1997
Construction of a Novel Virus That Targets HIV-1-Infected Cells and Controls HIV-1 Infection
Schnell M, Johnson J, Buonocore L, Rose J. Construction of a Novel Virus That Targets HIV-1-Infected Cells and Controls HIV-1 Infection. Cell 1997, 90: 849-857. PMID: 9298897, DOI: 10.1016/s0092-8674(00)80350-5.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCD4 AntigensCricetinaeGene DeletionGene Expression Regulation, ViralGlycoproteinsGTP-Binding ProteinsHIV InfectionsHIV-1HumansJurkat CellsKidneyMembrane GlycoproteinsMembrane ProteinsMicroscopy, ImmunoelectronMutagenesisReceptors, CXCR4Receptors, HIVRecombinant Fusion ProteinsVesicular stomatitis Indiana virusViral Envelope ProteinsVirus ReplicationConceptsHIV-1-infected cellsHIV-1HIV-1 receptors CD4HIV viral loadHIV-1 infectionInfectious HIV-1Recombinant vesicular stomatitis virusT cell linesHIV infectionViral loadVesicular stomatitis virusTherapeutic valueReceptor CD4Targeted virusInfectionVirusEnvelope proteinCell linesStomatitis virusNormal cellsNovel virusCellsGlycoprotein geneCD4CXCR4
1993
Membrane 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
Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
Brown D, Rose J. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 1992, 68: 533-544. PMID: 1531449, DOI: 10.1016/0092-8674(92)90189-j.Peer-Reviewed Original ResearchConceptsBasolateral marker proteinsCertain membrane proteinsApical cell surfaceDetergent-insoluble formGlycosylphosphatidyl inositol (GPI) anchorMembrane subdomainsMembrane proteinsIntracellular associationGolgi complexMicrodomains formGolgi apparatusInositol anchorMarker proteinsCell surfaceProteinApical surfaceEpithelial cellsGPIGlycosphingolipidsComplexesVesiclesLysatesGlycolipidsSortingMembrane
1989
Mechanism of Membrane Anchoring Affects Polarized Expression of Two Proteins in MDCK Cells
Brown D, Crise B, Rose J. Mechanism of Membrane Anchoring Affects Polarized Expression of Two Proteins in MDCK Cells. Science 1989, 245: 1499-1501. PMID: 2571189, DOI: 10.1126/science.2571189.Peer-Reviewed Original ResearchConceptsMembrane anchorageGPI anchorBasolateral plasma membrane domainsSorting of proteinsPlasma membrane domainsPolarized epithelial cellsClass of proteinsBasolateral surfaceVesicular stomatitis virus glycoproteinMembrane anchoringCytoplasmic domainMembrane domainsMembrane proteinsPolypeptide sequenceTransport signalVSV GPolarized expressionMDCK cellsApical expressionProteinApical surfaceEpithelial cellsVirus glycoproteinPlacental alkaline phosphataseExpression
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
1986
Cytoplasmic domains of cellular and viral integral membrane proteins substitute for the cytoplasmic domain of the vesicular stomatitis virus glycoprotein in transport to the plasma membrane.
Puddington L, Machamer C, Rose J. Cytoplasmic domains of cellular and viral integral membrane proteins substitute for the cytoplasmic domain of the vesicular stomatitis virus glycoprotein in transport to the plasma membrane. Journal Of Cell Biology 1986, 102: 2147-2157. PMID: 3011809, PMCID: PMC2114239, DOI: 10.1083/jcb.102.6.2147.Peer-Reviewed Original ResearchMeSH KeywordsB-LymphocytesBiological Transport, ActiveCell LineCell MembraneCoronaviridaeCytoplasmGenes, ViralHemagglutinin Glycoproteins, Influenza VirusHemagglutinins, ViralHumansImmunoglobulin mu-ChainsMembrane GlycoproteinsMembrane ProteinsOligonucleotidesTransfectionVesicular stomatitis Indiana virusViral Envelope ProteinsViral ProteinsConceptsNormal cytoplasmic domainIntegral membrane proteinsCytoplasmic domainVesicular stomatitis virus glycoproteinG proteinsPlasma membraneHybrid proteinMembrane proteinsCellular integral membrane proteinsViral integral membrane proteinsB cell line WEHI-231Wild-type G proteinCell line WEHI-231Amino acid sequenceRate of transportVirus glycoproteinEukaryotic cellsTransmembrane domainChimeric cDNAHybrid geneWEHI-231Acid sequenceType G proteinsHeavy chain moleculesGolgi complex
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 requirementsDomainMutagenesisAcidReticulumAnchoringTransportIncorporation 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
1984
Conversion of a secretory protein into a transmembrane protein results in its transport to the golgi complex but not to the cell surface
Guan J, Rose J. Conversion of a secretory protein into a transmembrane protein results in its transport to the golgi complex but not to the cell surface. Cell 1984, 37: 779-787. PMID: 6589049, DOI: 10.1016/0092-8674(84)90413-6.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsMembrane proteinsSecretory proteinsFusion proteinCell surfaceVesicular stomatitis virus glycoproteinRat growth hormoneMembrane spanningCytoplasmic domainCDNA clonesCarboxy terminusHybrid geneEucaryotic cellsTransmembrane configurationGolgi apparatusProtein resultsProteinMicrosomal membranesVirus glycoproteinRapid secretionMembranePalmitic acidGolgiGenesTerminus
1982
Expression from cloned cDNA of cell-surface secreted forms of the glycoprotein of vesicular stomatitis virus in eucaryotic cells
Rose J, Bergmann J. Expression from cloned cDNA of cell-surface secreted forms of the glycoprotein of vesicular stomatitis virus in eucaryotic cells. Cell 1982, 30: 753-762. PMID: 6291783, DOI: 10.1016/0092-8674(82)90280-x.Peer-Reviewed Original ResearchConceptsG proteinsVesicular stomatitis virusCOS1 cellsCOOH terminusStomatitis virusMouse L cellsSV40 early promoterSV40 late promoterNormal G proteinsTransmembrane domainCDNA clonesEucaryotic cellsLate promoterEarly promoterPlasmid vectorCell typesAmino acidsProteinLipid bilayersL cellsPromoterTerminusG-DNADNACells
1980
Vesicular stomatitis virus glycoprotein is anchored in the viral membrane by a hydrophobic domain near the COOH terminus
Rose J, Welch W, Sefton B, Esch F, Ling N. Vesicular stomatitis virus glycoprotein is anchored in the viral membrane by a hydrophobic domain near the COOH terminus. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 3884-3888. PMID: 6253998, PMCID: PMC349731, DOI: 10.1073/pnas.77.7.3884.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceGenesGlycoproteinsMembrane ProteinsMembranesSolubilityVesicular stomatitis Indiana virusViral ProteinsConceptsAmino acid sequencePartial amino acid sequenceVesicular stomatitis virus glycoproteinAcid sequenceAmino acidsProtein geneCOOH terminusHydrophobic domainViral membraneVSV G proteinLipid bilayersTerminal portionTerminal amino acid sequenceM protein geneG protein geneG protein sequencesTerminal amino acidsVirus glycoproteinErythrocyte membrane proteinsMembrane proteinsDNA insertsLeader sequenceComplete sequenceProtein sequencesRNA genome