Featured Publications
p185, 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
2014
Convergent and Divergent Cellular Responses by ErbB4 Isoforms in Mammary Epithelial Cells
Wali VB, Haskins JW, Gilmore-Hebert M, Platt JT, Liu Z, Stern DF. Convergent and Divergent Cellular Responses by ErbB4 Isoforms in Mammary Epithelial Cells. Molecular Cancer Research 2014, 12: 1140-1155. PMID: 24829397, PMCID: PMC4728083, DOI: 10.1158/1541-7786.mcr-13-0637.Peer-Reviewed Original ResearchConceptsYAP/Hippo pathwayIsogenic MCF10A cellsMultiple structural isoformsAlternative mRNA splicingDivergent cellular responsesChIP-seq experimentsProteases/protease inhibitorsErbB4 isoformsMammary epithelial cellsAssociation of ErbB4Hippo pathwayMRNA splicingNovel molecular targetsTranscriptional profilingDivergent functionsTranscription factorsCYT-1Signaling activitiesMevalonate pathwayCellular responsesLuminal breast cancer cell linesDiverse biologic activitiesMCF10A cellsCYT-2Intracellular isoforms
2011
NFBD1/MDC1 Regulates Cav1 and Cav2 Independently of DNA Damage and p53
Wilson KA, Colavito SA, Schulz V, Wakefield PH, Sessa W, Tuck D, Stern DF. NFBD1/MDC1 Regulates Cav1 and Cav2 Independently of DNA Damage and p53. Molecular Cancer Research 2011, 9: 766-781. PMID: 21551225, PMCID: PMC3901581, DOI: 10.1158/1541-7786.mcr-10-0317.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsAtaxia Telangiectasia Mutated ProteinsCaveolin 1Caveolin 2Cell AdhesionCell Cycle ProteinsCell Line, TumorCells, CulturedChromatinDNA DamageDNA RepairDNA-Binding ProteinsFibroblastsGene Knockdown TechniquesHistonesHumansMiceNuclear ProteinsProtein Serine-Threonine KinasesRNA, MessengerSignal TransductionTrans-ActivatorsTranscription, GeneticTumor Suppressor Protein p53Tumor Suppressor ProteinsConceptsDNA damage checkpoint signalingNFBD1 knockdownDNA damageNFBD1/MDC1Focal adhesion signalingDNA repair factorsDNA damage responseP53-mediated transcriptionAdhesion signalingCheckpoint signalingRepair factorsResponsive transcriptionDamage responseMitogenic signalingNFBD1DNA repairNovel functionTransactivation activityGene pathwaysAtaxia telangiectasiaMicroarray analysisSimilar phenotypeERK phosphorylationGenesTranscription
2005
Regulation of CHK2 by DNA-dependent Protein Kinase*
Li J, Stern DF. Regulation of CHK2 by DNA-dependent Protein Kinase*. Journal Of Biological Chemistry 2005, 280: 12041-12050. PMID: 15668230, DOI: 10.1074/jbc.m412445200.Peer-Reviewed Original ResearchMeSH KeywordsAndrostadienesAntigens, NuclearAtaxia Telangiectasia Mutated ProteinsCell Cycle ProteinsCells, CulturedCheckpoint Kinase 2DNADNA DamageDNA-Activated Protein KinaseDNA-Binding ProteinsEnzyme ActivationHumansKu AutoantigenNuclear ProteinsPhosphorylationProtein Serine-Threonine KinasesTumor Suppressor ProteinsWortmanninConceptsActivation of Chk2DNA-PKChk2 phosphorylationDNA damageDNA-Dependent Protein Kinase Catalytic SubunitProtein Kinase Catalytic SubunitDNA-dependent protein kinaseFunctional DNA-PKRegulation of Chk2Kinase catalytic subunitRegulation of DNAChk2 kinase activityATM-deficient cellsDiverse cellular responsesKinase inhibitor wortmanninATM-defective cellsChk2 activationExposure of cellsCatalytic subunitProtein kinaseKinase activityChk2Inhibitor wortmanninRabbit reticulocytesCellular responsesInteraction of Chromatin-associated Plk1 and Mcm7*
Tsvetkov L, Stern DF. Interaction of Chromatin-associated Plk1 and Mcm7*. Journal Of Biological Chemistry 2005, 280: 11943-11947. PMID: 15654075, DOI: 10.1074/jbc.m413514200.Peer-Reviewed Original ResearchMeSH KeywordsCell Cycle ProteinsCells, CulturedChromatinDNA DamageDNA ReplicationDNA-Binding ProteinsHumansImmunoprecipitationMinichromosome Maintenance Complex Component 3Minichromosome Maintenance Complex Component 7MitosisNuclear ProteinsPhosphorylationProtein KinasesProtein Serine-Threonine KinasesProto-Oncogene ProteinsTranscription FactorsConceptsPolo-box domainEndogenous Plk1Mcm2-7 protein complexPBD of Plk1DNA damage checkpointMultifunctional protein kinaseInteraction of chromatinFull-length Plk1Soluble chromatin fractionMinichromosome maintenance proteinsChromosome segregationMitotic exitDamage checkpointPlk1 interactsMitotic structuresProtein complexesMitotic entryDNA replicationChromatin fractionProtein kinaseMitotic eventsMaintenance proteinsCell cyclePlk1MCM7
