1997
Construction of a Novel Virus That Targets HIV-1-Infected Cells and Controls HIV-1 Infection
Schnell M, Johnson J, Buonocore L, Rose J. Construction of a Novel Virus That Targets HIV-1-Infected Cells and Controls HIV-1 Infection. Cell 1997, 90: 849-857. PMID: 9298897, DOI: 10.1016/s0092-8674(00)80350-5.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCD4 AntigensCricetinaeGene DeletionGene Expression Regulation, ViralGlycoproteinsGTP-Binding ProteinsHIV InfectionsHIV-1HumansJurkat CellsKidneyMembrane GlycoproteinsMembrane ProteinsMicroscopy, ImmunoelectronMutagenesisReceptors, CXCR4Receptors, HIVRecombinant Fusion ProteinsVesicular stomatitis Indiana virusViral Envelope ProteinsVirus ReplicationConceptsHIV-1-infected cellsHIV-1HIV-1 receptors CD4HIV viral loadHIV-1 infectionInfectious HIV-1Recombinant vesicular stomatitis virusT cell linesHIV infectionViral loadVesicular stomatitis virusTherapeutic valueReceptor CD4Targeted virusInfectionVirusEnvelope proteinCell linesStomatitis virusNormal cellsNovel virusCellsGlycoprotein geneCD4CXCR4
1993
Folding and Assembly of Viral Membrane Proteins
Doms R, Lamb R, Rose J, Helenius A. Folding and Assembly of Viral Membrane Proteins. Virology 1993, 193: 545-562. PMID: 8460475, DOI: 10.1006/viro.1993.1164.Peer-Reviewed Original ResearchConceptsViral membrane proteinsQuality control mechanismsMolecular chaperonesGRP78-BiPMembrane proteinsER molecular chaperonesEffects of mutationsMisfolded proteinsProtein transportConformational maturationMisfolded moleculesProtein foldingEnergy-driven processChaperonesProtein structureMolecular mechanismsER environmentGRP78 synthesisExogenous proteinsNascent moleculesProteinDirect roleStructural variabilityControl mechanismsExperimental strategies
1992
Identification of palmitoylation sites on CD4, the human immunodeficiency virus receptor.
Crise B, Rose J. Identification of palmitoylation sites on CD4, the human immunodeficiency virus receptor. Journal Of Biological Chemistry 1992, 267: 13593-13597. PMID: 1618861, DOI: 10.1016/s0021-9258(18)42253-3.Peer-Reviewed Original ResearchConceptsCytoplasmic domainBinding of p56lckHuman immunodeficiency virus receptorCell surface glycoprotein CD4Palmitoylation sitesCysteine residuesThioester linkageGlycoprotein CD4HeLa cellsCell surfaceVirus receptorProteinFatty acidsMutationsCysteineExpression of CD4Cys397Palmitic acidCys394P56lckTransmembraneCD4AcidPalmitateDomain
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