Branching Out: Constructing The Antennae Of N-Linked Sugars

  • Roslyn M. Bill
  • Leigh Revers
  • Iain B. H. Wilson


The study of glycobiology in the 1970s and 1980s was dominated by the determination of oligosaccharide structures and the search for the enzyme sources that could make them. The wide variety of oligosaccharide structures that were subsequently discovered inevitably led to the classic questions of why this diversity exists and how it has come about. More recently, scientists have examined the function of protein glycosylation and the molecular biology of the enzymes that are involved in this complex process. Indeed the current surge of interest in glycobiology is founded on the widespread belief that oligosaccharides, on account of their diversity, must have a string of roles to play in modulating and altering interactions between proteins, lipids, cells or indeed, entire organisms. As a result, it has become clear that the multiplicity of mammalian oligosaccharides arises from a complex set of processing and elongation events, to which the nascent oligosaccharides are subjected following their initial transfer to protein.


Bovine Colostrum GlcNAc Residue GlcNAc Transferase Trimannosyl Core Golgi Retention 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Roslyn M. Bill
    • 1
  • Leigh Revers
    • 2
  • Iain B. H. Wilson
    • 3
  1. 1.The Lundberg LaboratoryUniversity of GöteborgGöteborgSweden
  2. 2.Department of Biochemistry ResearchThe Hospital for Sick ChildrenTorontoCanada
  3. 3.Department of Biochemistry ResearchUniversity of DundeeDundeeScotland

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