메뉴 건너뛰기




Volumn 6, Issue 6, 2005, Pages 462-475

Eph receptor signalling casts a wide net on cell behaviour

Author keywords

[No Author keywords available]

Indexed keywords

EPHRIN; EPHRIN RECEPTOR; LIGAND; PROTEIN TYROSINE KINASE;

EID: 20344396123     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1662     Document Type: Review
Times cited : (890)

References (132)
  • 1
    • 0041669478 scopus 로고    scopus 로고
    • 'Eph' ective signaling: Forward, reverse and crosstalk
    • Murai, K. K. & Pasquale, E. B. 'Eph' ective signaling: forward, reverse and crosstalk. J. Cell Sci. 116, 2823-2832 (2003).
    • (2003) J. Cell Sci. , vol.116 , pp. 2823-2832
    • Murai, K.K.1    Pasquale, E.B.2
  • 2
    • 2142764419 scopus 로고    scopus 로고
    • Eph-ephrin promiscuity is now crystal clear
    • Pasquale, E. B. Eph-ephrin promiscuity is now crystal clear. Nature Neurosci. 7, 417-418 (2004).
    • (2004) Nature Neurosci. , vol.7 , pp. 417-418
    • Pasquale, E.B.1
  • 3
    • 0030807905 scopus 로고    scopus 로고
    • The Eph family: A multitude of receptors that mediate cell recognition signals
    • Zisch, A. H. & 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
  • 4
    • 11144354644 scopus 로고    scopus 로고
    • Repelling class discrimination: Ephrin-A5 binds to and activates EphB2 receptor signaling
    • Himanen, J. P. et al. Repelling class discrimination: ephrin-A5 binds to and activates EphB2 receptor signaling. Nature Neurosci. 7, 501-509 (2004).
    • (2004) Nature Neurosci. , vol.7 , pp. 501-509
    • Himanen, J.P.1
  • 5
    • 0031922119 scopus 로고    scopus 로고
    • The ephrins and Eph receptors in neural development
    • Flanagan, J. G. & Vanderhaeghen, P. The ephrins and Eph receptors in neural development. Annu. Rev. Neurosci. 21, 309-345 (1998).
    • (1998) Annu. Rev. Neurosci. , vol.21 , pp. 309-345
    • Flanagan, J.G.1    Vanderhaeghen, P.2
  • 6
    • 0035287473 scopus 로고    scopus 로고
    • Multiple roles of Eph receptors and ephrins in neural development
    • Wilkinson, D. G. Multiple roles of Eph receptors and ephrins in neural development. Nature Rev. Neurosci. 2, 155-164 (2001).
    • (2001) Nature Rev. Neurosci. , vol.2 , pp. 155-164
    • Wilkinson, D.G.1
  • 7
    • 0036303033 scopus 로고    scopus 로고
    • Mechanisms and functions of Eph and ephrin signalling
    • Kullander, K. & Klein, R. Mechanisms and functions of Eph and ephrin signalling. Nature Rev. Mol. Cell Biol. 3, 475-486 (2002).
    • (2002) Nature Rev. Mol. Cell Biol. , vol.3 , pp. 475-486
    • Kullander, K.1    Klein, R.2
  • 8
    • 0037213432 scopus 로고    scopus 로고
    • Eph signaling: A structural view
    • Himanen, J. P. & Nikolov, D. B. Eph signaling: a structural view. Trends Neurosci. 26, 46-51 (2003).
    • (2003) Trends Neurosci. , vol.26 , pp. 46-51
    • Himanen, J.P.1    Nikolov, D.B.2
  • 9
    • 0035924322 scopus 로고    scopus 로고
    • Crystal structure of an Eph receptor-ephrin complex
    • Himanen, J. P. et al. Crystal structure of an Eph receptor-ephrin complex. Nature 414, 933-938 (2001). Identifies two binding interfaces between EphB2 and ephrin-B2 and determines their high resolution structure. On the basis of the structural findings, it proposes that Eph-receptor-ephrin signalling complexes form tetramers that can further assemble into larger signalling clusters.
    • (2001) Nature , vol.414 , pp. 933-938
    • Himanen, J.P.1
  • 10
    • 0035409126 scopus 로고    scopus 로고
    • Crystal structure of an ephrin ectodomain
    • Toth, J. et al. Crystal structure of an ephrin ectodomain. Dev. Cell 1, 83-92 (2001).
    • (2001) Dev. Cell , vol.1 , pp. 83-92
    • Toth, J.1
  • 11
    • 1542364449 scopus 로고    scopus 로고
    • Dissecting the EphA3/Ephrin-A5 interactions using a novel functional mutagenesis screen
    • Smith, F. M. et al. Dissecting the EphA3/Ephrin-A5 interactions using a novel functional mutagenesis screen. J. Biol. Chem. 279, 9522-9531 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 9522-9531
    • Smith, F.M.1
  • 12
    • 1442358805 scopus 로고    scopus 로고
    • Recruitment of Eph receptors into signaling clusters does not require ephrin contact
    • Wimmer-Kleikamp, S. H., Janes, P. W., Squire, A., Bastiaens, P. I. & Lackmann, M. Recruitment of Eph receptors into signaling clusters does not require ephrin contact. J. Cell Biol. 164, 661-666 (2004).
    • (2004) J. Cell Biol. , vol.164 , pp. 661-666
    • Wimmer-Kleikamp, S.H.1    Janes, P.W.2    Squire, A.3    Bastiaens, P.I.4    Lackmann, M.5
  • 13
    • 0032879897 scopus 로고    scopus 로고
    • Signal transfer by Eph receptors
    • Kalo, M. S. & Pasquale, E. B. Signal transfer by Eph receptors. Cell Tissue Res. 298, 1-9 (1999).
    • (1999) Cell Tissue Res. , vol.298 , pp. 1-9
    • Kalo, M.S.1    Pasquale, E.B.2
  • 14
    • 17044448886 scopus 로고    scopus 로고
    • Src family kinases are involved in EphA receptor-mediated retinal axon guidance
    • Knoll, B. & Drescher, U. Src family kinases are involved in EphA receptor-mediated retinal axon guidance. J. Neurosci. 24, 6248-6257 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 6248-6257
    • Knoll, B.1    Drescher, U.2
  • 15
    • 0034642564 scopus 로고    scopus 로고
    • Replacing two conserved tyrosines of the EphB2 receptor with glutamic acid prevents binding of SH2 domains without abrogating kinase activity and biological responses
    • Zisch, A. H. et al. Replacing two conserved tyrosines of the EphB2 receptor with glutamic acid prevents binding of SH2 domains without abrogating kinase activity and biological responses. Oncogene 19, 177-187 (2000).
    • (2000) Oncogene , vol.19 , pp. 177-187
    • Zisch, A.H.1
  • 16
    • 0035929146 scopus 로고    scopus 로고
    • Structural basis for autoinhibition of the EphB2 receptor tyrosine kinase by the unphosphorylated juxtamembrane region
    • Wybenga-Groot, L. E. et al. Structural basis for autoinhibition of the EphB2 receptor tyrosine kinase by the unphosphorylated juxtamembrane region. Cell 106, 745-757 (2001).
