Featured Publications
Microcephalin Is a DNA Damage Response Protein Involved in Regulation of CHK1 and BRCA1 * ♦
Xu X, Lee J, Stern DF. Microcephalin Is a DNA Damage Response Protein Involved in Regulation of CHK1 and BRCA1 * ♦. Journal Of Biological Chemistry 2004, 279: 34091-34094. PMID: 15220350, DOI: 10.1074/jbc.c400139200.Peer-Reviewed Original ResearchMeSH KeywordsBlotting, NorthernBlotting, WesternBRCA1 ProteinCell CycleCell Cycle ProteinsCell LineCheckpoint Kinase 1Cytoskeletal ProteinsDNADNA DamageDown-RegulationG2 PhaseGene Expression RegulationGene Expression Regulation, NeoplasticHistonesHumansMicroscopy, FluorescenceMitosisNerve Tissue ProteinsPhosphorylationPlasmidsPrecipitin TestsProtein KinasesProtein Structure, TertiaryRadiation, IonizingRNA, MessengerRNA, Small InterferingConceptsDNA damage-induced cellular responsesDNA damage response proteinsCellular responsesDamage response proteinsNFBD1/MDC1Regulation of BRCA1Regulation of Chk1Radiation-induced fociEndogenous BRCA1BRCT domainFirst geneResponse proteinsTranscript levelsMCPH1Primary microcephalyProteinMicrocephalinChk1Autosomal recessive diseaseBRCA1RegulationRecessive diseaseMDC1PtcbGenesNFBD1/KIAA0170 Is a Chromatin-associated Protein Involved in DNA Damage Signaling Pathways*
Xu X, Stern DF. NFBD1/KIAA0170 Is a Chromatin-associated Protein Involved in DNA Damage Signaling Pathways*. Journal Of Biological Chemistry 2002, 278: 8795-8803. PMID: 12499369, DOI: 10.1074/jbc.m211392200.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceBase SequenceCell Cycle ProteinsChromatinDNA DamageDNA PrimersDNA ReplicationDNA-Binding ProteinsFluorescent Antibody Technique, IndirectG2 PhaseHeLa CellsHumansMitosisMolecular Sequence DataNuclear ProteinsPhosphorylationSequence Homology, Amino AcidSignal TransductionTrans-ActivatorsConceptsN-terminal FHA domainChromatin-associated proteinsDNA damageDNA Damage Signaling PathwayDNA double-strand breaksDiscrete nuclear fociDNA damage responseNumber of proteinsDouble-strand breaksBRCT domainFHA domainGamma-H2AX fociNuclear fociRad50 fociDamage responseDNA repairNFBD1Signaling pathwaysTandem repeatsProteinNuclear factorUntreated cellsHydroxyurea treatmentPathwayDiffuse nuclear stainingEGF‐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
2005
Global analysis of protein phosphorylation in yeast
Ptacek J, Devgan G, Michaud G, Zhu H, Zhu X, Fasolo J, Guo H, Jona G, Breitkreutz A, Sopko R, McCartney RR, Schmidt MC, Rachidi N, Lee SJ, Mah AS, Meng L, Stark MJ, Stern DF, De Virgilio C, Tyers M, Andrews B, Gerstein M, Schweitzer B, Predki PF, Snyder M. Global analysis of protein phosphorylation in yeast. Nature 2005, 438: 679-684. PMID: 16319894, DOI: 10.1038/nature04187.Peer-Reviewed Original ResearchConceptsProtein phosphorylationBasic cellular processesGlobal phosphorylation networksFirst-generation mapYeast kinasesPhosphorylation networksYeast proteinsCellular processesPhosphorylationKinaseYeastSearchable formatGlobal analysisProteinPrime targetEukaryotesNew resourcesProteomicsOrganismsRegulationPathwayChip technologyTarget
2004
A Ddc2-Rad53 Fusion Protein Can Bypass the Requirements for RAD9 and MRC1 in Rad53 Activation
Lee SJ, Duong JK, Stern DF. A Ddc2-Rad53 Fusion Protein Can Bypass the Requirements for RAD9 and MRC1 in Rad53 Activation. Molecular Biology Of The Cell 2004, 15: 5443-5455. PMID: 15456903, PMCID: PMC532024, DOI: 10.1091/mbc.e04-07-0608.Peer-Reviewed Original ResearchConceptsDNA damageDNA damage checkpoint pathwayFusion proteinDamage checkpoint pathwayRad53p activationRad53 activationMethyl methaneCheckpoint pathwaySignaling systemCell survivalMediator requirementMec1pEssential roleProteinCellsActivationExpressionRad53pRad9pDdc2Rad9Mrc1pMinimal requirementsMrc1OligomerizationEstablishment of a Cell-Free System to Study the Activation of Chk2
Xu X, Stern DF. Establishment of a Cell-Free System to Study the Activation of Chk2. Methods In Molecular Biology 2004, 280: 165-174. PMID: 15187252, DOI: 10.1385/1-59259-788-2:165.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAtaxia Telangiectasia Mutated ProteinsCell Cycle ProteinsCell-Free SystemCheckpoint Kinase 2DNA DamageDNA-Binding ProteinsGenetic VectorsHumansImmunoblottingPlasmidsPrecipitin TestsProtein BiosynthesisProtein Serine-Threonine KinasesRabbitsReticulocytesTranscription, GeneticTriticumTumor Suppressor ProteinsConceptsActivation of Chk2Cell-free systemVitro transcription/translation systemTranscription/translation systemCheckpoint kinase Chk2Rabbit reticulocyte lysateWheat germ extractKinase Chk2Identification of cofactorsReticulocyte lysateChk2Germ extractDNA damageTranslation systemActivationKinaseCofactorProteinATRLysatesPathway
