• Medientyp: E-Book; Hochschulschrift
  • Titel: Analysis of protein SUMOylation and its role in Alzheimer's disease using mouse models
  • Beteiligte: Stankova, Trayana [Verfasser:in]; Brose, Nils [Akademische:r Betreuer:in]; Brose, Nils [Sonstige Person, Familie und Körperschaft]; Stegmüller, Judith [Sonstige Person, Familie und Körperschaft]; Bayer, Thomas [Sonstige Person, Familie und Körperschaft]
  • Erschienen: Göttingen, 2016
  • Umfang: 1 Online-Ressource; Illustrationen, Diagramme
  • Sprache: Englisch
  • Identifikator:
  • Schlagwörter: Hochschulschrift
  • Entstehung:
  • Hochschulschrift: Dissertation, Georg-August-Universität Göttingen, 2017
  • Anmerkungen:
  • Beschreibung: Post-translational modifications serve as a cellular mechanism for the regulation of the activity, stability and localization of proteins. SUMOylation is a dynamic and reversible post-translational modification, which entails the attachment of a SUMO protein to a lysine residue of the target protein. SUMOylation is involved in the regulation of numerous cellular processes including transcription, nucleocytoplasmic trafficking, and DNA repair. Three or four SUMO paralogs are present in mammals – SUMO1, SUMO2, SUMO3 and SUMO4. SUMO2 and SUMO3 exhibit extremely high sequence homology and there...
  • Zugangsstatus: Freier Zugang