierska
    • Joost Schymkowitz
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-15

  • Aggregation is sequence-specific and nucleated by short aggregating protein segments (APR). Here authors use a multidisciplinary approach to show that in E.coli some frequently occurring APRs lead to protein aggregation and ultimately bacterial cell death, which could serve as antibacterial strategy.

    • Ladan Khodaparast
    • Laleh Khodaparast
    • Joost Schymkowitz
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-15