2023
EPIREGULIN creates a developmental niche for spatially organized human intestinal enteroids
Childs C, Holloway E, Sweet C, Tsai Y, Wu A, Vallie A, Eiken M, Capeling M, Zwick R, Palikuqi B, Trentesaux C, Wu J, Pellon-Cardenas O, Zhang C, Glass I, Loebel C, Yu Q, Camp J, Sexton J, Klein O, Verzi M, Spence J. EPIREGULIN creates a developmental niche for spatially organized human intestinal enteroids. JCI Insight 2023, 8: e165566. PMID: 36821371, PMCID: PMC10070114, DOI: 10.1172/jci.insight.165566.Peer-Reviewed Original ResearchConceptsHuman intestineHuman intestinal enteroidsEGF family membersIntestinal transcription factor CDX2Chromatin landscapeHuman cryptsTranscription factor CDX2Stem cell functionIntestinal enteroidsBiological discoveryCellular differentiationStandard culture conditionsNiche cuesEpithelial developmentEnteroidsEGFCrypt domainsOrgans in vitroPersonalized medicineCentral lumenCulture conditionsCell functionNiche in vitroSpatial organizationEGF in vitro
2015
EGFR mutations cause a lethal syndrome of epithelial dysfunction with progeroid features
Ganetzky R, Finn E, Bagchi A, Zollo O, Conlin L, Deardorff M, Harr M, Simpson MA, McGrath JA, Zackai E, Lemmon MA, Sondheimer N. EGFR mutations cause a lethal syndrome of epithelial dysfunction with progeroid features. Molecular Genetics & Genomic Medicine 2015, 3: 452-458. PMID: 26436111, PMCID: PMC4585453, DOI: 10.1002/mgg3.156.Peer-Reviewed Original ResearchEpidermal growth factor receptorExtracellular domainEpidermal growth factor signalingGrowth factor signalingPatient-derived fibroblastsBinding of EGFExtracellular signalsGrowth factor receptorEarly senescenceFactor signalingDownstream targetsOncogenic transformationTissue developmentTyrosine kinaseConstitutive activationReceptor phosphorylationLarge familyFactor receptorProgeroid featuresAccelerated expressionMutationsΒ-galactosidaseEGFEGFR genotypeActivationNetwork-based identification of feedback modules that control RhoA activity and cell migration
Kim TH, Monsefi N, Song JH, von Kriegsheim A, Vandamme D, Pertz O, Kholodenko BN, Kolch W, Cho KH. Network-based identification of feedback modules that control RhoA activity and cell migration. Journal Of Molecular Cell Biology 2015, 7: 242-252. PMID: 25780058, DOI: 10.1093/jmcb/mjv017.Peer-Reviewed Original ResearchConceptsRho family GTPasesCancer cell migrationCell migrationRhoA activityControl cell migrationBoolean network modelNetwork-based identificationPotential new targetsRho activationGTPasesSrc inhibitionGenetic backgroundCsk inhibitionMost cancer deathsActivation stateNew targetsNew insightsMigrationCskSrcFAKRewiringInhibitionEGFProtrusion
1998
Epidermal Growth Factor Receptor and the Adaptor Protein p52Shc Are Specific Substrates of T-Cell Protein Tyrosine Phosphatase
Tiganis T, Bennett A, Ravichandran K, Tonks N. Epidermal Growth Factor Receptor and the Adaptor Protein p52Shc Are Specific Substrates of T-Cell Protein Tyrosine Phosphatase. Molecular And Cellular Biology 1998, 18: 1622-1634. PMID: 9488479, PMCID: PMC108877, DOI: 10.1128/mcb.18.3.1622.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAnimalsBinding SitesCalcium-Calmodulin-Dependent Protein KinasesCell NucleusCOS CellsCytoplasmEndoplasmic ReticulumEpidermal Growth FactorErbB ReceptorsGRB2 Adaptor ProteinHeLa CellsHumansMiceMitogen-Activated Protein Kinase 1MutagenesisPhosphorylationPhosphotyrosineProtein Tyrosine Phosphatase, Non-Receptor Type 2Protein Tyrosine PhosphatasesProteinsProtein-Tyrosine KinasesShc Signaling Adaptor ProteinsSrc Homology 2 Domain-Containing, Transforming Protein 1Substrate SpecificityTyrosineConceptsT-cell protein tyrosine phosphataseSubstrate-trapping mutantEpidermal growth factor receptorProtein tyrosine phosphatasePTyr proteinsTyrosine phosphataseGrowth factor receptorPTP active siteTyrosine phosphorylated proteinsEGF-induced activationFactor receptorAlternative splicingCellular contextCOS cellsP52ShcNuclear formTC45Endoplasmic reticulumCatalytic acidSpecific substratesProteinMutantsComplex formationSpecific sitesEGF
1997
Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation
Burke C, Lemmon M, Coren B, Engelman D, Stern D. Dimerization of the p185neu transmembrane domain is necessary but not sufficient for transformation. Oncogene 1997, 14: 687-696. PMID: 9038376, DOI: 10.1038/sj.onc.1200873.Peer-Reviewed Original ResearchConceptsReceptor tyrosine kinasesTransmembrane domainEpidermal growth factor receptorSignal transductionWild-type domainSecond-site mutationsPosition 664Dimerization domainGrowth factor receptorTyrosine kinaseGlycophorin AFactor receptorValine substitutionDimerizationMutationsTransductionGlutamic acidDomainWeak dimerizationMutantsKinaseSignalingProteinEGFChimeras
