2017
Dimerization of Tie2 mediated by its membrane-proximal FNIII domains
Moore JO, Lemmon MA, Ferguson KM. Dimerization of Tie2 mediated by its membrane-proximal FNIII domains. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: 4382-4387. PMID: 28396397, PMCID: PMC5410832, DOI: 10.1073/pnas.1617800114.Peer-Reviewed Original ResearchConceptsExtracellular regionFNIII domainsResolution X-ray crystal structureMembrane-proximal fibronectin type III domainsDomain-mediated interactionsDifferent cellular contextsLigand-binding regionHigher-order oligomersTie2 activationFibronectin type III domainReceptor tyrosine kinasesTyrosine kinase familyEGF-homology domainThird FNIII domainType III domainPrevious structural studiesStructural studiesHomology domainCellular contextKinase familyDimer interfaceDimerization modeReceptor dimerizationTyrosine kinasePrimary activator
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