@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}
}
@article{SachseWuestenhagenSamalikovaetal.2013,
  author    = {Sachse, Rita and W{\"u}stenhagen, Doreen Anja and Samalikova, Maria and Gerrits, Michael and Bier, Frank Fabian and Kubick, Stefan},
  title     = {Synthesis of membrane proteins in eukaryotic cell-free systems},
  series = {Engineering in life sciences : Industry, Environment, Plant, Food},
  volume    = {13},
  journal   = {Engineering in life sciences : Industry, Environment, Plant, Food},
  number    = {1},
  publisher = {Wiley-Blackwell},
  address   = {Hoboken},
  issn      = {1618-0240},
  doi       = {10.1002/elsc.201100235},
  pages     = {39 -- 48},
  year      = {2013},
  abstract  = {Cell-free protein synthesis (CFPS) is a valuable method for the fast expression of difficult-to-express proteins as well as posttranslationally modified proteins. Since cell-free systems circumvent possible cytotoxic effects caused by protein overexpression in living cells, they significantly enlarge the scale and variety of proteins that can be characterized. We demonstrate the high potential of eukaryotic CFPS to express various types of membrane proteins covering a broad range of structurally and functionally diverse proteins. Our eukaryotic cell-free translation systems are capable to provide high molecular weight membrane proteins, fluorescent-labeled membrane proteins, as well as posttranslationally modified proteins for further downstream analysis.},
  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}
}