2014
Complex Relationship between Ligand Binding and Dimerization in the Epidermal Growth Factor Receptor
Bessman NJ, Bagchi A, Ferguson KM, Lemmon MA. Complex Relationship between Ligand Binding and Dimerization in the Epidermal Growth Factor Receptor. Cell Reports 2014, 9: 1306-1317. PMID: 25453753, PMCID: PMC4254573, DOI: 10.1016/j.celrep.2014.10.010.Peer-Reviewed Original ResearchConceptsEpidermal growth factor receptorLigand bindingExtracellular regionGrowth factor receptorIntact epidermal growth factor receptorEGFR extracellular regionComplex allosteric regulationExtracellular epidermal growth factor receptorFactor receptorLigand-binding affinityAllosteric regulationReceptor dimerizationEGFR dimerizationAllosteric linkagePathological mutationsOncogenic mutationsNegative cooperativityMutationsDimerizationUnexpected relationshipBindingSpecific ligandsPivotal roleRecent advancesReceptors
2006
Determining selectivity of phosphoinositide-binding domains
Narayan K, Lemmon MA. Determining selectivity of phosphoinositide-binding domains. Methods 2006, 39: 122-133. PMID: 16829131, PMCID: PMC3786563, DOI: 10.1016/j.ymeth.2006.05.006.Peer-Reviewed Original Research
1998
Specificity and Promiscuity in Phosphoinositide Binding by Pleckstrin Homology Domains*
Kavran J, Klein D, Lee A, Falasca M, Isakoff S, Skolnik E, Lemmon M. Specificity and Promiscuity in Phosphoinositide Binding by Pleckstrin Homology Domains*. Journal Of Biological Chemistry 1998, 273: 30497-30508. PMID: 9804818, DOI: 10.1074/jbc.273.46.30497.Peer-Reviewed Original ResearchConceptsPleckstrin homology domainPH domainGrp1 PH domainD-myo-inositolParticular phosphoinositidesPhosphoinositide bindingHomology domainDependent membrane recruitmentDifferent PH domainsPH domain bindsSmall protein modulesSoluble inositol phosphatesMembrane recruitmentDomain bindsProtein modulesSpecific phosphoinositideMammalian cellsPlasma membraneSingle speciesAbundant speciesMultiple phosphoinositidesCellular membranesPhosphoinositidePI 3Clear specificity
1996
Thermodynamic Studies of SHC Phosphotyrosine Interaction Domain Recognition of the NPXpY Motif (∗)
Mandiyan V, O'Brien R, Zhou M, Margolis B, Lemmon M, Sturtevant J, Schlessinger J. Thermodynamic Studies of SHC Phosphotyrosine Interaction Domain Recognition of the NPXpY Motif (∗). Journal Of Biological Chemistry 1996, 271: 4770-4775. PMID: 8617744, DOI: 10.1074/jbc.271.9.4770.Peer-Reviewed Original ResearchAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAmino Acid SequenceBinding SitesCalorimetryErbB ReceptorsGlutathione TransferaseMolecular Sequence DataMutagenesis, Site-DirectedPeptide FragmentsPhosphotyrosinePoint MutationProtein BiosynthesisProteinsRecombinant Fusion ProteinsShc Signaling Adaptor ProteinsSrc Homology DomainsThermodynamics
1994
Thermodynamic studies of tyrosyl-phosphopeptide binding to the SH2 domain of p56lck.
Lemmon MA, Ladbury JE. Thermodynamic studies of tyrosyl-phosphopeptide binding to the SH2 domain of p56lck. Biochemistry 1994, 33: 5070-6. PMID: 7513553, DOI: 10.1021/bi00183a010.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsBinding SitesCalorimetryCloning, MolecularConserved SequenceErbB ReceptorsEscherichia coliLymphocyte Specific Protein Tyrosine Kinase p56(lck)LymphocytesMolecular Sequence DataPeptide FragmentsPhosphopeptidesPhosphotyrosineProtein-Tyrosine KinasesRecombinant ProteinsSequence Homology, Amino AcidTyrosine