1994
Mutations 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
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
1980
Vesicular stomatitis virus glycoprotein is anchored in the viral membrane by a hydrophobic domain near the COOH terminus
Rose J, Welch W, Sefton B, Esch F, Ling N. Vesicular stomatitis virus glycoprotein is anchored in the viral membrane by a hydrophobic domain near the COOH terminus. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 3884-3888. PMID: 6253998, PMCID: PMC349731, DOI: 10.1073/pnas.77.7.3884.Peer-Reviewed Original ResearchConceptsAmino acid sequencePartial amino acid sequenceVesicular stomatitis virus glycoproteinAcid sequenceAmino acidsProtein geneCOOH terminusHydrophobic domainViral membraneVSV G proteinLipid bilayersTerminal portionTerminal amino acid sequenceM protein geneG protein geneG protein sequencesTerminal amino acidsVirus glycoproteinErythrocyte membrane proteinsMembrane proteinsDNA insertsLeader sequenceComplete sequenceProtein sequencesRNA genomeANALYSIS 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