1999
Recombinant Vesicular Stomatitis Virus Expressing Respiratory Syncytial Virus (RSV) Glycoproteins: RSV Fusion Protein Can Mediate Infection and Cell Fusion
Kahn J, Schnell M, Buonocore L, Rose J. Recombinant Vesicular Stomatitis Virus Expressing Respiratory Syncytial Virus (RSV) Glycoproteins: RSV Fusion Protein Can Mediate Infection and Cell Fusion. Virology 1999, 254: 81-91. PMID: 9927576, DOI: 10.1006/viro.1998.9535.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCell LineCricetinaeCytoplasmGene ExpressionGenetic VectorsGlycoproteinsHN ProteinHumansMembrane FusionMolecular Sequence DataRecombinant Fusion ProteinsRespiratory Syncytial Virus, HumanTumor Cells, CulturedVesicular stomatitis Indiana virusViral Envelope ProteinsViral Fusion ProteinsViral ProteinsVirionConceptsRecombinant vesicular stomatitis virusVesicular stomatitis virusRSV fusion proteinRSV F glycoproteinRSV vaccineF recombinantsRSV glycoproteinsRSV proteinsEnvelope glycoproteinVirus attachmentFusion (F) envelope glycoproteinsF glycoproteinG glycoproteinStomatitis virusLarge syncytiaGlycoproteinPH-independent pathwayCell surfaceCell fusionCytoplasmic tail sequencesVSV G.Endosomal pHFusion activityVaccineFusion protein
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 proteinTailHybridsRequirement for a non‐specific glycoprotein cytoplasmic domain sequence to drive efficient budding of vesicular stomatitis virus
Schnell M, Buonocore L, Boritz E, Ghosh H, Chernish R, Rose J. Requirement for a non‐specific glycoprotein cytoplasmic domain sequence to drive efficient budding of vesicular stomatitis virus. The EMBO Journal 1998, 17: 1289-1296. PMID: 9482726, PMCID: PMC1170477, DOI: 10.1093/emboj/17.5.1289.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCD4 AntigensCell LineCell MembraneCricetinaeCytopathogenic Effect, ViralCytoplasmHumansMembrane GlycoproteinsMolecular Sequence DataMutationRecombinant Fusion ProteinsSequence DeletionSerial PassageVesicular stomatitis Indiana virusViral Envelope ProteinsViral ProteinsVirionConceptsCytoplasmic domainEfficient buddingAmino acidsCytoplasmic domain deletion mutantEfficient virus buddingShort cytoplasmic domainCytoplasmic domain sequencesDomain deletion mutantVesicular stomatitis virus glycoproteinChimeric G proteinsTransmembrane domainDeletion mutantsInternal viral componentsVirus buddingGlycoprotein arrayVesicular stomatitis virusDomain sequencesViral buddingVirion morphologyG proteinsMatrix proteinsVSV GHuman CD4 proteinForeign sequencesBudding
1992
Fc receptor endocytosis is controlled by a cytoplasmic domain determinant that actively prevents coated pit localization.
Miettinen H, Matter K, Hunziker W, Rose J, Mellman I. Fc receptor endocytosis is controlled by a cytoplasmic domain determinant that actively prevents coated pit localization. Journal Of Cell Biology 1992, 116: 875-888. PMID: 1734021, PMCID: PMC2289334, DOI: 10.1083/jcb.116.4.875.Peer-Reviewed Original Research
1990
Short related sequences in the cytoplasmic domains of CD4 and CD8 mediate binding to the amino-terminal domain of the p56lck tyrosine protein kinase.
Shaw A, Chalupny J, Whitney J, Hammond C, Amrein K, Kavathas P, Sefton B, Rose J. Short related sequences in the cytoplasmic domains of CD4 and CD8 mediate binding to the amino-terminal domain of the p56lck tyrosine protein kinase. Molecular And Cellular Biology 1990, 10: 1853-1862. PMID: 2109184, PMCID: PMC360530, DOI: 10.1128/mcb.10.5.1853.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntigens, Differentiation, T-LymphocyteBase SequenceCD4 AntigensCD8 AntigensCysteineCytoplasmDNA Mutational AnalysisHumansIn Vitro TechniquesLymphocyte Specific Protein Tyrosine Kinase p56(lck)Molecular Sequence DataProtein BindingProtein-Tyrosine KinasesSignal TransductionStructure-Activity RelationshipConceptsAmino-terminal domainTyrosine protein kinaseCytoplasmic domainProtein kinaseBinding of p56lckCommon sequence motifsRelated amino acid sequencesAmino acid sequenceDisulfide bond formationCD8 alphaAmino acid residuesSequence motifsHybrid proteinCysteine residuesAcid sequenceUnrelated proteinsAlpha proteinRelated sequencesAcid residuesCD4 sequencesP56lckGlycoprotein CD4HeLa cellsProteinKinase
1989
The 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 glycoproteinP56lckKinaseResiduesGlycoprotein 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 assemblyFc 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
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 ResearchEffects of altered cytoplasmic domains on transport of the vesicular stomatitis virus glycoprotein are transferable to other proteins.
Guan J, Ruusala A, Cao H, Rose J. Effects of altered cytoplasmic domains on transport of the vesicular stomatitis virus glycoprotein are transferable to other proteins. Molecular And Cellular Biology 1988, 8: 2869-2874. PMID: 2841589, PMCID: PMC363506, DOI: 10.1128/mcb.8.7.2869.Peer-Reviewed Original ResearchConceptsVesicular stomatitis virus glycoproteinEndoplasmic reticulumCytoplasmic domainVesicular stomatitis virus G proteinMembrane-anchored formVirus G proteinVirus glycoproteinMutant proteinsProtein foldingCytoplasmic sideSecretory proteinsCytoplasmic mutationsG proteinsProteinReticulumDifferent assaysMonomeric structureDetectable effectMutationsSedimentation coefficientRecent studies
1987
Replacement 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
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