@misc{ZemellaThoringHoffmeisteretal.2018,
  author    = {Zemella, Anne and Thoring, Lena and Hoffmeister, Christian and Šamal{\´i}kov{\´a}, M{\´a}ria and Ehren, Patricia and W{\"u}stenhagen, Doreen Anja and Kubick, Stefan},
  title     = {Cell-free protein synthesis as a novel tool for directed glycoengineering of active erythropoietin},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch Naturwissenschaftliche Reihe},
  number    = {824},
  doi       = {10.25932/publishup-42701},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-427017},
  pages     = {14},
  year      = {2018},
  abstract  = {As one of the most complex post-translational modification, glycosylation is widely involved in cell adhesion, cell proliferation and immune response. Nevertheless glycoproteins with an identical polypeptide backbone mostly differ in their glycosylation patterns. Due to this heterogeneity, the mapping of different glycosylation patterns to their associated function is nearly impossible. In the last years, glycoengineering tools including cell line engineering, chemoenzymatic remodeling and site-specific glycosylation have attracted increasing interest. The therapeutic hormone erythropoietin (EPO) has been investigated in particular by various groups to establish a production process resulting in a defined glycosylation pattern. However commercially available recombinant human EPO shows batch-to-batch variations in its glycoforms. Therefore we present an alternative method for the synthesis of active glycosylated EPO with an engineered O-glycosylation site by combining eukaryotic cell-free protein synthesis and site-directed incorporation of non-canonical amino acids with subsequent chemoselective modifications.},
  language  = {en}
}
@misc{SperberWelkePetazzietal.2019,
  author    = {Sperber, Hannah Sabeth and Welke, Robert-William and Petazzi, Roberto Arturo and Bergmann, Ronny and Schade, Matthias and Shai, Yechiel and Chiantia, Salvatore and Herrmann, Andreas and Schwarzer, Roland},
  title     = {Self-association and subcellular localization of Puumala hantavirus envelope proteins},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {648},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-42504},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-425040},
  pages     = {15},
  year      = {2019},
  abstract  = {Hantavirus assembly and budding are governed by the surface glycoproteins Gn and Gc. In this study, we investigated the glycoproteins of Puumala, the most abundant Hantavirus species in Europe, using fluorescently labeled wild-type constructs and cytoplasmic tail (CT) mutants. We analyzed their intracellular distribution, co-localization and oligomerization, applying comprehensive live, single-cell fluorescence techniques, including confocal microscopy, imaging flow cytometry, anisotropy imaging and Number\&Brightness analysis. We demonstrate that Gc is significantly enriched in the Golgi apparatus in absence of other viral components, while Gn is mainly restricted to the endoplasmic reticulum (ER). Importantly, upon co-expression both glycoproteins were found in the Golgi apparatus. Furthermore, we show that an intact CT of Gc is necessary for efficient Golgi localization, while the CT of Gn influences protein stability. Finally, we found that Gn assembles into higher-order homo-oligomers, mainly dimers and tetramers, in the ER while Gc was present as mixture of monomers and dimers within the Golgi apparatus. Our findings suggest that PUUV Gc is the driving factor of the targeting of Gc and Gn to the Golgi region, while Gn possesses a significantly stronger self-association potential.},
  language  = {en}
}