메뉴 건너뛰기




Volumn 10, Issue 9, 1999, Pages 629-638

E-cadherin regulates the function of the EphA2 receptor tyrosine kinase

Author keywords

[No Author keywords available]

Indexed keywords

TYROSINE KINASE RECEPTOR; UVOMORULIN;

EID: 0032834125     PISSN: 10449523     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (233)

References (60)
  • 1
    • 0028170817 scopus 로고
    • Receptor protein-tyrosine kinases and their signal transduction pathways
    • van der Geer, P., Hunter, A. J., and Lindberg, R. A. Receptor protein-tyrosine kinases and their signal transduction pathways. Annu. Rev. Cell Biol., 10: 251-337, 1994.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 251-337
    • Van Der Geer, P.1    Hunter, A.J.2    Lindberg, R.A.3
  • 2
    • 0029003828 scopus 로고
    • Protein kinases in human breast cancer
    • Cance, W. G., and Liu, E. T. Protein kinases in human breast cancer. Breast Cancer Res. Treat., 35: 105-114, 1995.
    • (1995) Breast Cancer Res. Treat. , vol.35 , pp. 105-114
    • Cance, W.G.1    Liu, E.T.2
  • 4
    • 0027524592 scopus 로고
    • Enzymatic and immunohistochemical evaluation of tyrosine phosphorylation in breast cancer specimens
    • Lower, E. E., Franco, R. S., Miller, M. A., and Martelo, O. J. Enzymatic and immunohistochemical evaluation of tyrosine phosphorylation in breast cancer specimens. Breast Cancer Res. Treat., 26: 217-224, 1993.
    • (1993) Breast Cancer Res. Treat. , vol.26 , pp. 217-224
    • Lower, E.E.1    Franco, R.S.2    Miller, M.A.3    Martelo, O.J.4
  • 5
    • 0025251177 scopus 로고
    • cDNA cloning and characterization of eck, an epithelial cell receptor protein-tyrosine kinase in the eph/elk family of protein kinases
    • Lindberg, R. A., and Hunter, T. cDNA cloning and characterization of eck, an epithelial cell receptor protein-tyrosine kinase in the eph/elk family of protein kinases. Mol. Cell. Biol., 10: 6316-6324, 1990.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6316-6324
    • Lindberg, R.A.1    Hunter, T.2
  • 6
    • 0030728938 scopus 로고    scopus 로고
    • Ephrins and their receptors: A repulsive topic?
    • Gale, N. W., and Yancopoulos, G. D. Ephrins and their receptors: a repulsive topic? CeH Tissue Res., 290: 227-241, 1997.
    • (1997) CeH Tissue Res. , vol.290 , pp. 227-241
    • Gale, N.W.1    Yancopoulos, G.D.2
  • 7
    • 0030874979 scopus 로고    scopus 로고
    • The Eph family of receptors
    • Pasquale, E. B. The Eph family of receptors. Curr. Opin. Cell Biol., 9: 608-615, 1997.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 608-615
    • Pasquale, E.B.1
  • 8
    • 0030807905 scopus 로고    scopus 로고
    • The Eph family: A multitude of receptors that mediate cell recognition signals
    • Zisch, A. H., and Pasquale, E. B. The Eph family: a multitude of receptors that mediate cell recognition signals. Cell Tissue Res., 290: 217-226, 1997.
    • (1997) Cell Tissue Res. , vol.290 , pp. 217-226
    • Zisch, A.H.1    Pasquale, E.B.2
  • 9
    • 0030836237 scopus 로고    scopus 로고
    • Epithelial cell kinase-B61: An autocrine loop modulating intestinal epithelial migration and barrier function
    • Rosenberg, I. M., Goke, M., Kanai, M., Reinecker, H. C., and Podolsky, D. K. Epithelial cell kinase-B61: an autocrine loop modulating intestinal epithelial migration and barrier function. Am. J. Physiol., 273: G824-G832, 1997.
