1989
A single-amino-acid substitution eliminates the stringent carbohydrate requirement for intracellular transport of a viral glycoprotein
Pitta A, Rose J, Machamer C. A single-amino-acid substitution eliminates the stringent carbohydrate requirement for intracellular transport of a viral glycoprotein. Journal Of Virology 1989, 63: 3801-3809. PMID: 2760984, PMCID: PMC250973, DOI: 10.1128/jvi.63.9.3801-3809.1989.Peer-Reviewed Original Research
1988
Cell-surface expression of a membrane-anchored form of the human chorionic gonadotropin alpha subunit.
Guan J, Cao H, Rose J. Cell-surface expression of a membrane-anchored form of the human chorionic gonadotropin alpha subunit. Journal Of Biological Chemistry 1988, 263: 5306-5313. PMID: 2451667, DOI: 10.1016/s0021-9258(18)60716-1.Peer-Reviewed Original ResearchMeSH KeywordsBiological Transport, ActiveCloning, MolecularDNAElectrophoresis, Polyacrylamide GelFluorescent Antibody TechniqueGene Expression RegulationGlycoprotein Hormones, alpha SubunitGlycoside HydrolasesGlycosylationHexosaminidasesHumansKineticsMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseMembranesOligosaccharidesPituitary Hormones, AnteriorPlasmidsTunicamycinVesicular stomatitis Indiana virusViral Fusion ProteinsConceptsVesicular stomatitis virus glycoproteinAsparagine-linked glycansAnimal cellsAlpha subunitNovel cell surface proteinCarboxyl-terminal amino acidsGlycosylation inhibitor tunicamycinAbsence of glycosylationMembrane-anchored formCell surface proteinsSecond glycosylation siteHuman chorionic gonadotropin (hCG) alpha-subunitVirus glycoproteinEntire precursorCell surface expressionCytoplasmic domainGonadotropin alpha subunitHybrid proteinPlasma membraneGlycosylation sitesSecretory proteinsCellular membranesConformational changesCell surfaceAmino acidsInfluence of new glycosylation sites on expression of the vesicular stomatitis virus G protein at the plasma membrane.
Machamer C, Rose J. Influence of new glycosylation sites on expression of the vesicular stomatitis virus G protein at the plasma membrane. Journal Of Biological Chemistry 1988, 263: 5948-5954. PMID: 2833523, DOI: 10.1016/s0021-9258(18)60658-1.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceBinding SitesBiological TransportCell LineCell MembraneCloning, MolecularDNA, RecombinantFluorescent Antibody TechniqueGlycosylationImmunosorbent TechniquesIodine RadioisotopesLactoperoxidaseMembrane GlycoproteinsMolecular Sequence DataMutationOligosaccharidesTransfectionTunicamycinVesicular stomatitis Indiana virusViral Envelope ProteinsViral Matrix ProteinsConceptsVesicular stomatitis virus G proteinVirus G proteinG proteinsConsensus sitesIntracellular transportWild-type G proteinWild-type proteinOligonucleotide-directed mutagenesisNew consensus sitePlasma membrane glycoproteinsMutant proteinsNew glycosylation siteNew sitesAsparagine-linked oligosaccharidesPlasma membraneGlycosylation sitesMembrane glycoproteinsInhibition of transportProteinPolypeptide backboneNormal sitesIndirect roleOligosaccharidesExpressionSites