UDP-GlcNAc:Glycoprotein N-acetylglucosamine-1-phosphotransferase mediates the initial step in the formation of the methylphosphomannosyl residues on the high mannose oligosaccharides of Dictyostelium discoideum glycoproteins
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference17 articles.
1. Identification of methylphosphomannosyl residues as components of the high mannose oligosaccharides of Dictyostelium discoideum glycoproteins;Gabel;J. Biol. Chem.,1984
2. Glycoprotein phosphorylation in simple eucaryotic organisms. Identification of UDP-GlcNAc:glycoprotein N-acetylglucosamine-1-phosphotransferase activity and analysis of substrate specificity;Lang;J. Biol. Chem.,1986
3. A novel pathway for phosphorylated oligosaccharide biosynthesis. Identification of an oligosaccharide-specific phosphate methyltransferase in Dictyostelium discoideum;Freeze;J. Biol. Chem.,1992
4. High-throughput analysis of spatio-temporal dynamics in Dictyostelium;Sawai;Genome Biol.,2007
5. The spectrum of anionic oligosaccharides released by endo-beta-N-acetylglucosaminidase H from glycoproteins. Structural studies and interactions with the phosphomannosyl receptor;Varki;J. Biol. Chem.,1983
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