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 dimerizationMutantsKinaseSignalingProteinEGFChimeras
1992
A subdomain in the transmembrane domain is necessary for p185neu* activation.
Cao H, Bangalore L, Bormann BJ, Stern DF. A subdomain in the transmembrane domain is necessary for p185neu* activation. The EMBO Journal 1992, 11: 923-932. PMID: 1347745, PMCID: PMC556533, DOI: 10.1002/j.1460-2075.1992.tb05131.x.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnimalsBase SequenceBlotting, WesternCell MembraneElectrophoresis, Polyacrylamide GelErbB ReceptorsGliomaGlutamatesGlutamic AcidMiceMolecular Sequence DataMutagenesis, Site-DirectedNeuroblastomaPrecipitin TestsProtein-Tyrosine KinasesProto-Oncogene ProteinsRatsReceptor, ErbB-2Signal TransductionValineConceptsTransmembrane domainTyrosine kinase activityKinase activityElevated tyrosine kinase activitySite-directed mutagenesisSpecific amino acidsEpidermal growth factor receptorGlutamic acidGrowth factor receptorEGF receptorPrimary structureAmino acidsFactor receptorProteinSpecific interactionsActivationDomainMutagenesisReceptorsMolecular weightAcidNeu proteinP185neuHigh propensityRole
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 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 ResearchOncogenic Activation of p185 neu Stimulates Tyrosine Phosphorylation In Vivo
Stern D, Kamps M, Cao H. Oncogenic Activation of p185 neu Stimulates Tyrosine Phosphorylation In Vivo. Molecular And Cellular Biology 1988, 8: 3969-3973. DOI: 10.1128/mcb.8.9.3969-3973.1988.Peer-Reviewed Original Research