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Showing 1–4 of 4 results
Advanced filters: Author: Hugo van Ingen Clear advanced filters

  • 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

  • Integrated structural data show that the MAP7 microtubule binding domain stabilizes the microtubule lattice through binding along protofilaments. Both strong and weak interactions between MAP7 and the lattice extend beyond a single tubulin dimer and include the tubulin C-terminal tails.

    • Agnes Adler
    • Mamata Bangera
    • Marc Baldus
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-16

  • Ubiquitination of histone H2A can occur on distinct lysine residues, but how each site is recognised by the specific E3 ligase remains poorly understood. Here the authors demonstrate that the E3 ligase RNF168 binds the acidic patch on the nucleosome surface, directing the E2 to the target lysine K13/K15.

    • Velten Horn
    • Michael Uckelmann
    • Hugo van Ingen
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-12