1986
Amino-terminal mutation of the vesicular stomatitis virus glycoprotein does not affect its fusion activity
Woodgett C, Rose J. Amino-terminal mutation of the vesicular stomatitis virus glycoprotein does not affect its fusion activity. Journal Of Virology 1986, 59: 486-489. PMID: 3016308, PMCID: PMC253100, DOI: 10.1128/jvi.59.2.486-489.1986.Peer-Reviewed Original ResearchConceptsVesicular stomatitis virus glycoproteinAmino acid changesG proteinsFusion activityAmino terminusWild-type G proteinAcid changesAmino-terminal mutationsSingle amino acid changeMonkey fibroblast cell lineSame amino acid changeOligonucleotide-directed mutagenesisPH-dependent fusion activityVirus glycoproteinPH-dependent hemolytic activityMutant proteinsHemolytic activityFibroblast cell lineSynthetic peptidesProteinCell linesTerminusGlycoproteinPeptidesMutagenesis
1985
A single N-linked oligosaccharide at either of the two normal sites is sufficient for transport of vesicular stomatitis virus G protein to the cell surface.
Machamer C, Florkiewicz R, Rose J. A single N-linked oligosaccharide at either of the two normal sites is sufficient for transport of vesicular stomatitis virus G protein to the cell surface. Molecular And Cellular Biology 1985, 5: 3074-3083. PMID: 3018499, PMCID: PMC369121, DOI: 10.1128/mcb.5.11.3074.Peer-Reviewed Original ResearchConceptsCell surface expressionG proteinsGlycosylation sitesVesicular stomatitis virus G proteinCell surfaceWild-type proteinVesicular stomatitis virus glycoproteinRole of glycosylationSurface expressionSite-directed mutagenesisVirus G proteinAsparagine-linked glycansIndirect immunofluorescence microscopyIntracellular transportImmunofluorescence microscopyOligosaccharide processingProteinProteolytic breakdownVirus glycoproteinExpressionPalmitic acidCellsMutagenesisOligosaccharidesCDNAA Single N-Linked Oligosaccharide at Either of the Two Normal Sites Is Sufficient for Transport of Vesicular Stomatitis Virus G Protein to the Cell Surface
Machamer C, Florkiewicz R, Rose J. A Single N-Linked Oligosaccharide at Either of the Two Normal Sites Is Sufficient for Transport of Vesicular Stomatitis Virus G Protein to the Cell Surface. Molecular And Cellular Biology 1985, 5: 3074-3083. DOI: 10.1128/mcb.5.11.3074-3083.1985.Peer-Reviewed Original ResearchCell surface expressionG proteinsGlycosylation sitesVesicular stomatitis virus G proteinCell surfaceWild-type proteinVesicular stomatitis virus glycoproteinRole of glycosylationSurface expressionSite-directed mutagenesisVirus G proteinAsparagine-linked glycansIndirect immunofluorescence microscopyIntracellular transportImmunofluorescence microscopyOligosaccharide processingProteinProteolytic breakdownVirus glycoproteinExpressionPalmitic acidCellsMutagenesisOligosaccharidesCDNAStructural requirements of a membrane-spanning domain for protein anchoring and cell surface transport
Adams G, Rose J. Structural requirements of a membrane-spanning domain for protein anchoring and cell surface transport. Cell 1985, 41: 1007-1015. PMID: 3924407, DOI: 10.1016/s0092-8674(85)80081-7.Peer-Reviewed Original ResearchConceptsMembrane-spanning domainsCell surface transportTransmembrane domainG proteinsAmino acidsVesicular stomatitis virus glycoproteinOligonucleotide-directed mutagenesisHydrophobic amino acidsMembrane anchoringProtein anchoringIntracellular membranesTransmembrane configurationEndoplasmic reticulumCell surfaceProteinVirus glycoproteinDNASurface transportStructural requirementsDomainMutagenesisAcidReticulumAnchoringTransport