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Volumn 18, Issue 8, 1999, Pages 2165-2173

Surface densities of ephrin-B1 determine EphB1-coupled activation of cell attachment through α(v)β3 and α5β1 integrins

Author keywords

EphB1; Integrins; Ligand density discrimination

Indexed keywords

ARGINYLGLYCYLASPARTIC ACID; FIBRINOGEN; INTEGRIN; LIGAND;

EID: 0033560751     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (180)

References (35)
  • 2
    • 0028129144 scopus 로고
    • Molecular characterization of a family of ligands for eph-related tyrosine kinase receptors
    • Beckmann, M.P. et al. (1994) Molecular characterization of a family of ligands for eph-related tyrosine kinase receptors. EMBO J., 13, 3757-3762.
    • (1994) EMBO J. , vol.13 , pp. 3757-3762
    • Beckmann, M.P.1
  • 4
    • 0029773888 scopus 로고    scopus 로고
    • Cell-cell adhesion mediated by binding of membrane-anchored ligand LERK-2 to the EPH-related receptor human embryonal kinase 2 promotes tyrosine kinase activity
    • Bohme, B., VandenBos, T., Cerretti, D.P., Park, L.S., Holtrich, U., Ruebsamen-Waigmann, H. and Strebhardt, K. (1996) Cell-cell adhesion mediated by binding of membrane-anchored ligand LERK-2 to the EPH-related receptor human embryonal kinase 2 promotes tyrosine kinase activity. J. Biol. Chem., 271, 24747-24752.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24747-24752
    • Bohme, B.1    Vandenbos, T.2    Cerretti, D.P.3    Park, L.S.4    Holtrich, U.5    Ruebsamen-Waigmann, H.6    Strebhardt, K.7
  • 6
    • 0030891962 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of transmembrane ligands for EPH receptors
    • Bruckner, K., Pasquale, E.B. and Klein, R. (1997) Tyrosine phosphorylation of transmembrane ligands for EPH receptors. Science, 275, 1640-1643.
    • (1997) Science , vol.275 , pp. 1640-1643
    • Bruckner, K.1    Pasquale, E.B.2    Klein, R.3
  • 7
    • 0029086140 scopus 로고
    • Complementary gradients in expression and binding of ELF1 and Mek4 in development of the topographic retinotectal projection map
    • Cheng, H., Nakamoto, M., Bergemann, A.D. and Flanagan, J.G. (1995) Complementary gradients in expression and binding of ELF1 and Mek4 in development of the topographic retinotectal projection map. Cell, 82, 371-381.
    • (1995) Cell , vol.82 , pp. 371-381
    • Cheng, H.1    Nakamoto, M.2    Bergemann, A.D.3    Flanagan, J.G.4
  • 8
    • 0029082312 scopus 로고
    • In vitro guidance of retinal ganglion cell axons by RAGS, a 25 kDa tectal protein related to ligands for Eph receptor tyrosine kinases
    • Drescher, U., Kremoser, C., Handwerker, C., Loschinger, J., Noda, M. and Bonhoeffer, F. (1995) In vitro guidance of retinal ganglion cell axons by RAGS, a 25 kDa tectal protein related to ligands for Eph receptor tyrosine kinases. Cell, 82, 359-370.
    • (1995) Cell , vol.82 , pp. 359-370
    • Drescher, U.1    Kremoser, C.2    Handwerker, C.3    Loschinger, J.4    Noda, M.5    Bonhoeffer, F.6
  • 10
    • 15844429889 scopus 로고    scopus 로고
    • Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis
    • Gale, N.W. et al. (1996) Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis. Neuron, 17, 9-19.
    • (1996) Neuron , vol.17 , pp. 9-19
    • Gale, N.W.1
  • 11
    • 0029851690 scopus 로고    scopus 로고
    • Bidirectional signaling through the EPH-family receptor Nuk and its transmembrane ligands
    • Holland, S.J., Gale, N.W., Mbamalu, G., Yancopoulos, G.D., Henkemeyer, M. and Pawson, T. (1996) Bidirectional signaling through the EPH-family receptor Nuk and its transmembrane ligands. Nature, 383, 722-725.
