@book{HoffmeisterPapenfussRohloffetal.2001,
  author    = {Hoffmeister, Frank and Papenfuß, Anja and Rohloff, Christoph and Tietje, Christian and Weiß, Norman},
  title     = {Globale Probleml{\"o}sungen in der Bew{\"a}hrungsprobe},
  series = {Potsdamer UNO-Konferenzen},
  journal   = {Potsdamer UNO-Konferenzen},
  number    = {1},
  publisher = {Universit{\"a}tsverlag Potsdam},
  address   = {Potsdam},
  isbn      = {3-00-007657-3},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-69512},
  publisher      = {Universit{\"a}t Potsdam},
  pages     = {80},
  year      = {2001},
  abstract  = {Die erste Konferenz im Dezember 1999, die Gr{\"u}ndungskonferenz, m{\"u}ndete nach einer intensiven Diskussion {\"u}ber die Situation in der deutschen UN-Forschung in die Gr{\"u}ndung des Forschungskreises Vereinte Nationen. Dieser hat sich vor allem die bessere Kommunikation untereinander, die F{\"o}rderung des interdisziplin{\"a}ren Dialogs und des wissenschaftlichen Nachwuchses in der UN-Forschung zum Ziel gesetzt. Die zweite Konferenz des Forschungskreises fand am 30. Juni und 1. Juli 2000, ebenfalls in den R{\"a}umen der Juristischen Fakult{\"a}t der Universit{\"a}t Potsdam, im Vorfeld einer wichtigen UN-Konferenz, n{\"a}mlich des Milleni-um-Gipfels im September 2000 in New York statt. Sie widmete sich einer kritischen Bilanz der Rolle der Vereinten Nationen bei der Suche nach L{\"o}sungen f{\"u}r die globalen Probleme, in ihren Hauptaufgabengebieten Friedenssicherung, Demokratisierung, Schutz der Menschenrechte und F{\"o}rderung der wirtschaftlichen und sozialen Entwicklung. Die in dieser Brosch{\"u}re ver{\"o}ffentlichten Referate der zweiten Konferenz spiegeln zusammen mit den Diskussionen, die zusammenfassend dargestellt werden, die großen Herausforderungen, aber auch die Chancen der Vereinten Nationen bei der L{\"o}sung der globalen Probleme, vor die sich die V{\"o}lker der Welt zum Beginn des neuen Jahrtausend gestellt sehen.},
  language  = {de}
}
@article{ZemellaThoringHoffmeisteretal.2018,
  author    = {Zemella, Anne and Thoring, Lena and Hoffmeister, Christian and Samalikova, Maria 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 = {Scientific reports},
  volume    = {8},
  journal   = {Scientific reports},
  publisher = {Nature Publ. Group},
  address   = {London},
  issn      = {2045-2322},
  doi       = {10.1038/s41598-018-26936-x},
  pages     = {12},
  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{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}
}