1993
Dynamic equilibrium between vesicular stomatitis virus glycoprotein monomers and trimers in the Golgi and at the cell surface
Zagouras P, Rose J. Dynamic equilibrium between vesicular stomatitis virus glycoprotein monomers and trimers in the Golgi and at the cell surface. Journal Of Virology 1993, 67: 7533-7538. PMID: 8230472, PMCID: PMC238219, DOI: 10.1128/jvi.67.12.7533-7538.1993.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, ViralAntibody SpecificityBiological TransportBrefeldin ACell CompartmentationCell MembraneCells, CulturedCricetinaeCyclopentanesGolgi ApparatusHexosaminidasesMembrane GlycoproteinsMutationPostural BalanceProtein ConformationProtein Processing, Post-TranslationalVesicular stomatitis Indiana virusViral Envelope ProteinsConceptsEndoplasmic reticulumHeterotrimer formationG proteinsMutant G proteinsG protein trimersVesicular stomatitis virus glycoproteinG protein subunitsVSV G proteinProtein moleculesG protein moleculesWild-type trimersMutant proteinsCytoplasmic domainCellular compartmentsCoexpression experimentsGlycoprotein monomersLonger chase periodsPlasma membraneProtein subunitsMu proteinProtein trimerForms trimersCell surfaceMonomeric subunitsProtein
1988
Cell-surface expression of a membrane-anchored form of the human chorionic gonadotropin alpha subunit.
Guan J, Cao H, Rose J. Cell-surface expression of a membrane-anchored form of the human chorionic gonadotropin alpha subunit. Journal Of Biological Chemistry 1988, 263: 5306-5313. PMID: 2451667, DOI: 10.1016/s0021-9258(18)60716-1.Peer-Reviewed Original ResearchMeSH KeywordsBiological Transport, ActiveCloning, MolecularDNAElectrophoresis, Polyacrylamide GelFluorescent Antibody TechniqueGene Expression RegulationGlycoprotein Hormones, alpha SubunitGlycoside HydrolasesGlycosylationHexosaminidasesHumansKineticsMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseMembranesOligosaccharidesPituitary Hormones, AnteriorPlasmidsTunicamycinVesicular stomatitis Indiana virusViral Fusion ProteinsConceptsVesicular stomatitis virus glycoproteinAsparagine-linked glycansAnimal cellsAlpha subunitNovel cell surface proteinCarboxyl-terminal amino acidsGlycosylation inhibitor tunicamycinAbsence of glycosylationMembrane-anchored formCell surface proteinsSecond glycosylation siteHuman chorionic gonadotropin (hCG) alpha-subunitVirus glycoproteinEntire precursorCell surface expressionCytoplasmic domainGonadotropin alpha subunitHybrid proteinPlasma membraneGlycosylation sitesSecretory proteinsCellular membranesConformational changesCell surfaceAmino acidsVesicular 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