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Volumn 298, Issue 1, 1999, Pages 1-9

Signal transfer by Eph receptors

Author keywords

Axon guidance; Cell adhesion; Cell migration; Cytoskeleton; Receptor tyrosine kinase; Signaling pathways; Tissue organization

Indexed keywords

CELL RECEPTOR; LIGAND; PROTEIN TYROSINE KINASE;

EID: 0032879897     PISSN: 0302766X     EISSN: None     Source Type: Journal    
DOI: 10.1007/PL00008807     Document Type: Review
Times cited : (61)

References (95)
  • 1
    • 0028345221 scopus 로고
    • Expression of two novel eph-related receptor protein tyrosine kinases in mammary gland development and carcinogenesis
    • Andres AC, Reid HH, Zurcher G, Blaschke RJ, Albrecht D, Ziemiecki A (1994) Expression of two novel eph-related receptor protein tyrosine kinases in mammary gland development and carcinogenesis. Oncogene 9:1461-1467
    • (1994) Oncogene , vol.9 , pp. 1461-1467
    • Andres, A.C.1    Reid, H.H.2    Zurcher, G.3    Blaschke, R.J.4    Albrecht, D.5    Ziemiecki, A.6
  • 4
    • 0027282452 scopus 로고
    • Tyrosine phosphorylation in early embryonic growth cones
    • Bixby JL, Jhabvala P (1993) Tyrosine phosphorylation in early embryonic growth cones. J Neurosci 13:3421-3432
    • (1993) J Neurosci , vol.13 , pp. 3421-3432
    • Bixby, J.L.1    Jhabvala, P.2
  • 5
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • Boguski MS, McCormick F (1993) Proteins regulating Ras and its relatives. Nature 366:643-654
    • (1993) Nature , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 6
    • 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 DP, Park LS, Holtrich U, Rubsamen-Waigmann H, 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    Rubsamen-Waigmann, H.6    Strebhardt, K.7
  • 7
    • 0030875902 scopus 로고    scopus 로고
    • Src and Ras are involved in separate pathways in epithelial cell scattering
    • Boyer B, Roche S, Denoyelle M, Thiery JP (1997) Src and Ras are involved in separate pathways in epithelial cell scattering. EMBO J 16:5904-5913
    • (1997) EMBO J , vol.16 , pp. 5904-5913
    • Boyer, B.1    Roche, S.2    Denoyelle, M.3    Thiery, J.P.4
  • 9
    • 0030891962 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of transmembrane ligands for Eph receptors
    • Bruckner K, Pasquale EB, 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
  • 10
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge K, Fath K, Kelly T, Nuckolls G, Turner C (1988) Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu Rev Cell Biol 4:487-525
    • (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
  • 12
    • 0032549520 scopus 로고    scopus 로고
    • The Src and signal transducers and activators of transcription pathways as specific targets for low molecular weight phosphotyrosine-protein phosphatase in platelet-derived growth factor signaling
    • Chiarugi P, Cirri P, Marra F, Raugei G, Fiaschi T, Camici G, Manao G, Romanelli RG, Ramponi G (1998) The Src and signal transducers and activators of transcription pathways as specific targets for low molecular weight phosphotyrosine-protein phosphatase in platelet-derived growth factor signaling. J Biol Chem 273:6776-6785
    • (1998) J Biol Chem , vol.273 , pp. 6776-6785
    • Chiarugi, P.1    Cirri, P.2    Marra, F.3    Raugei, G.4    Fiaschi, T.5    Camici, G.6    Manao, G.7    Romanelli, R.G.8    Ramponi, G.9
