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Showing 1–5 of 5 results
Advanced filters: Author: Paul P. Geurink Clear advanced filters

  • Most insights into deubiquitinase (DUB) substrate specificity originate from studies with isolated di-ubiquitins (diUb), but in cells diUbs with different linkage types coexist. Here, the authors develop a mass spectrometric DUB activity assay that can probe all diUbs simultaneously under substrate competition conditions.

    • Bianca D. M. van Tol
    • Bjorn R. van Doodewaerd
    • Paul P. Geurink
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-14

  • The specificity of USP18's deconjugating activity toward ISG15, a ubiquitin-like protein induced by interferon, is revealed by structural and biochemistry studies of the mouse proteins.

    • Anja Basters
    • Paul P Geurink
    • Günter Fritz
    Research
    Nature Structural & Molecular Biology
    Volume: 24, P: 270-278

  • Deubiquitinating enzymes (DUBs) are critical regulators of cellular processes by removing ubiquitin from specific targets. Here global kinetic modelling reveals the mechanism by which the low intrinsic activity of USP7 is substantially enhanced on a specific physiological target.

    • Robbert Q. Kim
    • Paul P. Geurink
    • Titia K. Sixma
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-16

  • Biochemical, structural and functional studies on the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) papain-like protease PLpro reveal that it regulates host antiviral responses by preferentially cleaving the ubiquitin-like interferon-stimulated gene 15 protein (ISG15) and identify this protease as a potential therapeutic target for coronavirus disease 2019 (COVID-19).

    • Donghyuk Shin
    • Rukmini Mukherjee
    • Ivan Dikic
    Research
    Nature
    Volume: 587, P: 657-662