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
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
A 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
1989
Glycoprotein cytoplasmic domain sequences required for rescue of a vesicular stomatitis virus glycoprotein mutant
Whitt M, Chong L, Rose J. Glycoprotein cytoplasmic domain sequences required for rescue of a vesicular stomatitis virus glycoprotein mutant. Journal Of Virology 1989, 63: 3569-3578. PMID: 2547986, PMCID: PMC250946, DOI: 10.1128/jvi.63.9.3569-3578.1989.Peer-Reviewed Original ResearchConceptsCytoplasmic domainG proteinsAmino acidsWild-type G proteinNormal cytoplasmic domainG protein mutantsCytoplasmic domain sequencesVesicular stomatitis virus glycoproteinVSV G proteinTemperature-sensitive mutantViral G proteinSurface expressionG protein expressionProtein mutantsTransient expressionVirus buddingNonpermissive temperatureDomain sequencesMutantsCell surfaceGlycoprotein mutantsProteinImmunogold labelingSucrose gradientsEfficient assembly
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 acids
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 bilayersAn 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 constructsCells
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 acidCellsMutagenesisOligosaccharidesCDNA
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 ResearchConceptsCytoplasmic 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
Nucleotide sequence of a cDNA clone encoding the entire glycoprotein from the New Jersey serotype of vesicular stomatitis virus
Gallione C, Rose J. Nucleotide sequence of a cDNA clone encoding the entire glycoprotein from the New Jersey serotype of vesicular stomatitis virus. Journal Of Virology 1983, 46: 162-169. PMID: 6298453, PMCID: PMC255104, DOI: 10.1128/jvi.46.1.162-169.1983.Peer-Reviewed Original ResearchConceptsNew Jersey serotypeVesicular stomatitis virusCDNA clonesIndiana serotypeNucleotide sequenceTranslation termination codonVSV serotypesStomatitis virusTransmembrane domainSignal sequenceSerine residuesProtein sequencesTermination codonEsterification sitesGlycosylation sitesNoncoding nucleotidesGlycine residueShort homologiesAmino acidsNucleotidesMRNARabies virusClonesTerminusResidues
1981
Nucleotide sequences of the mRNA's encoding the vesicular stomatitis virus G and M proteins determined from cDNA clones containing the complete coding regions
Rose J, Gallione C. Nucleotide sequences of the mRNA's encoding the vesicular stomatitis virus G and M proteins determined from cDNA clones containing the complete coding regions. Journal Of Virology 1981, 39: 519-528. PMID: 6268840, PMCID: PMC171362, DOI: 10.1128/jvi.39.2.519-528.1981.Peer-Reviewed Original ResearchConceptsCDNA clonesAmino acidsSignal peptideNucleotide sequenceVesicular stomatitis virus M proteinFull-length cDNA cloneBasic amino-terminal domainComplete nucleotide sequenceVesicular stomatitis virus mRNAAmino-terminal domainComplete coding sequenceM protein sequencesComplete coding regionSite of glycosylationBasic amino acidsM proteinVesicular stomatitis virus GMembrane associationTransmembrane segmentsG protein mRNALarge hydrophobic domainsTerminal domainCoding sequenceProtein sequencesAsparagine residuesNucleotide sequences of the mRNA's encoding the vesicular stomatitis virus N and NS proteins
Gallione C, Greene J, Iverson L, Rose J. Nucleotide sequences of the mRNA's encoding the vesicular stomatitis virus N and NS proteins. Journal Of Virology 1981, 39: 529-535. PMID: 6268841, PMCID: PMC171363, DOI: 10.1128/jvi.39.2.529-535.1981.Peer-Reviewed Original ResearchConceptsNS proteinsAUG codonReading frameNucleotide sequenceThird AUG codonAmino acidsComplete nucleotide sequenceVesicular stomatitis virus mRNAOpen reading frameSodium dodecyl sulfate-polyacrylamide gelsAnomalous electrophoretic mobilityDodecyl sulfate-polyacrylamide gelsSecond reading frameSulfate-polyacrylamide gelsCDNA clonesTranslational initiationSmall proteinsMRNA sequencesN proteinVirus NPolyadenylic acidVirus mRNACodonProteinMRNA