  • 13
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark EA, Brugge JS (1995) Integrins and signal transduction pathways: the road taken. Science 268:233-239
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 16
    • 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, 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
  • 17
    • 0025037965 scopus 로고
    • Genetic analysis of a Drosophila neural cell adhesion molecule: Interaction of fasciclin 1 and Abelson tyrosine kinase mutations
    • Elkins T, Zinn K, McAllister L, Hoffmann FM, Goodman CS (1990) Genetic analysis of a Drosophila neural cell adhesion molecule: interaction of fasciclin 1 and Abelson tyrosine kinase mutations. Cell 60:565-575
    • (1990) Cell , vol.60 , pp. 565-575
    • Elkins, T.1    Zinn, K.2    McAllister, L.3    Hoffmann, F.M.4    Goodman, C.S.5
  • 18
    • 0029867243 scopus 로고    scopus 로고
    • A juxtamembrane autophosphorylation site in the Eph family receptor tyrosine kinase, Sek, mediates high affinity interaction with p59fyn
    • Ellis C, Kasmi F, Ganju P, Walls E, Panayotou G, Reith AD (1996) A juxtamembrane autophosphorylation site in the Eph family receptor tyrosine kinase, Sek, mediates high affinity interaction with p59fyn. Oncogene 12:1727-1736
    • (1996) Oncogene , vol.12 , pp. 1727-1736
    • Ellis, C.1    Kasmi, F.2    Ganju, P.3    Walls, E.4    Panayotou, G.5    Reith, A.D.6
  • 19
    • 0031559401 scopus 로고    scopus 로고
    • Unified nomenclature for Eph family receptors and their ligands, the ephrins
    • Eph Nomenclature Committee (1997) Unified nomenclature for Eph family receptors and their ligands, the ephrins. Cell 90: 403-404
    • (1997) Cell , vol.90 , pp. 403-404
  • 20
    • 0029943447 scopus 로고    scopus 로고
    • Drosophila photoreceptor axon guidance and targeting requires the dreadlocks SH2/SH3 adapter protein
    • Garrity PA, Rao Y, Salecker I, McGlade J, Pawson T, Zipursky SL (1996) Drosophila photoreceptor axon guidance and targeting requires the dreadlocks SH2/SH3 adapter protein. Cell 85: 639-650
    • (1996) Cell , vol.85 , pp. 639-650
    • Garrity, P.A.1    Rao, Y.2    Salecker, I.3    McGlade, J.4    Pawson, T.5    Zipursky, S.L.6
  • 21
    • 0032489430 scopus 로고    scopus 로고
    • The vab-1 Eph receptor tyrosine kinase functions in neural and epithelial morphogenesis in c-elegans
    • George SE, Simokat K, Hardin J, Chisholm AD (1998) The vab-1 Eph receptor tyrosine kinase functions in neural and epithelial morphogenesis in c-elegans. Cell 92:633-643
    • (1998) Cell , vol.92 , pp. 633-643
    • George, S.E.1    Simokat, K.2    Hardin, J.3    Chisholm, A.D.4
  • 22
    • 0029838320 scopus 로고    scopus 로고
    • pp60(c-src) is required for cell locomotion regulated by the hyaluronanreceptor RHAMM
    • Hall CL, Lange LA, Prober DA, Zhang S, Turley EA (1996a) pp60(c-src) is required for cell locomotion regulated by the hyaluronanreceptor RHAMM. Oncogene 13:2213-2224
    • (1996) Oncogene , vol.13 , pp. 2213-2224
    • Hall, C.L.1    Lange, L.A.2    Prober, D.A.3    Zhang, S.4    Turley, E.A.5
  • 23
    • 0029906430 scopus 로고    scopus 로고
    • Review: A role for the FGF receptor in the axonal growth response stimulated by cell adhesion molecules?