    • (2001) Cell , vol.106 , pp. 745-757
    • Wybenga-Groot, L.E.1
  • 17
    • 0036241054 scopus 로고    scopus 로고
    • EphrinB phosphorylation and reverse signaling: Regulation by Src kinases and PTP-BL phosphatase
    • Palmer, A. et al. EphrinB phosphorylation and reverse signaling: regulation by Src kinases and PTP-BL phosphatase. Mol. Cell 9, 725-737 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 725-737
    • Palmer, A.1
  • 18
    • 0042591409 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the well packed ephrinB cytoplasmic β-hairpin for reverse signaling. Structural consequences and binding properties
    • Song, J. Tyrosine phosphorylation of the well packed ephrinB cytoplasmic β-hairpin for reverse signaling. Structural consequences and binding properties. J. Biol. Chem. 278, 24714-24720 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 24714-24720
    • Song, J.1
  • 19
    • 4644290521 scopus 로고    scopus 로고
    • Eph receptor tyrosine kinases in tumor and tumor microenvironment
    • Brantley-Sieders, D., Parker, M. & Chen, J. Eph receptor tyrosine kinases in tumor and tumor microenvironment. Curr. Pharm. Des. 10, 3431-3442 (2004).
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 3431-3442
    • Brantley-Sieders, D.1    Parker, M.2    Chen, J.3
  • 20
    • 0141721499 scopus 로고    scopus 로고
    • Contact-dependent signaling during the late events of platelet activation
    • Prevost, N., Woulfe, D., Tognolini, M. & Brass, L. F. Contact-dependent signaling during the late events of platelet activation. J. Thromb. Haemost. 1, 1613-1627 (2003).
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 1613-1627
    • Prevost, N.1    Woulfe, D.2    Tognolini, M.3    Brass, L.F.4
  • 21
    • 1842828975 scopus 로고    scopus 로고
    • Eph receptor-ephrin bidirectional signals that target Ras and Rho proteins
    • Noren, N. K. & Pasquale, E. B. Eph receptor-ephrin bidirectional signals that target Ras and Rho proteins. Cell Signal. 16, 655-666 (2004).
    • (2004) Cell Signal. , vol.16 , pp. 655-666
    • Noren, N.K.1    Pasquale, E.B.2
  • 22
    • 0037131355 scopus 로고    scopus 로고
    • Regulation of the EphA2 kinase by the low molecular weight tyrosine phosphatase induces transformation
    • Kikawa, K. D., Vidale, D. R., Van Etten, R. L. & Kinch, M. S. Regulation of the EphA2 kinase by the low molecular weight tyrosine phosphatase induces transformation. J. Biol. Chem. 277, 39274-39279 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 39274-39279
    • Kikawa, K.D.1    Vidale, D.R.2    Van Etten, R.L.3    Kinch, M.S.4
  • 23
    • 0344127552 scopus 로고    scopus 로고
    • c-Cbl-dependent EphA2 protein degradation is induced by ligand binding
    • Walker-Daniels, J., Riese, D. J. II & Kinch, M. S. c-Cbl-dependent EphA2 protein degradation is induced by ligand binding. Mol. Cancer Res. 1, 79-87 (2002).
    • (2002) Mol. Cancer Res. , vol.1 , pp. 79-87
    • Walker-Daniels, J.1    Riese II, D.J.2    Kinch, M.S.3
  • 24
    • 0036039649 scopus 로고    scopus 로고
    • Negative regulation of EphA2 receptor by Cbl
    • Wang, Y. et al. Negative regulation of EphA2 receptor by Cbl. Biochem. Biophys. Res. Commun. 296, 214-220 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 214-220
    • Wang, Y.1
  • 25
    • 0037040281 scopus 로고    scopus 로고
    • The kinase-null EphB6 receptor undergoes transphosphorylation in a complex with EphB1
    • Freywald, A., Sharfe, N. & Roifman, C. M. The kinase-null EphB6 receptor undergoes transphosphorylation in a complex with EphB1. J. Biol. Chem. 277, 3823-3828 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 3823-3828
    • Freywald, A.1    Sharfe, N.2    Roifman, C.M.3
  • 26
    • 0034960682 scopus 로고    scopus 로고
    • The EphA8 receptor regulates integrin activity through p110γ phosphatidylinositol-3 kinase in a tyrosine kinase activity-independent manner
    • Gu, C. & Park, S. The EphA8 receptor regulates integrin activity through p110γ phosphatidylinositol-3 kinase in a tyrosine kinase activity-independent manner. Mol. Cell. Biol. 21, 4579-4597 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4579-4597
    • Gu, C.1    Park, S.2
  • 27
    • 12544252826 scopus 로고    scopus 로고
    • Inhibition of integrin-mediated cell adhesion but not directional cell migration requires catalytic activity of EphB3 receptor tyrosine kinase: Role of Rho family small GTPases
    • Miao, H. et al. Inhibition of integrin-mediated cell adhesion but not directional cell migration requires catalytic activity of EphB3 receptor tyrosine kinase: role of Rho family small GTPases. J. Biol. Chem. 280, 923-932 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 923-932
    • Miao, H.1
  • 28
    • 1242316215 scopus 로고    scopus 로고
    • EphA receptor tyrosine kinases interact with co-expressed ephrin-A ligands in cis
    • Yin, Y. et al. EphA receptor tyrosine kinases interact with co-expressed ephrin-A ligands in cis. Neurosci. Res. 48, 285-296 (2004).
    • (2004) Neurosci. Res. , vol.48 , pp. 285-296
    • Yin, Y.1
  • 29
    • 0031034679 scopus 로고    scopus 로고
    • Tyrosine kinase receptors concentrated in caveolae-like domains from neuronal plasma membrane
    • Wu, C., Butz, S., Ying, Y. & Anderson, R. G. Tyrosine kinase receptors concentrated in caveolae-like domains from neuronal plasma membrane. J. Biol. Chem. 272, 3554-3559 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 3554-3559
    • Wu, C.1    Butz, S.2    Ying, Y.3    Anderson, R.G.4
  • 30
    • 0033103887 scopus 로고    scopus 로고
    • EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains
    • Bruckner, K. et al. EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains. Neuron 22, 511-524 (1999).
    • (1999) Neuron , vol.22 , pp. 511-524
    • Bruckner, K.1
  • 31
    • 0035794136 scopus 로고    scopus 로고
    • An ephrin-A-dependent signaling pathway controls integrin function and is linked to the tyrosine phosphorylation of a 120-kDa protein
    • Huai, J. & Drescher, U. 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 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 6689-6694
    • Huai, J.1    Drescher, U.2
  • 32
    • 0242352659 scopus 로고    scopus 로고
    • Ephrin signaling: One raft to rule them all? One raft to sort them? One raft to spread their call and in signaling bind them?
    • Gauthier, L. R. & Robbins, S. M. Ephrin signaling: one raft to rule them all? One raft to sort them? One raft to spread their call and in signaling bind them? Life Sci. 74, 207-216 (2003).
    • (2003) Life Sci. , vol.74 , pp. 207-216
    • Gauthier, L.R.1    Robbins, S.M.2
  • 33
    • 0036498380 scopus 로고    scopus 로고
    • Ephrin-As as receptors in topographic projections
    • Knoll, B. & Drescher, U. Ephrin-As as receptors in topographic projections. Trends Neurosci. 25, 145-149 (2002).
    • (2002) Trends Neurosci. , vol.25 , pp. 145-149
    • Knoll, B.1    Drescher, U.2
  • 34
    • 0034626791 scopus 로고    scopus 로고
    • Regulation of repulsion versus adhesion by different splice forms of an Eph receptor
    • Holmberg, J., Clarke, D. L. & Frisen, J. Regulation of repulsion versus adhesion by different splice forms of an Eph receptor. Nature 408, 203-206 (2000).
    • (2000) Nature , vol.408 , pp. 203-206
    • Holmberg, J.1    Clarke, D.L.2    Frisen, J.3
  • 35
    • 3042587215 scopus 로고    scopus 로고
    • Bidirectional signaling mediated by ephrin-B 2 and EphB2 controls urorectal development
    • Dravis, C. et al. Bidirectional signaling mediated by ephrin-B2 and EphB2 controls urorectal development. Dev. Biol. 271, 272-290 (2004).