    • (1997) Am. J. Physiol. , vol.273
    • Rosenberg, I.M.1    Goke, M.2    Kanai, M.3    Reinecker, H.C.4    Podolsky, D.K.5
  • 10
    • 0029036501 scopus 로고
    • Role of B61, the ligand for the Eck receptor tyrosine kinase, in TNF-α-induced angiogenesis
    • Washington DC
    • Pandey, A., Shao, H., Marks, R. M., Polverini, P. J., and Dixit, V. M. Role of B61, the ligand for the Eck receptor tyrosine kinase, in TNF-α-induced angiogenesis. Science (Washington DC), 268: 567-569, 1995.
    • (1995) Science , vol.268 , pp. 567-569
    • Pandey, A.1    Shao, H.2    Marks, R.M.3    Polverini, P.J.4    Dixit, V.M.5
  • 11
    • 0029936456 scopus 로고    scopus 로고
    • B61, a ligand for the Eck receptor protein-tyrosine kinase, exhibits neurotrophic activity in cultures of rat spinal cord neurons
    • Magal, E., Holash, J. A., Toso, R. J., Chang, D., Lindberg, R. A., and Pasquale, E. B. B61, a ligand for the Eck receptor protein-tyrosine kinase, exhibits neurotrophic activity in cultures of rat spinal cord neurons. J. Neurosci. Res., 43: 735-744, 1996.
    • (1996) J. Neurosci. Res. , vol.43 , pp. 735-744
    • Magal, E.1    Holash, J.A.2    Toso, R.J.3    Chang, D.4    Lindberg, R.A.5    Pasquale, E.B.6
  • 12
    • 0029005355 scopus 로고
    • Protein B61 as a new growth factor: Expression of B61 and up-regulation of its receptor epithelial cell kinase during melanoma progression
    • Easty, D. J., Guthrie, B. A., Maung, K., Farr, C. J., Lindberg, R. A., Toso, R. J., Herlyn, M., and Bennett, D. C. Protein B61 as a new growth factor: expression of B61 and up-regulation of its receptor epithelial cell kinase during melanoma progression. Cancer Res., 55: 2528-2532, 1995.
    • (1995) Cancer Res. , vol.55 , pp. 2528-2532
    • Easty, D.J.1    Guthrie, B.A.2    Maung, K.3    Farr, C.J.4    Lindberg, R.A.5    Toso, R.J.6    Herlyn, M.7    Bennett, D.C.8
  • 13
    • 0028788451 scopus 로고
    • Protein tyrosine kinase expression during the estrous cycle and carcinogenesis of the mammary gland
    • Andres, A. C., Zuercher, G., Djonov, V., Flueck, M., and Ziemiecki, A. Protein tyrosine kinase expression during the estrous cycle and carcinogenesis of the mammary gland. Int. J. Cancer, 63: 288-296, 1995.
    • (1995) Int. J. Cancer , vol.63 , pp. 288-296
    • Andres, A.C.1    Zuercher, G.2    Djonov, V.3    Flueck, M.4    Ziemiecki, A.5
  • 14
    • 0012108774 scopus 로고
    • Phosphotyrosine-containing proteins are concentrated in focal adhesions and intercellular junctions in normal cells
    • Maher, P. A., Pasquale, E. B., Wang, J. Y., and Singer, S. J. Phosphotyrosine-containing proteins are concentrated in focal adhesions and intercellular junctions in normal cells. Proc. Natl. Acad. Sci. USA, 82: 6576-6580, 1985.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6576-6580
    • Maher, P.A.1    Pasquale, E.B.2    Wang, J.Y.3    Singer, S.J.4
  • 15
    • 0031826196 scopus 로고    scopus 로고
    • Identification of tyrosine phosphorylated adhesion proteins in human cancer cells
    • Kinch, M. S., Kilpatrick, K., and Zhong, C. Identification of tyrosine phosphorylated adhesion proteins in human cancer cells. Hybridoma, 17: 227-235, 1998.
