2020
Cell-penetrating peptide inhibits retromer-mediated human papillomavirus trafficking during virus entry
Zhang P, Moreno R, Lambert PF, DiMaio D. Cell-penetrating peptide inhibits retromer-mediated human papillomavirus trafficking during virus entry. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 6121-6128. PMID: 32123072, PMCID: PMC7084110, DOI: 10.1073/pnas.1917748117.Peer-Reviewed Original ResearchConceptsEssential protein-protein interactionsCellular protein complexesProtein-protein interactionsIntracellular virus traffickingRetrograde transport pathwaySites of replicationCell-penetrating sequenceProtein complexesCellular proteinsVirus replicationHPV16 pseudovirus infectionVirus traffickingL2 capsid proteinsAspects of infectionCapsid proteinHPV entryViral genomeViral proteinsIncoming virionsViral componentsHuman papillomavirus infectionProteinAntiviral targetDose-dependent blockVirus entry
2017
Single methyl groups can act as toggle switches to specify transmembrane Protein-protein interactions
He L, Steinocher H, Shelar A, Cohen EB, Heim EN, Kragelund BB, Grigoryan G, DiMaio D. Single methyl groups can act as toggle switches to specify transmembrane Protein-protein interactions. ELife 2017, 6: e27701. PMID: 28869036, PMCID: PMC5597333, DOI: 10.7554/elife.27701.Peer-Reviewed Original ResearchConceptsProtein-protein interactionsErythropoietin receptorTransmembrane proteinTransmembrane protein-protein interactionsTMD interactionsModel transmembrane proteinMouse erythropoietin receptorHuman erythropoietin receptorSingle methyl groupGrowth factor independenceSide chain methyl groupsCellular processesMouse cellsFactor independenceChain methyl groupsIntrinsic specificityToggle switchTraptamersMethyl groupProteinReceptor activitySpecific positionsReceptorsSpecificityOligomerization
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