1996
The Epidermal Growth Factor Receptor Couples Transforming Growth Factor-α, Heparin-binding Epidermal Growth Factor-like Factor, and Amphiregulin to Neu, ErbB-3, and ErbB-4*
Riese D, Kim E, Elenius K, Buckley S, Klagsbrun M, Plowman G, Stern D. The Epidermal Growth Factor Receptor Couples Transforming Growth Factor-α, Heparin-binding Epidermal Growth Factor-like Factor, and Amphiregulin to Neu, ErbB-3, and ErbB-4*. Journal Of Biological Chemistry 1996, 271: 20047-20052. PMID: 8702723, DOI: 10.1074/jbc.271.33.20047.Peer-Reviewed Original ResearchMeSH KeywordsAmphiregulinAnimalsCell DivisionCell LineCell SurvivalEGF Family of ProteinsEpidermal Growth FactorErbB ReceptorsGlycoproteinsGrowth SubstancesHeparin-binding EGF-like Growth FactorIntercellular Signaling Peptides and ProteinsInterleukin-3MicePhosphorylationPhosphotyrosineProto-Oncogene ProteinsReceptor Protein-Tyrosine KinasesReceptor, ErbB-2Receptor, ErbB-3Receptor, ErbB-4Recombinant ProteinsSignal TransductionTransforming Growth Factor alphaConceptsHeparin-binding EGF-like growth factorErbB family receptorsPhysiologic responsesReceptor tyrosine phosphorylationFamily receptorsGrowth factorEpidermal growth factor (EGF) familyBa/F3 cell lineEpidermal growth factor-like factorsCell linesEGF-like growth factorGrowth factor familyTGF-alphaReceptor couplingReceptors coupleHuman malignanciesAmphiregulinTyrosine phosphorylationEGF familyErbB-3ErbB-4ReceptorsStimulationEGFSimilar patternHeregulin-Induced Growth Factor Receptor Signaling and Breast Carcinogenesis.
Riese D, Stern D. Heregulin-Induced Growth Factor Receptor Signaling and Breast Carcinogenesis. 1996 DOI: 10.21236/ada315700.Peer-Reviewed Original ResearchErbB family receptorsCellular signaling proteinsGrowth factor receptor signalingFamily receptorsBa/F3 cell lineCell linesEGF-like growth factorNeu differentiation factorEpidermal growth factor (EGF) familyGrowth factor familySignaling proteinsFactor familyGrowth factor alphaCellular responsesReceptor phosphorylationReceptor signalingErbB familyDistinct activitiesPairwise combinationsDifferentiation factorEGFBetacellulinHeregulinGrowth factorProtein
1995
Inhibition of ligand-induced activation of epidermal growth factor receptor tyrosine phosphorylation by curcumin
Korutla L, Cheung J, Medelsohn J, Kumar R. Inhibition of ligand-induced activation of epidermal growth factor receptor tyrosine phosphorylation by curcumin. Carcinogenesis 1995, 16: 1741-1745. PMID: 7634398, DOI: 10.1093/carcin/16.8.1741.Peer-Reviewed Original ResearchConceptsGrowth stimulatory pathwaysTumor cell growthTime-dependent mannerAnti-proliferative strategyTyrosine phosphorylationEpidermal growth factorEpidermal growth factor receptor tyrosine phosphorylationCurcumin treatmentActivation of EGFCalcium releaseStimulatory pathwayReceptor tyrosine phosphorylationTreatment of cellsEGF receptor phosphorylationKinase inhibitorsGrowth factorSurface expressionReceptor phosphorylationHuman EGFCurcuminEGFInhibition of EGFPotent inhibitorActivationCell growth
1992
Colocalization of transforming growth factor-α and a functional epidermal growth factor receptor (EGFR) to the inner cell mass and preferential localization of the EGFR on the basolateral surface of the trophectoderm in the mouse blastocyst
Dardik A, Smith R, Schultz R. Colocalization of transforming growth factor-α and a functional epidermal growth factor receptor (EGFR) to the inner cell mass and preferential localization of the EGFR on the basolateral surface of the trophectoderm in the mouse blastocyst. Developmental Biology 1992, 154: 396-409. PMID: 1426645, DOI: 10.1016/0012-1606(92)90078-u.Peer-Reviewed Original ResearchConceptsEpidermal growth factor receptorFunctional epidermal growth factor receptorTGF-alphaAnti-EGFR antibodiesGrowth factor receptorParacrine roleBasolateral surfaceInner cell massCell massPotential autocrineMouse blastocystsGrowth factorFactor receptorImmunoelectron microscopy studiesReceptorsBlastocyst developmentTE cellsOvernight cultureEGF treatmentPolar trophectodermEGF receptorMouse preimplantation embryosBlastocystsAcid-insoluble materialEGFIndependent modulation of enterocyte migration and proliferation by growth factors, matrix proteins, and pharmacologic agents in an in vitro model of mucosal healing.
