2014
Small transmembrane protein inhibitors of the platelet‐derived growth factor β receptor (LB215)
Petti L, Talbert‐Slagle K, Chacon K, Hochstrasser M, DiMaio D. Small transmembrane protein inhibitors of the platelet‐derived growth factor β receptor (LB215). The FASEB Journal 2014, 28 DOI: 10.1096/fasebj.28.1_supplement.lb215.Peer-Reviewed Original ResearchTransmembrane domainTransmembrane proteinPlatelet-derived growth factor β receptorProtein inhibitorGrowth factor receptor signalingSingle conservative amino acid substitutionSmall transmembrane proteinConservative amino acid substitutionsGrowth factor β receptorParticular tyrosine residueReceptor tyrosine kinasesAmino acid substitutionsSequence similarityGrowth factor receptorTraptamersReceptor dimerizationEffects of PDGFSmall proteinsTyrosine residuesExtracellular domainTyrosine kinaseAcid substitutionsReceptor signalingRetroviral libraryPDGFβR
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 substitutions
1992
A glutamine residue in the membrane-associating domain of the bovine papillomavirus type 1 E5 oncoprotein mediates its binding to a transmembrane component of the vacuolar H(+)-ATPase
Goldstein D, Kulke R, Dimaio D, Schlegel R. A glutamine residue in the membrane-associating domain of the bovine papillomavirus type 1 E5 oncoprotein mediates its binding to a transmembrane component of the vacuolar H(+)-ATPase. Journal Of Virology 1992, 66: 405-413. PMID: 1370089, PMCID: PMC238300, DOI: 10.1128/jvi.66.1.405-413.1992.Peer-Reviewed Original ResearchConceptsK proteinGrowth factor receptorE5 oncoproteinGlutamine residuesRandom hydrophobic sequencesSpecific amino acid residuesMembrane-associated domainMajor transforming proteinK protein componentCarboxyl-terminal domainEndoplasmic reticulum membraneFactor receptorBovine papillomavirus type 1Colony-stimulating factor 1 receptorTransformation-defective mutantsAmino acid residuesPotential binding sitesPlatelet-derived growth factor receptorAmino acid substitutionsPapillomavirus type 1Hydrophilic amino acidsE5 dimerE5 mutantsFactor 1 receptorProtein complexes
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