    • (2004) Dev. Biol. , vol.271 , pp. 272-290
    • Dravis, C.1
  • 36
    • 0036679339 scopus 로고    scopus 로고
    • Ephrin-B ligands play a dual role in the control of neural crest cell migration
    • Santiago, A. & Erickson, C. A. Ephrin-B ligands play a dual role in the control of neural crest cell migration. Development 129, 3621-3632 (2002).
    • (2002) Development , vol.129 , pp. 3621-3632
    • Santiago, A.1    Erickson, C.A.2
  • 37
    • 0036685537 scopus 로고    scopus 로고
    • EphB forward signaling controls directional branch extension and arborization required for dorsal-ventral retinotopic mapping
    • Hindges, R., McLaughlin, T., Genoud, N., Henkemeyer, M. & O'Leary, D. EphB forward signaling controls directional branch extension and arborization required for dorsal-ventral retinotopic mapping. Neuron 35, 475-487 (2002).
    • (2002) Neuron , vol.35 , pp. 475-487
    • Hindges, R.1    McLaughlin, T.2    Genoud, N.3    Henkemeyer, M.4    O'Leary, D.5
  • 38
    • 0037832510 scopus 로고    scopus 로고
    • Bifunctional action of ephrin-B1 as a repellent and attractant to control bidirectional branch extension in dorsal-ventral retinotopjc mapping
    • McLaughlin, T., Hindges, R., Yates, P. A. & O'Leary, D. D. Bifunctional action of ephrin-B1 as a repellent and attractant to control bidirectional branch extension in dorsal-ventral retinotopjc mapping. Development 130, 2407-2418 (2003).
    • (2003) Development , vol.130 , pp. 2407-2418
    • McLaughlin, T.1    Hindges, R.2    Yates, P.A.3    O'Leary, D.D.4
  • 39
    • 0842282476 scopus 로고    scopus 로고
    • Ephrin-A5 exerts positive or inhibitory effects on distinct subsets of EphA4-positive motor neurons
    • Eberhart, J. et al. Ephrin-A5 exerts positive or inhibitory effects on distinct subsets of EphA4-positive motor neurons. J. Neurosci. 24, 1070-1078 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 1070-1078
    • Eberhart, J.1
  • 40
    • 0037730190 scopus 로고    scopus 로고
    • On the turning of Xeoopus retinal axons induced by ephrin-A 5
    • Weinl, C., Drescher, U., Lang, S., Bonhoeffer, F. & Loschinger, J. On the turning of Xeoopus retinal axons induced by ephrin-A5. Development 130, 1635-1643 (2003).
    • (2003) Development , vol.130 , pp. 1635-1643
    • Weinl, C.1    Drescher, U.2    Lang, S.3    Bonhoeffer, F.4    Loschinger, J.5
  • 41
    • 0033360412 scopus 로고    scopus 로고
    • Neuronal growth cone collapse triggers lateral extensions along trailing axons
    • Davenport, R. W., Thies, E. & Cohen, M. L. Neuronal growth cone collapse triggers lateral extensions along trailing axons. Mature Neurosci. 2, 254-259 (1999).
    • (1999) Mature Neurosci. , vol.2 , pp. 254-259
    • Davenport, R.W.1    Thies, E.2    Cohen, M.L.3
  • 42
    • 0032526731 scopus 로고    scopus 로고
    • Dual action of a ligand for Eph receptor tyrosine kinases on specific populations of axons during the development of cortical circuits
    • Castellani, V., Yue, Y., Gao, P. P., Zhou, R. & Bolz, J. Dual action of a ligand for Eph receptor tyrosine kinases on specific populations of axons during the development of cortical circuits. J. Neurosci. 18, 4663-4672 (1998).
    • (1998) J. Neurosci. , vol.18 , pp. 4663-4672
    • Castellani, V.1    Yue, Y.2    Gao, P.P.3    Zhou, R.4    Bolz, J.5
  • 43
    • 0035503703 scopus 로고    scopus 로고
    • Topographic-specific axon branching controlled by ephrin-As is the critical event in retinotectal map development
    • Yates, P. A., Roskies, A. L., McLaughlin, T. & O'Leary, D. D. Topographic-specific axon branching controlled by ephrin-As is the critical event in retinotectal map development. J. Neurosci. 21, 8548-8563 (2001). Provides evidence that an important effect of ephrin-A ligands in the regulation of topographic synaptic connections in the visual system involves inhibition of collateral branching rather than only growth cone repulsion, as was previously believed.
    • (2001) J. Neurosci. , vol.21 , pp. 8548-8563
    • Yates, P.A.1    Roskies, A.L.2    McLaughlin, T.3    O'Leary, D.D.4
  • 44
    • 0036679141 scopus 로고    scopus 로고
    • Ephrin-A 5 restricts topographically specific arborization in the chick retinotectal projection in vivo
    • Sakurai, T., Wong, E., Drescher, U., Tanaka, H. & Jay, D. G. Ephrin-A5 restricts topographically specific arborization in the chick retinotectal projection in vivo. Proc. Natl Acad. USA 99, 10795-10800 (2002).
    • (2002) Proc. Natl. Acad. USA , vol.99 , pp. 10795-10800
    • Sakurai, T.1    Wong, E.2    Drescher, U.3    Tanaka, H.4    Jay, D.G.5
  • 45
    • 2942534978 scopus 로고    scopus 로고
    • Retinal axon response to ephrin-As shows a graded, concentration- dependent transition from growth promotion to inhibition
    • Hansen, M. J., Dallal, G. E. & Flanagan, J. G. Retinal axon response to ephrin-As shows a graded, concentration-dependent transition from growth promotion to inhibition. Neuron 42, 717-730 (2004). Shows that ephrin-A ligands can promote retinal axon outgrowth when present on the substrate at low density, in contrast to the inhibitory effects of these ligands when they are at high density. The concentration of EphA receptors on the axons also influences axon growth promotion versus inhibition.
    • (2004) Neuron , vol.42 , pp. 717-730
    • Hansen, M.J.1    Dallal, G.E.2    Flanagan, J.G.3
  • 46
    • 0034714357 scopus 로고    scopus 로고
    • Regulated cleavage of a contact-mediated axon repellent
    • Hattori, M., Osterfield, M. & Flanagan, J. G. Regulated cleavage of a contact-mediated axon repellent. Science 289, 1360-1365 (2000). Identifies ephrin-A proteolysis as a mechanism to allow cell separation following formation of transcellular Eph-ephrin adhesive complexes.
    • (2000) Science , vol.289 , pp. 1360-1365
    • Hattori, M.1    Osterfield, M.2    Flanagan, J.G.3
  • 47
    • 0141839883 scopus 로고    scopus 로고
    • EphB-ephrinB bi-directional endocytosis terminates adhesion allowing contact mediated repulsion
    • Zimmer, M., Palmer, A., Kohler, J. & Klein, R. EphB-ephrinB bi-directional endocytosis terminates adhesion allowing contact mediated repulsion. Nature Cell Biol. 5, 869-878 (2003).
    • (2003) Nature Cell Biol. , vol.5 , pp. 869-878
    • Zimmer, M.1    Palmer, A.2    Kohler, J.3    Klein, R.4
  • 48
    • 0242721443 scopus 로고    scopus 로고
    • B-type Eph receptors and ephrins induce growth cone collapse through distinct intracellular pathways
    • Mann, F., Miranda, E., Weinl, C., Harmer, E. & Holt, C. E. B-type Eph receptors and ephrins induce growth cone collapse through distinct intracellular pathways. J. Neurobiol. 57, 323-336 (2003).
