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 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
2008
NFBD1/MDC1, 53BP1 and BRCA1 have both redundant and unique roles in the ATM pathway
Wilson KA, Stern DF. NFBD1/MDC1, 53BP1 and BRCA1 have both redundant and unique roles in the ATM pathway. Cell Cycle 2008, 7: 3584-3594. PMID: 19001859, PMCID: PMC2763172, DOI: 10.4161/cc.7.22.7102.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAtaxia Telangiectasia Mutated ProteinsBRCA1 ProteinCell Cycle ProteinsCell LineCheckpoint Kinase 2DNA-Binding ProteinsFibroblastsHumansIntracellular Signaling Peptides and ProteinsNuclear ProteinsPhosphorylationProtein Serine-Threonine KinasesRadiation, IonizingRNA, Small InterferingTrans-ActivatorsTumor Suppressor p53-Binding Protein 1Tumor Suppressor ProteinsConceptsNFBD1/MDC1DNA damage checkpoint proteinsRadiation-induced phosphorylationATM-Chk2 pathwayNormal genetic backgroundBRCT domainCheckpoint responseRedundant functionsPrimary human cellsRedundant rolesATM pathwayNFBD1Checkpoint proteinsMouse cellsHuman cellsGenetic backgroundMDC1Cancer cellsLocalization eventsPhosphorylationBRCA1Unique rolePathwayCellsHuman foreskin
2005
Activation of the Checkpoint Kinase Rad53 by the Phosphatidyl Inositol Kinase-like Kinase Mec1*
Ma JL, Lee SJ, Duong JK, Stern DF. Activation of the Checkpoint Kinase Rad53 by the Phosphatidyl Inositol Kinase-like Kinase Mec1*. Journal Of Biological Chemistry 2005, 281: 3954-3963. PMID: 16365046, DOI: 10.1074/jbc.m507508200.Peer-Reviewed Original ResearchConceptsPhosphorylation-dependent mechanismDNA damageKinase activityDNA replication checkpoint pathwayRad53 kinase activityCheckpoint kinase Rad53Essential protein kinaseReplication checkpoint pathwayActivation of Rad53Protein kinase activityMammalian Chk2Rad53 phosphorylationRad53 activationRad53Protein kinaseDownstream responsesCheckpoint pathwayOrthologsAutophosphorylationKinasePhosphorylationIntermolecular mechanismActivationPIKKsComplexesGlobal 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 technologyTargetPhosphoproteomics for oncology discovery and treatment
Stern DF. Phosphoproteomics for oncology discovery and treatment. Expert Opinion On Therapeutic Targets 2005, 9: 851-860. PMID: 16083347, DOI: 10.1517/14728222.9.4.851.Peer-Reviewed Original ResearchConceptsPhosphoproteomic analysisProtein phosphorylationReversible protein phosphorylationSignal transduction pathwaysCellular regulationProtein kinaseTransduction pathwaysHuman cancersDevelopment of drugsPathwayPhosphorylationGood targetImportant insightsCancer therapyCancer drugsPhosphoproteomicsCellsIndividual tumorsPowerful toolKinaseRegulationIntermediary levelDiscoveryTargetIdentification
1999
Erbb4 Signaling in the Mammary Gland Is Required for Lobuloalveolar Development and Stat5 Activation during Lactation
Jones F, Welte T, Fu X, Stern D. Erbb4 Signaling in the Mammary Gland Is Required for Lobuloalveolar Development and Stat5 Activation during Lactation. Journal Of Cell Biology 1999, 147: 77-88. PMID: 10508857, PMCID: PMC2164978, DOI: 10.1083/jcb.147.1.77.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell LineCell NucleusDNA-Binding ProteinsErbB ReceptorsFemaleGene Expression Regulation, DevelopmentalHumansLactationMammary Glands, AnimalMiceMice, TransgenicMilk ProteinsPhosphorylationPrecipitin TestsPregnancyReceptor, ErbB-4RNA, MessengerSequence DeletionSignal TransductionSrc Homology DomainsSTAT5 Transcription FactorTrans-ActivatorsTransgenesConceptsFunction of ErbB4Dominant-negative alleleMammary glandAlpha-lactalbumin mRNAEpidermal growth factor receptor familyBeta-casein mRNAGrowth factor receptor familyNormal mouse mammary glandMouse mammary glandSH2 domainFactor receptor familyTerminal differentiationProtein mRNAReceptor familyLobuloalveolar developmentAcidic protein mRNASitu hybridizationMammary developmentPhosphorylationErbB4MRNALobuloalveoliUnique responseExpressionImportant role
