1995
Replication and amplification of novel vesicular stomatitis virus minigenomes encoding viral structural proteins
Stillman E, Rose J, Whitt M. Replication and amplification of novel vesicular stomatitis virus minigenomes encoding viral structural proteins. Journal Of Virology 1995, 69: 2946-2953. PMID: 7707520, PMCID: PMC188993, DOI: 10.1128/jvi.69.5.2946-2953.1995.Peer-Reviewed Original ResearchConceptsVesicular stomatitis virusViral structural proteinsStructural proteinsMatrix protein geneFunctional viral proteinsM proteinNorthern blot analysisEncoded proteinsInfectious particlesTranscriptional eventsFunctional mRNAProtein geneL proteinLeader regionMinigenome RNAVSV genomeIndiana serotypePolymerase proteinOwn propagationGlycoprotein geneVSV proteinsViral proteinsProteinNucleocapsid proteinMinigenome
1993
Blockade of human immunodeficiency virus type 1 production in CD4+ T cells by an intracellular CD4 expressed under control of the viral long terminal repeat.
Buonocore L, Rose J. Blockade of human immunodeficiency virus type 1 production in CD4+ T cells by an intracellular CD4 expressed under control of the viral long terminal repeat. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 2695-2699. PMID: 8464877, PMCID: PMC46162, DOI: 10.1073/pnas.90.7.2695.Peer-Reviewed Original ResearchConceptsHuman immunodeficiency virus type 1 productionHIV-1 infectionInfectious HIV-1HIV envelope proteinHuman T cell lineSoluble CD4 proteinT cell linesT cellsHIV-1Viral spreadSyncytium formationInfected cellsViral long terminal repeatCD4CD4 proteinEnvelope proteinIntracellular CD4Intracellular trapsGene therapyLong terminal repeatRetroviral vectorsCellsCell surfaceHIVBlockadeCytoplasmic domain requirement for incorporation of a foreign envelope protein into vesicular stomatitis virus
Owens R, Rose J. Cytoplasmic domain requirement for incorporation of a foreign envelope protein into vesicular stomatitis virus. Journal Of Virology 1993, 67: 360-365. PMID: 8093220, PMCID: PMC237371, DOI: 10.1128/jvi.67.1.360-365.1993.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceCD4-Positive T-LymphocytesCell FusionFluorescent Antibody TechniqueGene Products, envHIV Envelope Protein gp120HIV Envelope Protein gp41HIV-1Membrane GlycoproteinsMolecular Sequence DataRecombinant Fusion ProteinsStructure-Activity RelationshipVesicular stomatitis Indiana virusViral Envelope ProteinsViral Fusion ProteinsConceptsHIV-1 envelope proteinEnvelope proteinAnti-HIV-1 seraHuman immunodeficiency virus type 1 (HIV-1) envelope proteinG proteinsHIV-1 entryVesicular stomatitis virus particlesHIV-1Vesicular stomatitis virusEnvelope glycoproteinWild-type G proteinStomatitis virusVSV particlesVSV G proteinVirus particlesTemperature-sensitive mutantPseudotypesSimultaneous expressionTransmembrane domainCytoplasmic domainCytoplasmic tailDefective transportVSV
1992
Human immunodeficiency virus type 1 glycoprotein precursor retains a CD4-p56lck complex in the endoplasmic reticulum
Crise B, Rose J. Human immunodeficiency virus type 1 glycoprotein precursor retains a CD4-p56lck complex in the endoplasmic reticulum. Journal Of Virology 1992, 66: 2296-2301. PMID: 1548763, PMCID: PMC289024, DOI: 10.1128/jvi.66.4.2296-2301.1992.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumHuman immunodeficiency virusTyrosine kinaseHIV infectionCD4-p56lck complexTransient expression systemGlycoprotein precursorCytoplasmic tyrosine kinaseConfocal immunofluorescence microscopyExpression of CD4HIV-1 gp160Cell surface glycoproteinExpression of gp160Cytoplasmic facePlasma membraneT cell activationExpression systemHeLa cellsImmunofluorescence microscopyCell surfaceImmunodeficiency virusT lymphocytesT cellsLymphocyte killingCD4
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
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 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
1987
Replacement of the cytoplasmic domain alters sorting of a viral glycoprotein in polarized cells.