    • (2003) J. Neurobiol. , vol.57 , pp. 323-336
    • Mann, F.1    Miranda, E.2    Weinl, C.3    Harmer, E.4    Holt, C.E.5
  • 49
    • 0141839882 scopus 로고    scopus 로고
    • Rac-dependent trans-endocytosis of ephrinBs regulates Eph-ephrin contact repulsion
    • Marston, D. J., Dickinson, S. & Nobes, C. D. Rac-dependent trans-endocytosis of ephrinBs regulates Eph-ephrin contact repulsion. Nature Cell Biol. 5, 879-888 (2003). References 47 and 49 identify endocytosis as a mechanism to remove intact Eph-receptor-ephrin adhesive complexes from sites of cell contact, thereby facilitating cell separation.
    • (2003) Nature Cell Biol. , vol.5 , pp. 879-888
    • Marston, D.J.1    Dickinson, S.2    Nobes, C.D.3
  • 50
    • 1642422313 scopus 로고    scopus 로고
    • Intramembrane cleavage of ephrinB3 by the human rhomboid family protease, RHBDL2
    • Pascall, J. C. & Brown, K. D. Intramembrane cleavage of ephrinB3 by the human rhomboid family protease, RHBDL2. Biochem. Biophys. Res. Commun. 317, 244-252 (2004).
    • (2004) Biochem. Biophys. Res. Commun. , vol.317 , pp. 244-252
    • Pascall, J.C.1    Brown, K.D.2
  • 51
    • 0032031705 scopus 로고    scopus 로고
    • Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses
    • Stein, E. et al. Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses. Genes Dev. 12, 667-678 (1998). First article to propose that the degree of Eph receptor clustering can change cellular responses to Eph signalling.
    • (1998) Genes Dev. , vol.12 , pp. 667-678
    • Stein, E.1
  • 52
    • 0036685610 scopus 로고    scopus 로고
    • Topographic mapping in dorsoventral axis of the Xenopus retinotectal system depends on signaling through Ephrin-B ligands
    • Mann, F., Ray, S., Harris, W. & Holt, C. Topographic mapping in dorsoventral axis of the Xenopus retinotectal system depends on signaling through Ephrin-B ligands. Neuron 35, 461-473 (2002).
    • (2002) Neuron , vol.35 , pp. 461-473
    • Mann, F.1    Ray, S.2    Harris, W.3    Holt, C.4
  • 53
    • 0036911338 scopus 로고    scopus 로고
    • Adaptor protein Crk is required for Ephrin-B1-induced membrane ruffling and focal complex assembly of human aortic endothelial cells
    • Nagashima, K. et al. Adaptor protein Crk is required for Ephrin-B1-induced membrane ruffling and focal complex assembly of human aortic endothelial cells. Mol. Biol. Cell 13, 4231-4242 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4231-4242
    • Nagashima, K.1
  • 54
    • 0033560751 scopus 로고    scopus 로고
    • 1 integrins
    • 1 integrins. EMBO J. 18, 2165-2173 (1999).
    • (1999) EMBO J. , vol.18 , pp. 2165-2173
    • Huynh-Do, U.1
  • 55
    • 1842732148 scopus 로고    scopus 로고
    • Interplay between EphB4 on tumor cells and vascular ephrin-B 2 regulates tumor growth
    • Noren, N. K., Lu, M., Freeman, A. L., Koolpe, M. & Pasquale, E. B. Interplay between EphB4 on tumor cells and vascular ephrin-B2 regulates tumor growth. Proc. Natl Acad. Sci. USA 101, 5583-5588 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 5583-5588
    • Noren, N.K.1    Lu, M.2    Freeman, A.L.3    Koolpe, M.4    Pasquale, E.B.5
  • 56
    • 0038497941 scopus 로고    scopus 로고
    • Forward EphB 4 signaling in endothelial cells controls cellular repulsion and segregation from ephrinB2 positive cells
    • Fuller, T., Korff, T., Kilian, A., Dandekar, G. & Augustin, H. G. Forward EphB4 signaling in endothelial cells controls cellular repulsion and segregation from ephrinB2 positive cells. J. Cell Sci. 116, 2461-2470 (2003).
    • (2003) J. Cell Sci. , vol.116 , pp. 2461-2470
    • Fuller, T.1    Korff, T.2    Kilian, A.3    Dandekar, G.4    Augustin, H.G.5
  • 57
    • 0037047122 scopus 로고    scopus 로고
    • Interactions between Eph kinases and ephrins provide a mechanism to support platelet aggregation once cell-to-cell contact has occurred
    • Prevost, N., Woulfe, D., Tanaka, T. & Brass, L. F. Interactions between Eph kinases and ephrins provide a mechanism to support platelet aggregation once cell-to-cell contact has occurred. Proc. Natl Acad. Sci. USA 99, 9219-9224 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9219-9224
    • Prevost, N.1    Woulfe, D.2    Tanaka, T.3    Brass, L.F.4
  • 58
    • 1442300147 scopus 로고    scopus 로고
    • L1/Laminin modulation of growth cone response to EphB triggers growth pauses and regulates the microtubule destabilizing protein SCG 10
    • Suh, L. H., Oster, S. F., Soehrman, S. S., Grenningloh, G. & Sretavan, D. W. L1/Laminin modulation of growth cone response to EphB triggers growth pauses and regulates the microtubule destabilizing protein SCG10. J. Neurosci. 24, 1976-1986 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 1976-1986
    • Suh, L.H.1    Oster, S.F.2    Soehrman, S.S.3    Grenningloh, G.4    Sretavan, D.W.5
  • 59
    • 0043198324 scopus 로고    scopus 로고
    • Area specificity and topography of thalamocortical projections are controlled by ephrin/Eph genes
    • Dufour, A. et al. Area specificity and topography of thalamocortical projections are controlled by ephrin/Eph genes. Neuron 39, 453-465 (2003).
    • (2003) Neuron , vol.39 , pp. 453-465
    • Dufour, A.1
  • 60
    • 0033215333 scopus 로고    scopus 로고
    • Ephrins and their Eph receptors: Multitalented directors of embryonic development
    • Frisen, J., Holmberg, J. & Barbacid, M. Ephrins and their Eph receptors: multitalented directors of embryonic development. EMBO J. 18, 5159-5165 (1999).
    • (1999) EMBO J. , vol.18 , pp. 5159-5165
    • Frisen, J.1    Holmberg, J.2    Barbacid, M.3
  • 61
    • 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. et al. 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). Identifies ephrin-A5 as the long sought-after repellent for retinal axons by biochemical purification from posterior chicken tectum.
    • (1995) Cell , vol.82 , pp. 359-370
    • Drescher, U.1
  • 62
    • 0034616944 scopus 로고    scopus 로고
    • Topographic mapping from the retina to the midbrain is controlled by relative but not absolute levels of EphA receptor signaling
    • Brown, A. et al. Topographic mapping from the retina to the midbrain is controlled by relative but not absolute levels of EphA receptor signaling. Cell 102, 77-88 (2000).
    • (2000) Cell , vol.102 , pp. 77-88
    • Brown, A.1
  • 63
    • 7244245371 scopus 로고    scopus 로고
    • A relative signalling model for the formation of a topographic neural map
    • Reber, M., Burrola, P. & Lemke, G. A relative signalling model for the formation of a topographic neural map. Nature 431, 847-853 (2004).
