1991
Fatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions
Whitt M, Rose J. Fatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions. Virology 1991, 185: 875-878. PMID: 1660205, DOI: 10.1016/0042-6822(91)90563-q.Peer-Reviewed Original ResearchConceptsFatty acid acylationVSV G proteinMembrane fusion activityVesicular stomatitis virusG proteinsWild-type G proteinFusion activityWild-type proteinTemperature-sensitive mutantCytoplasmic domainTransient expressionPresence of palmitateVSV virionsIndiana serotypeHeLa cellsExpression of CSProteinStomatitis virusLife cycleSyncytium formationExpressionMutantsAcylationVirionsVirus
1988
Vesicular 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
1985
A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein
Gallione C, Rose J. A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein. Journal Of Virology 1985, 54: 374-382. PMID: 2985803, PMCID: PMC254807, DOI: 10.1128/jvi.54.2.374-382.1985.Peer-Reviewed Original ResearchConceptsCDNA clonesHydrophobic domainAmino acidsCell surface transportSingle amino acid substitutionVesicular stomatitis virus glycoproteinWild-type parent strainDNA sequence analysisPolar amino acidsHydrophobic amino acidsAmino acid changesAmino acid substitutionsProtein transportDNA sequencesNonpermissive temperatureVesicular stomatitis virusCOS cellsNonconservative substitutionsSequence analysisSpontaneous revertantsAcid substitutionsAcid changesSingle substitutionTransport defectStomatitis virus