Featured Publications
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 ResearchMeSH KeywordsAmino AcidsAnimalsAntibodies, MonoclonalCell LineEpidermal Growth FactorErbB ReceptorsGenesModels, BiologicalPhosphorylationProtein-Tyrosine KinasesProto-OncogenesTyrosineConceptsEGF-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
2000
Tyrosine kinase signalling in breast cancer: ErbB family receptor tyrosine kinases
Stern D. Tyrosine kinase signalling in breast cancer: ErbB family receptor tyrosine kinases. Breast Cancer Research 2000, 2: 176. PMID: 11250707, PMCID: PMC138772, DOI: 10.1186/bcr51.Peer-Reviewed Original ResearchMeSH KeywordsAntibodies, MonoclonalAntibodies, Monoclonal, HumanizedBiomarkersBreast NeoplasmsEpidermal Growth FactorErbB ReceptorsFemaleGene AmplificationGene Expression Regulation, DevelopmentalGene Expression Regulation, NeoplasticGenes, erbBHumansProtein-Tyrosine KinasesReceptor, ErbB-2Signal TransductionTranscriptional ActivationTransforming Growth FactorsTrastuzumabConceptsBreast cancerErbB family receptor tyrosine kinasesReceptor tyrosine kinasesHER2/neuTyrosine kinaseEpidermal growth factor receptorGrowth factor receptorClinical trialsSteroid receptorsTherapeutic antibodiesErbB-2Factor receptorReceptorsCancerPhysiological regulatorSignificant subsetFamily membersKinaseOptimal useNeuHormoneTrialsAntibodiesHerceptin
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
1992
An extra cysteine proximal to the transmembrane domain induces differential cross-linking of p185neu and p185neu.
Cao H, Bangalore L, Dompé C, Bormann BJ, Stern DF. An extra cysteine proximal to the transmembrane domain induces differential cross-linking of p185neu and p185neu. Journal Of Biological Chemistry 1992, 267: 20489-20492. PMID: 1356980, DOI: 10.1016/s0021-9258(19)88728-8.Peer-Reviewed Original ResearchA subdomain in the transmembrane domain is necessary for p185neu* activation.
Cao H, Bangalore L, Bormann BJ, Stern DF. A subdomain in the transmembrane domain is necessary for p185neu* activation. The EMBO Journal 1992, 11: 923-932. PMID: 1347745, PMCID: PMC556533, DOI: 10.1002/j.1460-2075.1992.tb05131.x.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnimalsBase SequenceBlotting, WesternCell MembraneElectrophoresis, Polyacrylamide GelErbB ReceptorsGliomaGlutamatesGlutamic AcidMiceMolecular Sequence DataMutagenesis, Site-DirectedNeuroblastomaPrecipitin TestsProtein-Tyrosine KinasesProto-Oncogene ProteinsRatsReceptor, ErbB-2Signal TransductionValineConceptsTransmembrane domainTyrosine kinase activityKinase activityElevated tyrosine kinase activitySite-directed mutagenesisSpecific amino acidsEpidermal growth factor receptorGlutamic acidGrowth factor receptorEGF receptorPrimary structureAmino acidsFactor receptorProteinSpecific interactionsActivationDomainMutagenesisReceptorsMolecular weightAcidNeu proteinP185neuHigh propensityRole
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
1990
The epidermal growth factor receptor and the product of the neu protooncogene are members of a receptor tyrosine phosphorylation cascade.
Connelly PA, Stern DF. The epidermal growth factor receptor and the product of the neu protooncogene are members of a receptor tyrosine phosphorylation cascade. Proceedings Of The National Academy Of Sciences Of The United States Of America 1990, 87: 6054-6057. PMID: 1974718, PMCID: PMC54470, DOI: 10.1073/pnas.87.16.6054.Peer-Reviewed Original ResearchTyrosine phosphorylation is an early and specific event involved in primary keratinocyte differentiation.
Filvaroff E, Stern DF, Dotto GP. Tyrosine phosphorylation is an early and specific event involved in primary keratinocyte differentiation. Molecular And Cellular Biology 1990, 10: 1164-1173. PMID: 1689456, PMCID: PMC360987, DOI: 10.1128/mcb.10.3.1164.Peer-Reviewed Original Research
1989
The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain
Shaw A, Amrein K, Hammond C, Stern D, Sefton B, Rose J. The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain. Cell 1989, 59: 627-636. PMID: 2582490, DOI: 10.1016/0092-8674(89)90008-1.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCD4 AntigensCytoplasmHeLa CellsHumansLymphocyte Specific Protein Tyrosine Kinase p56(lck)Macromolecular SubstancesMembrane GlycoproteinsMolecular Sequence DataMutationOligonucleotide ProbesPhosphoproteinsPlasmidsProtein BindingProtein MultimerizationProtein-Tyrosine KinasesT-LymphocytesTransfectionConceptsAmino-terminal domainCytoplasmic domainTyrosine protein kinase p56lckUnique amino-terminal domainT cell-specific proteinsTyrosine protein kinaseSpecific transmembrane proteinsCell-specific proteinsIntracellular tyrosine kinaseAmino-terminal residuesCarboxy-terminal residuesTransmembrane proteinCytoplasmic tailSrc familyProtein kinaseKinase p56lckTyrosine kinaseHeLa cellsCell surfaceProteinDeleted formsSurface glycoproteinP56lckKinaseResidues
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