1991
A Dominant Negative Mutation Suppresses the Function of Normal Epidermal Growth Factor Receptors by Heterodimerization
Kashles O, Yarden Y, Fischer R, Ullrich A, Schlessinger J. A Dominant Negative Mutation Suppresses the Function of Normal Epidermal Growth Factor Receptors by Heterodimerization. Molecular And Cellular Biology 1991, 11: 1454-1463. DOI: 10.1128/mcb.11.3.1454-1463.1991.Peer-Reviewed Original ResearchDominant negative mutationWild-type receptorEpidermal growth factorNegative mutationMutant receptorsWild-type EGF receptorEGF receptorResponse to EGFInactive deletion mutantsCovalent cross-linking experimentsLiving cellsWild-typeEpidermal growth factor receptorRate of receptor endocytosisCross-linking experimentsDeletion mutantsTyrosine autophosphorylationCytoplasmic domainCells expressing wild-type receptorsReceptor endocytosisMurine embryogenesisKinase activityHigh-affinity binding sitesReceptor dimerizationNormal receptorsEpidermal Growth Factor (EGF) Stimulates Association and Kinase Activity of Raf-1 with the EGF Receptor
App H, Hazan R, Zilberstein A, Ullrich A, Schlessinger J, Rapp U. Epidermal Growth Factor (EGF) Stimulates Association and Kinase Activity of Raf-1 with the EGF Receptor. Molecular And Cellular Biology 1991, 11: 913-919. DOI: 10.1128/mcb.11.2.913-919.1991.Peer-Reviewed Original ResearchRaf-1Raf-1 kinaseEpidermal growth factorPhosphorylation of c-Raf-1Kinase activityKinase activity of Raf-1Activation of Raf-1Phosphorylation of Raf-1Sodium dodecyl sulfate gelsRaf-1 activationImmunocomplex kinase assayEGF signal transductionC-Raf-1Dodecyl sulfate gelsTyrosine kinase activityTyrosine phosphorylationSerine residuesHistone H1Kinase assaySignal transductionDownstream effectorsStimulated associationEGF receptorKinaseGrowth factor
1988
Release of a Phorbol Ester-Induced Mitogenic Block by Mutation at Thr-654 of the Epidermal Growth Factor Receptor
Livneh E, Dull T, Berent E, Prywes R, Ullrich A, Schlessinger J. Release of a Phorbol Ester-Induced Mitogenic Block by Mutation at Thr-654 of the Epidermal Growth Factor Receptor. Molecular And Cellular Biology 1988, 8: 2302-2308. DOI: 10.1128/mcb.8.6.2302-2308.1988.Peer-Reviewed Original ResearchThr-654Epidermal growth factorEpidermal growth factor receptorNIH 3T3 cellsTyr-654Ligand binding affinityIn vitro site-directed mutagenesisWild-type human EGF receptorMutant receptorsEGF receptor mutantKinase C phosphorylationPhosphorylation of serineSurface of NIH 3T3 cellsSite-directed mutagenesisHuman EGF receptorPhosphorylation of sitesStimulated receptor phosphorylationEGF-induced mitogenesisNegative control mechanismMouse NIH 3T3 fibroblastsWild-type receptorNIH 3T3 fibroblastsThreonine residuesC phosphorylationStimulate DNA synthesisChicken Epidermal Growth Factor (EGF) Receptor: cDNA Cloning, Expression in Mouse Cells, and Differential Binding of EGF and Transforming Growth Factor Alpha
Lax I, Johnson A, Howk R, Sap J, Bellot F, Winkler M, Ullrich A, Vennstrom B, Schlessinger J, Givol D. Chicken Epidermal Growth Factor (EGF) Receptor: cDNA Cloning, Expression in Mouse Cells, and Differential Binding of EGF and Transforming Growth Factor Alpha. Molecular And Cellular Biology 1988, 8: 1970-1978. DOI: 10.1128/mcb.8.5.1970-1978.1988.Peer-Reviewed Original ResearchHuman EGF receptorChicken EGF receptorEpidermal growth factorNIH 3T3 cellsEGF receptorCDNA clonesMammalian epidermal growth factorDifferential bindingTGF-aEndogenous EGF receptorsBinding of epidermal growth factorGrowth factorMurine epidermal growth factorCoding sequenceApparent molecular weightTransforming growth factor-alphaCDNA constructsAvian EGF receptorMouse cellsPrimary structureGrowth factor-alphaCDNAChicken receptorMammalian receptorsFactor-alpha