    • (1998) Hybridoma , vol.17 , pp. 227-235
    • Kinch, M.S.1    Kilpatrick, K.2    Zhong, C.3
  • 17
    • 0030589575 scopus 로고    scopus 로고
    • Cell contact-dependent signaling
    • Fagotto, F., and Gumbiner, B. M. Cell contact-dependent signaling. Dev. Biol., 180: 445-454, 1996.
    • (1996) Dev. Biol. , vol.180 , pp. 445-454
    • Fagotto, F.1    Gumbiner, B.M.2
  • 18
    • 0028248461 scopus 로고
    • Cell-cell adhesion in invasion and metastasis of carcinomas
    • Behrens, J., and Birchmeier, W. Cell-cell adhesion in invasion and metastasis of carcinomas. Cancer Treat. Res., 71: 251-266, 1994.
    • (1994) Cancer Treat. Res. , vol.71 , pp. 251-266
    • Behrens, J.1    Birchmeier, W.2
  • 19
    • 0027459346 scopus 로고
    • P60v-src causes tyrosine phosphorylation and inactivation of the N-cadherin-catenin cell adhesion system
    • Hamaguchi, M., Matsuyoshi, N., Ohnishi, Y., Gotoh, B., Takeichi, M., and Nagai, Y. p60v-src causes tyrosine phosphorylation and inactivation of the N-cadherin-catenin cell adhesion system. EMBO J., 12: 307-314, 1993.
    • (1993) EMBO J. , vol.12 , pp. 307-314
    • Hamaguchi, M.1    Matsuyoshi, N.2    Ohnishi, Y.3    Gotoh, B.4    Takeichi, M.5    Nagai, Y.6
  • 20
    • 0026742310 scopus 로고
    • Cadherin-mediated cell-cell adhesion is perturbed by v-src tyrosine phosphorylation in metastatic fibroblasts
    • Matsuyoshi, N., Hamaguchi, M., Taniguchi, S., Nagafuchi, A., Tsukita, S., and Takeichi, M. Cadherin-mediated cell-cell adhesion is perturbed by v-src tyrosine phosphorylation in metastatic fibroblasts. J. Cell Biol., 118: 703-714, 1992.
    • (1992) J. Cell Biol. , vol.118 , pp. 703-714
    • Matsuyoshi, N.1    Hamaguchi, M.2    Taniguchi, S.3    Nagafuchi, A.4    Tsukita, S.5    Takeichi, M.6
  • 21
    • 0029116143 scopus 로고
    • Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia
    • Kinch, M. S., Clark, G. J., Der, C. J., and Burridge, K. Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia. J. Cell Biol., 130: 461-471, 1995.
    • (1995) J. Cell Biol. , vol.130 , pp. 461-471
    • Kinch, M.S.1    Clark, G.J.2    Der, C.J.3    Burridge, K.4
  • 22
    • 0027507028 scopus 로고
    • Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/ β-catenin complex in cells transformed with a temperature-sensitive v-SRC gene
    • Behrens, J., Vakaet, L., Friis, R., Winterhager, E., Van, R. F., Mareel, M. M., and Birchmeier, W. Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/ β-catenin complex in cells transformed with a temperature-sensitive v-SRC gene. J. Cell Biol., 120: 757-766, 1993.
    • (1993) J. Cell Biol. , vol.120 , pp. 757-766
    • Behrens, J.1    Vakaet, L.2    Friis, R.3    Winterhager, E.4    Van, R.F.5    Mareel, M.M.6    Birchmeier, W.7
  • 23
    • 0026529501 scopus 로고
    • The effect of tyrosine-specific protein phosphorylation on the assembly of adherens-type junctions
    • Volberg, T., Zick, Y., Dror, R., Sabanay, I., Gilon, C., Levitzki, A., and Geiger, B. The effect of tyrosine-specific protein phosphorylation on the assembly of adherens-type junctions. EMBO J., 11: 1733-1742, 1992.
