Blar i Bergen Open Research Archive på forfatter "Drazic, Adrian"

Viser treff 1-7 av 7

    • Actin Post-translational Modifications: The Cinderella of Cytoskeletal Control 

      Varland, Sylvia; Vandekerckhove, Joel; Drazic, Adrian (Peer reviewed; Journal article, 2019)
      Actin is one of the most abundant proteins in eukaryotic cells and the main component of the microfilament system. It plays essential roles in numerous cellular activities including muscle contraction, maintenance of cell ...

    • Classification and phylogeny for the annotation of novel eukaryotic GNAT acetyltransferases 

      Krtenic, Bojan; Drazic, Adrian; Arnesen, Thomas; Reuter, Nathalie (Journal article; Peer reviewed, 2020)
      The enzymes of the GCN5-related N-acetyltransferase (GNAT) superfamily count more than 870 000 members through all kingdoms of life and share the same structural fold. GNAT enzymes transfer an acyl moiety from acyl coenzyme ...

    • The Final Maturation State of β-actin Involves N-terminal Acetylation by NAA80, not N-terminal Arginylation by ATE1 

      Drazic, Adrian; Timmerman, Evy; Kajan, Ulrike; Marie, Michaël Bruno Eric; Varland, Sylvia; Impens, Francis; Gevaert, Kris; Arnesen, Thomas (Journal article; Peer reviewed, 2022)
      Actin is a hallmark protein of the cytoskeleton in eukaryotic cells, affecting a range of cellular functions. Actin dynamics is regulated through a myriad of actin-binding proteins and post-translational modifications. The ...

    • First Things First: Vital Protein Marks by N-Terminal Acetyltransferases 

      Aksnes, Henriette; Drazic, Adrian; Marie, Michael Bruno Eric; Arnesen, Thomas (Peer reviewed; Journal article, 2016-09)
      N-terminal (Nt) acetylation is known to be a highly abundant co-translational protein modification, but the recent discovery of Golgi- and chloroplast-resident N-terminal acetyltransferases (NATs) revealed that it can also ...

    • Human NAA30 can rescue yeast mak3∆ mutant growth phenotypes 

      Drazic, Adrian; Varland, Sylvia (Journal article; Peer reviewed, 2021)
      N-terminal acetylation is an irreversible protein modification that primarily occurs co-translationally, and is catalyzed by a highly conserved family of N-terminal acetyltransferases (NATs). The NatC complex (NAA30–NAA35–NAA38) ...

    • Mechanism of actin N-terminal acetylation 

      Rebowski, Grzegorz; Boczkowska, Malgorzata; Drazic, Adrian; Ree, Rasmus Moen; Goris, Marianne; Arnesen, Thomas; Dominguez, Roberto (Journal article; Peer reviewed, 2020)
      About 80% of human proteins are amino-terminally acetylated (Nt-acetylated) by one of seven Nt-acetyltransferases (NATs). Actin, the most abundant protein in the cytoplasm, has its own dedicated NAT, NAA80, which acts ...

    • PFN2 and NAA80 cooperate to efficiently acetylate the N-terminus of actin 

      Reed, Rasmus; Kind, Laura; Kaziales, Anna; Varland, Sylvia; Dai, Minglu; Richter, Klaus; Drazic, Adrian; Arnesen, Thomas (Journal article; Peer reviewed, 2020)
      The actin cytoskeleton is of profound importance to cell shape, division, and intracellular force generation. Profilins bind to globular (G-)actin and regulate actin filament formation. Although profilins are well-established ...