2000
Expression of Human Immunodeficiency Virus Type 1 Gag Protein Precursor and Envelope Proteins from a Vesicular Stomatitis Virus Recombinant: High-Level Production of Virus-like Particles Containing HIV Envelope
Haglund K, Forman J, Kräusslich H, Rose J. Expression of Human Immunodeficiency Virus Type 1 Gag Protein Precursor and Envelope Proteins from a Vesicular Stomatitis Virus Recombinant: High-Level Production of Virus-like Particles Containing HIV Envelope. Virology 2000, 268: 112-121. PMID: 10683333, DOI: 10.1006/viro.1999.0120.Peer-Reviewed Original ResearchMeSH KeywordsAIDS VaccinesAnimalsCell LineDNA, RecombinantGene Products, gagGenetic VectorsHIV Envelope Protein gp120HIV-1HumansMembrane GlycoproteinsMicroscopy, ElectronPlasmidsProtein PrecursorsRecombinant Fusion ProteinsVaccines, AttenuatedVesicular stomatitis Indiana virusViral Envelope ProteinsVirionConceptsHIV virus-like particlesVirus-like particlesEnv proteinHIV-1HIV-1 envelope proteinAntibody-mediated immunityHigh-level productionRecombinant vesicular stomatitis virusVSV particlesHIV Env proteinEnvelope proteinEffective vaccine vectorHIV-like particlesProtein precursorHIV envelopeHigh-level expression vectorVaccine vectorHIV recombinantsVesicular stomatitis virusVirus titersVirus recombinantsVSV G proteinG proteinsStomatitis virusExpression vector
1999
Redesign and Genetic Dissection of The Rhabdoviruses
Roberts A, Rose J. Redesign and Genetic Dissection of The Rhabdoviruses. Advances In Virus Research 1999, 53: 301-319. PMID: 10582104, DOI: 10.1016/s0065-3527(08)60353-x.Peer-Reviewed Original ResearchConceptsNegative-strand RNA virusesGenetic dissectionNegative-strand genome RNAWild-type virusRNA virusesNonsegmented negative-strand RNA virusesBacteriophage T7 RNA polymeraseNegative-strand RNA genomeVaccine vector developmentT7 RNA polymeraseRNA polymeraseInfection of cellsT7 promoterGenome RNARNA genomeGenetic analysisPolymerase proteinNNS virusesViral transcriptionNotorious pathogenViral assemblyRhabdovirusDNA copiesRecombinant virusesPlasmid DNA
1998
Recovery of Negative-Strand RNA Viruses from Plasmid DNAs: A Positive Approach Revitalizes a Negative Field
Roberts A, Rose J. Recovery of Negative-Strand RNA Viruses from Plasmid DNAs: A Positive Approach Revitalizes a Negative Field. Virology 1998, 247: 1-6. PMID: 9683565, DOI: 10.1006/viro.1998.9250.Peer-Reviewed Original Research
1996
Positive strands to the rescue again: A segmented negative-strand RNA virus derived from cloned cDNAs
Rose J. Positive strands to the rescue again: A segmented negative-strand RNA virus derived from cloned cDNAs. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 14998-15000. PMID: 8986751, PMCID: PMC33647, DOI: 10.1073/pnas.93.26.14998.Peer-Reviewed Original Research
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
1994
Brefeldin A sensitivity and resistance in Schizosaccharomyces pombe. Isolation of multiple genes conferring resistance.
Turi T, Webster P, Rose J. Brefeldin A sensitivity and resistance in Schizosaccharomyces pombe. Isolation of multiple genes conferring resistance. Journal Of Biological Chemistry 1994, 269: 24229-24236. PMID: 7929079, DOI: 10.1016/s0021-9258(19)51072-9.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntifungal AgentsBrefeldin ACyclopentanesDrug Resistance, MicrobialFungal ProteinsGolgi ApparatusKaryopherinsMolecular Sequence DataMutationPancreatitis-Associated ProteinsPhenotypePlasmidsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiaeSchizosaccharomycesSequence Homology, Amino AcidConceptsBFA resistanceEffects of BFABrefeldin AGolgi complexMammalian cellsTranscription factor Pap1Fission yeast SchizosaccharomycesFungal metabolite brefeldin ASeparate linkage groupsWild-type cellsChromatin structureYeast SchizosaccharomycesSchizosaccharomyces pombeAP1 proteinLinkage groupsGolgi morphologyAnimal cellsMultiple genesDifferent genesGenetic analysisEndoplasmic reticulumProtein secretionGenesType cellsMutants
1992
Liposome‐Mediated Transfection
Whitt M, Buonocore L, Rose J. Liposome‐Mediated Transfection. Current Protocols In Immunology 1992, 3: 10.16.1-10.16.4. PMID: 18432679, DOI: 10.1002/0471142735.im1016s03.Peer-Reviewed Original ResearchConceptsDifferent eukaryotic cell typesEukaryotic cell typesTransient expression systemExpression of DNAStable transformationExpression systemCell typesTransfection methodAlternate protocolMonolayer cell culturesDNABasic protocolPlasmid DNACell culturesGenomeCationic lipidsTransfectionExpressionCellsLipidsIdentification 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 ResearchConceptsCytoplasmic domainBinding of p56lckHuman immunodeficiency virus receptorCell surface glycoprotein CD4Palmitoylation sitesCysteine residuesThioester linkageGlycoprotein CD4HeLa cellsCell surfaceVirus receptorProteinFatty acidsMutationsCysteineExpression of CD4Cys397Palmitic acidCys394P56lckTransmembraneCD4AcidPalmitateDomain
1991
Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein
Whitt M, Buonocor L, Prehaud C, Rose J. Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein. Virology 1991, 185: 681-688. PMID: 1660200, DOI: 10.1016/0042-6822(91)90539-n.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, ViralBase SequenceCell LineCentrifugation, Density GradientCricetinaeFlow CytometryGenetic Complementation TestGlycoproteinsHumansHydrogen-Ion ConcentrationKineticsMacromolecular SubstancesMembrane FusionMembrane GlycoproteinsMiceMolecular Sequence DataPlasmidsRabies virusRecombinant Fusion ProteinsVesicular stomatitis Indiana virusViral Envelope ProteinsViral Fusion ProteinsConceptsVSV G proteinG protein trimersMembrane fusion activityVirus G proteinG proteinsRabies G proteinFusion activityHybrid proteinProtein trimerVesicular stomatitis virus G proteinVirus glycoproteinRabies virus glycoproteinCytoplasmic domainMembrane fusionExtracellular domainHeLa cellsRabies virus G proteinCell surfaceProteinVSV particlesSucrose gradientsVSV infectivityGlycoproteinSpike glycoproteinChemical crosslinking
1989
Carboxy-terminal SEKDEL sequences retard but do not retain two secretory proteins in the endoplasmic reticulum.