    • (1992) EMBO J. , vol.11 , pp. 1733-1742
    • Volberg, T.1    Zick, Y.2    Dror, R.3    Sabanay, I.4    Gilon, C.5    Levitzki, A.6    Geiger, B.7
  • 26
    • 33744907308 scopus 로고    scopus 로고
    • Cadherin-mediated adhesion is required for normal growth regulation of human gingival epithelial cells
    • Kandikonda, S., Oda, D., Niederman, R., and Sorkin, B. C. Cadherin-mediated adhesion is required for normal growth regulation of human gingival epithelial cells. Cell Adhes. Commun., 4: 13-24, 1996.
    • (1996) Cell Adhes. Commun. , vol.4 , pp. 13-24
    • Kandikonda, S.1    Oda, D.2    Niederman, R.3    Sorkin, B.C.4
  • 27
    • 0031057785 scopus 로고    scopus 로고
    • E-cadherin mediates adhesion and suppresses cell motility via distinct mechanisms
    • Chen, H., Paradies, N. E., Fedor-Chaiken, M., and Brackenbury, R. E-cadherin mediates adhesion and suppresses cell motility via distinct mechanisms. J. Cell Sci., 110: 345-356, 1997.
    • (1997) J. Cell Sci. , vol.110 , pp. 345-356
    • Chen, H.1    Paradies, N.E.2    Fedor-Chaiken, M.3    Brackenbury, R.4
  • 28
    • 0031009585 scopus 로고    scopus 로고
    • E-cadherin engagement stimulates tyrosine phosphorylation
    • Kinch, M. S., Petch, L., Zhong, C., and Burridge, K. E-cadherin engagement stimulates tyrosine phosphorylation. Cell Adhes. Commun., 4: 425-437, 1997.
    • (1997) Cell Adhes. Commun. , vol.4 , pp. 425-437
    • Kinch, M.S.1    Petch, L.2    Zhong, C.3    Burridge, K.4
  • 29
    • 0026557242 scopus 로고
    • Characterization of epithelial phenotypes in mortal and immortal human breast cells
    • Paine, T. M., Soule, H. D., Pauley, R. J., and Dawson, P. J. Characterization of epithelial phenotypes in mortal and immortal human breast cells. Int. J. Cancer, 50: 463-473, 1992.
    • (1992) Int. J. Cancer , vol.50 , pp. 463-473
    • Paine, T.M.1    Soule, H.D.2    Pauley, R.J.3    Dawson, P.J.4
  • 30
    • 0027688586 scopus 로고
    • The MCF10 family of spontaneously immortalized human breast epithelial cell lines: Models of neoplastic progression
    • Pauley, R. J., Soule, H. D., Tait, L., Miller, F. R., Wolman, S. R., Dawson, P. J., and Heppner, G. H. The MCF10 family of spontaneously immortalized human breast epithelial cell lines: models of neoplastic progression. Eur. J. Cancer Prev., 2 (Suppl. 3): 67-76, 1993.
    • (1993) Eur. J. Cancer Prev. , vol.2 , Issue.3 SUPPL. , pp. 67-76
    • Pauley, R.J.1    Soule, H.D.2    Tait, L.3    Miller, F.R.4    Wolman, S.R.5    Dawson, P.J.6    Heppner, G.H.7
  • 31
    • 0029986283 scopus 로고    scopus 로고
    • Metastasis from human breast cancer cell lines
    • Price, J. E. Metastasis from human breast cancer cell lines. Breast Cancer Res. Treat., 39: 93-102, 1996.
    • (1996) Breast Cancer Res. Treat. , vol.39 , pp. 93-102
    • Price, J.E.1
  • 32
    • 0026351389 scopus 로고
    • Relative malignant potential of human breast carcinoma cell lines established from pleural effusions and a brain metastasis
    • Zhang, R. D., Fidler, I. J., and Price, J. E. Relative malignant potential of human breast carcinoma cell lines established from pleural effusions and a brain metastasis. Invasion Metastasis, 11: 204-215, 1991.
