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Showing 1–9 of 9 results
Advanced filters: Author: Rasmus Hartmann-Petersen Clear advanced filters

  • An important step in understanding and using proteins is to identify the residues that are important for function. The authors present a machine-learning based method to predict functional sites that leverages and combines the information available in protein sequences and structures.

    • Matteo Cagiada
    • Sandro Bottaro
    • Kresten Lindorff-Larsen
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-13

  • How misfolded proteins are selected by the ubiquitin-conjugating system for elimination is largely unknown. Here, the authors identify conserved features of proteome-derived degradation signals, including amino acid and structural preferences, that trigger quality-control-associated proteolysis.

    • Bayan Mashahreh
    • Shir Armony
    • Tommer Ravid
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-13

  • The details of how the protein folding and degradation systems collaborate to combat potentially toxic non-native proteins are unknown. Here the authors perform systematic studies of missense and nonsense variants of the cytosolic aspartoacylase, ASPA, where loss-of-function variants are linked to Canavan disease.

    • Martin Grønbæk-Thygesen
    • Vasileios Voutsinos
    • Rasmus Hartmann-Petersen
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-18

  • Gene variants can affect folding and stability of the encoded protein. Here, the authors apply deep mutational scanning to provide genotype-phenotype information for 99% of the possible PRKN variants and reveal mechanistic details on how some variants cause loss-of-function and Parkinsons disease.

    • Lene Clausen
    • Vasileios Voutsinos
    • Rasmus Hartmann-Petersen
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-17

  • The AAA ATPase p97 (VCP) is thought to remove specific proteins from chromatin at sites of DNA damage, to allow proper repair or processing, but how p97 targets those sites was unclear. The protein DVC1 is now shown to localize to sites of replication stress and UV-light damage, and to be required for p97 recruitment. DVC1's localization to DNA damage sites requires its UBZ domain and PCNA-interacting motif but not PCNA ubiquitination. DVC1 deficiency caused retention of error-prone translesion polymerase η at foci after UV-light damage and increased mutagenesis levels.

    • Anna Mosbech
    • Ian Gibbs-Seymour
    • Niels Mailand
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 1084-1092