Browsing Bergen Open Research Archive by Author "Glomnes, Nina"

Now showing items 1-4 of 4

    • Efficient and crucial quality control of HAP1 cell ploidy status 

      Beigl, Tobias B.; Kjosås, Ine; Seljeseth, Emilie; Glomnes, Nina; Aksnes, Henriette (Journal article; Peer reviewed, 2020)
      The near-haploid human cell line HAP1 recently became a popular subject for CRISPR/Cas9 editing, since only one allele requires modification. Through the gene-editing service at Horizon Discovery, there are at present more ...

    • Expanded in vivo substrate profile of the yeast N-terminal acetyltransferase NatC 

      Van Damme, Petra; Osberg, Camilla; Jonckheere, Veronique; Glomnes, Nina; Gevaert, Kris; Arnesen, Thomas; Aksnes, Henriette (Journal article; Peer reviewed, 2022)
      N-terminal acetylation is a conserved protein modification among eukaryotes. The yeast Saccharomyces cerevisiae is a valuable model system for studying this modification. The bulk of protein N-terminal acetylation in S. ...

    • The Human N-Alpha-Acetyltransferase 40 (hNaa40p/ hNatD) Is Conserved from Yeast and N-Terminally Acetylates Histones H2A and H4 

      Hole, Kristine; Van Damme, Petra; Dalva, Monica; Aksnes, Henriette; Glomnes, Nina; Varhaug, Jan Erik; Lillehaug, Johan; Gevaert, Kris; Arnesen, Thomas (Peer reviewed; Journal article, 2011-09-15)
      Protein Na-terminal acetylation (Nt-acetylation) is considered one of the most common protein modification in eukaryotes, and 80-90% of all soluble human proteins are modified in this way, with functional implications ...

    • An organellar Nα-acetyltransferase, Naa60, acetylates cytosolic n termini of transmembrane proteins and maintains golgi integrity 

      Aksnes, Henriette; Van Damme, Petra; Goris, Marianne; Starheim, Kristian K.; Marie, Michael Bruno Eric; Støve, Svein Isungset; Hoel, Camilla; Kalvik, Thomas Vikestad; Hole, Kristine; Glomnes, Nina; Furnes, Clemens; Ljostveit, Sonja; Ziegler, Mathias; Niere, Marc; Gevaert, Kris; Arnesen, Thomas (Peer reviewed; Journal article, 2015-02-26)
      N-terminal acetylation is a major and vital protein modification catalyzed by N-terminal acetyltransferases (NATs). NatF, or Nα-acetyltransferase 60 (Naa60), was recently identified as a NAT in multicellular eukaryotes. ...