2015
Biologically active LIL proteins built with minimal chemical diversity
Heim EN, Marston JL, Federman RS, Edwards AP, Karabadzhak AG, Petti LM, Engelman DM, DiMaio D. Biologically active LIL proteins built with minimal chemical diversity. Proceedings Of The National Academy Of Sciences Of The United States Of America 2015, 112: e4717-e4725. PMID: 26261320, PMCID: PMC4553812, DOI: 10.1073/pnas.1514230112.Peer-Reviewed Original ResearchConceptsAmino acidsTransmembrane proteinSpecific biological activityPlatelet-derived growth factor β receptorArtificial transmembrane proteinsChemical diversityGrowth factor β receptorHydrophobic amino acidsLIL proteinsKnown proteinsIndividual amino acidsTransmembrane domainCellular contextDifferent amino acidsComplete mutagenesisMost proteinsBiological activityActive proteinSimple proteinSingle isoleucineSpecific sequencesProteinDiversityLeucineΒ receptor
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