    • Hall H, Walsh FS, Doherty P (1996b) Review: a role for the FGF receptor in the axonal growth response stimulated by cell adhesion molecules? Cell Adhes Commun 3:441-450
    • (1996) Cell Adhes Commun , vol.3 , pp. 441-450
    • Hall, H.1    Walsh, F.S.2    Doherty, P.3
  • 24
    • 0026345394 scopus 로고
    • Protein kinase catalytic domain sequence database: Identification of conserved features of primary structure and classification of family members
    • Hanks SK, Quinn AM (1991) Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Methods Enzymol 200:38-62
    • (1991) Methods Enzymol , vol.200 , pp. 38-62
    • Hanks, S.K.1    Quinn, A.M.2
  • 26
    • 0032480889 scopus 로고    scopus 로고
    • Crystal structure of the ligand-binding domains of the receptor tyrosine kinase EphB2
    • Himanen J-P, Henkemeyer M, Nikolov DB (1998) Crystal structure of the ligand-binding domains of the receptor tyrosine kinase EphB2. Nature 396:486-491
    • (1998) Nature , vol.396 , pp. 486-491
    • Himanen, J.-P.1    Henkemeyer, M.2    Nikolov, D.B.3
  • 27
    • 0032537766 scopus 로고    scopus 로고
    • Tyrosine-614, the major autophosphorylation site of the receptor tyrosine kinase HEK2, functions as multi-docking site for SH2-domain mediated interactions
    • Hock B, Bohme B, Karn T, Feller S, Rübsamen-Waigmann H, Strebhardt K (1998a) Tyrosine-614, the major autophosphorylation site of the receptor tyrosine kinase HEK2, functions as multi-docking site for SH2-domain mediated interactions. Oncogene 17:255-260
    • (1998) Oncogene , vol.17 , pp. 255-260
    • Hock, B.1    Bohme, B.2    Karn, T.3    Feller, S.4    Rübsamen-Waigmann, H.5    Strebhardt, K.6
  • 29
    • 0031568818 scopus 로고    scopus 로고
    • Reciprocal expression of the Eph receptor Cek5 and its ligand(s) in the early retina
    • Holash JA, Soans C, Chong LD, Shao H, Dixit VM, Pasquale EB (1997) Reciprocal expression of the Eph receptor Cek5 and its ligand(s) in the early retina. Dev Biol 182:256-269
    • (1997) Dev Biol , vol.182 , pp. 256-269
    • Holash, J.A.1    Soans, C.2    Chong, L.D.3    Shao, H.4    Dixit, V.M.5    Pasquale, E.B.6
  • 30
    • 0029851690 scopus 로고    scopus 로고
    • Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands
    • Holland SJ, Gale NW, Mbamalu G, Yancopoulos GD, Henkemeyer M, Pawson T (1996) Bidirectional signalling 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
  • 32
    • 0030971098 scopus 로고    scopus 로고
    • Down-regulation of the filamentous actin cross-linking activity of cortactin by Src-mediated tyrosine phosphorylation
    • Huang C, Ni Y, Wang T, Gao Y, Haudenschild CC, Zhan X (1997) Down-regulation of the filamentous actin cross-linking activity of cortactin by Src-mediated tyrosine phosphorylation. J Biol Chem 272:13911-13915
    • (1997) J Biol Chem , vol.272 , pp. 13911-13915
    • Huang, C.1    Ni, Y.2    Wang, T.3    Gao, Y.4    Haudenschild, C.C.5    Zhan, X.6
  • 33
    • 0030809301 scopus 로고    scopus 로고
    • Rac1 mediates collapsin-1-induced growth cone collapse
    • Jin Z, Strittmatter SM (1997) Rac1 mediates collapsin-1-induced growth cone collapse. J Neurosci 17:6256-6263
    • (1997) J Neurosci , vol.17 , pp. 6256-6263
    • Jin, Z.1    Strittmatter, S.M.2
  • 35
    • 0031906668 scopus 로고    scopus 로고
    • Loss of cell adhesion in Xenopus laevis embryos mediated by the cytoplasmic domain of Xlerk, an erythropoietin-producing hepatocellular ligand
