Blar i forfatter Det helsevitenskapelige fakultet "Forst, Alexandra H."

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    • Dynamic subcellular localization of the mono-ADP-ribosyltransferase ARTD10 and interaction with the ubiquitin receptor p62 

      Kleine, Henning; Herrmann, Andreas; Lamark, Trond; Forst, Alexandra H.; Verheugd, Patricia; Lüscher-Firzlaff, Juliane; Lippok, Barbara; Feijs, Karla LH; Herzog, Nicolas; Kremmer, Elisabeth; Johansen, Terje; Müller-Newen, Gerhard; Lüscher, Bernhard (Journal article; Tidsskriftartikkel; Peer reviewed, 2012)
      ADP-ribosylation is a posttranslational modification catalyzed in cells by ADP-ribosyltransferases (ARTD or PARP enzymes). The ARTD family consists of 17 members. Some ARTDs modify their substrates by adding ADP-ribose in an iterative process, thereby synthesizing ADP-ribose polymers, the best-studied example being ARTD1/PARP1. Other ARTDs appear to mono-ADP-ribosylate their substrates and are unable ...