Featured Publications
The Cellular Response to Neuregulins Is Governed by Complex Interactions of the erbB Receptor Family
Riese D, van Raaij T, Plowman G, Andrews G, Stern D. The Cellular Response to Neuregulins Is Governed by Complex Interactions of the erbB Receptor Family. Molecular And Cellular Biology 1995, 15: 5770-5776. PMID: 7565730, PMCID: PMC230829, DOI: 10.1128/mcb.15.10.5770.Peer-Reviewed Original ResearchConceptsReceptor familyEpidermal growth factor receptor tyrosine kinase familyErbB family receptorsErbB receptor familyReceptor tyrosine kinase familyReceptor tyrosine phosphorylationPeptide agonistsFamily receptorsTyrosine kinase familyHuman cancersReceptor interactionEpidermal growth factor homology domainsCell linesCell survivalReceptorsNeuregulinCellular responsesTyrosine phosphorylationEGF‐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 factorP185ProteinP185neuReceptorsCellsp185, a product of the neu proto-oncogene, is a receptorlike protein associated with tyrosine kinase activity.
Stern DF, Heffernan PA, Weinberg RA. p185, a product of the neu proto-oncogene, is a receptorlike protein associated with tyrosine kinase activity. Molecular And Cellular Biology 1986, 6: 1729-1740. PMID: 2878363, PMCID: PMC367701, DOI: 10.1128/mcb.6.5.1729.Peer-Reviewed Original ResearchConceptsTyrosine kinase activityEGF receptorGrowth factor receptorProto-oncogeneKinase activityNeu proto-oncogeneC-erbB geneFactor receptorPresence of tunicamycinDistinct electrophoretic mobilitiesEpidermal growth factor receptorNormal culture conditionsMajor structural alterationsTyrosine phosphorylationGene productsNeu oncogeneNormal homologsOncogeneCell linesElectrophoretic mobilityCulture conditionsGrowth factorP185ProteinReceptors
1999
Neuregulin activation of ErbB receptors in vascular endothelium leads to angiogenesis
Russell K, Stern D, Polverini P, Bender J. Neuregulin activation of ErbB receptors in vascular endothelium leads to angiogenesis. American Journal Of Physiology 1999, 277: h2205-h2211. PMID: 10600838, DOI: 10.1152/ajpheart.1999.277.6.h2205.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCells, CulturedCorneaEndothelial Growth FactorsEndothelium, VascularErbB ReceptorsHumansLymphokinesMiceNeovascularization, PhysiologicNeuregulinsRatsReceptor, ErbB-2Receptor, ErbB-3Receptor, ErbB-4ThrombinUmbilical VeinsVascular Endothelial Growth Factor AVascular Endothelial Growth FactorsConceptsHuman umbilical vein endothelial cellsVascular endotheliumErbB receptorsReceptor tyrosine phosphorylationStimulation of HUVECsRapid calcium fluxReceptor family membersEndothelial cell growth factorTransmembrane tyrosine kinase receptorVascular endothelial cell growth factorEndothelial cell signalingReceptor-ligand interactionsTyrosine kinase receptorsEpidermal growth factor receptorVascular endothelial growthCell growth factorUmbilical vein endothelial cellsCell signalingGrowth factor receptorTyrosine phosphorylationVivo angiogenic responseExpression patternsGrowth regulationVein endothelial cellsIntracellular signaling
1997
Cripto Enhances the Tyrosine Phosphorylation of Shc and Activates Mitogen-activated Protein Kinase (MAPK) in Mammary Epithelial Cells*
Kannan S, De Santis M, Lohmeyer M, David J, Smith G, Hynes N, Seno M, Brandt R, Bianco C, Persico G, Kenney N, Normanno N, Martinez-Lacaci I, Ciardiello F, Stern D, Gullick W, Salomon D. Cripto Enhances the Tyrosine Phosphorylation of Shc and Activates Mitogen-activated Protein Kinase (MAPK) in Mammary Epithelial Cells*. Journal Of Biological Chemistry 1997, 272: 3330-3335. PMID: 9013573, DOI: 10.1074/jbc.272.6.3330.