2003
Parvoviruses
Tattersall P, Cotmore S. Parvoviruses. 2003 DOI: 10.1038/npg.els.0000423.Peer-Reviewed Original Research
1989
A genome-linked copy of the NS-1 polypeptide is located on the outside of infectious parvovirus particles
Cotmore S, Tattersall P. A genome-linked copy of the NS-1 polypeptide is located on the outside of infectious parvovirus particles. Journal Of Virology 1989, 63: 3902-3911. PMID: 2527311, PMCID: PMC250986, DOI: 10.1128/jvi.63.9.3902-3911.1989.Peer-Reviewed Original ResearchConceptsNS-1 moleculesHost cellsSingle-strand DNA genomeNonstructural protein NS-1Amino-terminal domainNew host cellsNS-1 polypeptideAutonomous parvovirus minute virusParvovirus minute virusNS-1Normal culture conditionsDNA genomeS2 formA9 cellsLimited proteolysisIncoming virusMinute virusProteolytic digestionDNADNA coreMost virionsCulture conditionsVirionsPolypeptideParvovirus particles
1988
The terminal protein of minute virus of mice is an 83 kilodalton polypeptide linked to specific forms of double‐stranded and single‐stranded viral DNA
Gunther M, Tattersall P. The terminal protein of minute virus of mice is an 83 kilodalton polypeptide linked to specific forms of double‐stranded and single‐stranded viral DNA. FEBS Letters 1988, 242: 22-26. PMID: 3203742, DOI: 10.1016/0014-5793(88)80977-3.Peer-Reviewed Original Research
1986
Identification of the major structural and nonstructural proteins encoded by human parvovirus B19 and mapping of their genes by procaryotic expression of isolated genomic fragments
Cotmore S, McKie V, Anderson L, Astell C, Tattersall P. Identification of the major structural and nonstructural proteins encoded by human parvovirus B19 and mapping of their genes by procaryotic expression of isolated genomic fragments. Journal Of Virology 1986, 60: 548-557. PMID: 3021988, PMCID: PMC288924, DOI: 10.1128/jvi.60.2.548-557.1986.Peer-Reviewed Original ResearchConceptsProtein sequencesViral capsid polypeptidesCapsid polypeptidesSucrose velocity gradientsB19 genomeBacterial plasmid vectorRestriction endonuclease fragmentsGenomic fragmentProtein speciesApparent molecular weightNonstructural polypeptidesExpression constructsSimilar proteinsBAL-31GenomeExpression vectorNonstructural proteinsEndonuclease fragmentsPlasmid vectorViral genomeViral polypeptidesPolypeptide fragmentsProcaryotic expressionPolypeptideProteinNucleotide sequence and genome organization of human parvovirus B19 isolated from the serum of a child during aplastic crisis
Shade R, Blundell M, Cotmore S, Tattersall P, Astell C. Nucleotide sequence and genome organization of human parvovirus B19 isolated from the serum of a child during aplastic crisis. Journal Of Virology 1986, 58: 921-936. PMID: 3701931, PMCID: PMC253001, DOI: 10.1128/jvi.58.3.921-936.1986.Peer-Reviewed Original ResearchConceptsNucleotide sequenceLarge open reading frameMajor nonstructural proteinOpen reading frameFull-length cloneMajor structural polypeptidesGenome organizationGenomic clonesPutative polypeptideTranscription unitEntire genomeReading frameDNA sequencesFourth promoterParvovirus genomeSequence informationNonstructural proteinsGenomeTerminal repeatDependovirus genusStructural polypeptidesViral DNAB19 genomePolypeptideSequenceThe NS-1 polypeptide of the autonomous parvovirus MVM is a nuclear phosphoprotein
Cotmore S, Tattersall P. The NS-1 polypeptide of the autonomous parvovirus MVM is a nuclear phosphoprotein. Virus Research 1986, 4: 243-250. PMID: 3739422, DOI: 10.1016/0168-1702(86)90003-1.Peer-Reviewed Original ResearchConceptsParvovirus MVMNS-1 proteinVitro translation productsMessenger RNA speciesNS-1 polypeptideSame primary sequencePeptide map analysisNon-structural proteinsRNA speciesNuclear phosphoproteinReplication complexTranslation productsKb transcriptPrimary sequenceVivo productNS-1SpeciesProteinPredominant formPhosphoproteinMVMTranscriptsPolypeptideNucleusMap analysis
1983
The autonomous parvovirus MVM encodes two nonstructural proteins in addition to its capsid polypeptides
Cotmore S, Sturzenbecker L, Tattersall P. The autonomous parvovirus MVM encodes two nonstructural proteins in addition to its capsid polypeptides. Virology 1983, 129: 333-343. PMID: 6623929, DOI: 10.1016/0042-6822(83)90172-1.Peer-Reviewed Original ResearchConceptsParvovirus MVMCapsid polypeptidesNS-1 proteinOpen reading frameNS-1 polypeptidePeptide map analysisMajor intronTranscription unitMVM genomeVitro translationApparent molecular weightReading frameNonstructural proteinsPolypeptideProteinVP-1NS-1VP-2GenomeIntronsComigratesMolecular weightTranscriptsMVMMap analysis
1977
Sequence homology between the structural polypeptides of minute virus of mice
Tattersall P, Shatkin A, Ward D. Sequence homology between the structural polypeptides of minute virus of mice. Journal Of Molecular Biology 1977, 111: 375-394. PMID: 864702, DOI: 10.1016/s0022-2836(77)80060-0.Peer-Reviewed Original ResearchConceptsA polypeptideEmpty virionsPolypeptide BTotal virion proteinsMinute virusPolypeptide speciesB polypeptidesSequence homologyPrecursor-product relationshipVirion proteinsC polypeptideStructural polypeptidesPolypeptideCommon sequenceEmpty particlesVirionsProteinDifferent conformationsEnzymePrevious kinetic studiesSequenceVivo observationsCleavageConformationVivo
1976
Three structural polypeptides coded for by minite virus of mice, a parvovirus
Tattersall P, Cawte P, Shatkin A, Ward D. Three structural polypeptides coded for by minite virus of mice, a parvovirus. Journal Of Virology 1976, 20: 273-289. PMID: 988192, PMCID: PMC354988, DOI: 10.1128/jvi.20.1.273-289.1976.Peer-Reviewed Original ResearchConceptsLate maturation stepPulse-chase experimentsNuclei of cellsSodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisDNA genomeSulfate-polyacrylamide gel electrophoresisThird polypeptideMaturation stepsVirion massProtein componentsHost cellsEmpty virionsStructural polypeptidesPolypeptideMinute virusGel electrophoresisCsCl gradientsProtein massUninfected cellsGrowth conditionsSequential harvestingEmpty particlesVirionsProtein