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
1987
Replacement of the cytoplasmic domain alters sorting of a viral glycoprotein in polarized cells.
Puddington L, Woodgett C, Rose J. Replacement of the cytoplasmic domain alters sorting of a viral glycoprotein in polarized cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1987, 84: 2756-2760. PMID: 3033661, PMCID: PMC304737, DOI: 10.1073/pnas.84.9.2756.Peer-Reviewed Original ResearchConceptsCytoplasmic domainG proteinsPlasma membraneVesicular stomatitis virusNormal cytoplasmic domainIntegral membrane proteinsPolarized epithelial cellsVSV G proteinApical plasma membraneBasolateral plasma membraneBasolateral membraneCanine kidney cell lineMadin-Darby canine kidney (MDCK) cell lineIndirect immunofluorescence microscopyMembrane proteinsKidney cell lineDomain altersPolarized expressionImmunofluorescence microscopyBasolateral surfaceProteinStomatitis virusCell linesViral glycoproteinsEpithelial cells
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 glycoprotein