Puddington L, Woodgett C, Rose J. Replacement of the cytoplasmic domain alters sorting of a viral glycoprotein in polarized cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1987, 84: 2756-2760. PMID: 3033661, PMCID: PMC304737, DOI: 10.1073/pnas.84.9.2756.Peer-Reviewed Original ResearchConceptsCytoplasmic domainG proteinsPlasma membraneVesicular stomatitis virusNormal cytoplasmic domainIntegral membrane proteinsPolarized epithelial cellsVSV G proteinApical plasma membraneBasolateral plasma membraneBasolateral membraneCanine kidney cell lineMadin-Darby canine kidney (MDCK) cell lineIndirect immunofluorescence microscopyMembrane proteinsKidney cell lineDomain altersPolarized expressionImmunofluorescence microscopyBasolateral surfaceProteinStomatitis virusCell linesViral glycoproteinsEpithelial cells
1985
Structural 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 ResearchMeSH KeywordsAnimalsBiological TransportCell LineCell MembraneEndoplasmic ReticulumFluorescent Antibody TechniqueGlycoside HydrolasesGolgi ApparatusMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseMembrane GlycoproteinsMembrane ProteinsMutationPalmitic AcidPalmitic AcidsPlasmidsViral Envelope ProteinsViral ProteinsConceptsMembrane-spanning domainsCell surface transportTransmembrane domainG proteinsAmino acidsVesicular stomatitis virus glycoproteinOligonucleotide-directed mutagenesisHydrophobic amino acidsMembrane anchoringProtein anchoringIntracellular membranesTransmembrane configurationEndoplasmic reticulumCell surfaceProteinVirus glycoproteinDNASurface transportStructural requirementsDomainMutagenesisAcidReticulumAnchoringTransport
1984
The presence of cysteine in the cytoplasmic domain of the vesicular stomatitis virus glycoprotein is required for palmitate addition.
Rose J, Adams G, Gallione C. The presence of cysteine in the cytoplasmic domain of the vesicular stomatitis virus glycoprotein is required for palmitate addition. Proceedings Of The National Academy Of Sciences Of The United States Of America 1984, 81: 2050-2054. PMID: 6326102, PMCID: PMC345434, DOI: 10.1073/pnas.81.7.2050.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsDNAFluorescent Antibody TechniqueMembrane GlycoproteinsMutationPalmitic AcidPalmitic AcidsTransfectionVesicular stomatitis Indiana virusViral Envelope ProteinsViral ProteinsConceptsCytoplasmic domainG proteinsVesicular stomatitis virusVesicular stomatitis virus glycoproteinVSV G proteinCarboxyl-terminal sideAmino acid residuesEukaryotic cellsTransmembrane domainCDNA clonesGene resultsAcid residuesCellular membranesPalmitate additionTransmembrane glycoproteinCellular glycoproteinsCell surfaceAmino acidsProteinStomatitis virusCysteineVirus glycoproteinPresence of cysteineFatty acidsGlycoprotein
1983
Isolation of stable mouse cell lines that express cell surface and secreted forms of the vesicular stomatitis virus glycoprotein.
Florkiewicz R, Smith A, Bergmann J, Rose J. Isolation of stable mouse cell lines that express cell surface and secreted forms of the vesicular stomatitis virus glycoprotein. Journal Of Cell Biology 1983, 97: 1381-1388. PMID: 6415065, PMCID: PMC2112694, DOI: 10.1083/jcb.97.5.1381.Peer-Reviewed Original ResearchConceptsVesicular stomatitis virus glycoproteinMouse cell linesG proteinsNormal G proteinsStable mouse cell linesEndoplasmic reticulumCell linesTg proteinRough endoplasmic reticulumVesicular stomatitis virus G proteinCell surfaceVirus G proteinBovine papilloma virusVirus glycoproteinComplex oligosaccharidesAnchor sequenceLevel of expressionPSV2 vectorCDNA encodingAnchorless proteinAberrant splicingDNA fragmentsGolgi apparatusMRNA sequencesRate-limiting step