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. 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 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. 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 glycoproteinA single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein
Gallione C, Rose J. A single amino acid substitution in a hydrophobic domain causes temperature-sensitive cell-surface transport of a mutant viral glycoprotein. Journal Of Virology 1985, 54: 374-382. PMID: 2985803, PMCID: PMC254807, DOI: 10.1128/jvi.54.2.374-382.1985.Peer-Reviewed Original ResearchConceptsCDNA clonesHydrophobic domainAmino acidsCell surface transportSingle amino acid substitutionVesicular stomatitis virus glycoproteinWild-type parent strainDNA sequence analysisPolar amino acidsHydrophobic amino acidsAmino acid changesAmino acid substitutionsProtein transportDNA sequencesNonpermissive temperatureVesicular stomatitis virusCOS cellsNonconservative substitutionsSequence analysisSpontaneous revertantsAcid substitutionsAcid changesSingle substitutionTransport defectStomatitis virus
1984
Conversion of a secretory protein into a transmembrane protein results in its transport to the golgi complex but not to the cell surface
Guan J, Rose J. Conversion of a secretory protein into a transmembrane protein results in its transport to the golgi complex but not to the cell surface. Cell 1984, 37: 779-787. PMID: 6589049, DOI: 10.1016/0092-8674(84)90413-6.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsMembrane proteinsSecretory proteinsFusion proteinCell surfaceVesicular stomatitis virus glycoproteinRat growth hormoneMembrane spanningCytoplasmic domainCDNA clonesCarboxy terminusHybrid geneEucaryotic cellsTransmembrane configurationGolgi apparatusProtein resultsProteinMicrosomal membranesVirus glycoproteinRapid secretionMembranePalmitic acidGolgiGenesTerminusThe presence of cysteine in the cytoplasmic domain of the vesicular stomatitis virus glycoprotein is required for palmitate addition.
Rose J, Adams G, Gallione C. The presence of cysteine in the cytoplasmic domain of the vesicular stomatitis virus glycoprotein is required for palmitate addition. Proceedings Of The National Academy Of Sciences Of The United States Of America 1984, 81: 2050-2054. PMID: 6326102, PMCID: PMC345434, DOI: 10.1073/pnas.81.7.2050.Peer-Reviewed Original ResearchConceptsCytoplasmic domainG proteinsVesicular stomatitis virusVesicular stomatitis virus glycoproteinVSV G proteinCarboxyl-terminal sideAmino acid residuesEukaryotic cellsTransmembrane domainCDNA clonesGene resultsAcid residuesCellular membranesPalmitate additionTransmembrane glycoproteinCellular glycoproteinsCell surfaceAmino acidsProteinStomatitis virusCysteineVirus glycoproteinPresence of cysteineFatty acidsGlycoprotein
1983
Nucleotide sequence of a cDNA clone encoding the entire glycoprotein from the New Jersey serotype of vesicular stomatitis virus
Gallione C, Rose J. Nucleotide sequence of a cDNA clone encoding the entire glycoprotein from the New Jersey serotype of vesicular stomatitis virus. Journal Of Virology 1983, 46: 162-169. PMID: 6298453, PMCID: PMC255104, DOI: 10.1128/jvi.46.1.162-169.1983.Peer-Reviewed Original ResearchConceptsNew Jersey serotypeVesicular stomatitis virusCDNA clonesIndiana serotypeNucleotide sequenceTranslation termination codonVSV serotypesStomatitis virusTransmembrane domainSignal sequenceSerine residuesProtein sequencesTermination codonEsterification sitesGlycosylation sitesNoncoding nucleotidesGlycine residueShort homologiesAmino acidsNucleotidesMRNARabies virusClonesTerminusResidues