    • (1996) Nature , vol.383 , pp. 722-725
    • Holland, S.J.1    Gale, N.W.2    Mbamalu, G.3    Yancopoulos, G.D.4    Henkemeyer, M.5    Pawson, T.6
  • 12
  • 13
    • 0029048813 scopus 로고
    • The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity
    • Hughes, P.E., O'Toole, T.E., Ylanne, J., Shattil, S.J. and Ginsberg, M.H. (1995) The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity. J. Biol. Chem., 270, 12411-12417.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12411-12417
    • Hughes, P.E.1    O'Toole, T.E.2    Ylanne, J.3    Shattil, S.J.4    Ginsberg, M.H.5
  • 14
    • 0030962317 scopus 로고    scopus 로고
    • The N-terminal globular domain of Eph receptors is sufficient for ligand binding and receptor signaling
    • Labrador, J.P., Brambilla, R. and Klein, R. (1997) The N-terminal globular domain of Eph receptors is sufficient for ligand binding and receptor signaling. EMBO J., 16, 3889-3897.
    • (1997) EMBO J. , vol.16 , pp. 3889-3897
    • Labrador, J.P.1    Brambilla, R.2    Klein, R.3
  • 15
    • 0025273452 scopus 로고
    • Nck, a melanoma cDNA encoding a cytoplasmic protein consisting of the src homology units SH2 and SH3
    • Lehmann, J.M., Riethmuller, G. and Johnson, J.P. (1990) Nck, a melanoma cDNA encoding a cytoplasmic protein consisting of the src homology units SH2 and SH3. Nucleic Acids Res., 18, 1048.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1048
    • Lehmann, J.M.1    Riethmuller, G.2    Johnson, J.P.3
  • 16
    • 0030973549 scopus 로고    scopus 로고
    • Identification of a subpopulation of human renal microvascular endothelial cells with capacity to form capillary-like cord and tube structures
    • Martin, M.M., Schoecklmann, H.O., Foster, G., Barley-Maloney, L., McKanna, J. and Daniel, T.O. (1997) Identification of a subpopulation of human renal microvascular endothelial cells with capacity to form capillary-like cord and tube structures. In Vitro Cell. Dev. Biol., 33, 261-269.
    • (1997) In Vitro Cell. Dev. Biol. , vol.33 , pp. 261-269
    • Martin, M.M.1    Schoecklmann, H.O.2    Foster, G.3    Barley-Maloney, L.4    McKanna, J.5    Daniel, T.O.6
  • 20
    • 0031034352 scopus 로고    scopus 로고
    • Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness
    • published erratum appears in Nature 1997, 388, 210
    • Palecek, S.P., Loftus, J.C., Ginsberg, M.H., Lauffenburger, D.A. and Horwitz, A.F. (1997) Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness [published erratum appears in Nature 1997, 388, 210]. Nature, 385, 537-540.
    • (1997) Nature , vol.385 , pp. 537-540
    • Palecek, S.P.1    Loftus, J.C.2    Ginsberg, M.H.3    Lauffenburger, D.A.4    Horwitz, A.F.5
  • 21
    • 0032513019 scopus 로고    scopus 로고
    • Integrin beta cytoplasmic domains differentially bind to cytoskeletal proteins
    • Pfaff, M., Liu, S., Erle, D.J. and Ginsberg, M.H. (1998) Integrin beta cytoplasmic domains differentially bind to cytoskeletal proteins. J. Biol. Chem., 273, 6104-6109.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6104-6109
    • Pfaff, M.1    Liu, S.2    Erle, D.J.3    Ginsberg, M.H.4
  • 22
    • 0029091904 scopus 로고
    • SAM: A novel motif in yeast sterile and Drosophilia polyhomeotic proteins
    • Ponting, C.P. (1995) SAM: A novel motif in yeast sterile and Drosophilia polyhomeotic proteins. Protein Sci., 4, 1928-1930.
    • (1995) Protein Sci. , vol.4 , pp. 1928-1930
    • Ponting, C.P.1
  • 23
    • 0030814976 scopus 로고    scopus 로고
    • 3 integrin associates with activated insulin and PDGFβ receptors and potentiates the biological activity of PDGF