    • Jones TL, Chong LD, Kim J, Xu RH, Kung HF, Daar IO (1998) Loss of cell adhesion in Xenopus laevis embryos mediated by the cytoplasmic domain of Xlerk, an erythropoietin-producing hepatocellular ligand. Proc Natl Acad Sci U S A 95:576-581
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 576-581
    • Jones, T.L.1    Chong, L.D.2    Kim, J.3    Xu, R.H.4    Kung, H.F.5    Daar, I.O.6
  • 36
    • 0030812083 scopus 로고    scopus 로고
    • Neural cell adhesion molecule L1: Signaling pathways and growth cone motility
    • Kamiguchi H, Lemmon V (1997) Neural cell adhesion molecule L1: signaling pathways and growth cone motility. J Neurosci Res 49:1-8
    • (1997) J Neurosci Res , vol.49 , pp. 1-8
    • Kamiguchi, H.1    Lemmon, V.2
  • 39
    • 0030962317 scopus 로고    scopus 로고
    • The N-terminal globular domain of Eph receptors is sufficient for ligand binding and receptor signaling
    • Labrador JP, Brambilla R, 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
  • 41
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger DA, Horwitz AF (1996) Cell migration: a physically integrated molecular process. Cell 84:359-369
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 42
    • 0027493163 scopus 로고
    • Biological and biochemical activities of a chimeric epidermal growth factor-Elk receptor tyrosine kinase
    • Lhotak V, Pawson T (1993) Biological and biochemical activities of a chimeric epidermal growth factor-Elk receptor tyrosine kinase. Mol Cell Biol 13:7071-7079
    • (1993) Mol Cell Biol , vol.13 , pp. 7071-7079
    • Lhotak, V.1    Pawson, T.2
  • 44
    • 0031065475 scopus 로고    scopus 로고
    • Rho family GTP-binding proteins in growth cone signalling
    • Luo L, Jan LY, Jan YN (1997) Rho family GTP-binding proteins in growth cone signalling. Curr Opin Neurobiol 7:81-86
    • (1997) Curr Opin Neurobiol , vol.7 , pp. 81-86
    • Luo, L.1    Jan, L.Y.2    Jan, Y.N.3
  • 45
    • 0028829750 scopus 로고
    • The Rho's progress: A potential role during neuritogenesis for the Rho family of GTPases
    • Mackay DJ, Nobes CD, Hall A (1995) The Rho's progress: a potential role during neuritogenesis for the Rho family of GTPases. Trends Neurosci 18:496-501
    • (1995) Trends Neurosci , vol.18 , pp. 496-501
    • Mackay, D.J.1    Nobes, C.D.2    Hall, A.3
  • 46
    • 0009666618 scopus 로고    scopus 로고
    • Negative regulator of mitogenesis by the adaptor protein SLAP (Src-like adaptor protein)
    • The Salk Institute for Biological Studies, La Jolla, CA
    • Manes G, Pandey A, Courtneidge SA, Roche S (1998) Negative regulator of mitogenesis by the adaptor protein SLAP (Src-like adaptor protein). Meeting on Tyrosine Phosphorylation and Cell Signaling, The Salk Institute for Biological Studies, La Jolla, CA, p 56
    • (1998) Meeting on Tyrosine Phosphorylation and Cell Signaling , pp. 56
    • Manes, G.1    Pandey, A.2    Courtneidge, S.A.3    Roche, S.4
  • 49
    • 0031057545 scopus 로고    scopus 로고
    • AL-1-induced growth cone collapse of rat cortical neurons is correlated with REK7 expression and rearrangement of the actin cytoskeleton
    • Meima L, Kljavin IJ, Moran P, Shih A, Winslow JW, Caras IW (1997a) AL-1-induced growth cone collapse of rat cortical neurons is correlated with REK7 expression and rearrangement of the actin cytoskeleton. Eur J Neurosci 9:177-188
    • (1997) Eur J Neurosci , vol.9 , pp. 177-188
    • Meima, L.1    Kljavin, I.J.2    Moran, P.3    Shih, A.4    Winslow, J.W.5    Caras, I.W.6
  • 50
    • 0030833727 scopus 로고    scopus 로고
