title: Glycosylation.
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.
authors: Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
authors: G W
authors: GW
authors: Hart
mesh_terms: D000818:Animals; D002240:Carbohydrate Sequence; D002467:Cell Nucleus / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D006031:Glycosylation; D017261:Glycosylphosphatidylinositols / Q000737:chemistry; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D012794:Sialic Acids / Q000737:chemistry / Q000502:physiology
chemical_list: D017261:Glycosylphosphatidylinositols; D008565:Membrane Proteins; D012794:Sialic Acids