1998
A single amino acid substitution in a WW‐like domain of diverse members of the PDGF receptor subfamily of tyrosine kinases causes constitutive receptor activation
Irusta P, DiMaio D. A single amino acid substitution in a WW‐like domain of diverse members of the PDGF receptor subfamily of tyrosine kinases causes constitutive receptor activation. The EMBO Journal 1998, 17: 6912-6923. PMID: 9843497, PMCID: PMC1171039, DOI: 10.1093/emboj/17.23.6912.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SequenceAmino Acid SubstitutionAnimalsBinding SitesCell Line, TransformedCloning, MolecularDimerizationEnzyme ActivationHumansInterleukin-3LigandsMiceMolecular Sequence DataMutagenesis, Site-DirectedPeptidesPhosphorylationPolymerase Chain ReactionReceptor Protein-Tyrosine KinasesReceptor, Platelet-Derived Growth Factor betaReceptors, Platelet-Derived Growth FactorSequence Homology, Amino AcidStructure-Activity RelationshipTyrosineValineConceptsTyrosine kinase activityKinase activityTyrosine kinasePlatelet-derived growth factor beta receptorCytoplasmic juxtamembrane domainPDGF receptorSignal transduction proteinsWW-like domainTransmembrane receptor tyrosine kinaseProtein-protein interactionsBa/F3 cellsGST fusion proteinSingle amino acid substitutionConstitutive receptor activationGrowth factor beta receptorAbsence of ligandReceptor tyrosine kinasesAmino acid substitutionsSequence PPXYTransduction proteinsWW domainsCellular functionsJuxtamembrane regionTyrosine phosphorylationAlanine substitutionsOncogenic activation of the PDGF β receptor by the transmembrane domain of p185neu*
Petti L, Irusta P, DiMaio D. Oncogenic activation of the PDGF β receptor by the transmembrane domain of p185neu*. Oncogene 1998, 16: 843-851. PMID: 9484775, DOI: 10.1038/sj.onc.1201590.Peer-Reviewed Original ResearchConceptsBa/F3 cellsTransmembrane domainBa/F3 hematopoietic cellsF3 cellsWild-type PDGF receptorNovel tyrosine phosphorylated proteinsIL-3-independent growthTyrosine phosphorylated proteinsDistinct signaling pathwaysWild-type PDGFLevels of phosphotyrosineWild-type receptorIL-3Β receptorPDGF β-receptorPhosphorylated proteinsTyrosine autophosphorylationOncogenic formsKinase activityMouse C127Receptor homodimerizationOncogenic activationSignaling pathwaysChimeric receptorsFoci formation
1989
Structure, Activity, and Regulation of the Bovine Papillomavirus E5 Gene and Its Transforming Protein Product
Horwitz B, Settleman J, Prakash S, DiMaio D. Structure, Activity, and Regulation of the Bovine Papillomavirus E5 Gene and Its Transforming Protein Product. Current Topics In Microbiology And Immunology 1989, 144: 143-151. PMID: 2551579, DOI: 10.1007/978-3-642-74578-2_18.Peer-Reviewed Original ResearchConceptsE5 geneFoci formationBovine papillomavirus type 1 DNACell focus formationBPV geneCodon resultsC127 cellsMouse cellsTumorigenic transformationProtein productsK polypeptideGenesViral mutantsBiochemical analysisEfficient transformationCellsMutantsPolypeptideDNARegulationExpressionDownstreamActivityTranslationFormation
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. 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