1992
Differential Effects of Carboxy-Terminal Sequence Deletions on Platelet-Derived Growth Factor Receptor Signaling Activities and Interactions with Cellular Substrates
Seedorf K, Millauer B, Kostka G, Schlessinger J, Ullrich A. Differential Effects of Carboxy-Terminal Sequence Deletions on Platelet-Derived Growth Factor Receptor Signaling Activities and Interactions with Cellular Substrates. Molecular And Cellular Biology 1992, 12: 4347-4356. DOI: 10.1128/mcb.12.10.4347-4356.1992.Peer-Reviewed Original ResearchNIH 3T3 cellsRas GTPase-activating proteinCarboxy-terminal amino acidsSignaling pathwayGTPase-activating proteinSignaling activityAmino acidsWild-type levelsPDGF-RSubstrates in vitroC-terminal truncationEGF-RReceptor signaling activityMitogenic activityPhosphotidylinositol 3-kinaseWild-type receptorBiological signaling activitiesSequence deletionsSubstrate phosphorylationCellular polypeptidesCellular proteinsCytoplasmic domainIntracellular sequencesSignaling potentialExtracellular domain
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