2002
Chk2 Activation and Phosphorylation-Dependent Oligomerization
Xu X, Tsvetkov LM, Stern DF. Chk2 Activation and Phosphorylation-Dependent Oligomerization. Molecular And Cellular Biology 2002, 22: 4419-4432. PMID: 12024051, PMCID: PMC133858, DOI: 10.1128/mcb.22.12.4419-4432.2002.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAtaxia Telangiectasia Mutated ProteinsBinding SitesCell Cycle ProteinsCell-Free SystemCells, CulturedCheckpoint Kinase 2DNA DamageDNA-Binding ProteinsEnzyme ActivationFibroblastsGenes, Tumor SuppressorHumansMutationPhosphorylationProtein KinasesProtein Serine-Threonine KinasesProtein Structure, TertiaryRabbitsRadiation, IonizingRecombinant ProteinsSignal TransductionTumor Suppressor ProteinsConceptsSQ/TQ cluster domainsChk2 activationDNA damageDNA damage checkpoint pathwaySerine/threonine kinaseAutophosphorylation of Chk2Phosphorylation-dependent oligomerizationDamage checkpoint pathwayKinase catalytic domainForkhead-associated (FHA) domainWortmannin-sensitive kinaseChk2 kinase activityLimited DNA damageAmino acid substitutionsCell-free systemEukaryotic proteinsFHA domainActive Chk2Threonine kinaseCheckpoint functionCatalytic domainOligomeric complexesCheckpoint pathwayKinase activityChk2
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
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 analysisImmunoprecipitation
1988
Oncogenic 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
Differential responsiveness of myc- and ras-transfected cells to growth factors: selective stimulation of myc-transfected cells by epidermal growth factor.
Stern DF, Roberts AB, Roche NS, Sporn MB, Weinberg RA. Differential responsiveness of myc- and ras-transfected cells to growth factors: selective stimulation of myc-transfected cells by epidermal growth factor. Molecular And Cellular Biology 1986, 6: 870-877. PMID: 3022135, PMCID: PMC367587, DOI: 10.1128/mcb.6.3.870.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, Polyomavirus TransformingAntigens, Viral, TumorCell DivisionCell Transformation, NeoplasticCells, CulturedEpidermal Growth FactorGenesGenes, ViralGrowth SubstancesOncogene Proteins, ViralOncogenesPeptidesPlatelet-Derived Growth FactorPolyomavirusRatsRats, Inbred F344TransfectionTransforming Growth FactorsConceptsEpidermal growth factorPlatelet-derived growth factorExogenous growth factorsSoft agarRas oncogeneGrowth factorEGF-like factorsPresence of PDGFControl cellsAnchorage-independent growthMyc-transfected cellsRas-transfected cellsPresence of EGFLike genesMYCResponsiveness of cellsGrowth factor productionOncogeneAutocrine stimulationNumerous coloniesTGF betaLack of responsivenessGenesSelective stimulationStimulatory effectDevelopment of monoclonal antibodies reactive with the product of the neu oncogene.
Drebin JA, Link VC, Stern DF, Weinberg RA, Greene MI. Development of monoclonal antibodies reactive with the product of the neu oncogene. Symposium On Fundamental Cancer Research 1986, 38: 277-89. PMID: 3749645.Peer-Reviewed Original Research
1985
Type beta transforming growth factor: a bifunctional regulator of cellular growth.
Roberts AB, Anzano MA, Wakefield LM, Roche NS, Stern DF, Sporn MB. Type beta transforming growth factor: a bifunctional regulator of cellular growth. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 119-123. PMID: 3871521, PMCID: PMC396983, DOI: 10.1073/pnas.82.1.119.Peer-Reviewed Original ResearchConceptsGrowth factorEpidermal growth factorColony formationAnchorage-independent growthNRK fibroblastsType betaPlatelet-derived growth factorHuman lung carcinoma cellsLung carcinoma cellsBreast carcinoma cell linesCarcinoma cell linesCellular myc geneLung carcinomaHuman tumor cellsHuman melanomaAnchorage-dependent growthHuman placentaTumor cellsCarcinoma cellsCell cycle timeHuman plateletsCell linesSoft agarTwo-chain polypeptideBifunctional regulator