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
2020
Acquired Resistance to HER2-Targeted Therapies Creates Vulnerability to ATP Synthase Inhibition
Gale M, Li Y, Cao J, Liu ZZ, Holmbeck MA, Zhang M, Lang SM, Wu L, Do Carmo M, Gupta S, Aoshima K, DiGiovanna MP, Stern DF, Rimm DL, Shadel GS, Chen X, Yan Q. Acquired Resistance to HER2-Targeted Therapies Creates Vulnerability to ATP Synthase Inhibition. Cancer Research 2020, 80: 524-535. PMID: 31690671, PMCID: PMC7002225, DOI: 10.1158/0008-5472.can-18-3985.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntineoplastic Combined Chemotherapy ProtocolsApoptosisBreast NeoplasmsCell ProliferationDrug Resistance, NeoplasmEnzyme InhibitorsFemaleHumansMiceMice, Inbred NODMice, SCIDMitochondrial Proton-Translocating ATPasesOligomycinsReceptor, ErbB-2TrastuzumabTumor Cells, CulturedXenograft Model Antitumor AssaysConceptsResistant cellsHER2-Targeted TherapyTrastuzumab-resistant tumorsNew therapeutic strategiesNovel potential targetDrug-free mediumAntibody therapySynthase inhibitionLow doseTherapeutic strategiesTrastuzumabBreast tumorsHER2TherapyAcquired ResistanceTumorsPotential targetMitochondrial respirationCellsSelective dependencyInhibitionMinimal changesNovel vulnerabilitiesATP synthase inhibitionOligomycin A
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
Phosphoproteomics 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
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 requirementsMrc1Oligomerization
1986
Differential Responsiveness of myc- and ras-Transfected Cells to Growth Factors: Selective Stimulation of myc-Transfected Cells by Epidermal Growth Factor
Stern D, Roberts A, Roche N, Sporn M, Weinberg R. 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. DOI: 10.1128/mcb.6.3.870-877.1986.Peer-Reviewed Original ResearchEpidermal growth factorSoft agarPlatelet-derived growth factorRas oncogeneEGF-like factorsMyc-like genesControl cellsAnchorage-independent growthPresence of epidermal growth factorPresence of platelet-derived growth factorCells to growth factorsTGF-betaRas-transfected cellsGrowth factorExogenous growth factorsResponse of cellsMYCAgarTransforming growth factor-betaOncogeneGrowth factor-betaRasDifferential responseCellsColonies
1985
Down-modulation of an oncogene protein product and reversion of the transformed phenotype by monoclonal antibodies
Drebin J, Link V, Stern D, Weinberg R, Greene M. Down-modulation of an oncogene protein product and reversion of the transformed phenotype by monoclonal antibodies. Cell 1985, 41: 695-706. PMID: 2860972, DOI: 10.1016/s0092-8674(85)80050-7.Peer-Reviewed Original ResearchConceptsNIH 3T3 cellsAnchorage-independent growthAnti-p185 monoclonal antibodiesColony formationSoft agar colony formationAgar colony formationOncogene protein productGene productsNontransformed phenotypeProtein productsAntibody treatmentRas oncogeneDNA transfectionMonoclonal antibodiesNeu gene productSoft agarOncogenePhenotypeCellsP185P185 levelsNeuroblastoma linesUnrelated specificityControl antibodyNeu oncogene
1984
Organization of the IBV Genome
Stern D, Sefton B. Organization of the IBV Genome. Advances In Experimental Medicine And Biology 1984, 173: 11-23. PMID: 6331104, DOI: 10.1007/978-1-4615-9373-7_2.Peer-Reviewed Original Research