Featured Publications
Genotype-Selective Combination Therapies for Melanoma Identified by High-Throughput Drug Screening
Held MA, Langdon CG, Platt JT, Graham-Steed T, Liu Z, Chakraborty A, Bacchiocchi A, Koo A, Haskins JW, Bosenberg MW, Stern DF. Genotype-Selective Combination Therapies for Melanoma Identified by High-Throughput Drug Screening. Cancer Discovery 2013, 3: 52-67. PMID: 23239741, PMCID: PMC3546137, DOI: 10.1158/2159-8290.cd-12-0408.Peer-Reviewed Original ResearchConceptsMutant BRAF melanomaCyclin-dependent kinase inhibitorBRAF melanomaSmall molecule inhibitorsHigh-throughput drug screeningDrug screeningEGF receptorCombination therapyDrug combinationsMelanoma culturesContext of genotypePairwise combinationsResistance phenotypeCombinatorial drug screeningUnique treatment regimensCombination of statinsVivo xenograftsKinase inhibitorsMutant BRAFMutationsEfficacious drug combinationsPartial responseTreatment regimensRAS mutationsBRAF mutations
2013
MERTK controls melanoma cell migration and survival and differentially regulates cell behavior relative to AXL
Tworkoski KA, Platt JT, Bacchiocchi A, Bosenberg M, Boggon TJ, Stern DF. MERTK controls melanoma cell migration and survival and differentially regulates cell behavior relative to AXL. Pigment Cell & Melanoma Research 2013, 26: 527-541. PMID: 23617806, PMCID: PMC3918898, DOI: 10.1111/pcmr.12110.Peer-Reviewed Original ResearchMeSH KeywordsAxl Receptor Tyrosine KinaseCdc42 GTP-Binding ProteinCell Line, TumorCell MovementCell ProliferationCell SurvivalC-Mer Tyrosine KinaseCytophotometryGene Expression ProfilingGene Expression Regulation, NeoplasticHEK293 CellsHumansMelanomaNeoplasm MetastasisOligonucleotide Array Sequence AnalysisPhosphorylationProto-Oncogene ProteinsReceptor Protein-Tyrosine KinasesSignal TransductionSkin NeoplasmsConceptsCell migrationCell behaviorMelanoma cellsAkt-dependent mannerShRNA-mediated knockdownDifferential cell behaviorDifferent transcriptional signaturesReceptor tyrosine kinase AXLMelanoma cell migrationMelanoma cell proliferationKinase domainTyrosine kinase AXLCell motilityTranscriptional signatureCell survivalColony formationCell proliferationOverexpression of AxlPossible therapeutic targetMelanoma pathogenesisNovel mutationsMerTKAxlTherapeutic targetMutations
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 dimerizationMutantsKinaseSignalingProteinEGFChimerasMutations in SPK1/RAD53 that specifically abolish checkpoint but not growth-related functions
Fay DS, Sun Z, Stern D. Mutations in SPK1/RAD53 that specifically abolish checkpoint but not growth-related functions. Current Genetics 1997, 31: 97-105. PMID: 9021124, DOI: 10.1007/s002940050181.Peer-Reviewed Original ResearchMeSH KeywordsAllelesCell Cycle ProteinsCheckpoint Kinase 2Cloning, MolecularElectrophoresis, Polyacrylamide GelGene Expression Regulation, EnzymologicGene Expression Regulation, FungalMutagenesisPlasmidsProtein KinasesProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence DeletionTransformation, GeneticConceptsCheckpoint functionKinase domainKinase activityEssential protein kinaseWild-type levelsGrowth-related functionsCheckpoint arrestProtein kinaseDeletional analysisN-terminusSPK1Cell cycleMutant allelesGrowth activityMutationsRad53Normal rateSaccharomycesMultiple stagesKinaseDomainCheckpointActivityAllelesRegulation
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