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding, CompetitiveBreast NeoplasmsCalcium-Calmodulin-Dependent Protein KinasesEnzyme ActivationEpidermal Growth FactorEpitheliumFemaleGPI-Linked ProteinsGrowth SubstancesHumansIntercellular Signaling Peptides and ProteinsMammary Glands, AnimalMembrane GlycoproteinsMiceMitogen-Activated Protein Kinase 1Neoplasm ProteinsPhosphorylationProtein-Tyrosine KinasesSrc Homology DomainsTumor Cells, CulturedTyrosineConceptsTyrosine phosphorylationHC-11 cellsMammary epithelial cellsErb BCripto-1Ras/Raf/MEK/MAPK pathwayTyrosine kinaseRaf/MEK/MAPK pathwayMitogen-activated protein kinase activityMEK/MAPK pathwayHC-11 mouse mammary epithelial cellsEpithelial cellsMouse mammary epithelial cellsProtein kinase activityTyrosine-phosphorylated ShcReceptor tyrosine kinasesDifferent human breast cancer cell linesSKBR-3 breast cancer cellsType 1 receptor tyrosine kinasesEGF-like growth factorHuman breast cancer cell linesEpidermal growth factor (EGF) familyBreast cancer cell linesActivates MitogenGrowth factor family
1996
Endothelial Nitric Oxide Synthase Is Regulated by Tyrosine Phosphorylation and Interacts with Caveolin-1*
García-Cardeña G, Fan R, Stern D, Liu J, Sessa W. Endothelial Nitric Oxide Synthase Is Regulated by Tyrosine Phosphorylation and Interacts with Caveolin-1*. Journal Of Biological Chemistry 1996, 271: 27237-27240. PMID: 8910295, DOI: 10.1074/jbc.271.44.27237.Peer-Reviewed Original ResearchConceptsNovel regulatory mechanismTyrosine phosphorylationCaveolin-1Bovine aortic endothelial cellsRegulatory mechanismsProtein tyrosine phosphatase inhibitorCaveolin-interacting proteinsPhosphoamino acid analysisTyrosine phosphatase inhibitorTreatment of BAECBovine lung microvascular endothelial cellsEndothelial nitric oxide synthaseSubcellular traffickingPhosphatase inhibitorCoat proteinEndothelial cellsMetabolic labelingSodium orthovanadatePhosphorylationCaveolaeAortic endothelial cellsLung microvascular endothelial cellsProteinAcid analysisImmunoprecipitationThe 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 patternType 1 receptor tyrosine kinases are differentially phosphorylated in mammary carcinoma and differentially associated with steroid receptors.
Bacus SS, Chin D, Yarden Y, Zelnick CR, Stern DF. Type 1 receptor tyrosine kinases are differentially phosphorylated in mammary carcinoma and differentially associated with steroid receptors. American Journal Of Pathology 1996, 148: 549-58. PMID: 8579117, PMCID: PMC1861670.Peer-Reviewed Original ResearchMeSH KeywordsBiomarkers, TumorBreast NeoplasmsErbB ReceptorsFemaleFrozen SectionsGenes, erbB-2HumansImmunohistochemistryPhosphorylationPhosphotyrosinePrognosisProto-Oncogene MasReceptor Protein-Tyrosine KinasesReceptor, ErbB-2Receptor, ErbB-4Receptors, EstrogenReceptors, ProgesteroneReceptors, SteroidRetrospective StudiesConceptsMammary carcinomaReceptor tyrosine kinasesType 1 receptor tyrosine kinasesMammary carcinoma patientsType 1 receptorExpression of neuAnti-neu antibodyEpidermal growth factor receptorGrowth factor receptorTyrosine kinaseCarcinoma patientsPrognostic factorsPoor prognosisClinical evaluationTherapeutic strategiesCarcinomaHER-4Frozen sectionsSteroid receptorsNeu/ErbBNeuFactor receptorReceptorsDifferent biological activitiesTyrosine phosphorylation
1991
TPA inhibits the tyrosine kinase activity of the neu protein in vivo and in vitro.
Cao H, Decker S, Stern DF. TPA inhibits the tyrosine kinase activity of the neu protein in vivo and in vitro. Oncogene 1991, 6: 705-11. PMID: 1675782.Peer-Reviewed Original ResearchConceptsImmune complex kinase assayReceptor-like proteinTyrosine kinase activityProtein kinase CThreonine phosphorylationThreonine residuesTransmembrane domainKinase assaysTyrosine phosphorylationKinase activityAntiphosphotyrosine antibodyIncubation of cellsKinase CPhosphorylationPoint mutationsProteinNeu/Neu proteinLabeling experimentsSerineP185PhosphotyrosineTPAOncogenicMutationsSpk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine.
