Glycosylation

Curr Opin Cell Biol. 1992 Dec;4(6):1017-23. doi: 10.1016/0955-0674(92)90134-x.

Abstract

Protein glycosylation is more abundant and structurally diverse than all other types of post-translational modifications combined. Protein-bound saccharides range from dynamic monosaccharides on nuclear and cytoplasmic proteins, to enormously complex 'recognition' molecules on extracellular N- or O-linked glycoproteins or proteoglycans. Recent elucidation of a few of the myriad functions of these saccharides has finally opened a crack in the door to one the last great frontiers of biochemistry.

Publication types

  • Review

MeSH terms

  • Animals
  • Carbohydrate Sequence
  • Cell Nucleus / metabolism
  • Cytoplasm / metabolism
  • Glycosylation
  • Glycosylphosphatidylinositols / chemistry
  • Humans
  • Membrane Proteins / chemistry
  • Molecular Sequence Data
  • Protein Processing, Post-Translational*
  • Sialic Acids / chemistry
  • Sialic Acids / physiology

Substances

  • Glycosylphosphatidylinositols
  • Membrane Proteins
  • Sialic Acids