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
1991
Dissociation and reassociation of oligomeric viral glycoprotein subunits in the endoplasmic reticulum
Zagouras P, Ruusala A, Rose J. Dissociation and reassociation of oligomeric viral glycoprotein subunits in the endoplasmic reticulum. Journal Of Virology 1991, 65: 1976-1984. PMID: 1848313, PMCID: PMC240033, DOI: 10.1128/jvi.65.4.1976-1984.1991.Peer-Reviewed Original ResearchConceptsWild-type ratesEndoplasmic reticulumMutant subunitsG proteinsCell surfaceG protein trimersWild-type subunitsFormation of heterotrimersWild-type moleculeWild-type trimersMutant proteinsRetention signalProtein trimerHeterotrimerSubunitsGlycoprotein subunitsProteinReticulumGlycoprotein formTrimerTransport blockHomotrimersReassociation
1990
CD4 is retained in the endoplasmic reticulum by the human immunodeficiency virus type 1 glycoprotein precursor
Crise B, Buonocore L, Rose J. CD4 is retained in the endoplasmic reticulum by the human immunodeficiency virus type 1 glycoprotein precursor. Journal Of Virology 1990, 64: 5585-5593. PMID: 2214026, PMCID: PMC248611, DOI: 10.1128/jvi.64.11.5585-5593.1990.Peer-Reviewed Original ResearchHeavy chain binding protein recognizes incompletely disulfide-bonded forms of vesicular stomatitis virus G protein.
Machamer C, Doms R, Bole D, Helenius A, Rose J. Heavy chain binding protein recognizes incompletely disulfide-bonded forms of vesicular stomatitis virus G protein. Journal Of Biological Chemistry 1990, 265: 6879-6883. PMID: 2157712, DOI: 10.1016/s0021-9258(19)39231-2.Peer-Reviewed Original ResearchConceptsMutant G proteinsHeavy chain binding proteinG proteinsEndoplasmic reticulumWild-type G proteinBinding proteinVesicular stomatitis virus G proteinPlasma membrane glycoproteinsVirus G proteinAnti-BiP antibodiesDisulfide-bonded formIntrachain disulfide bondsVesicular stomatitis virusMembrane glycoproteinsDisulfide bondsBiPProteinStomatitis virusReticulumImmunoprecipitationGlycoprotein
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
Effects of altered cytoplasmic domains on transport of the vesicular stomatitis virus glycoprotein are transferable to other proteins.
Guan J, Ruusala A, Cao H, Rose J. Effects of altered cytoplasmic domains on transport of the vesicular stomatitis virus glycoprotein are transferable to other proteins. Molecular And Cellular Biology 1988, 8: 2869-2874. PMID: 2841589, PMCID: PMC363506, DOI: 10.1128/mcb.8.7.2869.Peer-Reviewed Original ResearchConceptsVesicular stomatitis virus glycoproteinEndoplasmic reticulumCytoplasmic domainVesicular stomatitis virus G proteinMembrane-anchored formVirus G proteinVirus glycoproteinMutant proteinsProtein foldingCytoplasmic sideSecretory proteinsCytoplasmic mutationsG proteinsProteinReticulumDifferent assaysMonomeric structureDetectable effectMutationsSedimentation coefficientRecent studiesEffects of Altered Cytoplasmic Domains on Transport of the Vesicular Stomatitis Virus Glycoprotein Are Transferable to Other Proteins
Guan J, Ruusala A, Cao H, Rose J. Effects of Altered Cytoplasmic Domains on Transport of the Vesicular Stomatitis Virus Glycoprotein Are Transferable to Other Proteins. Molecular And Cellular Biology 1988, 8: 2869-2874. DOI: 10.1128/mcb.8.7.2869-2874.1988.Peer-Reviewed Original ResearchVesicular stomatitis virus glycoproteinEndoplasmic reticulumCytoplasmic domainVesicular stomatitis virus G proteinHuman chorionic gonadotropinMembrane-anchored formVirus G proteinVirus glycoproteinMutant proteinsProtein foldingChorionic gonadotropinCytoplasmic mutationsCytoplasmic sideSecretory proteinsG proteinsProteinDifferent assaysReticulum
1985
Structural requirements of a membrane-spanning domain for protein anchoring and cell surface transport
Adams G, Rose J. Structural requirements of a membrane-spanning domain for protein anchoring and cell surface transport. Cell 1985, 41: 1007-1015. PMID: 3924407, DOI: 10.1016/s0092-8674(85)80081-7.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiological TransportCell LineCell MembraneEndoplasmic ReticulumFluorescent Antibody TechniqueGlycoside HydrolasesGolgi ApparatusMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseMembrane GlycoproteinsMembrane ProteinsMutationPalmitic AcidPalmitic AcidsPlasmidsViral Envelope ProteinsViral ProteinsConceptsMembrane-spanning domainsCell surface transportTransmembrane domainG proteinsAmino acidsVesicular stomatitis virus glycoproteinOligonucleotide-directed mutagenesisHydrophobic amino acidsMembrane anchoringProtein anchoringIntracellular membranesTransmembrane configurationEndoplasmic reticulumCell surfaceProteinVirus glycoproteinDNASurface transportStructural requirementsDomainMutagenesisAcidReticulumAnchoringTransport