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</script>The sequence in which sugars are added to the Sindbis virus glycoproteins was studied. Infected cells contain three glycosylated virus-specific proteins: the two virion glycoproteins and the immediate precursor to the smaller virion glycoprotein. Larger Sindbis-specific proteins are not glycosylated. The cell-associated forms of both of the virion glycoproteins contain glucosamine, mannose, galactose, and fucose. The glycosylated precursor contains only glucosamine, mannose, and some galactose. The conversion of precursor to virion protein involves both the addition of galactose and fucose and the loss of mannose. The apparent extent of glycosylation of each virus-specific protein is not influenced by the host cell.
Glucosamine, Carbohydrates, Galactose, Chick Embryo, Kidney, Tritium, Cell Line, Viral Proteins, Cricetinae, Animals, Electrophoresis, Polyacrylamide Gel, Carbon Radioisotopes, Sindbis Virus, Amino Acids, Protein Precursors, Mannose, Fucose, Glycoproteins
Glucosamine, Carbohydrates, Galactose, Chick Embryo, Kidney, Tritium, Cell Line, Viral Proteins, Cricetinae, Animals, Electrophoresis, Polyacrylamide Gel, Carbon Radioisotopes, Sindbis Virus, Amino Acids, Protein Precursors, Mannose, Fucose, Glycoproteins
| citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 55 | |
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| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |
