1991
Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein
Whitt M, Buonocor L, Prehaud C, Rose J. Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein. Virology 1991, 185: 681-688. PMID: 1660200, DOI: 10.1016/0042-6822(91)90539-n.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, ViralBase SequenceCell LineCentrifugation, Density GradientCricetinaeFlow CytometryGenetic Complementation TestGlycoproteinsHumansHydrogen-Ion ConcentrationKineticsMacromolecular SubstancesMembrane FusionMembrane GlycoproteinsMiceMolecular Sequence DataPlasmidsRabies virusRecombinant Fusion ProteinsVesicular stomatitis Indiana virusViral Envelope ProteinsViral Fusion ProteinsConceptsVSV G proteinG protein trimersMembrane fusion activityVirus G proteinG proteinsRabies G proteinFusion activityHybrid proteinProtein trimerVesicular stomatitis virus G proteinVirus glycoproteinRabies virus glycoproteinCytoplasmic domainMembrane fusionExtracellular domainHeLa cellsRabies virus G proteinCell surfaceProteinVSV particlesSucrose gradientsVSV infectivityGlycoproteinSpike glycoproteinChemical crosslinking
1989
Oligomerization of glycolipid-anchored and soluble forms of the vesicular stomatitis virus glycoprotein
Crise B, Ruusala A, Zagouras P, Shaw A, Rose J. Oligomerization of glycolipid-anchored and soluble forms of the vesicular stomatitis virus glycoprotein. Journal Of Virology 1989, 63: 5328-5333. PMID: 2555557, PMCID: PMC251199, DOI: 10.1128/jvi.63.12.5328-5333.1989.Peer-Reviewed Original ResearchMeSH KeywordsAcetylglucosaminidaseAmino Acid SequenceBase SequenceCentrifugation, Density GradientCodonElectrophoresis, Polyacrylamide GelGlycolipidsHeLa CellsHumansKineticsMacromolecular SubstancesMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseMembrane GlycoproteinsMolecular Sequence DataRestriction MappingSolubilityVesicular stomatitis Indiana virusViral Envelope ProteinsConceptsG proteinsWild-type G proteinAmino acidsC-terminal amino acidsVesicular stomatitis virus glycoproteinMutant proteinsCytoplasmic domainAnchor sequenceExtracellular domainGolgi apparatusEndoplasmic reticulumCell surfaceTrimer formationProteinPhospholipase C.TransmembraneVirus glycoproteinSoluble formStructural informationSequenceGlycoproteinNormal transmembraneRate of transportGlycoprotein formThy-1.1
1988
Differential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein.
Doms R, Ruusala A, Machamer C, Helenius J, Helenius A, Rose J. Differential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein. Journal Of Cell Biology 1988, 107: 89-99. PMID: 2839523, PMCID: PMC2115181, DOI: 10.1083/jcb.107.1.89.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalAntibody SpecificityBiological TransportCell LineCentrifugation, Density GradientElectrophoresis, Polyacrylamide GelEndoplasmic ReticulumGlycosylationImmunoassayKineticsMacromolecular SubstancesMembrane GlycoproteinsMutationProtein ConformationTransfectionVesicular stomatitis Indiana virusViral Envelope ProteinsViral Matrix ProteinsConceptsG proteinsMutant proteinsCytoplasmic domainMutant G proteinsVesicular stomatitis virus G proteinIntegral membrane proteinsWild-type proteinTrimer formationVesicular stomatitis virus glycoproteinVirus G proteinAltered glycosylation patternConformation-specific antibodiesTail mutationsMembrane proteinsMin of synthesisOligomeric assembliesQuaternary structureMature formEndoplasmic reticulumInitial foldingGlycosylation patternsCell surfaceEctodomainProteinFolding