2019
Computational algorithms for in silico profiling of activating mutations in cancer
Jordan EJ, Patil K, Suresh K, Park JH, Mosse YP, Lemmon MA, Radhakrishnan R. Computational algorithms for in silico profiling of activating mutations in cancer. Cellular And Molecular Life Sciences 2019, 76: 2663-2679. PMID: 30982079, PMCID: PMC6589134, DOI: 10.1007/s00018-019-03097-2.Peer-Reviewed Original ResearchConceptsTarget proteinsSingle nucleotide polymorphismsB-RafSerine/threonine-protein kinase B-RafDifferent target proteinsEffects of mutationsStructure-based computational approachKinase domainStructure-based methodsStructure-based modelProtein structureProtein activationSilico profilingAnaplastic lymphoma kinaseInteraction of inhibitorsMutational landscapeHuman cancersPoint mutationsProteinMutationsMutational patternsDifferent mutationsActivation statusComputational approachLymphoma kinase
2009
Structural basis for EGFR ligand sequestration by Argos
Klein D, Stayrook S, Shi F, Narayan K, Lemmon M. Structural basis for EGFR ligand sequestration by Argos. The FASEB Journal 2009, 23: 883.7-883.7. DOI: 10.1096/fasebj.23.1_supplement.883.7.Peer-Reviewed Original ResearchEpidermal growth factor receptorHuman urokinase-type plasminogen activator receptorDiverse developmental processesClamp-like structureEGF-like domainGrowth factor ligandsArgos functionMammalian counterpartsLigand sequestrationEGF-like modulesUrokinase-type plasminogen activator receptorEGF domainsEGF ligandGrowth factor receptorEssential regulatorStructural basisDevelopmental processesStructural homologuesEGFR ligandsFactor ligandHuman cancersPlasminogen activator receptorFactor receptorErbB/Inappropriate activationErbB2/HER2/Neu resembles an autoinhibited invertebrate EGF receptor
Alvarado D, Klein D, Lemmon M. ErbB2/HER2/Neu resembles an autoinhibited invertebrate EGF receptor. The FASEB Journal 2009, 23: 884.3-884.3. DOI: 10.1096/fasebj.23.1_supplement.884.3.Peer-Reviewed Original ResearchReceptor tyrosine kinase ErbB2Human cancersAutoinhibitory interactionsExtracellular regionInterdomain interactionsEGF receptorErbB2 signalingOrphan receptorOncogenic propertiesHuman EGFRErbB receptorsImportant therapeutic targetErbB2Structural studiesTherapeutic targetNovel aspectsReceptorsAutoinhibitoryAutoinhibitionSignalingOverexpressionImportant implicationsRegulationTherapeutic approachesEGFR
2007
Activation and Inhibition of the EGF Receptor
Lemmon M. Activation and Inhibition of the EGF Receptor. The FASEB Journal 2007, 21: a46-a46. DOI: 10.1096/fasebj.21.5.a46-b.Peer-Reviewed Original ResearchReceptor tyrosine kinasesEGFR extracellular regionEGF-induced dimerizationActivation of EGFRErbB family receptor tyrosine kinasesKekkon-1D. melanogasterEpidermal growth factor receptorC. elegansLigand sinkMembrane proteinsGrowth factor receptorExtracellular regionEGF receptorExtracellular domainTyrosine kinaseCurrent mechanistic viewsCell surfaceHuman cancersCell growthOrthologsFactor receptorMechanistic viewNovel EGFRDimerization
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