2008
Direct resequencing of the complete ERBB2 coding sequence reveals an absence of activating mutations in ERBB2 amplified breast cancer
Zito CI, Riches D, Kolmakova J, Simons J, Egholm M, Stern DF. Direct resequencing of the complete ERBB2 coding sequence reveals an absence of activating mutations in ERBB2 amplified breast cancer. Genes Chromosomes And Cancer 2008, 47: 633-638. PMID: 18418848, PMCID: PMC6668724, DOI: 10.1002/gcc.20566.Peer-Reviewed Original Research
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 experimentsSerineP185PhosphotyrosineTPAOncogenicMutationsConstruction and expression of transforming gene resulting from fusion of basic fibroblast growth factor gene with signal peptide sequence
Rogelj S, Stern D, Klagsbrun M. Construction and expression of transforming gene resulting from fusion of basic fibroblast growth factor gene with signal peptide sequence. Methods In Enzymology 1991, 198: 117-124. PMID: 1906971, DOI: 10.1016/0076-6879(91)98013-v.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrainCattleCell LineCell Transformation, NeoplasticChimeraCloning, MolecularFibroblast Growth Factor 2Genes, SyntheticGenetic VectorsImmunoglobulin Heavy ChainsMiceMolecular Sequence DataProtein Sorting SignalsRecombinant Fusion ProteinsRecombinant ProteinsRestriction MappingTransfection
1990
The epidermal growth factor receptor and the product of the neu protooncogene are members of a receptor tyrosine phosphorylation cascade.
Connelly PA, Stern DF. The epidermal growth factor receptor and the product of the neu protooncogene are members of a receptor tyrosine phosphorylation cascade. Proceedings Of The National Academy Of Sciences Of The United States Of America 1990, 87: 6054-6057. PMID: 1974718, PMCID: PMC54470, DOI: 10.1073/pnas.87.16.6054.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
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
1987
Construction of a Novel Oncogene Based on Synthetic Sequences Encoding Epidermal Growth Factor
Stern DF, Hare DL, Cecchini MA, Weinberg RA. Construction of a Novel Oncogene Based on Synthetic Sequences Encoding Epidermal Growth Factor. Science 1987, 235: 321-324. PMID: 3492043, DOI: 10.1126/science.3492043.Peer-Reviewed Original Research
1986
Differential responsiveness of myc- and ras-transfected cells to growth factors: selective stimulation of myc-transfected cells by epidermal growth factor.
Stern DF, Roberts AB, Roche NS, Sporn MB, Weinberg RA. 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. PMID: 3022135, PMCID: PMC367587, DOI: 10.1128/mcb.6.3.870.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, Polyomavirus TransformingAntigens, Viral, TumorCell DivisionCell Transformation, NeoplasticCells, CulturedEpidermal Growth FactorGenesGenes, ViralGrowth SubstancesOncogene Proteins, ViralOncogenesPeptidesPlatelet-Derived Growth FactorPolyomavirusRatsRats, Inbred F344TransfectionTransforming Growth FactorsConceptsEpidermal growth factorPlatelet-derived growth factorExogenous growth factorsSoft agarRas oncogeneGrowth factorEGF-like factorsPresence of PDGFControl cellsAnchorage-independent growthMyc-transfected cellsRas-transfected cellsPresence of EGFLike genesMYCResponsiveness of cellsGrowth factor productionOncogeneAutocrine stimulationNumerous coloniesTGF betaLack of responsivenessGenesSelective stimulationStimulatory effectMolecular 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
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