2018
Regulation of Kinase Activity in the Caenorhabditis elegans EGF Receptor, LET-23
Liu L, Thaker TM, Freed DM, Frazier N, Malhotra K, Lemmon MA, Jura N. Regulation of Kinase Activity in the Caenorhabditis elegans EGF Receptor, LET-23. Structure 2018, 26: 270-281.e4. PMID: 29358026, PMCID: PMC5803352, DOI: 10.1016/j.str.2017.12.012.Peer-Reviewed Original ResearchConceptsLET-23Allosteric activatorEGF receptorAllosteric activation mechanismFull-length receptorCaenorhabditis elegansActive kinaseKinase domainAllosteric activationKinase activityReceptor dimersEGFR kinaseKinaseHuman EGFRDistinct rolesHuman counterpartActivation mechanismActivatorReceptorsElegansHeterodimerizationMutationsCrystal structureRegulationEGFR
2009
ErbB2 resembles an autoinhibited invertebrate epidermal growth factor receptor
Alvarado D, Klein DE, Lemmon MA. ErbB2 resembles an autoinhibited invertebrate epidermal growth factor receptor. Nature 2009, 461: 287-291. PMID: 19718021, PMCID: PMC2762480, DOI: 10.1038/nature08297.Peer-Reviewed Original ResearchErbB2/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
2000
Study of the Regulation of erbB Signaling by Receptor-mediated Endocytosis
Lee A, Lemmon M. Study of the Regulation of erbB Signaling by Receptor-mediated Endocytosis. 2000 DOI: 10.21236/ada383058.Peer-Reviewed Original Research
1997
Regulatory recruitment of signalling molecules to the cell membrane by pleckstrinhomology domains
M.A. L, M. F, J. S, K. F. Regulatory recruitment of signalling molecules to the cell membrane by pleckstrinhomology domains. Trends In Cell Biology 1997, 7: 237-242. PMID: 17708952, DOI: 10.1016/s0962-8924(97)01065-9.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsCell membraneSmall protein modulesPleckstrin homology domainPH domainProtein modulesBiological functionsDiverse processesCertain proteinsSpecific membraneProtein synthesisCell adhesionDNA synthesisProteinMembraneRecent studiesRecruitmentDomainPhosphoinositideEfficient mechanismRegulationPathwayCellsFunctionAdhesion