1996
Membrane Association of Influenza Virus Matrix Protein Does Not Require Specific Hydrophobic Domains or the Viral Glycoproteins
KRETZSCHMAR E, BUI M, ROSE J. Membrane Association of Influenza Virus Matrix Protein Does Not Require Specific Hydrophobic Domains or the Viral Glycoproteins. Virology 1996, 220: 37-45. PMID: 8659126, DOI: 10.1006/viro.1996.0283.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceBinding SitesCell LineCell MembraneChick EmbryoDogsHeLa CellsHemagglutinin Glycoproteins, Influenza VirusHemagglutinins, ViralHumansInfluenza A virusMolecular Sequence DataMutagenesis, Site-DirectedNeuraminidaseOligodeoxyribonucleotidesRecombinant ProteinsViral Matrix ProteinsConceptsMembrane associationSpecific hydrophobic domainsM1 proteinMatrix proteinsHydrophobic domainInfluenza virus matrix proteinVirus matrix proteinInteraction of M1Viral glycoproteinsMajor structural componentRibonucleocapsid coreCytoplasmic tailIntegral proteinsMembrane proteinsMembrane bindingSubcellular fractionationMembrane envelopeCellular membranesHeLa cellsViral proteinsHydrophobic regionProteinIsolated membranesMembraneInfluenza proteins
1994
Signals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction.
Rodgers W, Crise B, Rose J. Signals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction. Molecular And Cellular Biology 1994, 14: 5384-5391. PMID: 8035816, PMCID: PMC359057, DOI: 10.1128/mcb.14.8.5384.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCell CompartmentationDNA PrimersGlycolipidsGlycosylphosphatidylinositolsHeLa CellsHumansLymphocyte Specific Protein Tyrosine Kinase p56(lck)Molecular Sequence DataMutagenesis, Site-DirectedMyristatesPalmitatesProteinsProtein-Tyrosine KinasesStructure-Activity RelationshipConceptsProtein tyrosine kinasesCertain protein tyrosine kinasesTyrosine kinaseMembrane fractionSrc family protein tyrosine kinasesFamily protein tyrosine kinasesAnalysis of mutantsN-terminal myristateCy-3Glycolipid-enriched membranesAssociation of p56lckCys-5Membrane domainsMembrane proteinsAnchored proteinsGPI anchorGlycosyl phosphatidylinositolKinaseP56lckCell typesHeLa cellsMDCK cellsGPIProteinGentle disruptionSignals Determining Protein Tyrosine Kinase and Glycosyl-Phosphatidylinositol-Anchored Protein Targeting to a Glycolipid-Enriched Membrane Fraction
Rodgers W, Crise B, Rose J. Signals Determining Protein Tyrosine Kinase and Glycosyl-Phosphatidylinositol-Anchored Protein Targeting to a Glycolipid-Enriched Membrane Fraction. Molecular And Cellular Biology 1994, 14: 5384-5391. DOI: 10.1128/mcb.14.8.5384-5391.1994.Peer-Reviewed Original ResearchProtein tyrosine kinasesCertain protein tyrosine kinasesP56 lckTyrosine kinaseMembrane fractionGlycosyl phosphatidylinositolSrc family protein tyrosine kinasesFamily protein tyrosine kinasesAnalysis of mutantsN-terminal myristateCy-3Glycolipid-enriched membranesAssociation of p56lckCys-5Membrane domainsMembrane proteinsAnchored proteinsGPI anchorKinaseCell typesHeLa cellsLckMDCK cellsGPIProteinSignals Determining Protein Tyrosine Kinase and Glycosyl-Phosphatidylinositol-Anchored Protein Targeting to a Glycolipid-Enriched Membrane Fraction
Rodgers W, Crise B, Rose J. Signals Determining Protein Tyrosine Kinase and Glycosyl-Phosphatidylinositol-Anchored Protein Targeting to a Glycolipid-Enriched Membrane Fraction. Molecular And Cellular Biology 1994, 14: 5384-5391. DOI: 10.1128/mcb.14.8.5384-5391.1994.Peer-Reviewed Original ResearchGPI-anchored proteinsProtein tyrosine kinasesGlycolipid-enriched membraneP56 LckTyrosine kinaseMembrane fractionCys-3Glycosyl-phosphatidylinositol (GPI)-anchored membrane proteinsGlycolipid-enriched membrane fractionCys-5Src family protein tyrosine kinasesTriton X-100-insolubleAnalysis of mutantsGlycosyl-phosphatidylinositol-anchored proteinsN-terminal myristateAssociation of p56lckGPI anchorTransmembrane signalingMembrane proteinsMembrane domainsHeLa cellsKinaseLckProteinTarget signalMutations in the membrane-spanning domain of the human immunodeficiency virus envelope glycoprotein that affect fusion activity
