References
- Burgess W. H., Maciag T. The heparin-binding (fibroblast) growth factor family of proteins. Ann. Rev. Biochem. 1989; 58: 575–606
- Ruta M., Howk R., Ricca G., Drohan W., Labelshansky M., Laureys M., Barton G., Francke E., Schlessinger J., Givol D. A novel protein-tyrosine-kinase gene whose expression is modulated during endothelial cell differentiation. Oncogene 1988; 3: 9–15
- Kornbluth S., Paulson K. E., Hanafusa H. Novel tyrosine kinase identified by phosphotyrosine antibody screening of cDNA libraries. Mol. Cell. Biol. 1988; 8: 5541–5544
- Keegan K., Johnson D. E., Williams L. T., Hayman M. J. Isolation of an additional member of the fibroblast growth factor receptor family. FGFR-3, Proc. Natl. Acad. Sci. USA 1991; 88: 1095–1099
- Partanen J., Makela T. P., Eerola E., Korhonen J., Hirvonen H., Claesson W. L., Alitalo K. FGFR-4. a novel acidic fibroblast growth factor receptor with a distinct expression pattern, EMBO J. 1991; 10: 1347–1354
- Williams A. F., Barclay A. N. The immunoglobulin superfamilydomains for cell surface recognition. Ann. Rev. Immunol. 1988; 6: 381–405
- Yayon A., Zimmer Y., Guo-Hong S., Avivi A., Yarden Y., Givol D. A confined variable region confers ligand specificity on fibroblast growth factor receptors: implications for the origin of the immunoglobulin fold. EMBO J. 1992; 11: 1885–1890
- Miki T., Bottaro D. P., Fleming T. P., Smith C. L., Burgess W. H., Chan A. M., Aaronson S. A. Determination of ligand-binding specificity by alternative splicing: two distinct growth factor receptors encoded by a single gene. Proc. Natl. Acad. Sci. USA 1992; 89: 246–250
- Flanagan J. G., Leder P. The kit ligand: A cell surface molecule altered in Steel mutant fibroblasts. Cell 1990; 63: 185–194
- Jaye M., Schlessinger J., Dionne C. A. Fibroblast growth factor receptor tyrosine kinases: molecular analysis and signal transduction. Biochim. Biophys. Acta. 1992; 1135: 185–199
- Riedel H., Dull T. J., Schlessinger J., Ullrich A. A chimeric receptor allows insulin to stimulate tyrosine kinase activity of epidermal growth factor receptor. Nature 1986; 324: 68–70
- Cheon H.-G., LaRochelle W. J., Bottaro D. P., Burgess W. H., Aaronson S. A. High-affinity binding sites for related fibroblast growth factor ligands reside within different receptor immunoglobulin-like domains. Proc. Natl. Acad. Sci. USA 1994; 91: 989–993
- Horovitz A. Non-additivity in protein-protein interactions. J. Mol. Biol. 1987; 196: 733–736
- Bottaro D. P., Fortney E., Rubin J. S., Aaronson S. A. A keratinocyte growth factor receptor-derived peptide antagonist identifies part of the ligand binding site. J. Biol. Chem. 1993; 268: 9180–9193
- Johnson D. E., Lu J., Chen H., Werner S., Williams L. T. The human fibroblast growth factor receptor genes: a common structural arrangement underlies the mechanisms for generating receptor forms that differ in their third immunoglobulin domain. Mol. Cell. Biol. 1991; 11: 4627–4634
- Duan D. S., Werner S., Williams L. T. A naturally occurring secreted form of fibroblast growth factor (FGF) receptor 1 binds basic FGF in preference over acidic FGF. J. Biol. Chem. 1992; 267: 16076–16080