Zagouras P, Rose J. Carboxy-terminal SEKDEL sequences retard but do not retain two secretory proteins in the endoplasmic reticulum. Journal Of Cell Biology 1989, 109: 2633-2640. PMID: 2592401, PMCID: PMC2115906, DOI: 10.1083/jcb.109.6.2633.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumSEKDEL sequenceSecretory proteinsSequence Ser-GluAmino acidsMonkey COS cellsOligonucleotide-directed mutagenesisLast amino acidFirst amino acidProtein exitIndirect immunofluorescence microscopyAnimal cellsCOS cellsCOOH terminusAlpha subunitProtein structureGolgi apparatusLys-AspImmunofluorescence microscopyOligosaccharide processingProteinReticulumSEKDELSer-GluSpecific interactionsThe Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain
Shaw A, Amrein K, Hammond C, Stern D, Sefton B, Rose J. The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain. Cell 1989, 59: 627-636. PMID: 2582490, DOI: 10.1016/0092-8674(89)90008-1.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCD4 AntigensCytoplasmHeLa CellsHumansLymphocyte Specific Protein Tyrosine Kinase p56(lck)Macromolecular SubstancesMembrane GlycoproteinsMolecular Sequence DataMutationOligonucleotide ProbesPhosphoproteinsPlasmidsProtein BindingProtein MultimerizationProtein-Tyrosine KinasesT-LymphocytesTransfectionConceptsAmino-terminal domainCytoplasmic domainTyrosine protein kinase p56lckUnique amino-terminal domainT cell-specific proteinsTyrosine protein kinaseSpecific transmembrane proteinsCell-specific proteinsIntracellular tyrosine kinaseAmino-terminal residuesCarboxy-terminal residuesTransmembrane proteinCytoplasmic tailSrc familyProtein kinaseKinase p56lckTyrosine kinaseHeLa cellsCell surfaceProteinDeleted formsSurface glycoproteinP56lckKinaseResidues
1988
Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum.
Shaw A, Rottier P, Rose J. Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 7592-7596. PMID: 2845415, PMCID: PMC282238, DOI: 10.1073/pnas.85.20.7592.Peer-Reviewed Original ResearchConceptsSignal sequenceEndoplasmic reticulumC-terminal transmembraneType II transmembrane proteinInsertion of proteinsCleaved signal sequenceSignal sequence functionN-terminal extensionShort hydrophobic domainVesicular stomatitis virus glycoproteinMembrane anchorMutant proteinsCytoplasmic domainMembrane insertionTransmembrane proteinC-terminusCytoplasmic sideN-terminusBlock cleavageHydrophobic domainCleavage siteHeLa cellsPoint mutationsProteinMicrosomal membranesCell-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 acids
1987
An internalized amino-terminal signal sequence retains full activity in vivo but not in vitro.
Rottier P, Florkiewicz R, Shaw A, Rose J. An internalized amino-terminal signal sequence retains full activity in vivo but not in vitro. Journal Of Biological Chemistry 1987, 262: 8889-8895. PMID: 3036834, DOI: 10.1016/s0021-9258(18)47498-4.Peer-Reviewed Original ResearchConceptsSignal sequenceAmino-terminal signal sequenceAmino-terminal presequenceAmino-terminal extensionAmino-terminal coding sequenceVesicular stomatitis virus glycoproteinWild-type efficiencyEukaryotic cellsMembrane insertionSignal peptideCoding sequenceSignal cleavageAmino acidsVirus glycoproteinFull activitySequenceVivoGlycoproteinPresequenceSubsequent transportCleavageGlycosylationInternalizationSuch constructsCellsReplacement 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
1981
Conditional expression of the vesicular stomatitis virus glycoprotein gene in Escherichia coli.
Rose J, Shafferman A. Conditional expression of the vesicular stomatitis virus glycoprotein gene in Escherichia coli. Proceedings Of The National Academy Of Sciences Of The United States Of America 1981, 78: 6670-6674. PMID: 6273881, PMCID: PMC349111, DOI: 10.1073/pnas.78.11.6670.Peer-Reviewed Original ResearchConceptsGlycoprotein geneEscherichia coliNH2-terminal domainTryptic peptide mappingRegulatory regionsProtein sequencesBacterial plasmidsCOOH terminusGene regionG proteinsConditional expressionAmino acidsProteinHydrophobic segmentsPeptide mappingPlasmidStomatitis virusGenesDeletionColiLethalitySequenceExpressionAntigenic determinantsTerminus