Owens R, Burke C, Rose J. Mutations in the membrane-spanning domain of the human immunodeficiency virus envelope glycoprotein that affect fusion activity. Journal Of Virology 1994, 68: 570-574. PMID: 8254774, PMCID: PMC236324, DOI: 10.1128/jvi.68.1.570-574.1994.Peer-Reviewed Original ResearchConceptsTransmembrane domainFusion activityVesicular stomatitis virus G proteinMembrane-spanning domainsCell surfaceSpecific amino acid sequencesAmino acid sequenceMembrane fusion activityAmino acid residuesMembrane fusion processCytoplasmic tail domainVirus G proteinCytoplasmic domainMutagenic analysisAcid sequenceChimeric proteinBasic residuesProtein ectodomainAcid residuesG proteinsHeLa cellsVirus envelope glycoproteinLipid bilayersProteinGp41 transmembrane
1993
Membrane association of functional vesicular stomatitis virus matrix protein in vivo
Chong L, Rose J. Membrane association of functional vesicular stomatitis virus matrix protein in vivo. Journal Of Virology 1993, 67: 407-414. PMID: 8380086, PMCID: PMC237377, DOI: 10.1128/jvi.67.1.407-414.1993.Peer-Reviewed Original ResearchMeSH KeywordsCell MembraneCytosolHeLa CellsHumansMacromolecular SubstancesMembrane ProteinsModels, BiologicalOctoxynolPolyethylene GlycolsProtein ConformationRecombinant ProteinsRibonucleoproteinsSolubilitySubcellular FractionsVesicular stomatitis Indiana virusViral Core ProteinsViral Matrix ProteinsConceptsVesicular stomatitis virusRNP coresMatrix proteinsVesicular stomatitis virus matrix proteinM proteinVirus matrix proteinSoluble M proteinMajor structural componentRibonucleocapsid coreMembrane associationMembrane proteinsM protein moleculeVirus buddingSubcellular fractionationCellular membranesMembrane envelopeHeLa cellsVSV proteinsViral proteinsDetergent Triton XProteinProtein moleculesConformational differencesStomatitis virusMembrane
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 acidCys394P56lckTransmembraneCD4AcidPalmitateDomainHuman immunodeficiency virus type 1 glycoprotein precursor retains a CD4-p56lck complex in the endoplasmic reticulum
Crise B, Rose J. Human immunodeficiency virus type 1 glycoprotein precursor retains a CD4-p56lck complex in the endoplasmic reticulum. Journal Of Virology 1992, 66: 2296-2301. PMID: 1548763, PMCID: PMC289024, DOI: 10.1128/jvi.66.4.2296-2301.1992.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumHuman immunodeficiency virusTyrosine kinaseHIV infectionCD4-p56lck complexTransient expression systemGlycoprotein precursorCytoplasmic tyrosine kinaseConfocal immunofluorescence microscopyExpression of CD4HIV-1 gp160Cell surface glycoproteinExpression of gp160Cytoplasmic facePlasma membraneT cell activationExpression systemHeLa cellsImmunofluorescence microscopyCell surfaceImmunodeficiency virusT lymphocytesT cellsLymphocyte killingCD4
1991
Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein
Whitt M, Buonocor L, Prehaud C, Rose J. Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein. Virology 1991, 185: 681-688. PMID: 1660200, DOI: 10.1016/0042-6822(91)90539-n.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, ViralBase SequenceCell LineCentrifugation, Density GradientCricetinaeFlow CytometryGenetic Complementation TestGlycoproteinsHumansHydrogen-Ion ConcentrationKineticsMacromolecular SubstancesMembrane FusionMembrane GlycoproteinsMiceMolecular Sequence DataPlasmidsRabies virusRecombinant Fusion ProteinsVesicular stomatitis Indiana virusViral Envelope ProteinsViral Fusion ProteinsConceptsVSV G proteinG protein trimersMembrane fusion activityVirus G proteinG proteinsRabies G proteinFusion activityHybrid proteinProtein trimerVesicular stomatitis virus G proteinVirus glycoproteinRabies virus glycoproteinCytoplasmic domainMembrane fusionExtracellular domainHeLa cellsRabies virus G proteinCell surfaceProteinVSV particlesSucrose gradientsVSV infectivityGlycoproteinSpike glycoproteinChemical crosslinkingFatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions
Whitt M, Rose J. Fatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions. Virology 1991, 185: 875-878. PMID: 1660205, DOI: 10.1016/0042-6822(91)90563-q.Peer-Reviewed Original ResearchConceptsFatty acid acylationVSV G proteinMembrane fusion activityVesicular stomatitis virusG proteinsWild-type G proteinFusion activityWild-type proteinTemperature-sensitive mutantCytoplasmic domainTransient expressionPresence of palmitateVSV virionsIndiana serotypeHeLa cellsExpression of CSProteinStomatitis virusLife cycleSyncytium formationExpressionMutantsAcylationVirionsVirus
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 ResearchShort related sequences in the cytoplasmic domains of CD4 and CD8 mediate binding to the amino-terminal domain of the p56lck tyrosine protein kinase.
