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Showing 1–13 of 13 results
Advanced filters: Author: "Frederic Rousseau" 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

  • While artificial intelligence (AI) is quickly becoming ubiquitous, biology still suffers from the lack of interfaces connecting biological structures and modern AI methods. Here, the authors report PyUUL, a library to translate biological structures into 3D differentiable tensorial representations.

    • Gabriele Orlando
    • Daniele Raimondi
    • Frederic Rousseau
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-9

  • An increasing number of amyloid structures are determined. Here, the authors present the structure-based amyloid core sequence prediction method Cordax that is based on machine learning and allows the detection of aggregation-prone regions with higher solubility, disorder and surface exposure, and furthermore predicts the structural topology, orientation and overall architecture of the resulting putative fibril core.

    • Nikolaos Louros
    • Gabriele Orlando
    • Joost Schymkowitz
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-13

  • 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

  • Protein aggregation is associated with more than 50 human pathologies, including prevalent conditions such as Alzheimer's and Parkinson's diseases. A phenotypic screen in Escherichia coli associating antibiotic resistance with the inhibition of protein aggregation now allows screening for chemical inhibitors of protein aggregation in a simple, fast and inexpensive manner.

    • Joost Schymkowitz
    • Frederic Rousseau
    News & Views
    Nature Chemical Biology
    Volume: 12, P: 58-59

  • 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

  • Mutant p53 can attenuate the function of wild-type p53, p63 and p73. An aggregation-nucleating sequence in p53 that is revealed in structurally destabilized mutants can induce coaggregation with p63 and p73, resulting in their sequestration in cellular inclusions.

    • Jie Xu
    • Joke Reumers
    • Joost Schymkowitz
    Research
    Nature Chemical Biology
    Volume: 7, P: 285-295

  • High-throughput screening of large libraries of cyclic peptides expressed in bacteria yields rescuers of the pathogenic misfolding of proteins associated with neurodegenerative diseases.

    • Tobias Langenberg
    • Joost Schymkowitz
    • Frederic Rousseau
    News & Views
    Nature Biomedical Engineering
    Volume: 1, P: 782-783

  • In this Review, the authors outline the thermodynamic and kinetic principles of protein misfolding and amyloid formation. Mechanisms of toxicity are discussed, focusing on the effect of amyloid interactions with cellular components, and the association of aggregation with healthy ageing and pathology.

    • Nikolaos Louros
    • Joost Schymkowitz
    • Frederic Rousseau
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 24, P: 912-933