    • (1991) Invasion Metastasis , vol.11 , pp. 204-215
    • Zhang, R.D.1    Fidler, I.J.2    Price, J.E.3
  • 33
    • 0022391165 scopus 로고
    • Purification and characterization of a protein-tyrosine kinase encoded by the Abelson murine leukemia virus
    • Foulkes, J. G., Chow, M., Gorka, C., Frackelton, A. R. J., and Baltimore, D. Purification and characterization of a protein-tyrosine kinase encoded by the Abelson murine leukemia virus. J. Biol. Chem., 260: 8070-8077, 1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8070-8077
    • Foulkes, J.G.1    Chow, M.2    Gorka, C.3    Frackelton, A.R.J.4    Baltimore, D.5
  • 34
    • 0025873239 scopus 로고
    • B lymphocyte activation is accompanied by phosphorylation of a 72-kDa protein-tyrosine kinase
    • Hutchcroft, J. E., Harrison, M. L., and Geahlen, R. L. B lymphocyte activation is accompanied by phosphorylation of a 72-kDa protein-tyrosine kinase. J. Biol. Chem., 266: 14846-14849, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14846-14849
    • Hutchcroft, J.E.1    Harrison, M.L.2    Geahlen, R.L.3
  • 35
    • 0028104680 scopus 로고
    • Activation of the Eck receptor protein tyrosine kinase stimulates phosphatidylinositol 3-kinase activity
    • Pandey, A., Lazar, D. F., Saltiel, A. R., and Dixit, V. M. Activation of the Eck receptor protein tyrosine kinase stimulates phosphatidylinositol 3-kinase activity. J. Biol. Chem., 269: 30154-30157, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30154-30157
    • Pandey, A.1    Lazar, D.F.2    Saltiel, A.R.3    Dixit, V.M.4
  • 37
    • 0021354908 scopus 로고
    • Rabbit antiserum against a purified surface glycoprotein decompacts mouse preimplantation embryos and reacts with specific adult tissues
    • Vestweber, D., and Kemler, R. Rabbit antiserum against a purified surface glycoprotein decompacts mouse preimplantation embryos and reacts with specific adult tissues. Exp. Cell Res., 152: 169-178, 1984.
    • (1984) Exp. Cell Res. , vol.152 , pp. 169-178
    • Vestweber, D.1    Kemler, R.2
  • 38
    • 0025651841 scopus 로고
    • A possible new adhesive site in the cell-adhesion molecule uvomorulin
    • Ozawa, M., Hoschutzky, H., Herrenknecht, K., and Kemler, R. A possible new adhesive site in the cell-adhesion molecule uvomorulin. Mech. Dev., 33: 49-56, 1990.
    • (1990) Mech. Dev. , vol.33 , pp. 49-56
    • Ozawa, M.1    Hoschutzky, H.2    Herrenknecht, K.3    Kemler, R.4
  • 40
    • 0029965695 scopus 로고    scopus 로고
    • Integrin-mediated signalling: Regulation by protein tyrosine kinases and small GTP-bindirg proteins
    • Parsons, J. T. Integrin-mediated signalling: regulation by protein tyrosine kinases and small GTP-bindirg proteins. Curr. Opin. Cell Biol., 8: 146-152, 1996.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 146-152
    • Parsons, J.T.1
  • 41
  • 42
    • 0023681190 scopus 로고
    • Epidermal growth factor gene expression in human breast cancer cells: Regulation of expression by progestins
    • Murphy, L. C., Murphy, L. J., Dubik, D., Bell, G. I., and Shiu, R. P. Epidermal growth factor gene expression in human breast cancer cells: regulation of expression by progestins. Cancer Res., 48: 4555-4560, 1988.
