1999
Replication-Competent Rhabdoviruses with Human Immunodeficiency Virus Type 1 Coats and Green Fluorescent Protein: Entry by a pH-Independent Pathway
Boritz E, Gerlach J, Johnson J, Rose J. Replication-Competent Rhabdoviruses with Human Immunodeficiency Virus Type 1 Coats and Green Fluorescent Protein: Entry by a pH-Independent Pathway. Journal Of Virology 1999, 73: 6937-6945. PMID: 10400792, PMCID: PMC112779, DOI: 10.1128/jvi.73.8.6937-6945.1999.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCD4 AntigensCD4-Positive T-LymphocytesCell LineCricetinaeGreen Fluorescent ProteinsHeLa CellsHIV AntibodiesHIV Envelope Protein gp160HIV-1HumansHydrogen-Ion ConcentrationLigandsLuminescent ProteinsNeutralization TestsReceptors, CCR5Receptors, CXCR4Receptors, HIVRecombination, GeneticVesicular stomatitis Indiana virusVirus ReplicationConceptsVesicular stomatitis virusHuman immunodeficiency virus type 1 (HIV-1) envelope proteinSurrogate virusesRecombinant vesicular stomatitis virusPH-independent pathwayHIV bindingHIV vaccineHIV receptor CD4Coreceptor CXCR4HIV entryCoreceptor specificitySDF-1HIVReceptor CD4Single transmembrane glycoproteinAntibodiesVirusCD4Envelope proteinStomatitis virusCXCR4InfectionTransmembrane glycoproteinGreen fluorescent proteinAdditional recombinants
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
1996
Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains.
Rodgers W, Rose J. Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains. Journal Of Cell Biology 1996, 135: 1515-1523. PMID: 8978819, PMCID: PMC2133949, DOI: 10.1083/jcb.135.6.1515.Peer-Reviewed Original ResearchConceptsExclusion of CD45Low kinase activityGEM fractionMembrane domainsKinase activitySrc family tyrosine kinasesReservoir of enzymesSpecific membrane domainsActivity of p56lckTyrosine phosphatase CD45Family tyrosine kinasesT cell developmentTX-100-soluble fractionGEM domainsPhosphatase CD45Membrane proteinsKinase specific activityLckTyrosine kinaseMembrane fractionJurkat cellsPeptide mappingP56lckPhosphorylationHyperphosphorylationMembrane Association of Influenza Virus Matrix Protein Does Not Require Specific Hydrophobic Domains or the Viral Glycoproteins
KRETZSCHMAR E, BUI M, ROSE J. Membrane Association of Influenza Virus Matrix Protein Does Not Require Specific Hydrophobic Domains or the Viral Glycoproteins. Virology 1996, 220: 37-45. PMID: 8659126, DOI: 10.1006/viro.1996.0283.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceBinding SitesCell LineCell MembraneChick EmbryoDogsHeLa CellsHemagglutinin Glycoproteins, Influenza VirusHemagglutinins, ViralHumansInfluenza A virusMolecular Sequence DataMutagenesis, Site-DirectedNeuraminidaseOligodeoxyribonucleotidesRecombinant ProteinsViral Matrix ProteinsConceptsMembrane associationSpecific hydrophobic domainsM1 proteinMatrix proteinsHydrophobic domainInfluenza virus matrix proteinVirus matrix proteinInteraction of M1Viral glycoproteinsMajor structural componentRibonucleocapsid coreCytoplasmic tailIntegral proteinsMembrane proteinsMembrane bindingSubcellular fractionationMembrane envelopeCellular membranesHeLa cellsViral proteinsHydrophobic regionProteinIsolated membranesMembraneInfluenza proteins
1994
Stimulation of Heterologous Protein Degradation by the Vpu Protein of HIV-1 Requires the Transmembrane and Cytoplasmic Domains of CD4
Buonocore L, Turi T, Crise B, Rose J. Stimulation of Heterologous Protein Degradation by the Vpu Protein of HIV-1 Requires the Transmembrane and Cytoplasmic Domains of CD4. Virology 1994, 204: 482-486. PMID: 8091684, DOI: 10.1006/viro.1994.1560.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCD4 AntigensGlycoproteinsHeLa CellsHIV-1Human Immunodeficiency Virus ProteinsHumansMembrane GlycoproteinsMolecular Sequence DataProtein Structure, TertiaryRecombinant Fusion ProteinsRecombinant ProteinsViral Envelope ProteinsViral Regulatory and Accessory ProteinsConceptsCytoplasmic domainTransmembrane domainHybrid proteinHeterologous protein degradationVesicular stomatitis virus glycoproteinRapid degradationAdditional hybridsProtein degradationExtracellular domainProtein VpuRelated sequencesVpu proteinDegradation systemEndoplasmic reticulumVSV GVpu expressionProteinVpuTransmembraneVirus glycoproteinRecent studiesDomainHuman immunodeficiency virus type 1Immunodeficiency virus type 1DegradationSignals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction.
