1994
Novel infectious particles generated by expression of the vesicular stomatitis virus glycoprotein from a self-replicating RNA
Rolls M, Webster P, Balba N, Rose J. Novel infectious particles generated by expression of the vesicular stomatitis virus glycoprotein from a self-replicating RNA. Cell 1994, 79: 497-506. PMID: 7954815, DOI: 10.1016/0092-8674(94)90258-5.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta-GalactosidaseCells, CulturedGenetic VectorsHumansMembrane GlycoproteinsModels, GeneticNeutralization TestsParticle SizeRepliconRNA VirusesRNA-Dependent RNA PolymeraseSemliki forest virusSerial PassageSpecies SpecificityTransfectionViral Envelope ProteinsViral Fusion ProteinsVirus ReplicationConceptsVesicular stomatitis virus glycoproteinVSV G proteinSemliki Forest virusStructural proteinsMembrane-enveloped vesiclesRNA repliconsSFV structural proteinsInfectious particlesViral structural proteinsTissue culture cellsVirus glycoproteinAnimal cellsSelf-replicating RNARNA replicaseG proteinsCulture cellsProteinRepliconVirus-like particlesVesiclesVSV serumCellsGlycoproteinExpressionReplicaseBrefeldin A sensitivity and resistance in Schizosaccharomyces pombe. Isolation of multiple genes conferring resistance.
Turi T, Webster P, Rose J. Brefeldin A sensitivity and resistance in Schizosaccharomyces pombe. Isolation of multiple genes conferring resistance. Journal Of Biological Chemistry 1994, 269: 24229-24236. PMID: 7929079, DOI: 10.1016/s0021-9258(19)51072-9.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntifungal AgentsBrefeldin ACyclopentanesDrug Resistance, MicrobialFungal ProteinsGolgi ApparatusKaryopherinsMolecular Sequence DataMutationPancreatitis-Associated ProteinsPhenotypePlasmidsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiaeSchizosaccharomycesSequence Homology, Amino AcidConceptsBFA resistanceEffects of BFABrefeldin AGolgi complexMammalian cellsTranscription factor Pap1Fission yeast SchizosaccharomycesFungal metabolite brefeldin ASeparate linkage groupsWild-type cellsChromatin structureYeast SchizosaccharomycesSchizosaccharomyces pombeAP1 proteinLinkage groupsGolgi morphologyAnimal cellsMultiple genesDifferent genesGenetic analysisEndoplasmic reticulumProtein secretionGenesType cellsMutants
1989
Carboxy-terminal SEKDEL sequences retard but do not retain two secretory proteins in the endoplasmic reticulum.
Zagouras P, Rose J. Carboxy-terminal SEKDEL sequences retard but do not retain two secretory proteins in the endoplasmic reticulum. Journal Of Cell Biology 1989, 109: 2633-2640. PMID: 2592401, PMCID: PMC2115906, DOI: 10.1083/jcb.109.6.2633.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumSEKDEL sequenceSecretory proteinsSequence Ser-GluAmino acidsMonkey COS cellsOligonucleotide-directed mutagenesisLast amino acidFirst amino acidProtein exitIndirect immunofluorescence microscopyAnimal cellsCOS cellsCOOH terminusAlpha subunitProtein structureGolgi apparatusLys-AspImmunofluorescence microscopyOligosaccharide processingProteinReticulumSEKDELSer-GluSpecific interactions
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 acids
1985
Incorporation of a Charged Amino Acid into the Membrane-Spanning Domain Blocks Cell Surface Transport But Not Membrane Anchoring of a Viral Glycoprotein
Adams G, Rose J. Incorporation of a Charged Amino Acid into the Membrane-Spanning Domain Blocks Cell Surface Transport But Not Membrane Anchoring of a Viral Glycoprotein. Molecular And Cellular Biology 1985, 5: 1442-1448. DOI: 10.1128/mcb.5.6.1442-1448.1985.Peer-Reviewed Original ResearchMembrane anchoringG proteinsAmino acidsCell surfaceIsoleucine residueMembrane-spanning domainsCell surface transportVesicular stomatitis virus glycoproteinOligonucleotide-directed mutagenesisAmino acid sequenceUncharged amino acidsDetectable protein levelsHydrophobic amino acidsAnimal cellsCDNA clonesIntracellular membranesAcid sequencePunctate patternGolgi regionProteinContinuous stretchVesicular patternProtein levelsViral glycoproteinsVirus glycoproteinIncorporation of a charged amino acid into the membrane-spanning domain blocks cell surface transport but not membrane anchoring of a viral glycoprotein.
Adams G, Rose J. Incorporation of a charged amino acid into the membrane-spanning domain blocks cell surface transport but not membrane anchoring of a viral glycoprotein. Molecular And Cellular Biology 1985, 5: 1442-1448. PMID: 2993864, PMCID: PMC366875, DOI: 10.1128/mcb.5.6.1442.Peer-Reviewed Original ResearchConceptsMembrane anchoringG proteinsAmino acidsCell surfaceIsoleucine residueMembrane-spanning domainsCell surface transportVesicular stomatitis virus glycoproteinOligonucleotide-directed mutagenesisAmino acid sequenceUncharged amino acidsDetectable protein levelsHydrophobic amino acidsAnimal cellsCDNA clonesIntracellular membranesAcid sequencePunctate patternGolgi regionProteinContinuous stretchVesicular patternProtein levelsViral glycoproteinsVirus glycoprotein
1976
5'-terminal structure of poliovirus polyribosomal RNA is pUp.
Hewlett M, Rose J, Baltimore D. 5'-terminal structure of poliovirus polyribosomal RNA is pUp. Proceedings Of The National Academy Of Sciences Of The United States Of America 1976, 73: 327-330. PMID: 174102, PMCID: PMC335900, DOI: 10.1073/pnas.73.2.327.Peer-Reviewed Original Research