    • (1988) Cancer Res. , vol.48 , pp. 4555-4560
    • Murphy, L.C.1    Murphy, L.J.2    Dubik, D.3    Bell, G.I.4    Shiu, R.P.5
  • 43
    • 0031001812 scopus 로고    scopus 로고
    • Juxtamembrane tyrosine residues couple the Eph family receptor EphB2/ Nuk to specific SH2 domain proteins in neuronal cells
    • Holland, S. J., Gale, N. W., Gish, G. D., Roth, R. A., Songyang, Z., Cantley, L. C., Henkemeyer, M., Yancopoulos, G. D., and Pawson, T. Juxtamembrane tyrosine residues couple the Eph family receptor EphB2/ Nuk to specific SH2 domain proteins in neuronal cells. EMBO J., 16: 3877-3888, 1997.
    • (1997) EMBO J. , vol.16 , pp. 3877-3888
    • Holland, S.J.1    Gale, N.W.2    Gish, G.D.3    Roth, R.A.4    Songyang, Z.5    Cantley, L.C.6    Henkemeyer, M.7    Yancopoulos, G.D.8    Pawson, T.9
  • 44
    • 0032489430 scopus 로고    scopus 로고
    • The VAB-1 Eph receptor tyrosine kinase functions in neural and epithelial morphogenesis in C. elegans
    • George, S. E., Simokat, K., Hardin, J., and Chisholm, A. D. The VAB-1 Eph receptor tyrosine kinase functions in neural and epithelial morphogenesis in C. elegans. Cell, 92: 633-643, 1998.
    • (1998) Cell , vol.92 , pp. 633-643
    • George, S.E.1    Simokat, K.2    Hardin, J.3    Chisholm, A.D.4
  • 45
    • 0344816258 scopus 로고    scopus 로고
    • Nuk controls pathfinding of commissural axons in the mammalian central nervous system
    • Henkemeyer, M., Orioli, D., Henderson, J. T., Saxton, T. M., Roder, J., Pawson, T., and Klein, R. Nuk controls pathfinding of commissural axons in the mammalian central nervous system. Cell, 86: 35-46, 1996.
    • (1996) Cell , vol.86 , pp. 35-46
    • Henkemeyer, M.1    Orioli, D.2    Henderson, J.T.3    Saxton, T.M.4    Roder, J.5    Pawson, T.6    Klein, R.7
  • 46
    • 0027058972 scopus 로고
    • Molecular and cellular analysis of basement membrane invasion by human breast cancer cells in Matrigel-based in vitro assays
    • Bae, S. N., Arand, G., Azzam, H., Pavasant, P., Torri, J., Frandsen, T. L., and Thompson, E. W. Molecular and cellular analysis of basement membrane invasion by human breast cancer cells in Matrigel-based in vitro assays. Breast Cancer Res. Treat., 24: 241-255, 1993.
    • (1993) Breast Cancer Res. Treat. , vol.24 , pp. 241-255
    • Bae, S.N.1    Arand, G.2    Azzam, H.3    Pavasant, P.4    Torri, J.5    Frandsen, T.L.6    Thompson, E.W.7
  • 47
    • 0021733283 scopus 로고
    • Some structural and functional aspects of the cell adhesion molecule uvomorulin
    • Vestweber, D., and Kemler, R. Some structural and functional aspects of the cell adhesion molecule uvomorulin. Cell Differ., 15: 269-273, 1984.
    • (1984) Cell Differ. , vol.15 , pp. 269-273
    • Vestweber, D.1    Kemler, R.2
  • 48
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge, K., Fath, K., Kelly, T., Nuckolls, G., and Turner, C. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol., 4: 487-525, 1988.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.5
  • 49
    • 0029130473 scopus 로고
    • Altered adhesions in ras-transformed breast epithelial cells
    • Kinch, M. S., and Burridge, K. Altered adhesions in ras-transformed breast epithelial cells. Biochem. Soc. Trans., 23: 446-450, 1995.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 446-450
    • Kinch, M.S.1    Burridge, K.2
  • 50
    • 0022427780 scopus 로고
    • Identification of a putative cell adhesion domain of uvomorulin
    • Vestweber, D., and Kemler, R. Identification of a putative cell adhesion domain of uvomorulin. EMBO J., 4: 3393-3398, 1985.