Stern DF, Zheng P, Beidler DR, Zerillo C. Spk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine. Molecular And Cellular Biology 1991, 11: 987-1001. PMID: 1899289, PMCID: PMC359764, DOI: 10.1128/mcb.11.2.987.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBinding SitesCell Cycle ProteinsCheckpoint Kinase 2Cloning, MolecularEscherichia coliFungal ProteinsGene LibraryGenes, FungalImmunoblottingMolecular Sequence DataProtein KinasesProtein Serine-Threonine KinasesProtein-Tyrosine KinasesRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Nucleic AcidSerineSubstrate SpecificityThreonineTyrosineConceptsSerine/threonine kinaseProtein kinaseFusion proteinThreonine kinaseTyrosine phosphorylationGlutathione S-transferase fusion proteinCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseSerine protein kinaseSerine/threonineCalmodulin-dependent protein kinase IICalcium/calmodulin-dependent protein kinase IITyrosine protein kinaseOpen reading frameProtein kinase IILambda gt11 libraryPutative kinaseNew kinasesThreonine phosphorylationCatalytic subunitSaccharomyces cerevisiaeBacterial proteinsReading frameAntiphosphotyrosine antibodyKinase II
1988
Oncogenic Activation of p185 neu Stimulates Tyrosine Phosphorylation In Vivo
Stern D, Kamps M, Cao H. Oncogenic Activation of p185 neu Stimulates Tyrosine Phosphorylation In Vivo. Molecular And Cellular Biology 1988, 8: 3969-3973. DOI: 10.1128/mcb.8.9.3969-3973.1988.Peer-Reviewed Original ResearchOncogenic activation of p185neu stimulates tyrosine phosphorylation in vivo.
Stern DF, Kamps MP, Cao H. Oncogenic activation of p185neu stimulates tyrosine phosphorylation in vivo. Molecular And Cellular Biology 1988, 8: 3969-3973. PMID: 2464744, PMCID: PMC365461, DOI: 10.1128/mcb.8.9.3969.Peer-Reviewed Original Research
1986
p185, a Product of the neu Proto-Oncogene, Is a Receptorlike Protein Associated with Tyrosine Kinase Activity
Stern D, Heffernan P, Weinberg R. p185, a Product of the neu Proto-Oncogene, Is a Receptorlike Protein Associated with Tyrosine Kinase Activity. Molecular And Cellular Biology 1986, 6: 1729-1740. DOI: 10.1128/mcb.6.5.1729-1740.1986.Peer-Reviewed Original ResearchTyrosine kinase activityEGF receptorGrowth factor receptorProto-oncogeneKinase activityNeu proto-oncogeneC-erbB geneFactor receptorPresence of tunicamycinDistinct electrophoretic mobilitiesEpidermal growth factor receptorNormal culture conditionsMajor structural alterationsTyrosine phosphorylationGene productsNeu oncogeneNormal homologsOncogeneCell linesElectrophoretic mobilityCulture conditionsGrowth factorP185ProteinReceptorsp185, a Product of the neu Proto-Oncogene, Is a Receptorlike Protein Associated with Tyrosine Kinase Activity
Stern D, Heffernan P, Weinberg R. p185, a Product of the neu Proto-Oncogene, Is a Receptorlike Protein Associated with Tyrosine Kinase Activity. Molecular And Cellular Biology 1986, 6: 1729-1740. DOI: 10.1128/mcb.6.5.1729-1740.1986.Peer-Reviewed Original ResearchEpidermal growth factorTyrosine kinase activityEpidermal growth factor receptorNeu proto-oncogeneAssociated with tyrosine kinase activityProto-oncogeneKinase activityNeu oncogenePresence of tunicamycinTyrosine phosphorylationNormal culture conditionsGene productsC-erbB geneMutated versionGrowth factorTransformed counterpartsGrowth factor receptorCell linesStimulated degradationElectrophoretic mobilityC-erbBCulture conditionsOncogeneGenesP185