Rodgers W, Crise B, Rose J. Signals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction. Molecular And Cellular Biology 1994, 14: 5384-5391. PMID: 8035816, PMCID: PMC359057, DOI: 10.1128/mcb.14.8.5384.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCell CompartmentationDNA PrimersGlycolipidsGlycosylphosphatidylinositolsHeLa CellsHumansLymphocyte Specific Protein Tyrosine Kinase p56(lck)Molecular Sequence DataMutagenesis, Site-DirectedMyristatesPalmitatesProtein-Tyrosine KinasesProteinsStructure-Activity RelationshipConceptsProtein tyrosine kinasesCertain protein tyrosine kinasesTyrosine kinaseMembrane fractionSrc family protein tyrosine kinasesFamily protein tyrosine kinasesAnalysis of mutantsN-terminal myristateCy-3Glycolipid-enriched membranesAssociation of p56lckCys-5Membrane domainsMembrane proteinsAnchored proteinsGPI anchorGlycosyl phosphatidylinositolKinaseP56lckCell typesHeLa cellsMDCK cellsGPIProteinGentle disruptionMutations in the membrane-spanning domain of the human immunodeficiency virus envelope glycoprotein that affect fusion activity
Owens R, Burke C, Rose J. Mutations in the membrane-spanning domain of the human immunodeficiency virus envelope glycoprotein that affect fusion activity. Journal Of Virology 1994, 68: 570-574. PMID: 8254774, PMCID: PMC236324, DOI: 10.1128/jvi.68.1.570-574.1994.Peer-Reviewed Original ResearchConceptsTransmembrane domainFusion activityVesicular stomatitis virus G proteinMembrane-spanning domainsCell surfaceSpecific amino acid sequencesAmino acid sequenceMembrane fusion activityAmino acid residuesMembrane fusion processCytoplasmic tail domainVirus G proteinCytoplasmic domainMutagenic analysisAcid sequenceChimeric proteinBasic residuesProtein ectodomainAcid residuesG proteinsHeLa cellsVirus envelope glycoproteinLipid bilayersProteinGp41 transmembrane
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 developmentMembrane association of functional vesicular stomatitis virus matrix protein in vivo
Chong L, Rose J. Membrane association of functional vesicular stomatitis virus matrix protein in vivo. Journal Of Virology 1993, 67: 407-414. PMID: 8380086, PMCID: PMC237377, DOI: 10.1128/jvi.67.1.407-414.1993.Peer-Reviewed Original ResearchMeSH KeywordsCell MembraneCytosolHeLa CellsHumansMacromolecular SubstancesMembrane ProteinsModels, BiologicalOctoxynolPolyethylene GlycolsProtein ConformationRecombinant ProteinsRibonucleoproteinsSolubilitySubcellular FractionsVesicular stomatitis Indiana virusViral Core ProteinsViral Matrix ProteinsConceptsVesicular stomatitis virusRNP coresMatrix proteinsVesicular stomatitis virus matrix proteinM proteinVirus matrix proteinSoluble M proteinMajor structural componentRibonucleocapsid coreMembrane associationMembrane proteinsM protein moleculeVirus buddingSubcellular fractionationCellular membranesMembrane envelopeHeLa cellsVSV proteinsViral proteinsDetergent Triton XProteinProtein moleculesConformational differencesStomatitis virusMembrane