1998
Rad53 FHA Domain Associated with Phosphorylated Rad9 in the DNA Damage Checkpoint
Sun Z, Hsiao J, Fay D, Stern D. Rad53 FHA Domain Associated with Phosphorylated Rad9 in the DNA Damage Checkpoint. Science 1998, 281: 272-274. PMID: 9657725, DOI: 10.1126/science.281.5374.272.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCell Cycle ProteinsCheckpoint Kinase 2DNA DamageDNA ReplicationFungal ProteinsG2 PhaseHydroxyureaMethyl MethanesulfonateMitosisMutationOligopeptidesPeptidesPhosphorylationProtein KinasesProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription, GeneticConceptsRad53 phosphorylationRad53 protein kinaseDNA damage signalsDNA damage checkpointProtein-binding domainsCell cycle phase arrestRNR3 transcriptionRad9 proteinFHA domainDamage checkpointG2/M cell cycle phase arrestCell divisionProtein kinaseSaccharomyces cerevisiaeDamage signalsRad9DNA damageRad53Phase arrestPhosphorylationCheckpointDomainCerevisiaeTranscriptionKinase
1997
A role for DNA primase in coupling DNA replication to DNA damage response
Marini F, Pellicioli A, Paciotti V, Lucchini G, Plevani P, Stern D, Foiani M. A role for DNA primase in coupling DNA replication to DNA damage response. The EMBO Journal 1997, 16: 639-650. PMID: 9034345, PMCID: PMC1169666, DOI: 10.1093/emboj/16.3.639.Peer-Reviewed Original ResearchMeSH KeywordsBlotting, WesternCell CycleCell Cycle ProteinsCheckpoint Kinase 2DNADNA DamageDNA PrimaseDNA ReplicationEnzyme StabilityFlow CytometryFungal ProteinsGene Expression Regulation, FungalGenes, FungalInterphaseMethyl MethanesulfonateMitosisModels, BiologicalMutagenesis, Site-DirectedMutagensMutationPhosphorylationProtein KinasesProtein Serine-Threonine KinasesRNA NucleotidyltransferasesS PhaseSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTemperatureUltraviolet RaysConceptsDNA damage responseDNA replicationDamage responseDNA damageDNA primaseS-phase progressionSignal transduction pathwaysDNA-damaging agentsCell cycle progressionCell cycle delayG1-S transitionRad53p phosphorylationTransduction pathwaysCheckpoint pathwayCycle progressionCycle delayPhase progressionEarly stepsEssential rolePrimaseReplicationPathwayMitosisPhosphorylationOverexpression
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 analysisImmunoprecipitationSpk1/Rad53 is regulated by Mec1-dependent protein phosphorylation in DNA replication and damage checkpoint pathways.
Sun Z, Fay DS, Marini F, Foiani M, Stern DF. Spk1/Rad53 is regulated by Mec1-dependent protein phosphorylation in DNA replication and damage checkpoint pathways. Genes & Development 1996, 10: 395-406. PMID: 8600024, DOI: 10.1101/gad.10.4.395.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseCell CycleCell Cycle ProteinsCell DivisionCheckpoint Kinase 2DNA DamageDNA ReplicationDNA, FungalFungal ProteinsGene Expression Regulation, FungalGenes, FungalHydroxyureaImmunoblottingIntracellular Signaling Peptides and ProteinsMethyl MethanesulfonateMutagenesisPhosphorylationPrecipitin TestsProtein KinasesProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionTemperatureConceptsProtein kinaseCheckpoint pathwayEssential protein kinaseDamage checkpoint pathwayDamage-induced phosphorylationKinase-defective formG1/S boundarySignal transduction pathwaysRegulation of phosphorylationTreatment of cellsCheckpoint functionCdc mutantsDNA replicationProtein phosphorylationUpstream kinaseCheckpoint arrestRegulated phosphorylationTransduction pathwaysKinase activityCell cyclePhosphorylationS boundaryDamage DNACycle arrestKinase
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 experimentsSerineP185PhosphotyrosineTPAOncogenicMutations
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