Featured Publications
Phosphoproteomic Screen Identifies Potential Therapeutic Targets in Melanoma
Tworkoski K, Singhal G, Szpakowski S, Zito CI, Bacchiocchi A, Muthusamy V, Bosenberg M, Krauthammer M, Halaban R, Stern DF. Phosphoproteomic Screen Identifies Potential Therapeutic Targets in Melanoma. Molecular Cancer Research 2011, 9: 801-812. PMID: 21521745, PMCID: PMC3117976, DOI: 10.1158/1541-7786.mcr-10-0512.Peer-Reviewed Original ResearchMeSH KeywordsApoptosisCell Line, TumorCell MovementCell ProliferationErbB ReceptorsGene Expression Regulation, NeoplasticGene Knockdown TechniquesHEK293 CellsHumansInfant, NewbornMelanocytesMelanomaPhosphoproteinsPhosphorylationProteomicsReceptor Protein-Tyrosine KinasesReceptor, IGF Type 2RNA, Small InterferingSignal TransductionSkin NeoplasmsSTAT3 Transcription FactorConceptsTherapeutic targetReceptor tyrosine kinasesMelanoma cellsPotential therapeutic targetIdentifies potential therapeutic targetsActive receptor tyrosine kinasesTyrosine kinaseMelanoma cell migrationReceptor expressionBreast cancerAxl knockdownAutocrine circuitTherapeutic interventionsCancer subtypesReceptor tyrosine kinase activationTyrosine kinase activationNovel targetActivated receptorsAxlRNA knockdownMelanomaCell migrationHER3KnockdownIGF1RAntiserum raised against a synthetic phosphotyrosine-containing peptide selectively recognizes p185neu/erbB-2 and the epidermal growth factor receptor.
Bangalore L, Tanner AJ, Laudano AP, Stern DF. Antiserum raised against a synthetic phosphotyrosine-containing peptide selectively recognizes p185neu/erbB-2 and the epidermal growth factor receptor. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 11637-11641. PMID: 1280833, PMCID: PMC50608, DOI: 10.1073/pnas.89.23.11637.Peer-Reviewed Original Research
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 mechanismActivationPIKKsComplexesPhosphoproteomics 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 ResearchMeSH KeywordsAntineoplastic AgentsGene Expression ProfilingHumansNeoplasmsPhosphoproteinsProtein KinasesProteomicsConceptsPhosphoproteomic 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
2002
Production of Antibodies That Recognize Specific Tyrosine‐Phosphorylated Peptides
DiGiovanna MP, Roussel RR, Stern DF. Production of Antibodies That Recognize Specific Tyrosine‐Phosphorylated Peptides. Current Protocols In Cell Biology 2002, 13: 16.6.1-16.6.18. PMID: 18228399, DOI: 10.1002/0471143030.cb1606s13.Books
2001
Phosphoproteomics
Stern D. Phosphoproteomics. Experimental And Molecular Pathology 2001, 70: 327-331. PMID: 11418011, DOI: 10.1006/exmp.2001.2370.Peer-Reviewed Original Research
1990
Tyrosine 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
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
Monoclonal antibodies identify a cell-surface antigen associated with an activated cellular oncogene
Drebin J, Stern D, Link V, Weinberg R, Greene M. Monoclonal antibodies identify a cell-surface antigen associated with an activated cellular oncogene. Nature 1984, 312: 545-548. PMID: 6504162, DOI: 10.1038/312545a0.Peer-Reviewed Original ResearchConceptsNIH 3T3 cellsCell surface antigensCellular oncogenesAnimal cancer cellsNormal NIH 3T3 cellsMonoclonal antibodiesTumor-associated antigensVariety of antigensRelative molecular massCell surface determinantsNon-malignant cellsGenetic elementsDifferent histological originDNA transfectantsDNA transfectionMolecular massNeoplastic processAntibody reactivityNeoplastic cellsMalignant cellsHistological originAntigenIdentical antigensOncogeneCancer cells