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
1996
Membrane 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
1995
Characterization of a Novel Schizosaccharomyces pombe Multidrug Resistance Transporter Conferring Brefeldin A Resistance
Turi T, Rose J. Characterization of a Novel Schizosaccharomyces pombe Multidrug Resistance Transporter Conferring Brefeldin A Resistance. Biochemical And Biophysical Research Communications 1995, 213: 410-418. PMID: 7646493, DOI: 10.1006/bbrc.1995.2147.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SequenceATP-Binding Cassette TransportersBase SequenceBinding SitesBrefeldin ACloning, MolecularCyclopentanesDNA, FungalDrug Resistance, MultipleFungal ProteinsMolecular Sequence DataOpen Reading FramesPancreatitis-Associated ProteinsRestriction MappingSchizosaccharomycesSchizosaccharomyces pombe ProteinsSequence AnalysisSequence HomologyConceptsTranscription factorsHbA2 expressionWild-type S. pombeS. pombe proteinPap1 transcription factorSignificant sequence similarityWild type SchizosaccharomycesMultiple transcription factorsPombe proteinsCRM1 genesS. pombeSequence similarityMammalian cellsTransport proteinsDifferent genesMutant strainBrefeldin AGolgi complexEndoplasmic reticulumProtein secretionGenesMultiple copiesSchizosaccharomycesCRM1A Resistance
1988
Influence of new glycosylation sites on expression of the vesicular stomatitis virus G protein at the plasma membrane.
Machamer C, Rose J. Influence of new glycosylation sites on expression of the vesicular stomatitis virus G protein at the plasma membrane. Journal Of Biological Chemistry 1988, 263: 5948-5954. PMID: 2833523, DOI: 10.1016/s0021-9258(18)60658-1.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceBinding SitesBiological TransportCell LineCell MembraneCloning, MolecularDNA, RecombinantFluorescent Antibody TechniqueGlycosylationImmunosorbent TechniquesIodine RadioisotopesLactoperoxidaseMembrane GlycoproteinsMolecular Sequence DataMutationOligosaccharidesTransfectionTunicamycinVesicular stomatitis Indiana virusViral Envelope ProteinsViral Matrix ProteinsConceptsVesicular stomatitis virus G proteinVirus G proteinG proteinsConsensus sitesIntracellular transportWild-type G proteinWild-type proteinOligonucleotide-directed mutagenesisNew consensus sitePlasma membrane glycoproteinsMutant proteinsNew glycosylation siteNew sitesAsparagine-linked oligosaccharidesPlasma membraneGlycosylation sitesMembrane glycoproteinsInhibition of transportProteinPolypeptide backboneNormal sitesIndirect roleOligosaccharidesExpressionSitesVesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding.
Machamer C, Rose J. Vesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding. Journal Of Biological Chemistry 1988, 263: 5955-5960. PMID: 2833524, DOI: 10.1016/s0021-9258(18)60659-3.Peer-Reviewed Original ResearchBinding SitesBiological TransportCell LineCell MembraneDisulfidesDNA, RecombinantEndoplasmic ReticulumFluorescent Antibody TechniqueGlycosylationHexosaminidasesImmunosorbent TechniquesIodine RadioisotopesLactoperoxidaseMembrane GlycoproteinsMutationOligosaccharidesProtein ConformationStructure-Activity RelationshipTemperatureTransfectionVesicular stomatitis Indiana virusViral Envelope ProteinsViral Matrix Proteins