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 receptors
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 synthesis