    • Lerk2 (ephrin-B1) is a collapsing factor for a subset of cortical growth cones and acts by a mechanism different from AL-1 (ephrin-A5)
    • Meima L, Moran P, Matthews W, Caras IW (1997b) Lerk2 (ephrin-B1) is a collapsing factor for a subset of cortical growth cones and acts by a mechanism different from AL-1 (ephrin-A5). Mol Cell Neurosci 9:314-328
    • (1997) Mol Cell Neurosci , vol.9 , pp. 314-328
    • Meima, L.1    Moran, P.2    Matthews, W.3    Caras, I.W.4
  • 51
    • 0031952518 scopus 로고    scopus 로고
    • Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP
    • Miki H, Sasaki T, Takai Y, Takenawa T (1998) Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP. Nature 391:93-96
    • (1998) Nature , vol.391 , pp. 93-96
    • Miki, H.1    Sasaki, T.2    Takai, Y.3    Takenawa, T.4
  • 53
    • 0032559211 scopus 로고    scopus 로고
    • Coupling of Ras and Rac guanosine triphosphatases through the Ras exchanger Sos
    • Nimnual AS, Yatsula BA, Bar-Sagi D (1998) Coupling of Ras and Rac guanosine triphosphatases through the Ras exchanger Sos. Science 279:560-563
    • (1998) Science , vol.279 , pp. 560-563
    • Nimnual, A.S.1    Yatsula, B.A.2    Bar-Sagi, D.3
  • 55
    • 0029858435 scopus 로고    scopus 로고
    • Sek4 and Nuk receptors cooperate in guidance of commissural axons and in palate formation
    • Orioli D, Henkemeyer M, Lemke G, Klein R, Pawson T (1996) Sek4 and Nuk receptors cooperate in guidance of commissural axons and in palate formation. EMBO J 15:6035-6049
    • (1996) EMBO J , vol.15 , pp. 6035-6049
    • Orioli, D.1    Henkemeyer, M.2    Lemke, G.3    Klein, R.4    Pawson, T.5
  • 56
    • 0028104680 scopus 로고
    • Activation of the Eck receptor protein tyrosine kinase stimulates phosphatidylinositol 3-kinase activity
    • Pandey A, Lazar DF, Saltiel AR, Dixit VM (1994) Activation of the Eck receptor protein tyrosine kinase stimulates phosphatidylinositol 3-kinase activity. J Biol Chem 269:30154-30157
    • (1994) J Biol Chem , vol.269 , pp. 30154-30157
    • Pandey, A.1    Lazar, D.F.2    Saltiel, A.R.3    Dixit, V.M.4
  • 57
    • 0029095073 scopus 로고
    • Characterization of a novel Src-like adapter protein that associates with the Eck receptor tyrosine kinase
    • Pandey A, Duan H, Dixit VM (1995a) Characterization of a novel Src-like adapter protein that associates with the Eck receptor tyrosine kinase. J Biol Chem 270:19201-19204
    • (1995) J Biol Chem , vol.270 , pp. 19201-19204
    • Pandey, A.1    Duan, H.2    Dixit, V.M.3
  • 58
    • 0029362995 scopus 로고
    • Cell signalling. Receptor orphans find a family
    • Pandey A, Lindberg RA, Dixit VM (1995b) Cell signalling. Receptor orphans find a family. Curr Biol 5:986-989
    • (1995) Curr Biol , vol.5 , pp. 986-989
    • Pandey, A.1    Lindberg, R.A.2    Dixit, V.M.3
  • 59
    • 0029036501 scopus 로고
    • Role of B61, the ligand for the Eek receptor tyrosine kinase, in TNF-alpha-induced angiogenesis
    • Pandey A, Shao H, Marks RM, Polverini PJ, Dixit VM (1995c) Role of B61, the ligand for the Eek receptor tyrosine kinase, in TNF-alpha-induced angiogenesis. Science 268:567-569
    • (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
  • 60
    • 0030957996 scopus 로고    scopus 로고
    • Aberrant axonal projections in mice lacking EphA8 (Eek) tyrosine protein kinase receptors
    • Park S, Frisen J, Barbacid M (1997) Aberrant axonal projections in mice lacking EphA8 (Eek) tyrosine protein kinase receptors. EMBO J 16:3106-3114
    • (1997) EMBO J , vol.16 , pp. 3106-3114
    • Park, S.1    Frisen, J.2    Barbacid, M.3
  • 61
