Blar i Brage INN på forfatter "Demko, Viktor"
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An intragenic mutagenesis strategy in Physcomitrella patens to preserve intron splicing.
Ako, Ako Eugene; Perroud, Pierre-François; Innocent, Joseph; Demko, Viktor; Olsen, Odd-Arne; Johansen, Wenche (Journal article; Peer reviewed, 2017)Gene targeting is a powerful reverse genetics technique for site-specific genome modification. Intrinsic homologous recombination in the moss Physcomitrella patens permits highly effective gene targeting, a characteristic ... -
Membrane-anchored calpains – hidden regulators of growth and development beyond plants?
Safranek, Martin; Shumbusho, Alain; Johansen, Wenche; Sarkanova, Julia; Vosko, Stanislav; Bokor, Boris; Jasik, Jan; Demko, Viktor (Peer reviewed; Journal article, 2023)Calpains are modulatory proteases that modify diverse cellular substrates and play essential roles in eukaryots. The best studied are animal cytosolic calpains. Here, we focus on enigmatic membrane-anchored calpains, their ... -
The nuclear GUCT domain-containing DEAD-box RNA helicases govern gametophytic and sporophytic development in Physcomitrium patens
Perroud, Pierre-francois; Demko, Viktor; Ako, Ako Eugene; Khanal, Rajendra; Bokor, Boris; Pavlovic, Andrej; Jasik, Jan; Johansen, Wenche (Peer reviewed; Journal article, 2021)Key message In Physcomitrium patens, PpRH1/PpRH2 are GUCT-domain-containing DEAD-BOX RNA helicases localize to the nucleus. They are implicated in cell and tissue development in all stages of the moss life cycle. Abstract ... -
Regulation of developmental gatekeeping and cell fate transition by the calpain protease DEK1 in Physcomitrium patens
Demko, Viktor; Belova, Tatiana; Messerer, Maxim; Hvidsten, Torgeir Rhoden; Perroud, Pierre-François; Ako, Ako Eugene; Johansen, Wenche; Mayer, Klaus F. X.; Olsen, Odd-Arne; Lang, Daniel (Peer reviewed; Journal article, 2024)Calpains are cysteine proteases that control cell fate transitions whose loss of function causes severe, pleiotropic phenotypes in eukaryotes. Although mainly considered as modulatory proteases, human calpain targets are ...