Welcome to the Switch Laboratory

Mapping aggregation-specific interactions in human disease

Our research focuses on understanding the mechanisms gearing protein folding and misfolding and their relation to human disease. In particular, we are investigating how protein aggregation affects the interactome by suppressing native interactions but also by introducing novel aggregation-specific interactions. These latter are especially relevant as they are usually associated with gain of function activities such as neurotoxicity (neurodegeneration).

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Newest publications

  • publication

    Investigating the Sequence Determinants of the Curling of Amyloid Fibrils Using Ovalbumin as a Case Study

    Joëlle A J Housmans, Bert Houben, Margarita Monge-Morera, Diego Asvestas, Hung Huy Nguyen, Grigoria Tsaka, Nikolaos Louros, Sebastien Carpentier, Jan A Delcour, Frederic Rousseau, Joost Schymkowitz
    Biomacromolecules . 2022 Aug 26
    PubMed
  • publication

    Impact of heat and enzymatic treatment on ovalbumin amyloid-like fibril formation and enzyme-induced gelation

    Huyst, AMR; Deleu, LJ; Luyckx, T; Meeren, LV; Housmans, JAJ; Grootaert, C; Monge-Morera, M; Delcour, JA; Skirtach, AG; Rousseau, F; Schymkowitz, J; Dewettinck, K; van der Meeren, P
    FOOD HYDROCOLLOIDS
  • publication

    HPMPdb: A machine learning-ready database of protein molecular phenotypes associated to human missense variants

    Daniele Raimondi, Francesco Codicè, Gabriele Orlando, Joost Schymkowitz, Frederic Rousseau, Yves Moreau
    Curr Res Struct Biol . 2022 May 13
    PubMed
  • publication

    The effect of mutation on an aggregation-prone protein: An in vivo, in vitro, and in silico analysis

    N Guthertz, R van der Kant, R M Martinez, Y Xu, C Trinh, B I Iorga, F Rousseau, J Schymkowitz, D J Brockwell, S E Radford
    Proc Natl Acad Sci U S A . 2022 May 31
    PubMed
  • publication

    Thermodynamic analysis of amyloid fibril structures reveals a common framework for stability in amyloid polymorphs

    Rob van der Kant, Nikolaos Louros, Joost Schymkowitz, Frederic Rousseau
    Structure . 2022 May 15
    PubMed
  • publication

    Mapping the sequence specificity of heterotypic amyloid interactions enables the identification of aggregation modifiers

    Nikolaos Louros, Meine Ramakers, Emiel Michiels, Katerina Konstantoulea, Chiara Morelli, Teresa Garcia, Nele Moonen, Sam D'Haeyer, Vera Goossens, Dietmar Rudolf Thal, Dominique Audenaert, Frederic Rousseau, Joost Schymkowitz
    Nat Commun . 2022 Mar 15
    PubMed