1993
Cell fusion by the envelope glycoproteins of persistent measles viruses which caused lethal human brain disease
Cattaneo R, Rose J. Cell fusion by the envelope glycoproteins of persistent measles viruses which caused lethal human brain disease. Journal Of Virology 1993, 67: 1493-1502. PMID: 8437226, PMCID: PMC237519, DOI: 10.1128/jvi.67.3.1493-1502.1993.Peer-Reviewed Original ResearchMeSH KeywordsAutopsyBacteriophage T7Biological TransportBrain DiseasesCell FusionCell LineCloning, MolecularDNA, ViralGlycosylationHeLa CellsHemagglutinins, ViralHumansMeaslesMeasles virusOligosaccharidesPromoter Regions, GeneticProtein ConformationProtein Processing, Post-TranslationalRecombinant ProteinsRNA, ViralViral Envelope ProteinsViral Fusion ProteinsViral InterferenceViral Matrix ProteinsVirulenceConceptsIntegral membrane proteinsH proteinCell fusionMembrane proteinsIntracellular domainViral buddingM proteinHS-protein interactionsF protein functionProtein interactionsMV genesIntracellular transportFusion proteinOligosaccharide modificationViral envelope proteinsMatrix proteinsHuman brain diseasesProteinMeasles virusReduced expressionEnvelope proteinPersistent measles virusBuddingSyncytium formationDisease development
1990
Prevention of HIV-1 glycoprotein transport by soluble CD4 retained in the endoplasmic reticulum
Buonocore L, Rose J. Prevention of HIV-1 glycoprotein transport by soluble CD4 retained in the endoplasmic reticulum. Nature 1990, 345: 625-628. PMID: 2190096, DOI: 10.1038/345625a0.Peer-Reviewed Original ResearchConceptsCD4 moleculeHIV glycoproteinSoluble CD4 moleculesHuman immunodeficiency virusCellular CD4 receptorWild-type CD4Human T cellsInfectious HIVCD4 cellsImmunodeficiency virusSoluble CD4T cellsTherapeutic strategiesCD4 receptorImmunization procedureEnvelope glycoproteinVirus entrySurface expressionCD4HIVIdeal targetEndoplasmic reticulumVirusExpressionCells
1988
Effects of altered cytoplasmic domains on transport of the vesicular stomatitis virus glycoprotein are transferable to other proteins.
Guan J, Ruusala A, Cao H, Rose J. Effects of altered cytoplasmic domains on transport of the vesicular stomatitis virus glycoprotein are transferable to other proteins. Molecular And Cellular Biology 1988, 8: 2869-2874. PMID: 2841589, PMCID: PMC363506, DOI: 10.1128/mcb.8.7.2869.Peer-Reviewed Original ResearchConceptsVesicular stomatitis virus glycoproteinEndoplasmic reticulumCytoplasmic domainVesicular stomatitis virus G proteinMembrane-anchored formVirus G proteinVirus glycoproteinMutant proteinsProtein foldingCytoplasmic sideSecretory proteinsCytoplasmic mutationsG proteinsProteinReticulumDifferent assaysMonomeric structureDetectable effectMutationsSedimentation coefficientRecent studiesCell-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 roleOligosaccharidesExpressionSitesVesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding.
Machamer C, Rose J. Vesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding. Journal Of Biological Chemistry 1988, 263: 5955-5960. PMID: 2833524, DOI: 10.1016/s0021-9258(18)60659-3.Peer-Reviewed Original ResearchBinding SitesBiological TransportCell LineCell MembraneDisulfidesDNA, RecombinantEndoplasmic ReticulumFluorescent Antibody TechniqueGlycosylationHexosaminidasesImmunosorbent TechniquesIodine RadioisotopesLactoperoxidaseMembrane GlycoproteinsMutationOligosaccharidesProtein ConformationStructure-Activity RelationshipTemperatureTransfectionVesicular stomatitis Indiana virusViral Envelope ProteinsViral Matrix Proteins
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 acidCellsMutagenesisOligosaccharidesCDNAGlycosylation allows cell-surface transport of an anchored secretory protein
Guan J, Machamer C, Rose J. Glycosylation allows cell-surface transport of an anchored secretory protein. Cell 1985, 42: 489-496. PMID: 3928168, DOI: 10.1016/0092-8674(85)90106-0.Peer-Reviewed Original ResearchConceptsCell surfaceProtein transportMutant proteinsCarboxy-terminal extensionCell surface transportVesicular stomatitis virus glycoproteinMembrane-anchored formSingle amino acidCytoplasmic domainHybrid geneGlycosylation sitesConsensus sequenceSecretory proteinsGolgi apparatusCellular membranesAmino acidsProteinRandom sitesGlycosylationVirus glycoproteinRat growth hormoneGrowth hormoneTransmembraneGenesSites