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
CD4 is retained in the endoplasmic reticulum by the human immunodeficiency virus type 1 glycoprotein precursor
Crise B, Buonocore L, Rose J. CD4 is retained in the endoplasmic reticulum by the human immunodeficiency virus type 1 glycoprotein precursor. Journal Of Virology 1990, 64: 5585-5593. PMID: 2214026, PMCID: PMC248611, DOI: 10.1128/jvi.64.11.5585-5593.1990.Peer-Reviewed Original ResearchA fusion-defective mutant of the vesicular stomatitis virus glycoprotein
Whitt M, Zagouras P, Crise B, Rose J. A fusion-defective mutant of the vesicular stomatitis virus glycoprotein. Journal Of Virology 1990, 64: 4907-4913. PMID: 2168975, PMCID: PMC247981, DOI: 10.1128/jvi.64.10.4907-4913.1990.Peer-Reviewed Original ResearchConceptsWild-type G proteinG proteinsMutant proteinsFusion activityMutant G proteinsFusion-defective mutantsAmino acids 117Vesicular stomatitis virus glycoproteinFormation of heterotrimersUncharged amino acidsTemperature-sensitive mutantNew glycosylation siteMutant glycoproteinsVesicular stomatitis virusGlycosylation sitesMembrane fusionRescue of virusVSV virionsExtracellular domainAmino acidsCell surfaceProteinVSV serotypesStomatitis virusMutantsHeavy chain binding protein recognizes incompletely disulfide-bonded forms of vesicular stomatitis virus G protein.
Machamer C, Doms R, Bole D, Helenius A, Rose J. Heavy chain binding protein recognizes incompletely disulfide-bonded forms of vesicular stomatitis virus G protein. Journal Of Biological Chemistry 1990, 265: 6879-6883. PMID: 2157712, DOI: 10.1016/s0021-9258(19)39231-2.Peer-Reviewed Original ResearchConceptsMutant G proteinsHeavy chain binding proteinG proteinsEndoplasmic reticulumWild-type G proteinBinding proteinVesicular stomatitis virus G proteinPlasma membrane glycoproteinsVirus G proteinAnti-BiP antibodiesDisulfide-bonded formIntrachain disulfide bondsVesicular stomatitis virusMembrane glycoproteinsDisulfide bondsBiPProteinStomatitis virusReticulumImmunoprecipitationGlycoprotein
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
Regulation of Protein Export From the Endoplasmic Reticulum
Rose J, Doms R. Regulation of Protein Export From the Endoplasmic Reticulum. Annual Review Of Cell And Developmental Biology 1988, 4: 257-288. PMID: 3058161, DOI: 10.1146/annurev.cb.04.110188.001353.Peer-Reviewed Original ResearchDifferential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein.
Doms R, Ruusala A, Machamer C, Helenius J, Helenius A, Rose J. Differential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein. Journal Of Cell Biology 1988, 107: 89-99. PMID: 2839523, PMCID: PMC2115181, DOI: 10.1083/jcb.107.1.89.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalAntibody SpecificityBiological TransportCell LineCentrifugation, Density GradientElectrophoresis, Polyacrylamide GelEndoplasmic ReticulumGlycosylationImmunoassayKineticsMacromolecular SubstancesMembrane GlycoproteinsMutationProtein ConformationTransfectionVesicular stomatitis Indiana virusViral Envelope ProteinsViral Matrix ProteinsConceptsG proteinsMutant proteinsCytoplasmic domainMutant G proteinsVesicular stomatitis virus G proteinIntegral membrane proteinsWild-type proteinTrimer formationVesicular stomatitis virus glycoproteinVirus G proteinAltered glycosylation patternConformation-specific antibodiesTail mutationsMembrane proteinsMin of synthesisOligomeric assembliesQuaternary structureMature formEndoplasmic reticulumInitial foldingGlycosylation patternsCell surfaceEctodomainProteinFoldingCell-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 acidsA membrane-anchored form but not the secretory form of human chorionic gonadotropin-alpha chain acquires polylactosaminoglycan.
Fukuda M, Guan J, Rose J. A membrane-anchored form but not the secretory form of human chorionic gonadotropin-alpha chain acquires polylactosaminoglycan. Journal Of Biological Chemistry 1988, 263: 5314-5318. PMID: 2451668, DOI: 10.1016/s0021-9258(18)60717-3.Peer-Reviewed Original ResearchConceptsMembrane-anchored formHuman chorionic gonadotropin (hCG) alpha-subunitMembrane anchoringGonadotropin alpha subunitSecretory formVesicular stomatitis virus glycoproteinMonkey COS-1 cellsCOS-1 cellsMembrane-bound formCytoplasmic domainMembrane proteinsSecretory proteinsComplex-type oligosaccharidesSecretory glycoproteinsProteinDNAVirus glycoproteinSubunitsPolylactosaminoglycansCarbohydrate structuresGlycoproteinGlycansAnchoringAsnEnzymeInfluence 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