Shaw A, Chalupny J, Whitney J, Hammond C, Amrein K, Kavathas P, Sefton B, Rose J. Short related sequences in the cytoplasmic domains of CD4 and CD8 mediate binding to the amino-terminal domain of the p56lck tyrosine protein kinase. Molecular And Cellular Biology 1990, 10: 1853-1862. PMID: 2109184, PMCID: PMC360530, DOI: 10.1128/mcb.10.5.1853.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntigens, Differentiation, T-LymphocyteBase SequenceCD4 AntigensCD8 AntigensCysteineCytoplasmDNA Mutational AnalysisHumansIn Vitro TechniquesLymphocyte Specific Protein Tyrosine Kinase p56(lck)Molecular Sequence DataProtein BindingProtein-Tyrosine KinasesSignal TransductionStructure-Activity RelationshipConceptsAmino-terminal domainTyrosine protein kinaseCytoplasmic domainProtein kinaseBinding of p56lckCommon sequence motifsRelated amino acid sequencesAmino acid sequenceDisulfide bond formationCD8 alphaAmino acid residuesSequence motifsHybrid proteinCysteine residuesAcid sequenceUnrelated proteinsAlpha proteinRelated sequencesAcid residuesCD4 sequencesP56lckGlycoprotein CD4HeLa cellsProteinKinaseShort Related Sequences in the Cytoplasmic Domains of CD4 and CD8 Mediate Binding to the Amino-Terminal Domain of the p56 lck Tyrosine Protein Kinase
Shaw A, Chalupny J, Whitney J, Hammond C, Amrein K, Kavathas P, Sefton B, Rose J. Short Related Sequences in the Cytoplasmic Domains of CD4 and CD8 Mediate Binding to the Amino-Terminal Domain of the p56 lck Tyrosine Protein Kinase. Molecular And Cellular Biology 1990, 10: 1853-1862. DOI: 10.1128/mcb.10.5.1853-1862.1990.Peer-Reviewed Original ResearchAmino-terminal domainTyrosine protein kinaseCytoplasmic domainP56 lckProtein kinaseCommon sequence motifsRelated amino acid sequencesAmino acid sequenceDisulfide bond formationAmino acid residuesSequence motifsHybrid proteinCysteine residuesAcid sequenceUnrelated proteinsRelated sequencesAcid residuesCD4 sequencesLckGlycoprotein CD4HeLa cellsMediate bindingProteinKinaseSequence
1989
The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain
Shaw A, Amrein K, Hammond C, Stern D, Sefton B, Rose J. The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain. Cell 1989, 59: 627-636. PMID: 2582490, DOI: 10.1016/0092-8674(89)90008-1.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCD4 AntigensCytoplasmHeLa CellsHumansLymphocyte Specific Protein Tyrosine Kinase p56(lck)Macromolecular SubstancesMembrane GlycoproteinsMolecular Sequence DataMutationOligonucleotide ProbesPhosphoproteinsPlasmidsProtein BindingProtein MultimerizationProtein-Tyrosine KinasesT-LymphocytesTransfectionConceptsAmino-terminal domainCytoplasmic domainTyrosine protein kinase p56lckUnique amino-terminal domainT cell-specific proteinsTyrosine protein kinaseSpecific transmembrane proteinsCell-specific proteinsIntracellular tyrosine kinaseAmino-terminal residuesCarboxy-terminal residuesTransmembrane proteinCytoplasmic tailSrc familyProtein kinaseKinase p56lckTyrosine kinaseHeLa cellsCell surfaceProteinDeleted formsSurface glycoproteinP56lckKinaseResidues
1988
Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum.
Shaw A, Rottier P, Rose J. Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 7592-7596. PMID: 2845415, PMCID: PMC282238, DOI: 10.1073/pnas.85.20.7592.Peer-Reviewed Original ResearchConceptsSignal sequenceEndoplasmic reticulumC-terminal transmembraneType II transmembrane proteinInsertion of proteinsCleaved signal sequenceSignal sequence functionN-terminal extensionShort hydrophobic domainVesicular stomatitis virus glycoproteinMembrane anchorMutant proteinsCytoplasmic domainMembrane insertionTransmembrane proteinC-terminusCytoplasmic sideN-terminusBlock cleavageHydrophobic domainCleavage siteHeLa cellsPoint mutationsProteinMicrosomal membranes