• Dynamics of SARS-CoV-2 Spike-IgG throughout Three COVID-19 Vaccination Regimens: A 21-Month Longitudinal Study of 82 Norwegian Healthcare Workers 

      Augustinussen, Marita Helen; Tylden, Garth Daryl; Rinaldo, Christine Hanssen (Journal article; Tidsskriftartikkel; Peer reviewed, 2023-02-23)
      To facilitate interpretation of clinical SARS-CoV-2 anti-spike IgG analyses post-vaccination, 82 healthcare workers were followed through three vaccination-regimens: two regimens were comprised of two doses of BNT162b2 three or six weeks apart, followed by a dose of mRNA-vaccine, and in the other regimen, the first dose was replaced by ChAdOx1 nCov-19. After each dose, anti-spike IgG was compared ...
    • Strategimøte 2019 - Mikrobiologisk diagnostikk ved virale CNS-infeksjoner 

      Christensen, Andreas; Lind, Andreas; Kanestrøm, Anita; Tylden, Garth Daryl (Research report; Forskningsrapport, 2021-09)
      I regi av Referansegruppen for ekstern kvalitetssikring i virologi og serologi, ble det den 31.10.2019 holdt strategimøte med temaet «Mikrobiologisk diagnostikk ved virale CNS-infeksjoner» på Gjestehuset, Lovisenberg sykehus i Oslo. Årets strategimøte var en oppdatering av et tidligere strategimøte fra 2002 med samme tittel. Nylig omtalte infeksjoner ble utelatt pga. tidshensyn, deriblant nevroborreliose ...
    • The third helix of the homeodomain of paired class homeodomain proteins acts as a recognition helix both for DNA and protein interactions 

      Bruun, Jack-Ansgar; Thomassen, Ernst I.s.; Kristiansen, Kurt; Tylden, Garth Daryl; Holm, Turid; Mikkola, Ingvild; Bjørkøy, Geir; Johansen, Terje (Journal article; Tidsskriftartikkel; Peer reviewed, 2005)
      The transcription factor Pax6 is essential for the development of the eyes and the central nervous system of vertebrates and invertebrates. Pax6 contains two DNA-binding domains; an N-terminal paired domain and a centrally located homeodomain. We have previously shown that the vertebrate paired-less isoform of Pax6 (Pax6ΔPD), and several other homeodomain proteins, interact with the full-length ...