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 ResearchConceptsCytoplasmic domainBinding of p56lckHuman immunodeficiency virus receptorCell surface glycoprotein CD4Palmitoylation sitesCysteine residuesThioester linkageGlycoprotein CD4HeLa cellsCell surfaceVirus receptorProteinFatty acidsMutationsCysteineExpression of CD4Cys397Palmitic acidCys394P56lckTransmembraneCD4AcidPalmitateDomainHuman 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
1991
Fatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions
Whitt M, Rose J. Fatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions. Virology 1991, 185: 875-878. PMID: 1660205, DOI: 10.1016/0042-6822(91)90563-q.Peer-Reviewed Original ResearchConceptsFatty acid acylationVSV G proteinMembrane fusion activityVesicular stomatitis virusG proteinsWild-type G proteinFusion activityWild-type proteinTemperature-sensitive mutantCytoplasmic domainTransient expressionPresence of palmitateVSV virionsIndiana serotypeHeLa cellsExpression of CSProteinStomatitis virusLife cycleSyncytium formationExpressionMutantsAcylationVirionsVirusA new cationic liposome reagent mediating nearly quantitative transfection of animal cells.
Rose J, Buonocore L, Whitt M. A new cationic liposome reagent mediating nearly quantitative transfection of animal cells. BioTechniques 1991, 10: 520-5. PMID: 1867862.Peer-Reviewed Original Research
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 ResearchPrevention 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
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 interactionsOligomerization of glycolipid-anchored and soluble forms of the vesicular stomatitis virus glycoprotein
Crise B, Ruusala A, Zagouras P, Shaw A, Rose J. Oligomerization of glycolipid-anchored and soluble forms of the vesicular stomatitis virus glycoprotein. Journal Of Virology 1989, 63: 5328-5333. PMID: 2555557, PMCID: PMC251199, DOI: 10.1128/jvi.63.12.5328-5333.1989.Peer-Reviewed Original ResearchMeSH KeywordsAcetylglucosaminidaseAmino Acid SequenceBase SequenceCentrifugation, Density GradientCodonElectrophoresis, Polyacrylamide GelGlycolipidsHeLa CellsHumansKineticsMacromolecular SubstancesMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseMembrane GlycoproteinsMolecular Sequence DataRestriction MappingSolubilityVesicular stomatitis Indiana virusViral Envelope ProteinsConceptsG proteinsWild-type G proteinAmino acidsC-terminal amino acidsVesicular stomatitis virus glycoproteinMutant proteinsCytoplasmic domainAnchor sequenceExtracellular domainGolgi apparatusEndoplasmic reticulumCell surfaceTrimer formationProteinPhospholipase C.TransmembraneVirus glycoproteinSoluble formStructural informationSequenceGlycoproteinNormal transmembraneRate of transportGlycoprotein formThy-1.1The 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 membranes
1980
Purification of a factor that restores translation of vesicular stomatitis virus mRNA in extracts from poliovirus-infected HeLa cells.
Trachsel H, Sonenberg N, Shatkin A, Rose J, Leong K, Bergmann J, Gordon J, Baltimore D. Purification of a factor that restores translation of vesicular stomatitis virus mRNA in extracts from poliovirus-infected HeLa cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 770-774. PMID: 6244584, PMCID: PMC348362, DOI: 10.1073/pnas.77.2.770.Peer-Reviewed Original Research