    • (1985) EMBO J. , vol.4 , pp. 3393-3398
    • Vestweber, D.1    Kemler, R.2
  • 51
    • 0031893255 scopus 로고    scopus 로고
    • Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase
    • Stein, E., Huynh-Do, U., Lane, A. A., Cerretti, D. P., and Daniel, T. O. Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase. J. Biol. Chem., 273: 1303-1308, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1303-1308
    • Stein, E.1    Huynh-Do, U.2    Lane, A.A.3    Cerretti, D.P.4    Daniel, T.O.5
  • 52
    • 0032031705 scopus 로고    scopus 로고
    • Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses
    • R.L.
    • Stein, E., Lane, A. A., Cerretti, D. P., Schoecklmann, H. O., Schroff, A. D., Van, E., RL, and Daniel, T. O. Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses. Genes Dev., 12: 667-678, 1998.
    • (1998) Genes Dev. , vol.12 , pp. 667-678
    • Stein, E.1    Lane, A.A.2    Cerretti, D.P.3    Schoecklmann, H.O.4    Schroff, A.D.5    Van, E.6    Daniel, T.O.7
  • 53
    • 0032554762 scopus 로고    scopus 로고
    • Complex formation between EphB2 and Src requires phosphorylation of tyrosine 611 in the EphB2 juxtamembrane region
    • Zisch, A. H., Kalo, M. S., Chong, L. D., and Pasquale, E. B. Complex formation between EphB2 and Src requires phosphorylation of tyrosine 611 in the EphB2 juxtamembrane region. Oncogene, 16: 2657-2670, 1998.
    • (1998) Oncogene , vol.16 , pp. 2657-2670
    • Zisch, A.H.1    Kalo, M.S.2    Chong, L.D.3    Pasquale, E.B.4
  • 55
    • 0025373765 scopus 로고
    • Overexpression confers an oncogenic potential upon the eph gene
    • Maru, Y., Hirai, H., and Takaku, F. Overexpression confers an oncogenic potential upon the eph gene. Oncogene, 5: 445-447, 1990.
    • (1990) Oncogene , vol.5 , pp. 445-447
    • Maru, Y.1    Hirai, H.2    Takaku, F.3
  • 56
    • 0029095073 scopus 로고
    • Characterization of a novel Src-like adapter protein that associates with the Eck receptor tyrosine kinase
    • Pandey, A., Duan, H., and Dixit, V. M. Characterization of a novel Src-like adapter protein that associates with the Eck receptor tyrosine kinase. J. Biol. Chem., 270: 19201-19204, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19201-19204
    • Pandey, A.1    Duan, H.2    Dixit, V.M.3
  • 58
    • 0027685701 scopus 로고
    • Cadherins in cancer: Implications for invasion and metastasis
    • Takeichi, M. Cadherins in cancer: implications for invasion and metastasis. Curr. Opin. Cell Biol., 5: 806-811, 1993.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 806-811
    • Takeichi, M.1
  • 59
    • 0024295439 scopus 로고
    • Expressed recombinant cadherins mediate cell sorting in model systems
    • Nose, A., Nagafuchi, A., and Takeichi, M. Expressed recombinant cadherins mediate cell sorting in model systems. Cell, 54: 993-1001, 1988.
    • (1988) Cell , vol.54 , pp. 993-1001
    • Nose, A.1    Nagafuchi, A.2    Takeichi, M.3
  • 60
    • 0019989719 scopus 로고
    • Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter
    • Southern, P. J., and Berg, P. Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter. J. Mol. Appl. Genet., 1: 327-341, 1982.
    • (1982) J. Mol. Appl. Genet. , vol.1 , pp. 327-341
    • Southern, P.J.1    Berg, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.