1996
Characterization of a Nuclear Protein Conferring Brefeldin A Resistance in Schizosaccharomyces pombe (∗)
Turi T, Mueller U, Sazer S, Rose J. Characterization of a Nuclear Protein Conferring Brefeldin A Resistance in Schizosaccharomyces pombe (∗). Journal Of Biological Chemistry 1996, 271: 9166-9171. PMID: 8621569, DOI: 10.1074/jbc.271.15.9166.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntifungal AgentsBase SequenceBrefeldin ACell CompartmentationConsensus SequenceCyclopentanesDNA PrimersDrug Resistance, MicrobialFungal ProteinsGenes, FungalGolgi ApparatusGTP-Binding ProteinsMolecular Sequence DataNuclear ProteinsPhosphoproteinsRan GTP-Binding ProteinRestriction MappingSchizosaccharomycesSequence AlignmentSequence Homology, Amino AcidConceptsNuclear pore complexWild type SchizosaccharomycesPore complexS. pombeSchizosaccharomyces pombeProtein RanBP1Essential proteinsGolgi complexEndoplasmic reticulumProtein secretionPeptide motifsMultiple copiesNovel mechanismGenesProteinPombeA ResistanceBrefeldinDrug resistanceSchizosaccharomycesYrb1RanBP1HomologyComplexesReticulum
1995
Characterization of a Novel Schizosaccharomyces pombe Multidrug Resistance Transporter Conferring Brefeldin A Resistance
Turi T, Rose J. Characterization of a Novel Schizosaccharomyces pombe Multidrug Resistance Transporter Conferring Brefeldin A Resistance. Biochemical And Biophysical Research Communications 1995, 213: 410-418. PMID: 7646493, DOI: 10.1006/bbrc.1995.2147.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SequenceATP-Binding Cassette TransportersBase SequenceBinding SitesBrefeldin ACloning, MolecularCyclopentanesDNA, FungalDrug Resistance, MultipleFungal ProteinsMolecular Sequence DataOpen Reading FramesPancreatitis-Associated ProteinsRestriction MappingSchizosaccharomycesSchizosaccharomyces pombe ProteinsSequence AnalysisSequence HomologyConceptsTranscription factorsHbA2 expressionWild-type S. pombeS. pombe proteinPap1 transcription factorSignificant sequence similarityWild type SchizosaccharomycesMultiple transcription factorsPombe proteinsCRM1 genesS. pombeSequence similarityMammalian cellsTransport proteinsDifferent genesMutant strainBrefeldin AGolgi complexEndoplasmic reticulumProtein secretionGenesMultiple copiesSchizosaccharomycesCRM1A Resistance
1994
Brefeldin 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
1992
Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
Brown D, Rose J. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 1992, 68: 533-544. PMID: 1531449, DOI: 10.1016/0092-8674(92)90189-j.Peer-Reviewed Original ResearchConceptsBasolateral marker proteinsCertain membrane proteinsApical cell surfaceDetergent-insoluble formGlycosylphosphatidyl inositol (GPI) anchorMembrane subdomainsMembrane proteinsIntracellular associationGolgi complexMicrodomains formGolgi apparatusInositol anchorMarker proteinsCell surfaceProteinApical surfaceEpithelial cellsGPIGlycosphingolipidsComplexesVesiclesLysatesGlycolipidsSortingMembrane
1986
Cytoplasmic domains of cellular and viral integral membrane proteins substitute for the cytoplasmic domain of the vesicular stomatitis virus glycoprotein in transport to the plasma membrane.
Puddington L, Machamer C, Rose J. Cytoplasmic domains of cellular and viral integral membrane proteins substitute for the cytoplasmic domain of the vesicular stomatitis virus glycoprotein in transport to the plasma membrane. Journal Of Cell Biology 1986, 102: 2147-2157. PMID: 3011809, PMCID: PMC2114239, DOI: 10.1083/jcb.102.6.2147.Peer-Reviewed Original ResearchMeSH KeywordsB-LymphocytesBiological Transport, ActiveCell LineCell MembraneCoronaviridaeCytoplasmGenes, ViralHemagglutinin Glycoproteins, Influenza VirusHemagglutinins, ViralHumansImmunoglobulin mu-ChainsMembrane GlycoproteinsMembrane ProteinsOligonucleotidesTransfectionVesicular stomatitis Indiana virusViral Envelope ProteinsViral ProteinsConceptsNormal cytoplasmic domainIntegral membrane proteinsCytoplasmic domainVesicular stomatitis virus glycoproteinG proteinsPlasma membraneHybrid proteinMembrane proteinsCellular integral membrane proteinsViral integral membrane proteinsB cell line WEHI-231Wild-type G proteinCell line WEHI-231Amino acid sequenceRate of transportVirus glycoproteinEukaryotic cellsTransmembrane domainChimeric cDNAHybrid geneWEHI-231Acid sequenceType G proteinsHeavy chain moleculesGolgi complex