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
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
1985
A 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
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