2001
Mechanisms of Loss of Foreign Gene Expression in Recombinant Vesicular Stomatitis Viruses
Quiñones-Kochs M, Schnell M, Buonocore L, Rose J. Mechanisms of Loss of Foreign Gene Expression in Recombinant Vesicular Stomatitis Viruses. Virology 2001, 287: 427-435. PMID: 11531419, DOI: 10.1006/viro.2001.1058.Peer-Reviewed Original Research
1998
A Plasma Membrane Localization Signal in the HIV-1 Envelope Cytoplasmic Domain Prevents Localization at Sites of Vesicular Stomatitis Virus Budding and Incorporation into VSV Virions
Johnson J, Rodgers W, Rose J. A Plasma Membrane Localization Signal in the HIV-1 Envelope Cytoplasmic Domain Prevents Localization at Sites of Vesicular Stomatitis Virus Budding and Incorporation into VSV Virions. Virology 1998, 251: 244-252. PMID: 9837788, DOI: 10.1006/viro.1998.9429.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell MembraneCells, CulturedCricetinaeCytoplasmGene Products, envHIV Envelope Protein gp120HIV-1HumansMembrane GlycoproteinsMicroscopy, ConfocalMolecular Sequence DataProtein Sorting SignalsRecombinant ProteinsStructure-Activity RelationshipVesicular stomatitis Indiana virusViral Envelope ProteinsVirionConceptsVSV virionsMembrane-proximal amino acidsMembrane localization signalAmino acidsVesicular stomatitis virus (VSV) virionsLocalization signalMembrane domainsG-tailsCytoplasmic tailVirus buddingPrevents localizationVirus virionsMutantsVSV proteinsProteinConfocal microscopyVSV recombinantsEnvelope proteinVSV glycoproteinHuman Immunodeficiency Virus Type 1 EnvVirionsHIV-1 envelope proteinEnv proteinTailHybrids
1997
Optimization of Transfection
Rose J. Optimization of Transfection. Current Protocols In Neuroscience 1997, 1: a.1b.1-a.1b.3. PMID: 18428433, DOI: 10.1002/0471142301.nsa01bs01.Peer-Reviewed Original Research
1994
Novel infectious particles generated by expression of the vesicular stomatitis virus glycoprotein from a self-replicating RNA
Rolls M, Webster P, Balba N, Rose J. Novel infectious particles generated by expression of the vesicular stomatitis virus glycoprotein from a self-replicating RNA. Cell 1994, 79: 497-506. PMID: 7954815, DOI: 10.1016/0092-8674(94)90258-5.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta-GalactosidaseCells, CulturedGenetic VectorsHumansMembrane GlycoproteinsModels, GeneticNeutralization TestsParticle SizeRepliconRNA VirusesRNA-Dependent RNA PolymeraseSemliki forest virusSerial PassageSpecies SpecificityTransfectionViral Envelope ProteinsViral Fusion ProteinsVirus ReplicationConceptsVesicular stomatitis virus glycoproteinVSV G proteinSemliki Forest virusStructural proteinsMembrane-enveloped vesiclesRNA repliconsSFV structural proteinsInfectious particlesViral structural proteinsTissue culture cellsVirus glycoproteinAnimal cellsSelf-replicating RNARNA replicaseG proteinsCulture cellsProteinRepliconVirus-like particlesVesiclesVSV serumCellsGlycoproteinExpressionReplicaseInteractions of normal and mutant vesicular stomatitis virus matrix proteins with the plasma membrane and nucleocapsids
Chong L, Rose J. Interactions of normal and mutant vesicular stomatitis virus matrix proteins with the plasma membrane and nucleocapsids. Journal Of Virology 1994, 68: 441-447. PMID: 8254754, PMCID: PMC236304, DOI: 10.1128/jvi.68.1.441-447.1994.Peer-Reviewed Original ResearchConceptsMembrane associationPlasma membraneAmino-terminal basic domainVesicular stomatitis virusWild-type M proteinCellular membranesMatrix proteinsVesicular stomatitis virus matrix proteinM proteinStable membrane associationTruncated M proteinsVirus matrix proteinVSV nucleocapsidsBasic domainAmino terminusNucleocapsid bindingNucleocapsid interactionMembrane fractionVSV proteinsAmino acidsMembrane specificityProteinStomatitis virusNucleocapsidsMembrane
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 subunitsProtein
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 lipidsTransfectionExpressionCellsLipids
1991
Dissociation and reassociation of oligomeric viral glycoprotein subunits in the endoplasmic reticulum
Zagouras P, Ruusala A, Rose J. Dissociation and reassociation of oligomeric viral glycoprotein subunits in the endoplasmic reticulum. Journal Of Virology 1991, 65: 1976-1984. PMID: 1848313, PMCID: PMC240033, DOI: 10.1128/jvi.65.4.1976-1984.1991.Peer-Reviewed Original ResearchConceptsWild-type ratesEndoplasmic reticulumMutant subunitsG proteinsCell surfaceG protein trimersWild-type subunitsFormation of heterotrimersWild-type moleculeWild-type trimersMutant proteinsRetention signalProtein trimerHeterotrimerSubunitsGlycoprotein subunitsProteinReticulumGlycoprotein formTrimerTransport blockHomotrimersReassociation
1989
Fc receptor isoforms exhibit distinct abilities for coated pit localization as a result of cytoplasmic domain heterogeneity
Miettinen H, Rose J, Mellman I. Fc receptor isoforms exhibit distinct abilities for coated pit localization as a result of cytoplasmic domain heterogeneity. Cell 1989, 58: 317-327. PMID: 2568890, DOI: 10.1016/0092-8674(89)90846-5.Peer-Reviewed Original Research