References
- Berti, A., Rigacci, S., Raugei, G., Degl'Innocenti, D. and Ramponi, G. (1994) Inhibition of cellular response to platelet-derived growth factor by low M(r) phosphotyrosine protein phosphatase overexpression. FEBS Lett. 349, 7-12. https://doi.org/10.1016/0014-5793(94)00620-2
- Chiarugi, P., Marzocchini, R., Raugei, G., Pazzagli, C., Berti, A., Camici, G., Manao, G., Cappugi, G. and Ramponi, G. (1992) Differential role of four cysteines on the activity of a low M(r) phosphotyrosine protein phosphatase. FEBS Lett. 310, 9-12. https://doi.org/10.1016/0014-5793(92)81134-8
- Choi, S. and Park, S. (1999) Phosphorylation at Tyr-838 in the kinase domain of EphA8 modulates Fyn binding to the Tyr-615 site by enhancing tyrosine kinase activity. Oncogene 18, 5413-5422. https://doi.org/10.1038/sj.onc.1202917
- Cirri, P., Chiarugi, P., Camici, G., Manao, G., Raugei, G., Cappugi, G. and Ramponi, G. (1993) The role of Cys12, Cys17 and Arg18 in the catalytic mechanism of low-M(r) cytosolic phosphotyrosine protein phosphatase. Eur. J. Biochem. 214, 647-657, https://doi.org/10.1111/j.1432-1033.1993.tb17965.x
- Davy, A., Gale, N. W., Murray, E. W., Klinghoffer, R. A., Soriano, P., Feuerstein, C. and Robbins, S. M. (1999) Compartmentalized signaling by GPI-anchored ephrin-A5 requires the Fyn tyrosine kinase to regulate cellular adhesion. Genes Dev. 13, 3125-3135. https://doi.org/10.1101/gad.13.23.3125
- Dodelet, V. C., Pazzagli, C., Zisch, A. H., Hauser, C. A. and Pasquale, E. B. (1999) A novel signaling intermediate, SHEP1, directly couples Eph receptors to R-Ras and Rap1A. J. BioI. Chem. 274, 31941-31946. https://doi.org/10.1074/jbc.274.45.31941
- Elowe, S., Holland, S. J., Kulkarni, S. and Pawson, T. (2001) Downregulation of the Ras-mitogen-activated protein kinase pathway by the EphB2 receptor tyrosine kinase is required for ephrin-induced neurite retraction. Mol. Cell. Biol. 21, 7429-7441. https://doi.org/10.1128/MCB.21.21.7429-7441.2001
- Eph Nomenclature Committee. (1997) Unified nomenclature for Eph family receptors and their ligands, the ephrins. Cell 90, 403-404, https://doi.org/10.1016/S0092-8674(00)80500-0
- Flanagan, J. G. and Vanderhaeghen, P. (1998) The ephrins and Eph receptors in neural development. Annu. Rev. Neurosci. 21, 309-345, https://doi.org/10.1146/annurev.neuro.21.1.309
- Graham, F. L. and van der Eb. A. J. (1973) Transformation of rat cells by DNA of human adenovirus 5. Virology 54, 536-539. https://doi.org/10.1016/0042-6822(73)90163-3
- Gu, C. and Park, S. (2001) The EphA8 receptor regulates integrin activity through p110gamma phosphatidylinositol-3 kinase in a tyrosine kinase activity-independent manner. Mol. Cell. Biol. 21, 4579-4597. https://doi.org/10.1128/MCB.21.14.4579-4597.2001
- Huai, J, and Drescher, U. (2001) An ephrin-A-dependent signaling pathway controls integrin function and is linked to the tyrosine phosphorylation of a 120-kDa protein. J. Biol. Chem. 276, 6689-6694. https://doi.org/10.1074/jbc.M008127200
- Huynh-Do, U., Stein, E., Lane, A. A., Liu, H., Cerretti, D. P. and Daniel, T. O. (1999) Surface densities of ephrin-B1 determine EphB1-coupled activation of cell attachment through alphavbeta3 and alpha5beta1 integrins. EMBO J. 18, 2165-2173. https://doi.org/10.1093/emboj/18.8.2165
- Kim, Y. S., Ha, K. S., Kim, Y. H. and Bae, Y. S. (2002) The Ring-H2 finger motif of CKBBP1/SAG is necessary for interaction with protein kinase CKII and optimal cell proliferation. J. Biochem. Mol. Biol. 35, 629-636. https://doi.org/10.5483/BMBRep.2002.35.6.629
- Knoll, B., Zarbalis, K., Wurst, W. and Drescher, U. (2001) A role for the EphA family in the topographic targeting of vomeronasal axons. Development 128, 895-906.