    • 3 integrin associates with activated insulin and PDGFβ receptors and potentiates the biological activity of PDGF. EMBO J., 16, 5600-5607.
    • (1997) EMBO J. , vol.16 , pp. 5600-5607
    • Schneller, M.1    Vuori, K.2    Ruoslahti, E.3
  • 25
    • 15644379801 scopus 로고    scopus 로고
    • Recognition of unique carboxyl-terminal motifs by distinct PDZ domains
    • Songyang, Z. et al. (1997) Recognition of unique carboxyl-terminal motifs by distinct PDZ domains. Science, 275, 73-77.
    • (1997) Science , vol.275 , pp. 73-77
    • Songyang, Z.1
  • 26
    • 78651127719 scopus 로고
    • Chemoaffinity in the orderly growth of nerve fiber patterns and connections
    • Sperry, R.W. (1963) Chemoaffinity in the orderly growth of nerve fiber patterns and connections. Proc. Natl Acad. Sci. USA, 50, 703-710.
    • (1963) Proc. Natl Acad. Sci. USA , vol.50 , pp. 703-710
    • Sperry, R.W.1
  • 27
    • 0029813872 scopus 로고    scopus 로고
    • Ligand activation of ELK receptor tyrosine kinase promotes its association with Grb10 and Grb2 in vascular endothelial cells
    • Stein, E., Cerretti, D.P. and Daniel, T.O. (1996) Ligand activation of ELK receptor tyrosine kinase promotes its association with Grb10 and Grb2 in vascular endothelial cells. J. Biol. Chem., 271, 23588-23593.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23588-23593
    • Stein, E.1    Cerretti, D.P.2    Daniel, T.O.3
  • 28
    • 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. (1998a) Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase. J. Biol. Chem., 273, 1303-1308.
    • (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
  • 29
    • 0032031705 scopus 로고    scopus 로고
    • Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment and assembly responses
    • 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.
    • (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 Etten, R.L.6    Daniel, T.O.7
  • 31
    • 0033524982 scopus 로고    scopus 로고
    • Oligomeric structure of the human EphB2 receptor SAM domain
    • Thanos, C.D., Goodwill, K.E. and Bowie, J.U. (1999) Oligomeric structure of the human EphB2 receptor SAM domain. Science, 283, 833-836.
    • (1999) Science , vol.283 , pp. 833-836
    • Thanos, C.D.1    Goodwill, K.E.2    Bowie, J.U.3
  • 32
    • 0030890656 scopus 로고    scopus 로고
    • EPH family transmembrane ligands can mediate repulsive guidance of trunk neural crest migration and motor axon outgrowth
    • Wang, H.U. and Anderson, D.J. (1997) EPH family transmembrane ligands can mediate repulsive guidance of trunk neural crest migration and motor axon outgrowth. Neuron, 18, 383-396.
    • (1997) Neuron , vol.18 , pp. 383-396
    • Wang, H.U.1    Anderson, D.J.2
  • 33
    • 0032577446 scopus 로고    scopus 로고
    • Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4
    • Wang, H.U., Chen, Z.F. and Anderson, D.J. (1998) Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4. Cell, 93, 741-753.
    • (1998) Cell , vol.93 , pp. 741-753
    • Wang, H.U.1    Chen, Z.F.2    Anderson, D.J.3
  • 35
    • 0002598194 scopus 로고
    • The three dimensional structure, chemical mechanism and function of the low molecular weight protein tyrosine phosphatases
    • Zhang, M., Stauffacher, C.V. and VanEtten, R.L. (1995) The three dimensional structure, chemical mechanism and function of the low molecular weight protein tyrosine phosphatases. Adv. Prot. Phosphatases, 9, 1-23.
    • (1995) Adv. Prot. Phosphatases , vol.9 , pp. 1-23
    • Zhang, M.1    Stauffacher, C.V.2    VanEtten, R.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.