2023
Sequence-independent activity of a predicted long disordered segment of the human papillomavirus type 16 L2 capsid protein during virus entry
Oh C, Buckley P, Choi J, Hierro A, DiMaio D. Sequence-independent activity of a predicted long disordered segment of the human papillomavirus type 16 L2 capsid protein during virus entry. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2307721120. PMID: 37819982, PMCID: PMC10589650, DOI: 10.1073/pnas.2307721120.Peer-Reviewed Original ResearchConceptsAmino acid sequenceAcid sequenceProtein segmentsVirus traffickingUnrelated cellular proteinsSequence-independent mannerIntracellular virus traffickingActivity of proteinsAmino acid segmentComplex biological functionsVirus entryTandem arraysProtein functionTrafficking factorsCellular proteinsEndosome membraneBiological functionsHPV16 pseudovirus infectionCellular factorsDiverse sequencesL2 capsid proteins
1992
The central hydrophobic domain of the bovine papillomavirus E5 transforming protein can be functionally replaced by many hydrophobic amino acid sequences containing a glutamine
Kulke R, Horwitz B, Zibello T, DiMaio D. The central hydrophobic domain of the bovine papillomavirus E5 transforming protein can be functionally replaced by many hydrophobic amino acid sequences containing a glutamine. Journal Of Virology 1992, 66: 505-511. PMID: 1727496, PMCID: PMC238311, DOI: 10.1128/jvi.66.1.505-511.1992.Peer-Reviewed Original ResearchConceptsHydrophobic amino acidsAmino acidsE5 proteinRandom hydrophobic sequencesHydrophobic domainRodent fibroblast cell linesCentral hydrophobic domainHydrophobic amino acid sequenceCarboxyl-terminal amino acidsMouse C127 cellsAmino acid sequenceClasses of mutantsAbsence of glutamineBovine papillomavirus E5Mutant proteinsTransforming proteinDefective mutantsHydrophobic sequenceFibroblast cell lineProtein stabilityAcid sequenceC127 cellsHomodimer formationEfficient transformationProtein
1989
Transforming activity of a 16-amino-acid segment of the bovine papillomavirus E5 protein linked to random sequences of hydrophobic amino acids
Horwitz B, Weinstat D, DiMaio D. Transforming activity of a 16-amino-acid segment of the bovine papillomavirus E5 protein linked to random sequences of hydrophobic amino acids. Journal Of Virology 1989, 63: 4515-4519. PMID: 2552136, PMCID: PMC251082, DOI: 10.1128/jvi.63.11.4515-4519.1989.Peer-Reviewed Original ResearchConceptsE5 proteinAmino acidsWild-type E5 proteinBovine papillomavirus E5 proteinAmino acid sequence requirementsHydrophobic amino acid sequenceCarboxyl-terminal amino acidsMouse C127 cellsAmino acid sequenceBovine papillomavirus type 1Carboxyl-terminal portionWild-type onesHydrophobic amino acidsPapillomavirus type 1Hydrophobic sequenceDifferent amino acidsAcid sequenceC127 cellsSequence requirementsE5 geneCell transformationFoci formationSubstitution mutationsCell membraneProtein
1988
44-Amino-Acid E5 Transforming Protein of Bovine Papillomavirus Requires a Hydrophobic Core and Specific Carboxyl-Terminal Amino Acids
Horwitz B, Burkhardt A, Schlegel R, DiMaio D. 44-Amino-Acid E5 Transforming Protein of Bovine Papillomavirus Requires a Hydrophobic Core and Specific Carboxyl-Terminal Amino Acids. Molecular And Cellular Biology 1988, 8: 4071-4078. DOI: 10.1128/mcb.8.10.4071-4078.1988.Peer-Reviewed Original ResearchAmino acid substitutionsE5 proteinAmino acidsTransforming proteinAcid substitutionsCarboxyl-terminal thirdCarboxyl-terminal amino acidsCharacterization of mutantsSpecific amino acid sequencesMouse C127 cellsAmino acid sequenceBovine papillomavirus type 1Specific amino acidsHydrophobic amino acidsPapillomavirus type 1Focus-forming activityCysteine residuesAcid sequenceC127 cellsSaturation mutagenesisE5 geneTransforming activityEssential amino acidsFoci formationMissense mutations44-amino-acid E5 transforming protein of bovine papillomavirus requires a hydrophobic core and specific carboxyl-terminal amino acids.
Horwitz B, Burkhardt A, Schlegel R, DiMaio D. 44-amino-acid E5 transforming protein of bovine papillomavirus requires a hydrophobic core and specific carboxyl-terminal amino acids. Molecular And Cellular Biology 1988, 8: 4071-4078. PMID: 2847028, PMCID: PMC365476, DOI: 10.1128/mcb.8.10.4071.Peer-Reviewed Original ResearchConceptsAmino acid substitutionsE5 proteinAmino acidsTransforming proteinAcid substitutionsCarboxyl-terminal thirdCarboxyl-terminal amino acidsCharacterization of mutantsSpecific amino acid sequencesMouse C127 cellsAmino acid sequenceBovine papillomavirus type 1Specific amino acidsHydrophobic amino acidsPapillomavirus type 1Focus-forming activityCysteine residuesAcid sequenceC127 cellsSaturation mutagenesisE5 geneTransforming activityEssential amino acidsFoci formationMissense mutations
1987
Mutational analysis of open reading frame E4 of bovine papillomavirus type 1
Neary K, Horwitz B, DiMaio D. Mutational analysis of open reading frame E4 of bovine papillomavirus type 1. Journal Of Virology 1987, 61: 1248-1252. PMID: 3029420, PMCID: PMC254088, DOI: 10.1128/jvi.61.4.1248-1252.1987.Peer-Reviewed Original ResearchConceptsBovine papillomavirus type 1Papillomavirus type 1E4 proteinLate gene expressionMouse C127 cellsAmino acid sequenceAcid sequenceExtrachromosomal plasmidsBiological activityC127 cellsMutational analysisGene expressionFoci formationORF E2ORFProteinViral DNAMutationsSoft agaroseCellsMutantsType 1Papilloma formationDNAPlasmid