    • (2004) Nature , vol.431 , pp. 847-853
    • Reber, M.1    Burrola, P.2    Lemke, G.3
  • 64
    • 0345687441 scopus 로고    scopus 로고
    • Competition between retinal ganglion axons for targets under the servomechanism model explains abnormal retinocollicular projection of Eph receptor-overexpressing or ephrin-lacking mice
    • Honda, H. Competition between retinal ganglion axons for targets under the servomechanism model explains abnormal retinocollicular projection of Eph receptor-overexpressing or ephrin-lacking mice. J. Neurosci. 23, 10368-10377 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 10368-10377
    • Honda, H.1
  • 65
    • 12944266755 scopus 로고    scopus 로고
    • A stochastic model for retinocollicular map development
    • Koulakov, A. A. & Tsigankov, D. N. A stochastic model for retinocollicular map development. BMC Neurosci. 5, 30-47 (2004).
    • (2004) BMC Neurosci. , vol.5 , pp. 30-47
    • Koulakov, A.A.1    Tsigankov, D.N.2
  • 66
    • 1642267005 scopus 로고    scopus 로고
    • Computational modeling of retinotopic map development to define contributions of EphA-ephrinA gradients, axon-axon interactions, and patterned activity
    • Yates, P. A., Holub, A. D., McLaughlin, T., Sejnowski, T. J. & O'Leary, D. D. Computational modeling of retinotopic map development to define contributions of EphA-ephrinA gradients, axon-axon interactions, and patterned activity. J. Neurobiol. 59, 95-113 (2004).
    • (2004) J. Neurobiol. , vol.59 , pp. 95-113
    • Yates, P.A.1    Holub, A.D.2    McLaughlin, T.3    Sejnowski, T.J.4    O'Leary, D.D.5
  • 67
    • 1542327615 scopus 로고    scopus 로고
    • Loss-of-function analysis of EphA receptors in retinotectal mapping
    • Feldheim, D. A. et al. Loss-of-function analysis of EphA receptors in retinotectal mapping. J. Neurosci. 24, 2542-2550 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 2542-2550
    • Feldheim, D.A.1
  • 68
    • 0033681554 scopus 로고    scopus 로고
    • Genetic analysis of ephrin-A2 and ephrin-A 5 shows their requirement in multiple aspects of retinocollicular mapping
    • Feldheim, D. A. et al. Genetic analysis of ephrin-A2 and ephrin-A5 shows their requirement in multiple aspects of retinocollicular mapping. Neuron 25, 563-574 (2000).
    • (2000) Neuron , vol.25 , pp. 563-574
    • Feldheim, D.A.1
  • 69
    • 0032006223 scopus 로고    scopus 로고
    • Ephrin-A5 (AL-1/RAGS) is essential for proper retinal axon guidance and topographic mapping in the mammalian visual system
    • Frisen, J. et al. Ephrin-A5 (AL-1/RAGS) is essential for proper retinal axon guidance and topographic mapping in the mammalian visual system. Neuron 20, 235-243 (1998).
    • (1998) Neuron , vol.20 , pp. 235-243
    • Frisen, J.1
  • 70
    • 0034034802 scopus 로고    scopus 로고
    • Kinase independent function of EphB receptors in retinal axon pathfinding to the optic disc from dorsal but not ventral retina
    • Birgbauer, E., Cowan, C. A., Sretavan, D. W. & Henkemeyer, M. Kinase independent function of EphB receptors in retinal axon pathfinding to the optic disc from dorsal but not ventral retina. Development 127, 1231-1241 (2000).
    • (2000) Development , vol.127 , pp. 1231-1241
    • Birgbauer, E.1    Cowan, C.A.2    Sretavan, D.W.3    Henkemeyer, M.4
  • 71
    • 0141786827 scopus 로고    scopus 로고
    • Ephrin-B2 and EphB1 mediate retinal axon divergence at the optic chiasm
    • Williams, S. E. et al. Ephrin-B2 and EphB1 mediate retinal axon divergence at the optic chiasm. Neuron 39, 919-935 (2003).
    • (2003) Neuron , vol.39 , pp. 919-935
    • Williams, S.E.1
  • 72
    • 0033681555 scopus 로고    scopus 로고
    • Ephrin-B regulates the ipsilateral routing of retinal axons at the optic chiasm
    • Nakagawa, S. et al. Ephrin-B regulates the ipsilateral routing of retinal axons at the optic chiasm. Neuron 25, 599-610 (2000).
    • (2000) Neuron , vol.25 , pp. 599-610
    • Nakagawa, S.1
  • 73
    • 0037832510 scopus 로고    scopus 로고
    • Bifunctional action of ephrin-B1 as a repellent and attractant to control bidirectional branch extension in dorsal-ventral retinotopic mapping
    • McLaughlin, T., Hindges, R., Yates, P. A. & O'Leary, D. D. Bifunctional action of ephrin-B1 as a repellent and attractant to control bidirectional branch extension in dorsal-ventral retinotopic mapping. Development 130, 2407-2418 (2003).
    • (2003) Development , vol.130 , pp. 2407-2418
    • McLaughlin, T.1    Hindges, R.2    Yates, P.A.3    O'Leary, D.D.4
  • 74
    • 0028989595 scopus 로고
    • Cloning of AL-1, a ligand for an Eph-related tyrosine kinase receptor involved in axon bundle formation
    • Winslow, J. W. et al. Cloning of AL-1, a ligand for an Eph-related tyrosine kinase receptor involved in axon bundle formation. Neuron 14, 973-981 (1995).
    • (1995) Neuron , vol.14 , pp. 973-981
    • Winslow, J.W.1
  • 75
    • 1542267748 scopus 로고    scopus 로고
    • Abnormal hippocampal axon bundling in EphB receptor mutant mice
    • Chen, Z. Y. et al. Abnormal hippocampal axon bundling in EphB receptor mutant mice. J. Neurosci. 24, 2366-2374 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 2366-2374
    • Chen, Z.Y.1
  • 76
    • 3242781607 scopus 로고    scopus 로고
    • Eph receptors, ephrins, and synaptic function
    • Murai, K. K. & Pasquale, E. B. Eph receptors, ephrins, and synaptic function. Neuroscientist 10, 304-314 (2004).
    • (2004) Neuroscientist , vol.10 , pp. 304-314
    • Murai, K.K.1    Pasquale, E.B.2
  • 78
    • 0035959932 scopus 로고    scopus 로고
    • EphB/syndecan-2 signaling in dendritic spine morphogenesis
    • Ethell, I. M. et al. EphB/syndecan-2 signaling in dendritic spine morphogenesis. Neuron 31, 1001-1013 (2001).
    • (2001) Neuron , vol.31 , pp. 1001-1013
    • Ethell, I.M.1
  • 79
    • 0347993700 scopus 로고    scopus 로고
    • Multiple EphB receptor tyrosine kinases shape dendritic spines in the hippocampus
    • Henkemeyer, M., Itkis, O. S., Ngo, M., Hickmott, P. W. & Ethell, I. M. Multiple EphB receptor tyrosine kinases shape dendritic spines in the hippocampus. J. Cell Biol. 163, 1313-1326 (2003).
    • (2003) J. Cell Biol. , vol.163 , pp. 1313-1326
    • Henkemeyer, M.1    Itkis, O.S.2    Ngo, M.3    Hickmott, P.W.4    Ethell, I.M.5
  • 80
    • 0037461752 scopus 로고    scopus 로고
    • Rapid induction of dendritic spine morphogenesis by trans-synaptic EphrinB-EphB receptor activation of the Rho-GEF kalirin
    • Penzes, P. et al. Rapid induction of dendritic spine morphogenesis by trans-synaptic EphrinB-EphB receptor activation of the Rho-GEF kalirin. Neuron 37, 263-274 (2003).
    • (2003) Neuron , vol.37 , pp. 263-274
    • Penzes, P.1
  • 81
    • 0033635736 scopus 로고    scopus 로고
    • EphB receptors interact with NMDA receptors and regulate excitatory synapse formation
    • Dalva, M. B. et al. EphB receptors interact with NMDA receptors and regulate excitatory synapse formation. Cell 103, 945-956 (2000).
