• Medientyp: E-Book; Hochschulschrift
  • Titel: Ezrin activation in vitro: Investigation of ezrin's conformation and the interaction between ezrin and F-actin
  • Beteiligte: Braunger, Julia Anna [VerfasserIn]; Steinem, Claudia [Betreuer]; Steinem, Claudia [Gutachter]; Köster, Sarah [Gutachter]; Schaap, Iwan [Gutachter]
  • Erschienen: 2013
  • Umfang: Online-Ressource (PDF-Datei: 4,9 MB)
  • Sprache: Englisch
  • Identifikator:
  • Schlagwörter: Hochschulschrift
  • Entstehung:
  • Hochschulschrift: Göttingen, Univ., Diss., 2013
  • Anmerkungen:
  • Beschreibung: The function of ezrin, a member of the ezrin-radixin-moesin (ERM) protein family, is to regulate the cell membrane architecture within the context of fundamental biological processes by linking the membrane and the actin cytoskeleton. In the inactive state, ezrin is conformationally masked by self-association of N- and C-terminal domains. Ezrin activation is thought to rely on a conformational change induced by binding to L-α-phosphatidylinositol-4,5-bisphosphate (PIP2) and followed by phosphorylation of a conserved threonine (T) residue, thus rendering the binding site for filamentous acti...
  • Zugangsstatus: Freier Zugang