2008
Functional selectivity of EGF family peptide growth factors: Implications for cancer
Wilson KJ, Gilmore JL, Foley J, Lemmon MA, Riese DJ. Functional selectivity of EGF family peptide growth factors: Implications for cancer. Pharmacology & Therapeutics 2008, 122: 1-8. PMID: 19135477, PMCID: PMC2665203, DOI: 10.1016/j.pharmthera.2008.11.008.Peer-Reviewed Original ResearchConceptsEGF family membersPeptide growth factorsFunctional selectivityGrowth factorErbB family receptorsFamily membersNeck cancerReceptor couplingReceptor tyrosine phosphorylationMalignant phenotypeDivergent biological responsesSame receptorFamily receptorsEGF familyReceptorsErbB receptorsG proteinsCancerCancer chemotherapeuticsCell culturesLigand activityTyrosine phosphorylationColorectalSubsequent differencesBiological responsesHarnessing Novel Secreted Inhibitors of EGF Receptor Signaling for Breast Cancer Treatment
Lemmon M. Harnessing Novel Secreted Inhibitors of EGF Receptor Signaling for Breast Cancer Treatment. 2008 DOI: 10.21236/ada488172.Peer-Reviewed Original ResearchEGF receptor family membersEGF receptor signalingEGF-like ligandsReceptor family membersNew structural informationFruit flyYeast surface displayEGF receptorEGFR ligandsSecreted inhibitorsProtein scaffoldsReceptor signalingFunctional fragmentsSurface displayHuman EGFProtein therapeuticsTherapeutic designGrowth factorStructural informationNew therapeuticsExperimental approachStructure determinationFamily membersDrosophilaReceptors
2007
Harnessing Novel Secreted Inhibitors of EGF Receptor Signaling for Breast Cancer Treatment
Lemmon M. Harnessing Novel Secreted Inhibitors of EGF Receptor Signaling for Breast Cancer Treatment. 2007 DOI: 10.21236/ada471085.Peer-Reviewed Original ResearchEGF receptor family membersEGF receptor signalingEGF-like ligandsReceptor family membersNew structural informationFruit flyYeast surface displayEGF receptorSecreted inhibitorsEGFR ligandsProtein scaffoldsReceptor signalingFunctional fragmentsSurface displayHuman EGFProtein therapeuticsTherapeutic designGrowth factorNew therapeuticsStructural informationExperimental approachStructure determinationFamily membersDrosophilaReceptors
2004
Rapid Visual Assays of Oncogenic Aberrant ErbB Receptor Activation Using Fluorescence Microscopy
Berger M, Lemmon M. Rapid Visual Assays of Oncogenic Aberrant ErbB Receptor Activation Using Fluorescence Microscopy. 2004 DOI: 10.21236/ada427040.Peer-Reviewed Original ResearchErbB receptor activationHeteromeric complexesHuman cancersReceptor tyrosine kinase familyTyrosine kinase familyCell surface receptorsErbB receptor tyrosine kinase familyErbB receptor familyGrowth factorPeptide growth factorsCell biologicalKinase familyReceptor activationGrowth of cellsBiophysical approachesEGF receptorErbB2/HERReceptor familyFluorescence microscopyMajor targetClinical trialsPhysiologic outcomesReceptorsChemotherapeutic agentsFamily
2001
Development of Strategies to Manipulate ErbB Receptor Heterodimerization from a Quantitative Analysis of Receptor/Ligand Relationships
Lemmon M. Development of Strategies to Manipulate ErbB Receptor Heterodimerization from a Quantitative Analysis of Receptor/Ligand Relationships. 2001 DOI: 10.21236/ada398353.Peer-Reviewed Original ResearchBreast cancerErbB-1Growth factorHuman breast cancer casesBreast cancer casesInappropriate receptor activationEpidermal growth factor receptorGrowth factor receptorSame growth factorsCancer casesReceptor activationExtracellular domainReceptor heterodimerizationReceptor tyrosine kinasesFactor receptorErbB receptorsReceptorsErbB2ErbB familyErbB2 activationReceptor transmodulationDevelopment of strategiesCancerTyrosine kinaseReceptor homo
1997
Kit Receptor Dimerization Is Driven by Bivalent Binding of Stem Cell Factor*
Lemmon M, Pinchasi D, Zhou M, Lax I, Schlessinger J. Kit Receptor Dimerization Is Driven by Bivalent Binding of Stem Cell Factor*. Journal Of Biological Chemistry 1997, 272: 6311-6317. PMID: 9045650, DOI: 10.1074/jbc.272.10.6311.Peer-Reviewed Original ResearchConceptsStem cell factorKIT dimerizationReceptor dimerizationExtracellular domainCell factorFourth Ig-like domainColony-stimulating factor-1Receptor tyrosine kinasesIg-like domainsCytokine stem cell factorDomain bindsPlatelet-derived growth factorGrowth factorLike domainDimer bindsMost growth factorsTyrosine kinaseDimerization siteConformational changesReceptor KITAnalytical ultracentrifugationForms of KITBivalent bindingFactor 1DimerizationTwo EGF molecules contribute additively to stabilization of the EGFR dimer
Lemmon M, Bu Z, Ladbury J, Zhou M, Pinchasi D, Lax I, Engelman D, Schlessinger J. Two EGF molecules contribute additively to stabilization of the EGFR dimer. The EMBO Journal 1997, 16: 281-294. PMID: 9029149, PMCID: PMC1169635, DOI: 10.1093/emboj/16.2.281.Peer-Reviewed Original ResearchConceptsEpidermal growth factorReceptor dimerizationEGF moleculesPrecise molecular detailsHuman growth hormone receptorReceptor-receptor interactionsGrowth factorInterferon-gamma receptorEGFR dimersSignaling eventsMolecular detailsReceptor oligomerizationGrowth hormone receptorExtracellular domainEGFR familyCell surfaceMonomer bindsSubsequent associationDimerizationHormone receptorsTitration calorimetrySmall-angle X-ray scatteringBindingReceptorsMultivalent binding
1994
Regulation of signal transduction and signal diversity by receptor oligomerization
Lemmon M, Schlessinger J. Regulation of signal transduction and signal diversity by receptor oligomerization. Trends In Biochemical Sciences 1994, 19: 459-463. PMID: 7855887, DOI: 10.1016/0968-0004(94)90130-9.Peer-Reviewed Original ResearchConceptsReceptor oligomerizationProtein tyrosine kinase activityTyrosine kinase activityDiversity of ligandsGrowth factorCytoplasmic domainSignal transductionEpidermal growth factorKinase activityExtracellular domainDifferent complementsSame receptor familySignal diversityReceptor familyIndividual receptorsOligomerizationHeterodimerizationDiversityAccessory moleculesReceptorsImportant roleSH2TransmembraneTransductionDomain