    • (2000) Cell , vol.103 , pp. 945-956
    • Dalva, M.B.1
  • 82
    • 0037314984 scopus 로고    scopus 로고
    • Control of hippocampal dendritic spine morphology through ephrin-A3/EphA4 signaling
    • Murai, K. K., Nguyen, L. N., Irie, F., Yamaguchi, Y. & Pasquale, E. B. Control of hippocampal dendritic spine morphology through ephrin-A3/EphA4 signaling. Nature Neurosci. 6, 153-160 (2003). Identifies a form of neuroglial crosstalk that regulates dendritic spine shape through repulsive signalling by an EphA receptor on hippocampal pyramidal neurons and an ephrin-A ligand on glial cells.
    • (2003) Nature Neurosci. , vol.6 , pp. 153-160
    • Murai, K.K.1    Nguyen, L.N.2    Irie, F.3    Yamaguchi, Y.4    Pasquale, E.B.5
  • 83
    • 0348011611 scopus 로고    scopus 로고
    • How actin filaments and microtubules steer growth cones to their targets
    • Zhou, F. Q. & Cohan, C. S. How actin filaments and microtubules steer growth cones to their targets. J. Neurobiol. 58, 84-91 (2004).
    • (2004) J. Neurobiol. , vol.58 , pp. 84-91
    • Zhou, F.Q.1    Cohan, C.S.2
  • 84
    • 0035920134 scopus 로고    scopus 로고
    • Laminin-10/11 and fibronectin differentially regulate integrin-dependent Rho and Rac activation via p130(Cas)-Crkll-DOCK 180 pathway
    • Gu, J., Sumida, Y., Sanzen, N. & Sekiguchi, K. Laminin-10/11 and fibronectin differentially regulate integrin-dependent Rho and Rac activation via p130(Cas)-Crkll-DOCK180 pathway. J. Biol. Chem. 276, 27090-27097 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 27090-27097
    • Gu, J.1    Sumida, Y.2    Sanzen, N.3    Sekiguchi, K.4
  • 85
    • 0037413913 scopus 로고    scopus 로고
    • Independent roles of Rho-GTPases in growth cone and axonal behavior
    • Thies, E. & Davenport, R. W. Independent roles of Rho-GTPases in growth cone and axonal behavior. J. Neurobiol. 54, 358-369 (2003).
    • (2003) J. Neurobiol. , vol.54 , pp. 358-369
    • Thies, E.1    Davenport, R.W.2
  • 87
    • 0141641133 scopus 로고    scopus 로고
    • EphA kinase activation regulates HGF-induced epithelial branching morphogenesis
    • Miao, H. et al. EphA kinase activation regulates HGF-induced epithelial branching morphogenesis. J. Cell Biol. 162, 1281-1292 (2003).
    • (2003) J. Cell Biol. , vol.162 , pp. 1281-1292
    • Miao, H.1
  • 88
    • 0030667174 scopus 로고    scopus 로고
    • Eph family receptors and ligands in vascular cell targeting and assembly
    • Stein, E., Schoecklmann, H. & Daniel, T. O. Eph family receptors and ligands in vascular cell targeting and assembly. Trends Cardiovasc. Med. 7, 329-334 (1997).
    • (1997) Trends Cardiovasc. Med. , vol.7 , pp. 329-334
    • Stein, E.1    Schoecklmann, H.2    Daniel, T.O.3
  • 89
    • 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. & Anderson, D. J. Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4. Cell 93, 741-753 (1998). Identifies ephrin-B2 as a marker for embryonic arterial endothelial cells and, together with reference 90, reveals the essential role in cardiovascular development of this ephrin and the EphB4 receptor in venous endothelial cells.
    • (1998) Cell , vol.93 , pp. 741-753
    • Wang, H.U.1    Chen, Z.F.2    Anderson, D.J.3
  • 90
    • 0033197535 scopus 로고    scopus 로고
    • Symmetrical mutant phenotypes of the receptor EphB4 and its specific transmembrane ligand ephrin-B2 in cardiovascular development
    • Gerety, S. S., Wang, H. U., Chen, Z. F. & Anderson, D. J. Symmetrical mutant phenotypes of the receptor EphB4 and its specific transmembrane ligand ephrin-B2 in cardiovascular development. Mol. Cell 4, 403-414 (1999).
    • (1999) Mol. Cell , vol.4 , pp. 403-414
    • Gerety, S.S.1    Wang, H.U.2    Chen, Z.F.3    Anderson, D.J.4
  • 91
    • 0033082959 scopus 로고    scopus 로고
    • Roles of ephrinB ligands and EphB receptors in cardiovascular development: Demarcation of arterial/venous domains, vascular morphogenesis, and sprouting angiogenesis
    • Adams, R. H. et al. Roles of ephrinB ligands and EphB receptors in cardiovascular development: demarcation of arterial/venous domains, vascular morphogenesis, and sprouting angiogenesis. Genes Dev. 13, 295-306 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 295-306
    • Adams, R.H.1
  • 92
    • 13244292521 scopus 로고    scopus 로고
    • PDZ interaction site in ephrinB2 is required for the remodeling of lymphatic vasculature
    • Makinen, T. et al. PDZ interaction site in ephrinB2 is required for the remodeling of lymphatic vasculature. Genes Dev. 19, 397-410 (2005). Reports an essential role for ephrin-B2 in the formation of the lymphatic vasculature and begins to identify the reverse signalling pathways involved using genetic approches.
    • (2005) Genes Dev. , vol.19 , pp. 397-410
    • Makinen, T.1
  • 93
    • 0029036501 scopus 로고
    • Role of B61, the ligand for the Eck receptor tyrosine kinase, in TNF-α-induced angiogenesis
    • Pandey, A., Shao, H., Marks, R. M., Polverini, P. J. & Dixit, V. M. Role of B61, the ligand for the Eck receptor tyrosine kinase, in TNF-α-induced angiogenesis. Science 268, 567-569 (1995). First demonstration that an Eph receptor, EphA2, has a role in pathological angiogenesis in the adult.
    • (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
  • 94
    • 18644379904 scopus 로고    scopus 로고
    • Soluble Eph A receptors inhibit tumor angiogenesis and progression in vivo
    • Brantley, D. M. et al. Soluble Eph A receptors inhibit tumor angiogenesis and progression in vivo. Oncogene 21, 7011-7026 (2002).
    • (2002) Oncogene , vol.21 , pp. 7011-7026
    • Brantley, D.M.1
  • 95
    • 0842282623 scopus 로고    scopus 로고
    • Antiangiogenic and antitumor efficacy of EphA2 receptor antagonist
    • Dobrzanski, P. et al. Antiangiogenic and antitumor efficacy of EphA2 receptor antagonist. Cancer Res. 64, 910-919 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 910-919
    • Dobrzanski, P.1
  • 96
    • 2942605976 scopus 로고    scopus 로고
    • EphA2 receptor tyrosine kinase regulates endothelial cell migration and vascular assembly through phosphoinositide 3-kinase-mediated Rac 1 GTPase activation
    • Brantley-Sieders, D. M. et al. EphA2 receptor tyrosine kinase regulates endothelial cell migration and vascular assembly through phosphoinositide 3-kinase-mediated Rac1 GTPase activation. J. Cell Sci. 117, 2037-2049 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 2037-2049
    • Brantley-Sieders, D.M.1
  • 97
    • 3042680296 scopus 로고    scopus 로고
    • Ephrin-B2 reverse signaling is required for axon pathfinding and cardiac valve formation but not early vascular development
    • Cowan, C. A. et al. Ephrin-B2 reverse signaling is required for axon pathfinding and cardiac valve formation but not early vascular development. Dev. Biol. 271, 263-271 (2004).
