Control of glycoprotein synthesis. Processing of asparagine-linked oligosaccharides by one or more rat liver Golgi alpha-D-mannosidases dependent on the prior action of UDP-N-acetylglucosamine: alpha-D-mannoside beta 2-N-acetylglucosaminyltransferase I.

This publication has 34 references indexed in Scilit:

• Structure of the lipid-linked oligosaccharides that accumulate in class E Thy-1-negative mutant lymphomas
  Cell, 1979
• Glycosylation of a membrane protein is restricted to the growing polypeptide chain but is not necessary for insertion as a transmembrane protein
  Cell, 1978
• α ₁ -Antitrypsin: The Presence of Excess Mannose in the Z Variant Isolated from Liver
  Science, 1978
• Specific changes in the oligosaccharide moieties of VSV grown in different lectin-resistant CHO cells
  Cell, 1978
• Proposal for a common oligosaccharide intermediate in the synthesis of membrane glycoproteins
  Cell, 1977
• Structure of Seven Oligosaccharides Excreted in the Urine of a Patient with Sandhoff's Disease (GM₂ Gangliosidosis‐Variant O)
  European Journal of Biochemistry, 1977
• The substrate specificities of endo-β-N-acetylglucosaminidases CII and H
  Biochemical and Biophysical Research Communications, 1977
• The control of glycoprotein synthesis: N-acetylgluocosamine linkage to a mannose residue as a signal for the attachment of L-fucose to the asparagine-linked N-acetylglucosamine residue of glycopeptide from α1-acid glycoprotein
  Biochemical and Biophysical Research Communications, 1976
• Endo-β-N-acetylglucosaminidases acting on carbohydrate moieties of glycoproteins: Purification and properties of the two enzymes with different specificities from Clostridium perfringens
  Archives of Biochemistry and Biophysics, 1975
• The Golgi complex
  The Journal of Membrane Biology, 1973