1998
Requirement 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
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
1994
Interactions 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
Cell fusion by the envelope glycoproteins of persistent measles viruses which caused lethal human brain disease
Cattaneo R, Rose J. Cell fusion by the envelope glycoproteins of persistent measles viruses which caused lethal human brain disease. Journal Of Virology 1993, 67: 1493-1502. PMID: 8437226, PMCID: PMC237519, DOI: 10.1128/jvi.67.3.1493-1502.1993.Peer-Reviewed Original ResearchMeSH KeywordsAutopsyBacteriophage T7Biological TransportBrain DiseasesCell FusionCell LineCloning, MolecularDNA, ViralGlycosylationHeLa CellsHemagglutinins, ViralHumansMeaslesMeasles virusOligosaccharidesPromoter Regions, GeneticProtein ConformationProtein Processing, Post-TranslationalRecombinant ProteinsRNA, ViralViral Envelope ProteinsViral Fusion ProteinsViral InterferenceViral Matrix ProteinsVirulenceConceptsIntegral membrane proteinsH proteinCell fusionMembrane proteinsIntracellular domainViral buddingM proteinHS-protein interactionsF protein functionProtein interactionsMV genesIntracellular transportFusion proteinOligosaccharide modificationViral envelope proteinsMatrix proteinsHuman brain diseasesProteinMeasles virusReduced expressionEnvelope proteinPersistent measles virusBuddingSyncytium formationDisease developmentMembrane 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
1987
Rhabdovirus Genomes and Their Products
Rose J, Schubert M. Rhabdovirus Genomes and Their Products. The Viruses 1987, 129-166. DOI: 10.1007/978-1-4684-7032-1_4.Peer-Reviewed Original ResearchGenomic RNANucleocapsid coreRNA-dependent RNA polymeraseVirus particlesMembrane-enveloped virusesSingle glycoprotein speciesRhabdovirus genomesRNA polymeraseRNA genomeMembrane envelopeMatrix proteinsMessenger RNAGlycoprotein speciesRhabdovirusRNAGenomeProteinMembraneInvertebratesVertebratesBacilliformPolymeraseSpeciesPlantsNegative sense