2000
Production of Antibodies That Recognize Specific Tyrosine‐Phosphorylated Peptides
DiGiovanna M, Roussel R, Stern D. Production of Antibodies That Recognize Specific Tyrosine‐Phosphorylated Peptides. Current Protocols In Molecular Biology 2000, 50: 18.6.1-18.6.19. PMID: 18265171, DOI: 10.1002/0471142727.mb1806s50.BooksConceptsAnti-phosphopeptide antibodiesIndividual phosphorylation sitesAnalysis of phosphoproteinsAnti-phosphoamino acid antibodiesPhosphorylation sitesUnphosphorylated proteinTyrosine phosphorylated peptidesCognate proteinPhosphorylated stateParticular proteinAffinity matrixProteinUnique specificityPhosphoproteinFunctional stateDifferential isolationSuch reagentsPhosphotyrosinePeptidesSupport protocolSpeciesAbundanceProduction of antibodiesConventional antibodies
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
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 analysisImmunoprecipitationHeregulin-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
ScSpk1 Spk1 (S. cerevisiae)
Zheng P, Fay D, Stern D. ScSpk1 Spk1 (S. cerevisiae). 1995, 126-127. DOI: 10.1016/b978-012324719-3/50028-5.Peer-Reviewed Original ResearchKinase domainProtein kinaseMluI cell cycle boxS-phase-specific genesS phase-specific expressionPhase-specific genesPhase-specific expressionTyr kinase activitySer/ThrSpecific protein kinasesProtein tyrosine kinasesTranscriptional regulationMutant cellsNuclear proteinsNuclear localizationKinase activitySPK1DNA damageKinaseDNA synthesisProteinRepair synthesisGenesLatter activityImportant role
1992
A 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
Membrane-anchored forms of EGF stimulate focus formation and intercellular communication.
Dobashi Y, Stern DF. Membrane-anchored forms of EGF stimulate focus formation and intercellular communication. Oncogene 1991, 6: 1151-9. PMID: 1861865.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell CommunicationCell LineEpidermal Growth FactorErbB ReceptorsFibroblastsFluorescent Antibody TechniqueGene ExpressionGenes, ImmunoglobulinGenetic VectorsHeLa CellsImmunoblottingMembrane GlycoproteinsMembrane ProteinsPlasmidsProtein Sorting SignalsRatsRecombinant Fusion ProteinsSignal TransductionTransfectionViral Envelope ProteinsConceptsSoluble epidermal growth factorEpidermal growth factorEGF receptorFusion proteinFoci formationFunction of EGFG fusion proteinCytoplasmic domain sequencesMembrane-anchored formRat fibroblastsLarge propeptideTransmembrane domainAutocrine transformationPlasma membraneDomain sequencesExpression systemSoluble proteinForms of EGFIntercellular communicationHeLa cellsNeighboring cellsProteinSmall familyAnchored formCell linesTPA 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 experimentsSerineP185PhosphotyrosineTPAOncogenicMutations
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 ResearchOncogenic 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 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 factorP185ProteinReceptorsMolecular cloning of the neu gene: absence of gross structural alteration in oncogenic alleles.
Hung MC, Schechter AL, Chevray PY, Stern DF, Weinberg RA. Molecular cloning of the neu gene: absence of gross structural alteration in oncogenic alleles. Proceedings Of The National Academy Of Sciences Of The United States Of America 1986, 83: 261-264. PMID: 3001730, PMCID: PMC322837, DOI: 10.1073/pnas.83.2.261.Peer-Reviewed Original ResearchConceptsOncogenic alleleIdentical restriction enzyme patternsOncogene-encoded proteinsDihydrofolate reductase geneNIH 3T3 cellsProtein-encoding regionsCell surface proteinsMethotrexate-resistant coloniesGross structural alterationsRestriction enzyme patternsNeu geneGene clonesMolecular cloningGrowth factor receptorDNA sequencesErbB geneReductase geneGenesSurface proteinsNeu oncogeneFactor receptorMolecular cloneEnzyme patternsProteinP185 protein