    • 0029965695 scopus 로고    scopus 로고
    • Integrin-mediated signalling: Regulation by protein tyrosine kinases and small GTP-binding proteins
    • Parsons JT (1996) Integrin-mediated signalling: regulation by protein tyrosine kinases and small GTP-binding proteins. Curr Opin Cell Biol 8:146-152
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 146-152
    • Parsons, J.T.1
  • 62
    • 0030898418 scopus 로고    scopus 로고
    • Src family protein tyrosine kinases: Cooperating with growth factor and adhesion signaling pathways
    • Parsons JT, Parsons SJ (1997) Src family protein tyrosine kinases: cooperating with growth factor and adhesion signaling pathways. Curr Opin Cell Biol 9:187-192
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 187-192
    • Parsons, J.T.1    Parsons, S.J.2
  • 63
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson T (1995) Protein modules and signalling networks. Nature 373:573-580
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 64
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson T, Scott JD (1997) Signaling through scaffold, anchoring, and adaptor proteins. Science 278:2075-2080
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 65
    • 0028198388 scopus 로고
    • Activation of phosphatidylinositol-3′ kinase by Src-family kinase SH3 binding to the p85 subunit
    • Pleiman CM, Hertz WM, Cambier JC (1994) Activation of phosphatidylinositol-3′ kinase by Src-family kinase SH3 binding to the p85 subunit. Science 263:1609-1612
    • (1994) Science , vol.263 , pp. 1609-1612
    • Pleiman, C.M.1    Hertz, W.M.2    Cambier, J.C.3
  • 66
    • 0029294676 scopus 로고
    • Guanine nucleotide exchange factors: Activators of the Ras superfamily of proteins
    • Quilliam LA, Khosravi-Far R, Huff SY, Der CJ (1995) Guanine nucleotide exchange factors: activators of the Ras superfamily of proteins. Bioessays 17:395-404
    • (1995) Bioessays , vol.17 , pp. 395-404
    • Quilliam, L.A.1    Khosravi-Far, R.2    Huff, S.Y.3    Der, C.J.4
  • 67
    • 0029126878 scopus 로고
    • Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains
    • Rivero-Lezcano OM, Marcilla A, Sameshima JH, Robbins KC (1995) Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains. Mol Cell Biol 15:5725-5731
    • (1995) Mol Cell Biol , vol.15 , pp. 5725-5731
    • Rivero-Lezcano, O.M.1    Marcilla, A.2    Sameshima, J.H.3    Robbins, K.C.4
  • 68
    • 0031040085 scopus 로고    scopus 로고
    • The GDNF-RET signalling partnership
    • Robertson K, Mason I (1997) The GDNF-RET signalling partnership. Trends Genet 13:1-3
    • (1997) Trends Genet , vol.13 , pp. 1-3
    • Robertson, K.1    Mason, I.2
  • 69
    • 0027317743 scopus 로고
    • Five novel avian Eph-related tyrosine kinases are differentially expressed
    • Sajjadi FG, Pasquale EB (1993) Five novel avian Eph-related tyrosine kinases are differentially expressed. Oncogene 8: 1807-1813
    • (1993) Oncogene , vol.8 , pp. 1807-1813
    • Sajjadi, F.G.1    Pasquale, E.B.2
  • 71
    • 0031022602 scopus 로고    scopus 로고
    • SAM as a protein interaction domain involved in developmental regulation
    • Schultz J, Ponting CP, Hofmann K, Bork P (1997) SAM as a protein interaction domain involved in developmental regulation. Protein Sci 6:249-253
    • (1997) Protein Sci , vol.6 , pp. 249-253
    • Schultz, J.1    Ponting, C.P.2    Hofmann, K.3    Bork, P.4
  • 72
    • 0030273003 scopus 로고    scopus 로고
    • PDZs and receptor/channel clustering: Rounding up the latest suspects