- Mellitzer, G., Xu, Q. and Wilkinson, D. G. (2000) Control of cell behavior by signaling through Eph receptors and ephrins. Curr. Opin. Neurobiol. 10, 400-408. https://doi.org/10.1016/S0959-4388(00)00095-7
- Menzel, P., Valencia, F., Godement, P., Dodelet, V. C. and Pasquale, E. B. (2001) Ephrin-A6, a new ligand for EphA receptors in the developing visual system. Dev. BioI. 230, 74-88. https://doi.org/10.1006/dbio.2000.0109
- Miao, H., Burnett, E., Kinch, M., Simon, E. and Wang, B. (2000) Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation. Nat. Cell Biol. 2, 62-69. https://doi.org/10.1038/35000008
- Ramponi, G., Manao, G., Camici, G., Cappugi, G., Ruggiero, M. and Botturo, D. P. (1989) The 18 kDa cytosolic acid phosphatase from bovine live has phosphotyrosine phosphatase activity on the autophosphorylated epidermal growth factor receptor. FEBS Lett. 250, 469-473 https://doi.org/10.1016/0014-5793(89)80778-1
- Rigacci, S., Degl'Innocenti, D., Bucciantini, M., Cirri. P., Berti, A. and Ramponi, G. (1996) pp60v-src phosphorylates and activates low molecular weight phosphotyrosine-protein phosphatase. J. Biol. Chem. 271, 1278-1281. https://doi.org/10.1074/jbc.271.3.1278
- Shamah, S. M., Lin, M. Z., Goldberg, J. L., Estrach, S., Sahin, M., Hu, L., Bazalakova, M., Neve, R. L., Corfas, G., Debant, A. and Greenberg, M. E. (2001) EphA receptors regulate growth cone dynamics through the novel guanine nucleotide exchange factor ephexin. Cell 105, 233-244. https://doi.org/10.1016/S0092-8674(01)00314-2
- Stein, E., Huynh-Do, U., Lane, A. A., Cerretti, D. P. and Daniel, T. O. (1988a) Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase. J. Biol. Chem. 273, 1303-1308. https://doi.org/10.1074/jbc.273.3.1303
- Stein, E., Lane, A. A., Cerretti, D. P., Schoecklmann, H. O., Schroff, A. D., Van Etten, R. L. and Daniel, T. O. (1998b) Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses. Genes Dev. 12, 667-678. https://doi.org/10.1101/gad.12.5.667
- Wahl, S., Barth, H., Ciossek. T., Aktories, K. and Mueller, B. K. (2000) Ephrin-A5 induces collapse of growth cones by activating Rho and Rho kinase. J. Cell BioI. 149, 263-270. https://doi.org/10.1083/jcb.149.2.263
- Yi, J. Y., Hong, W. S. and Son, Y. S. (2001) Biochemical characterization of adriamycin-resistance in PC-14 human lung adenocarcinoma cell line, J. Biochem. Mol. Biol. 34, 66-72.
- Zou, J. X., Wang, B., Kalo, M. S., Zisch, A. H., Pasquale, E. B. and Ruoslallti, E. (1999) An Eph receptor regulates integrin activity through R-Ras. Proc. Natl. Acad. Sci. USA 96, 13813-13818. https://doi.org/10.1073/pnas.96.24.13813
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