1997
Specific targeting to CD4+ cells of recombinant vesicular stomatitis viruses encoding human immunodeficiency virus envelope proteins
Johnson J, Schnell M, Buonocore L, Rose J. Specific targeting to CD4+ cells of recombinant vesicular stomatitis viruses encoding human immunodeficiency virus envelope proteins. Journal Of Virology 1997, 71: 5060-5068. PMID: 9188571, PMCID: PMC191739, DOI: 10.1128/jvi.71.7.5060-5068.1997.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCD4-Positive T-LymphocytesCell LineCricetinaeGene ExpressionGenetic VectorsHeLa CellsHIV Envelope Protein gp160HIV-1HumansMembrane GlycoproteinsProtein Processing, Post-TranslationalRabbitsRecombinant Fusion ProteinsRecombination, GeneticVesicular stomatitis Indiana virusViral Envelope ProteinsVirionConceptsRecombinant vesicular stomatitis virusHuman immunodeficiency virus envelope proteinHIV envelope proteinVesicular stomatitis virusHIV envelopeVirus envelope proteinEnvelope proteinHIV type 1 envelopeChimeric envelopesCD4-positive cellsReplication-competent recombinant virusesStomatitis virusHIV seraRecombinant virusesHIV vaccineSpecific infectionsPrimary isolatesHIV-1HIV gp120Chimeric envelope proteinsAlternative receptorLow titersVSV serumVSV infectivityVSV glycoprotein
1993
Dynamic equilibrium between vesicular stomatitis virus glycoprotein monomers and trimers in the Golgi and at the cell surface
Zagouras P, Rose J. Dynamic equilibrium between vesicular stomatitis virus glycoprotein monomers and trimers in the Golgi and at the cell surface. Journal Of Virology 1993, 67: 7533-7538. PMID: 8230472, PMCID: PMC238219, DOI: 10.1128/jvi.67.12.7533-7538.1993.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, ViralAntibody SpecificityBiological TransportBrefeldin ACell CompartmentationCell MembraneCells, CulturedCricetinaeCyclopentanesGolgi ApparatusHexosaminidasesMembrane GlycoproteinsMutationPostural BalanceProtein ConformationProtein Processing, Post-TranslationalVesicular stomatitis Indiana virusViral Envelope ProteinsConceptsEndoplasmic reticulumHeterotrimer formationG proteinsMutant G proteinsG protein trimersVesicular stomatitis virus glycoproteinG protein subunitsVSV G proteinProtein moleculesG protein moleculesWild-type trimersMutant proteinsCytoplasmic domainCellular compartmentsCoexpression experimentsGlycoprotein monomersLonger chase periodsPlasma membraneProtein subunitsMu proteinProtein trimerForms trimersCell surfaceMonomeric subunitsProteinFolding and Assembly of Viral Membrane Proteins
Doms R, Lamb R, Rose J, Helenius A. Folding and Assembly of Viral Membrane Proteins. Virology 1993, 193: 545-562. PMID: 8460475, DOI: 10.1006/viro.1993.1164.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsEndoplasmic ReticulumGlycoproteinsMutagenesisProtein BiosynthesisProtein FoldingProtein Processing, Post-TranslationalViral Envelope ProteinsVirusesConceptsViral membrane proteinsQuality control mechanismsMolecular chaperonesGRP78-BiPMembrane proteinsER molecular chaperonesEffects of mutationsMisfolded proteinsProtein transportConformational maturationMisfolded moleculesProtein foldingEnergy-driven processChaperonesProtein structureMolecular mechanismsER environmentGRP78 synthesisExogenous proteinsNascent moleculesProteinDirect roleStructural variabilityControl mechanismsExperimental strategiesCell 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
1992
Identification of palmitoylation sites on CD4, the human immunodeficiency virus receptor.
Crise B, Rose J. Identification of palmitoylation sites on CD4, the human immunodeficiency virus receptor. Journal Of Biological Chemistry 1992, 267: 13593-13597. PMID: 1618861, DOI: 10.1016/s0021-9258(18)42253-3.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCD4 AntigensChromatography, LiquidCysteineHeLa CellsHIVHumansMethionineMolecular Sequence DataMutagenesisPalmitic AcidPalmitic AcidsPlasmidsPrecipitin TestsProtein Processing, Post-TranslationalConceptsCytoplasmic domainBinding of p56lckHuman immunodeficiency virus receptorCell surface glycoprotein CD4Palmitoylation sitesCysteine residuesThioester linkageGlycoprotein CD4HeLa cellsCell surfaceVirus receptorProteinFatty acidsMutationsCysteineExpression of CD4Cys397Palmitic acidCys394P56lckTransmembraneCD4AcidPalmitateDomain
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 ResearchMeSH KeywordsCD4 AntigensCell CompartmentationCloning, MolecularEndoplasmic ReticulumGene Products, envGlycosylationHeLa CellsHIV Envelope Protein gp120HumansIn Vitro TechniquesProtein BindingProtein Processing, Post-Translational
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 Research
1987
Effects of mutations in three domains of the vesicular stomatitis viral glycoprotein on its lateral diffusion in the plasma membrane.
Scullion B, Hou Y, Puddington L, Rose J, Jacobson K. Effects of mutations in three domains of the vesicular stomatitis viral glycoprotein on its lateral diffusion in the plasma membrane. Journal Of Cell Biology 1987, 105: 69-75. PMID: 3038931, PMCID: PMC2114925, DOI: 10.1083/jcb.105.1.69.Peer-Reviewed Original ResearchConceptsCytoplasmic domainTransmembrane domainMutant proteinsMembrane proteinsExtracellular domainWild-type G proteinG proteinsMutant G proteinsVesicular stomatitis viral glycoproteinIntegral membrane proteinsEntire cytoplasmic domainLateral mobilitySite-directed mutagenesisEffects of mutationsCOS-1 cellsSlow mutantsFastest mutantPlasma membraneChimeric proteinType G proteinsG cDNAVirus spike glycoproteinPalmitate additionFluorescence recoveryArtificial bilayers
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 hormoneTransmembraneGenesSitesIncorporation of a charged amino acid into the membrane-spanning domain blocks cell surface transport but not membrane anchoring of a viral glycoprotein.
Adams G, Rose J. Incorporation of a charged amino acid into the membrane-spanning domain blocks cell surface transport but not membrane anchoring of a viral glycoprotein. Molecular And Cellular Biology 1985, 5: 1442-1448. PMID: 2993864, PMCID: PMC366875, DOI: 10.1128/mcb.5.6.1442.Peer-Reviewed Original ResearchConceptsMembrane anchoringG proteinsAmino acidsCell surfaceIsoleucine residueMembrane-spanning domainsCell surface transportVesicular stomatitis virus glycoproteinOligonucleotide-directed mutagenesisAmino acid sequenceUncharged amino acidsDetectable protein levelsHydrophobic amino acidsAnimal cellsCDNA clonesIntracellular membranesAcid sequencePunctate patternGolgi regionProteinContinuous stretchVesicular patternProtein levelsViral glycoproteinsVirus glycoprotein