1982
Expression from cloned cDNA of cell-surface secreted forms of the glycoprotein of vesicular stomatitis virus in eucaryotic cells
Rose J, Bergmann J. Expression from cloned cDNA of cell-surface secreted forms of the glycoprotein of vesicular stomatitis virus in eucaryotic cells. Cell 1982, 30: 753-762. PMID: 6291783, DOI: 10.1016/0092-8674(82)90280-x.Peer-Reviewed Original ResearchConceptsG proteinsVesicular stomatitis virusCOS1 cellsCOOH terminusStomatitis virusMouse L cellsSV40 early promoterSV40 late promoterNormal G proteinsTransmembrane domainCDNA clonesEucaryotic cellsLate promoterEarly promoterPlasmid vectorCell typesAmino acidsProteinLipid bilayersL cellsPromoterTerminusG-DNADNACells
1981
Nucleotide sequences of the mRNA's encoding the vesicular stomatitis virus G and M proteins determined from cDNA clones containing the complete coding regions
Rose J, Gallione C. Nucleotide sequences of the mRNA's encoding the vesicular stomatitis virus G and M proteins determined from cDNA clones containing the complete coding regions. Journal Of Virology 1981, 39: 519-528. PMID: 6268840, PMCID: PMC171362, DOI: 10.1128/jvi.39.2.519-528.1981.Peer-Reviewed Original ResearchConceptsCDNA clonesAmino acidsSignal peptideNucleotide sequenceVesicular stomatitis virus M proteinFull-length cDNA cloneBasic amino-terminal domainComplete nucleotide sequenceVesicular stomatitis virus mRNAAmino-terminal domainComplete coding sequenceM protein sequencesComplete coding regionSite of glycosylationBasic amino acidsM proteinVesicular stomatitis virus GMembrane associationTransmembrane segmentsG protein mRNALarge hydrophobic domainsTerminal domainCoding sequenceProtein sequencesAsparagine residuesNucleotide sequences of the mRNA's encoding the vesicular stomatitis virus N and NS proteins
Gallione C, Greene J, Iverson L, Rose J. Nucleotide sequences of the mRNA's encoding the vesicular stomatitis virus N and NS proteins. Journal Of Virology 1981, 39: 529-535. PMID: 6268841, PMCID: PMC171363, DOI: 10.1128/jvi.39.2.529-535.1981.Peer-Reviewed Original ResearchConceptsNS proteinsAUG codonReading frameNucleotide sequenceThird AUG codonAmino acidsComplete nucleotide sequenceVesicular stomatitis virus mRNAOpen reading frameSodium dodecyl sulfate-polyacrylamide gelsAnomalous electrophoretic mobilityDodecyl sulfate-polyacrylamide gelsSecond reading frameSulfate-polyacrylamide gelsCDNA clonesTranslational initiationSmall proteinsMRNA sequencesN proteinVirus NPolyadenylic acidVirus mRNACodonProteinMRNA
1980
ANALYSIS OF VSV GLYCOPROTEIN STRUCTURE AND GENOME STRUCTURE USING CLONED DNA11This work was supported by Public Health Service Grant No. AI 15481 from NIAID, National Science Foundation Grant No. PCM 77974, NCI Grant No. CA 14195
Rose J, Welch W, Sefton B, Iverson L. ANALYSIS OF VSV GLYCOPROTEIN STRUCTURE AND GENOME STRUCTURE USING CLONED DNA11This work was supported by Public Health Service Grant No. AI 15481 from NIAID, National Science Foundation Grant No. PCM 77974, NCI Grant No. CA 14195. 1980, 81-93. DOI: 10.1016/b978-0-12-255850-4.50012-3.Peer-Reviewed Original ResearchNH2-terminal sequenceVSV genomeCOOH terminusSite of polyadenylationDNA primersVesicular stomatitis virus glycoproteinGenome structureIntergenic regionTranscription eventsCDNA clonesDNA insertsDNA sequencesL geneU residuesRepetitive copyingM geneTerminal sequenceHydrophobic domainCOOH-terminalG geneGenesFunctional significanceLipid bilayersGenomePolyadenylation