A new Chinese hamster ovary cell line expressing α2,6-sialyltransferase used as universal host for the production of human-like sialylated recombinant glycoproteins

This publication has 32 references indexed in Scilit:

• Stable expression of human α-2,6-sialyltransferase in Chinese hamster ovary cells: functional consequences for human erythropoietin expression and bioactivity
  Biochimica et Biophysica Acta (BBA) - General Subjects, 1998
• Posttranslational processing of recombinant human interferon‐γ in animal expression systems
  Protein Science, 1996
• N‐glycans of recombinant human interferon‐γ change during batch culture of chinese hamster ovary cells
  Biotechnology & Bioengineering, 1995
• Double immunofluorescent staining of α2,6 sialyltransferase and β1,4 galactosyltransferase in monensin‐treated cells: Evidence for different Golgi compartments?
  Journal of Cellular Biochemistry, 1993
• Recognition of complex oligosaccharides by the multi-subunit asialoglycoprotein receptor
  Trends in Biochemical Sciences, 1991
• Influence of Sialic Acids on the Galactose-Recognizing Receptor of Rat Peritoneal Macrophages
  Biological Chemistry Hoppe-Seyler, 1990
• Molecular trapping of a fluorescent ceramide analogue at the Golgi apparatus of fixed cells: interaction with endogenous lipids provides a trans-Golgi marker for both light and electron microscopy.
  The Journal of cell biology, 1989
• Demonstration of an extensive trans-tubular network continuous with the Golgi apparatus stack that may function in glycosylation
  Cell, 1985
• Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity
  Nature, 1985
• A Vital Stain for the Golgi Apparatus
  Science, 1985