    • Sheng M (1996) PDZs and receptor/channel clustering: rounding up the latest suspects. Neuron 17:575-578
    • (1996) Neuron , vol.17 , pp. 575-578
    • Sheng, M.1
  • 73
    • 0029583193 scopus 로고
    • A role for phosphatidylinositol 3-kinase in the regulation of beta 1 integrin activity by the CD2 antigen
    • Shimizu Y, Mobley JL, Finkelstein LD, Chan AS (1995) A role for phosphatidylinositol 3-kinase in the regulation of beta 1 integrin activity by the CD2 antigen. J Cell Biol 131:1867-1880
    • (1995) J Cell Biol , vol.131 , pp. 1867-1880
    • Shimizu, Y.1    Mobley, J.L.2    Finkelstein, L.D.3    Chan, A.S.4
  • 74
    • 0031213749 scopus 로고    scopus 로고
    • The EphA4 and EphB1 receptor tyrosine kinases and ephrin-B2 ligand regulate targeted migration of branchial neural crest cells
    • Smith A, Robinson V, Patel K, Wilkinson DG (1997) The EphA4 and EphB1 receptor tyrosine kinases and ephrin-B2 ligand regulate targeted migration of branchial neural crest cells. Curr Biol 7:561-570
    • (1997) Curr Biol , vol.7 , pp. 561-570
    • Smith, A.1    Robinson, V.2    Patel, K.3    Wilkinson, D.G.4
  • 75
    • 0028875162 scopus 로고
    • Recognition and specificity in protein tyrosine kinase-mediatcd signalling
    • Songyang Z, Cantley LC (1995) Recognition and specificity in protein tyrosine kinase-mediatcd signalling. Trends Biochem Sci 20:470-475
    • (1995) Trends Biochem Sci , vol.20 , pp. 470-475
    • Songyang, Z.1    Cantley, L.C.2
  • 78
    • 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 DP, Daniel TO (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
  • 79
    • 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 AA, Cerretti DP, Daniel TO (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
  • 80
    • 0032031705 scopus 로고    scopus 로고
    • Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses
    • Stein E, Lane AA, Cerretti DP, Schoecklmann HO, Schroff AD, Van Etten RL, Daniel TO (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
  • 81
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton
    • Tapon N, Hall A (1997) Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr Opin Cell Biol 9:86-92
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 82
    • 0029045815 scopus 로고
    • Specific and redundant roles of Src and Fyn in organizing the cytoskelelon
    • Thomas SM, Soriano P, Imamoto A (1995) Specific and redundant roles of Src and Fyn in organizing the cytoskelelon. Nature 376:267-271
    • (1995) Nature , vol.376 , pp. 267-271
    • Thomas, S.M.1    Soriano, P.2    Imamoto, A.3
  • 83
    • 0028170817 scopus 로고
    • Receptor protein-tyrosine kinases and their signal transduction pathways
    • van der Geer P, Hunter T, Lindberg RA (1994) Receptor protein-tyrosine kinases and their signal transduction pathways. Annu Rev Cell Biol 10:251-337
    • (1994) Annu Rev Cell Biol , vol.10 , pp. 251-337
    • Van Der Geer, P.1    Hunter, T.2    Lindberg, R.A.3
  • 84
    • 85101729935 scopus 로고    scopus 로고
    • Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4
    • Wang HU, Zhou-Feng C, Anderson DJ (1998) Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4. Cell 93:7411-7753
    • (1998) Cell , vol.93 , pp. 7411-7753
    • Wang, H.U.1    Zhou-Feng, C.2    Anderson, D.J.3
  • 85
    • 0028089005 scopus 로고
    • Membrane ruffling and chemotaxis transduced by the PDGF beta-receptor require the binding site for phosphatidylinositol 3′ kinase