Basson M, Modlin I, Flynn S, Jena B, Madri J. Independent modulation of enterocyte migration and proliferation by growth factors, matrix proteins, and pharmacologic agents in an in vitro model of mucosal healing. Surgery 1992, 112: 299-307; discussion 307-8. PMID: 1353641.Peer-Reviewed Original ResearchConceptsMucosal healingPharmacologic agentsGrowth factorEGF-stimulated proliferationCaco-2 enterocytesHuman Caco-2 enterocytesInhibited basalAlpha 2 integrin subunitMatrix proteinsEnterocyte migrationCollagen IInhibitor genisteinIntegrin subunitsHealingIndomethacinProliferationTyrosine kinaseEGFLamininBasalGenisteinAltered organizationIndependent modulationChanges in camp phosphodiesterase activity and cAMP concentration during mouse preimplantation development
Dardik A, Schultz R. Changes in camp phosphodiesterase activity and cAMP concentration during mouse preimplantation development. Molecular Reproduction And Development 1992, 32: 349-353. PMID: 1323307, DOI: 10.1002/mrd.1080320407.Peer-Reviewed Original ResearchConceptsTGF-alpha/EGFMid-blastocyst stageBlastocoel expansionBlastocyst stageMouse preimplantation developmentMouse preimplantation embryosTGF-alphaPreimplantation developmentCAMP concentrationCell shapePreimplantation embryosElevation of cAMPCell typesPhosphodiesterase activityEmbryo volumeIntracellular volumeEmbryosCAMP levelsEGF
1991
Deletion-mutant epidermal growth factor receptor in human gliomas: Effect of type II mutation on receptor function
Humphrey P, Gangarosa L, Wong A, Archer G, Lund-Johansen M, Bjerkvig R, Laerum O, Friedman H, Bigner D. Deletion-mutant epidermal growth factor receptor in human gliomas: Effect of type II mutation on receptor function. Biochemical And Biophysical Research Communications 1991, 178: 1413-1420. PMID: 1678600, DOI: 10.1016/0006-291x(91)91051-d.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCell LineChromosome DeletionEpidermal Growth FactorErbB ReceptorsGene AmplificationGene RearrangementGliomaHumansKineticsMolecular Sequence DataPhosphorylationProtein-Tyrosine KinasesProto-Oncogene MasProto-Oncogene ProteinsProto-OncogenesReceptor, ErbB-2Transforming Growth Factor alphaConceptsEGFR kinase activityMutant EGFRDeletion-mutant epidermal growth factor receptorGrowth factor receptor geneMutant EGFR proteinEpidermal growth factor receptorGrowth factorFactor receptor geneEpidermal growth factor receptor (EGFR) geneGrowth factor receptorKinase activityExtracellular domainGlioma cell proliferationDomain IVFrame deletionType II mutationAmino acidsEGFR proteinFactor receptorReceptor geneThree-dimensional spheroid modelCell proliferationReceptor functionEGFHuman gliomas
1988
EGF‐stimulated tyrosine phosphorylation of p185neu: a potential model for receptor interactions.
Stern DF, Kamps MP. EGF‐stimulated tyrosine phosphorylation of p185neu: a potential model for receptor interactions. The EMBO Journal 1988, 7: 995-1001. PMID: 3261240, PMCID: PMC454426, DOI: 10.1002/j.1460-2075.1988.tb02906.x.Peer-Reviewed Original ResearchConceptsEGF-stimulated tyrosine phosphorylationTyrosine phosphorylationEGF receptorKinase activityReceptor-like proteinEGF receptor kinaseIntrinsic kinase activityRat-1 cellsTyrosine kinase activityEpidermal growth factor receptorReceptor kinaseGrowth factor receptorIncubation of cellsPhosphorylationEGFNeu/Factor receptorReceptor interactionSimilar kineticsGrowth factorP185ProteinP185neuReceptorsCells
1984
DO EGF AND GLUCOCORTICOIDS ACT AT THE SAME METABOLIC SITES IN FETAL RAT LUNG?
Gross I, Dynia D. DO EGF AND GLUCOCORTICOIDS ACT AT THE SAME METABOLIC SITES IN FETAL RAT LUNG? Pediatric Research 1984, 18: 392-392. DOI: 10.1203/00006450-198404001-01797.Peer-Reviewed Original ResearchFetal rat lungCholine incorporationEffect of EGFRat lungFetal lung maturationEffect of DexDose-dependent fashionMetabolic sitesGestational ageLung maturationOrgan culture systemFetal lungGlucocorticoids actSerum-free organ culture systemMaximal effectDistribution of radioactivityThymidine incorporationMouse skinLungDependent fashionBiochemical developmentPhosphatidylglycerol fractionT3T4 actionEGF
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply