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Boni-Schnetzler, M., Pilch, P. F. (1987) Mechanism of epidermal growth factor receptor autophosphorylation and high-affinity binding. Proceedings of the National Academy of Sciences, 84 (22) 7832-7836 doi:10.1073/pnas.84.22.7832

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Reference TypeJournal (article/letter/editorial)
TitleMechanism of epidermal growth factor receptor autophosphorylation and high-affinity binding.
JournalProceedings of the National Academy of Sciences
AuthorsBoni-Schnetzler, M.Author
Pilch, P. F.Author
Year1987 (November 1)Volume84
Issue22
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.84.22.7832Search in ResearchGate
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Mindat Ref. ID1461839Long-form Identifiermindat:1:5:1461839:6
GUID0
Full ReferenceBoni-Schnetzler, M., Pilch, P. F. (1987) Mechanism of epidermal growth factor receptor autophosphorylation and high-affinity binding. Proceedings of the National Academy of Sciences, 84 (22) 7832-7836 doi:10.1073/pnas.84.22.7832
Plain TextBoni-Schnetzler, M., Pilch, P. F. (1987) Mechanism of epidermal growth factor receptor autophosphorylation and high-affinity binding. Proceedings of the National Academy of Sciences, 84 (22) 7832-7836 doi:10.1073/pnas.84.22.7832
In(1987, November) Proceedings of the National Academy of Sciences Vol. 84 (22) Proceedings of the National Academy of Sciences

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Aviezer, D., Yayon, A. (1994) Heparin-dependent binding and autophosphorylation of epidermal growth factor (EGF) receptor by heparin-binding EGF-like growth factor but not by EGF. Proceedings of the National Academy of Sciences, 91 (25) 12173-12177 doi:10.1073/pnas.91.25.12173
Bernard, O., Fazekas de St Groth, B., Ullrich, A., Green, W., Schlessinger, J. (1987) High-affinity interleukin 2 binding by an oncogenic hybrid interleukin 2-epidermal growth factor receptor molecule. Proceedings of the National Academy of Sciences, 84 (8) 2125-2129 doi:10.1073/pnas.84.8.2125
Massague, J., Czech, M. P., Iwata, K., DeLarco, J. E., Todaro, G. J. (1982) Affinity labeling of a transforming growth factor receptor that does not interact with epidermal growth factor. Proceedings of the National Academy of Sciences, 79 (22) 6822-6826 doi:10.1073/pnas.79.22.6822
Ghosh-Dastidar, P., Coty, W. A., Griest, R. E., Woo, D. D., Fox, C. F. (1984) Progesterone receptor subunits are high-affinity substrates for phosphorylation by epidermal growth factor receptor. Proceedings of the National Academy of Sciences, 81 (6) 1654-1658 doi:10.1073/pnas.81.6.1654
Das, M., Fox, C. F. (1978) Molecular mechanism of mitogen action: Processing of receptor induced by epidermal growth factor. Proceedings of the National Academy of Sciences, 75 (6) 2644-2648 doi:10.1073/pnas.75.6.2644
Guinivan, P., Ladda, R. L. (1979) Decrease in epidermal growth factor receptor levels and production of material enhancing epidermal growth factor binding accompany the temperature-dependent changes from normal to transformed phenotype. Proceedings of the National Academy of Sciences, 76 (7) 3377-3381 doi:10.1073/pnas.76.7.3377
(1979) Correction: Molecular Mechanism of Mitogen Action: Processing of Receptor Induced by Epidermal Growth Factor. Proceedings of the National Academy of Sciences, 76 (1) 547 doi:10.1073/pnas.76.1.547
Kizaka-Kondoh, S., Matsuda, M., Okayama, H. (1996) CrkII signals from epidermal growth factor receptor to Ras. Proceedings of the National Academy of Sciences, 93 (22) 12177-12182 doi:10.1073/pnas.93.22.12177
Kawamoto, T., Sato, J. D., Le, A., Polikoff, J., Sato, G. H., Mendelsohn, J. (1983) Growth stimulation of A431 cells by epidermal growth factor: identification of high-affinity receptors for epidermal growth factor by an anti-receptor monoclonal antibody. Proceedings of the National Academy of Sciences, 80 (5) 1337-1341 doi:10.1073/pnas.80.5.1337
Chen, F., Weinberg, R. A. (1995) Biochemical evidence for the autophosphorylation and transphosphorylation of transforming growth factor beta receptor kinases. Proceedings of the National Academy of Sciences, 92 (5) 1565-1569 doi:10.1073/pnas.92.5.1565
Moriai, T., Kobrin, M. S., Hope, C., Speck, L., Korc, M. (1994) A variant epidermal growth factor receptor exhibits altered type alpha transforming growth factor binding and transmembrane signaling. Proceedings of the National Academy of Sciences, 91 (21) 10217-10221 doi:10.1073/pnas.91.21.10217
 
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