    • Wennstrom S, Siegbahn A, Yokote K, Arvidsson AK, Heldin CH, Mori S, Claesson-Welsh L (1994) Membrane ruffling and chemotaxis transduced by the PDGF beta-receptor require the binding site for phosphatidylinositol 3′ kinase. Oncogene 9: 651-660
    • (1994) Oncogene , vol.9 , pp. 651-660
    • Wennstrom, S.1    Siegbahn, A.2    Yokote, K.3    Arvidsson, A.K.4    Heldin, C.H.5    Mori, S.6    Claesson-Welsh, L.7
  • 86
    • 0030296507 scopus 로고    scopus 로고
    • Disruption of cell adhesion in Xenopus embryos by Pagliaccio, an Eph-class receptor tyrosine kinase
    • Winning RS, Scales JB, Sargent TD (1996) Disruption of cell adhesion in Xenopus embryos by Pagliaccio, an Eph-class receptor tyrosine kinase. Dev Biol 179:309-319
    • (1996) Dev Biol , vol.179 , pp. 309-319
    • Winning, R.S.1    Scales, J.B.2    Sargent, T.D.3
  • 88
    • 0031034679 scopus 로고    scopus 로고
    • Tyrosine kinase receptors concentrated in caveolae-like domains from neuronal plasma membrane
    • Wu C, Butz S, Ying Y, Anderson RG (1997) Tyrosine kinase receptors concentrated in caveolae-like domains from neuronal plasma membrane. J Biol Chem 272:3554-3559
    • (1997) J Biol Chem , vol.272 , pp. 3554-3559
    • Wu, C.1    Butz, S.2    Ying, Y.3    Anderson, R.G.4
  • 89
    • 13344261393 scopus 로고
    • Expression of truncated Sek-1 receptor tyrosine kinase disrupts the segmental restriction of gene expression in the Xenopus and zebrafish hindbrain
    • Xu Q, Alldus G, Holder N, Wilkinson DG (1995) Expression of truncated Sek-1 receptor tyrosine kinase disrupts the segmental restriction of gene expression in the Xenopus and zebrafish hindbrain. Development 121:4005-4016
    • (1995) Development , vol.121 , pp. 4005-4016
    • Xu, Q.1    Alldus, G.2    Holder, N.3    Wilkinson, D.G.4
  • 90
    • 0031444245 scopus 로고    scopus 로고
    • Identification of the Abl-and rasGAP-associated 62 kDa protein as a docking protein, Dok
    • Yamanashi Y, Baltimore D (1997) Identification of the Abl-and rasGAP-associated 62 kDa protein as a docking protein, Dok. Cell 88:205-211
    • (1997) Cell , vol.88 , pp. 205-211
    • Yamanashi, Y.1    Baltimore, D.2
  • 91
    • 0029165973 scopus 로고
    • The glypiated neuronal cell adhesion molecule contactin/F11 complexes with Src-family protein tyrosine kinase Fyn
    • Zisch AH, D'Alessandri L, Amrein K, Rauscht B, Winterhalter KH, Vaughan L (1995) The glypiated neuronal cell adhesion molecule contactin/F11 complexes with Src-family protein tyrosine kinase Fyn. Mol Cell Neurosci 6:263-279
    • (1995) Mol Cell Neurosci , vol.6 , pp. 263-279
    • Zisch, A.H.1    D'Alessandri, L.2    Amrein, K.3    Rauscht, B.4    Winterhalter, K.H.5    Vaughan, L.6
  • 92
    • 0030807905 scopus 로고    scopus 로고
    • The Eph family: A multitude of receptors that mediate cell recognition signals
    • Zisch AH, Pasquale EB (1997) The Eph family: a multitude of receptors that mediate cell recognition signals. Cell Tiss Res 290:217-226
    • (1997) Cell Tiss Res , vol.290 , pp. 217-226
    • Zisch, A.H.1    Pasquale, E.B.2
  • 95
    • 0032554762 scopus 로고    scopus 로고
    • Complex formation between EphB2 and Src requires phosphorylation of tyrosine 611 in the EphB2 juxtamembrane region
    • Zisch AH, Kalo MS, Chong LD, Pasquale EB (1998b) Complex formation between EphB2 and Src requires phosphorylation of tyrosine 611 in the EphB2 juxtamembrane region. Oncogene 16:2657-2670
    • (1998) Oncogene , vol.16 , pp. 2657-2670
    • Zisch, A.H.1    Kalo, M.S.2    Chong, L.D.3    Pasquale, E.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.