    • (2004) Dev. Biol. , vol.271 , pp. 263-271
    • Cowan, C.A.1
  • 98
    • 0042442460 scopus 로고    scopus 로고
    • Control of skeletal patterning by ephrinB1-EphB interactions
    • Compagni, A., Logan, M., Klein, R. & Adams, R. H. Control of skeletal patterning by ephrinB1-EphB interactions. Dev. Cell 5, 217-230 (2003). This article and reference 99 demonstrate the crucial role of ephrin-B1 in embryonic patterning by the formation of tissue boundaries.
    • (2003) Dev. Cell , vol.5 , pp. 217-230
    • Compagni, A.1    Logan, M.2    Klein, R.3    Adams, R.H.4
  • 99
    • 1642273208 scopus 로고    scopus 로고
    • Ephrin-B1 forward and reverse signaling are required during mouse development
    • Davy, A., Aubin, J. & Soriano, P. Ephrin-B1 forward and reverse signaling are required during mouse development. Genes Dev 18, 572-583 (2004).
    • (2004) Genes Dev , vol.18 , pp. 572-583
    • Davy, A.1    Aubin, J.2    Soriano, P.3
  • 100
    • 2942560339 scopus 로고    scopus 로고
    • Mutations of ephrin-B1 (EFNB1), a marker of tissue boundary formation, cause craniofrontonasal syndrome
    • Twigg, S. R. et al. Mutations of ephrin-B1 (EFNB1), a marker of tissue boundary formation, cause craniofrontonasal syndrome. Proc. Natl Acad. Sci. USA 101, 8652-8657 (2004). This article and reference 101 implicate ephrin-B1 mutations in a human genetic disease, craniofrontonasal syndrome. The disease phenotype is probably the result of abnormalities in the formation of embryonic tissue boundaries (see also references 98 and 99).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8652-8657
    • Twigg, S.R.1
  • 101
    • 2442661362 scopus 로고    scopus 로고
    • Mutations of the ephrin-B1 gene cause craniofrontonasal syndrome
    • Wieland, I. et al. Mutations of the ephrin-B1 gene cause craniofrontonasal syndrome. Am. J. Hum. Genet. 74, 1209-1215 (2004).
    • (2004) Am. J. Hum. Genet. , vol.74 , pp. 1209-1215
    • Wieland, I.1
  • 102
    • 18644376279 scopus 로고    scopus 로고
    • β-catenin and TCF mediate cell positioning in the intestinal epithelium by controlling the expression of EphB/EphrinB
    • Batlle, E. et al. β-Catenin and TCF mediate cell positioning in the intestinal epithelium by controlling the expression of EphB/EphrinB. Cell 111, 251-263 (2002).
    • (2002) Cell , vol.111 , pp. 251-263
    • Batlle, E.1
  • 104
    • 0035815305 scopus 로고    scopus 로고
    • Ephrin-B reverse signaling is mediated by a novel PDZ-RGS protein and selectively inhibits G protein-coupled chemoattraction
    • Lu, Q., Sun, E. E., Klein, R. S. & Flanagan, J. G. Ephrin-B reverse signaling is mediated by a novel PDZ-RGS protein and selectively inhibits G protein-coupled chemoattraction. Cell 105, 69-79 (2001).
    • (2001) Cell , vol.105 , pp. 69-79
    • Lu, Q.1    Sun, E.E.2    Klein, R.S.3    Flanagan, J.G.4
  • 105
    • 0036677161 scopus 로고    scopus 로고
    • Ephrin-B1 transduces signals to activate integrin-mediated migration, attachment and angiogenesis
    • Huynh-Do, U. et al. Ephrin-B1 transduces signals to activate integrin-mediated migration, attachment and angiogenesis. J. Cell Sci. 115, 3073-3081 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 3073-3081
    • Huynh-Do, U.1
  • 106
    • 0041976992 scopus 로고    scopus 로고
    • EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote chemotaxis
    • Vindis, C., Cerretti, D. P., Daniel, T. O. & Huynh-Do, U. EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote chemotaxis. J. Cell Biol. 162, 661-671 (2003).
    • (2003) J. Cell Biol. , vol.162 , pp. 661-671
    • Vindis, C.1    Cerretti, D.P.2    Daniel, T.O.3    Huynh-Do, U.4
  • 107
    • 3142619126 scopus 로고    scopus 로고
    • EphB1-mediated cell migration requires the phosphorylation of paxillin at Tyr-31/Tyr-118
    • Vindis, C., Teli, T., Cerretti, D. P., Turner, C. E. & Huynh-Do, U. EphB1-mediated cell migration requires the phosphorylation of paxillin at Tyr-31/Tyr-118. J. Biol. Chem. 279, 27965-27970 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 27965-27970
    • Vindis, C.1    Teli, T.2    Cerretti, D.P.3    Turner, C.E.4    Huynh-Do, U.5
  • 109
    • 0347634454 scopus 로고    scopus 로고
    • Defining the epithelial stem cell niche in skin
    • Tumbar, T. et al. Defining the epithelial stem cell niche in skin. Science 303, 359-363 (2004).
    • (2004) Science , vol.303 , pp. 359-363
    • Tumbar, T.1
  • 110
    • 3543044348 scopus 로고    scopus 로고
    • EphA receptors direct the differentiation of mammalian neural precursor cells through a mitogen-activated protein kinase-dependent pathway
    • Aoki, M., Yamashita, T. & Tohyama, M. EphA receptors direct the differentiation of mammalian neural precursor cells through a mitogen-activated protein kinase-dependent pathway. J. Biol. Chem. 279, 32643-32650 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 32643-32650
    • Aoki, M.1    Yamashita, T.2    Tohyama, M.3
  • 111
    • 0036297329 scopus 로고    scopus 로고
    • A role of EphB4 receptor and its ligand, ephrin-B2, in erythropoiesis
    • Suenobu, S. et al. A role of EphB4 receptor and its ligand, ephrin-B2, in erythropoiesis. Biochem. Biophys. Res. Commun. 293, 1124-1131 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 1124-1131
    • Suenobu, S.1
  • 112
    • 0037089330 scopus 로고    scopus 로고
    • Receptor tyrosine kinase, EphB4 (HTK), accelerates differentiation of select human hematopoietic cells
    • Wang, Z. et al. Receptor tyrosine kinase, EphB4 (HTK), accelerates differentiation of select human hematopoietic cells. Blood 99, 2740-2747 (2002).
    • (2002) Blood , vol.99 , pp. 2740-2747
    • Wang, Z.1
  • 113
    • 0347597774 scopus 로고    scopus 로고
    • Ephrin receptor, EphB4, regulates ES cell differentiation of primitive mammalian hemangioblasts, blood, cardiomyocytes, and blood vessels
    • Wang, Z. et al. Ephrin receptor, EphB4, regulates ES cell differentiation of primitive mammalian hemangioblasts, blood, cardiomyocytes, and blood vessels. Blood 103, 100-109 (2004).
    • (2004) Blood , vol.103 , pp. 100-109
    • Wang, Z.1
  • 114
    • 0033769334 scopus 로고    scopus 로고
    • Disruption of Eph/ephrin signaling affects migration and proliferation in the adult subventricular zone
    • Conover, J. C. et al. Disruption of Eph/ephrin signaling affects migration and proliferation in the adult subventricular zone. Nature Neurosci. 3, 1091-1097 (2000).
    • (2000) Nature Neurosci. , vol.3 , pp. 1091-1097
    • Conover, J.C.1
  • 115
    • 13844269325 scopus 로고    scopus 로고
    • Ephrin-A2 reverse signaling negatively regulates neural progenitor proliferation and neurogenesis
    • Holmberg, J. et al. Ephrin-A2 reverse signaling negatively regulates neural progenitor proliferation and neurogenesis. Genes Dev. 19, 462-471 (2005).
