An insertional mutant of epidermal growth factor receptor allows dissection of diverse receptor functions.

@article{Livneh1987AnIM,
  title={An insertional mutant of epidermal growth factor receptor allows dissection of diverse receptor functions.},
  author={Etta Livneh and Nachum Reiss and E Berent and Axel Ullrich and Joseph Schlessinger},
  journal={The EMBO journal},
  year={1987},
  volume={6 9},
  pages={2669-76}
}
Cultured NIH-3T3 cells devoid of endogenous EGF-receptors were transfected with cDNA constructs encoding normal human EGF-receptor and with a construct encoding an insertional mutant of the EGF-receptor containing four additional amino acids in the kinase domain after residue 708. Unlike the wild-type receptor expressed in these cells which exhibits EGF-stimulatable protein tyrosine kinase activity, the mutant receptor lacks protein tyrosine kinase activity both in vitro and in vivo. Despite… CONTINUE READING

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