    • (2005) Genes Dev. , vol.19 , pp. 462-471
    • Holmberg, J.1
  • 116
    • 0346503239 scopus 로고    scopus 로고
    • Morphogenetic movements underlying eye field formation require interactions between the FGF and ephrinB 1 signaling pathways
    • Moore, K. B., Mood, K., Daar, I. O. & Moody, S. A. Morphogenetic movements underlying eye field formation require interactions between the FGF and ephrinB1 signaling pathways. Dev. Cell 6, 55-67 (2004).
    • (2004) Dev. Cell , vol.6 , pp. 55-67
    • Moore, K.B.1    Mood, K.2    Daar, I.O.3    Moody, S.A.4
  • 117
    • 0030026594 scopus 로고    scopus 로고
    • Function of the Eph-related kinase rtk1 in patterning of the zebrafish forebrain
    • Xu, Q., Alldus, G., Macdonald, R., Wilkinson, D. G. & Holder, N. Function of the Eph-related kinase rtk1 in patterning of the zebrafish forebrain. Nature 381, 319-322 (1996).
    • (1996) Nature , vol.381 , pp. 319-322
    • Xu, Q.1    Alldus, G.2    Macdonald, R.3    Wilkinson, D.G.4    Holder, N.5
  • 118
    • 0141504149 scopus 로고    scopus 로고
    • Eph/Ephrin signaling regulates the mesenchymal-to-epithelial transition of the paraxial mesoderm during somite morphogenesis
    • Barrios, A. et al. Eph/Ephrin signaling regulates the mesenchymal-to-epithelial transition of the paraxial mesoderm during somite morphogenesis. Curr. Biol. 13, 1571-1582 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 1571-1582
    • Barrios, A.1
  • 119
    • 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. & 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
  • 120
    • 4444326581 scopus 로고    scopus 로고
    • Nonsense-mediated decay microarray analysis identifies mutations of EPHB 2 in human prostate cancer
    • Huusko, P. et al. Nonsense-mediated decay microarray analysis identifies mutations of EPHB2 in human prostate cancer. Nature Genet. 36, 979-983 (2004).
    • (2004) Nature Genet. , vol.36 , pp. 979-983
    • Huusko, P.1
  • 121
    • 0031105418 scopus 로고    scopus 로고
    • ECK, a human EPH-related gene, maps to 1p36. 1, a common region of alteration in human cancers
    • Sulman, E. P. et al. ECK, a human EPH-related gene, maps to 1p36.1, a common region of alteration in human cancers. Genomics 40, 371-374 (1997).
    • (1997) Genomics , vol.40 , pp. 371-374
    • Sulman, E.P.1
  • 122
    • 0038670241 scopus 로고    scopus 로고
    • Mutational analysis of the tyrosine kinome in colorectal cancers
    • Bardelli, A. et al. Mutational analysis of the tyrosine kinome in colorectal cancers. Science 300, 949 (2003).
    • (2003) Science , vol.300 , pp. 949
    • Bardelli, A.1
  • 123
    • 4444257965 scopus 로고    scopus 로고
    • Decreased tumorigenic potential of EphA2-overexpressing breast cancer cells following treatment with adenoviral vectors that express EphrinA 1
    • Noblitt, L. W. et al. Decreased tumorigenic potential of EphA2-overexpressing breast cancer cells following treatment with adenoviral vectors that express EphrinA1. Cancer Gene Ther. 11, 757-766 (2004).
    • (2004) Cancer Gene Ther. , vol.11 , pp. 757-766
    • Noblitt, L.W.1
  • 124
    • 0344816258 scopus 로고    scopus 로고
    • Nuk controls pathfinding of commissural axons in the mammalian central nervous system
    • Henkemeyer, M. et al. 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
  • 125
    • 0029851690 scopus 로고    scopus 로고
    • Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands
    • Holland, S. J. et al. Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands. Nature 383, 722-725 (1996).
    • (1996) Nature , vol.383 , pp. 722-725
    • Holland, S.J.1
  • 126
    • 0030891962 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of transmembrane ligands for Eph receptors
    • Bruckner, K., Pasquale, E. B. & Klein, R. Tyrosine phosphorylation of transmembrane ligands for Eph receptors. Science 275, 1640-1643 (1997).
    • (1997) Science , vol.275 , pp. 1640-1643
    • Bruckner, K.1    Pasquale, E.B.2    Klein, R.3
  • 127
    • 0037093097 scopus 로고    scopus 로고
    • Antibody targeting of the EphA2 tyrosine kinase inhibits malignant cell behavior
    • Carles-Kinch, K., Kilpatrick, K. E., Stewart, J. C. & Kinch, M. S. Antibody targeting of the EphA2 tyrosine kinase inhibits malignant cell behavior. Cancer Res. 62, 2840-2847 (2002).
    • (2002) Cancer Res. , vol.62 , pp. 2840-2847
    • Carles-Kinch, K.1    Kilpatrick, K.E.2    Stewart, J.C.3    Kinch, M.S.4
  • 128
    • 20344376236 scopus 로고    scopus 로고
    • EphB receptor-binding peptides identified by phage display enable design of an antagonist with ephrin-like affinity
    • Koolpe, M., Burgess, R., Dail, M. & Pasquale, E. B. EphB receptor-binding peptides identified by phage display enable design of an antagonist with ephrin-like affinity. J. Biol. Chem. 280, 17301-17311 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 17301-17311
    • Koolpe, M.1    Burgess, R.2    Dail, M.3    Pasquale, E.B.4
  • 129
    • 0037033004 scopus 로고    scopus 로고
    • An ephrin mimetic peptide that selectively targets the EphA2 receptor
    • Koolpe, M., Dail, M. & Pasquale, E. B. An ephrin mimetic peptide that selectively targets the EphA2 receptor. J. Biol. Chem. 277, 46974-46979 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 46974-46979
    • Koolpe, M.1    Dail, M.2    Pasquale, E.B.3
  • 130
    • 10744222441 scopus 로고    scopus 로고
    • EphB2 as a therapeutic antibody drug target for the treatment of colorectal cancer
    • Mao, W. et al. EphB2 as a therapeutic antibody drug target for the treatment of colorectal cancer. Cancer Res. 64, 781-788 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 781-788
    • Mao, W.1
  • 131
    • 8544237780 scopus 로고    scopus 로고
    • Axonal regeneration and lack of astrocytic gliosis in EphA4-deficient mice
    • Goldshmit, Y., Galea, M. P., Wise, G., Bartlett, P. F. & Turnley, A. M. Axonal regeneration and lack of astrocytic gliosis in EphA4-deficient mice. J. Neurosci. 24, 10064-10073 (2004). Proposes that EphA4 receptor signalling contributes to the failure of axon regeneration after spinal cord injury mainly by mediating the formation of a glial scar.
    • (2004) J. Neurosci. , vol.24 , pp. 10064-10073
    • Goldshmit, Y.1    Galea, M.P.2    Wise, G.3    Bartlett, P.F.4    Turnley, A.M.5
  • 132
    • 17044377138 scopus 로고    scopus 로고
    • Coexpressed EphA receptors and ephrin-A ligands mediate opposing actions on growth cone navigation from distinct membrane domains
    • Marquardt, T. et al. Coexpressed EphA receptors and ephrin-A ligands mediate opposing actions on growth cone navigation from distinct membrane domains. Cell 121, 127-139 (2005). Shows that EphA receptors and ephrin-A ligands expressed on the same growth cone segregate laterally into distinct membrane subdomains and both contribute to axon guidance: the EphA receptors by mediating repulsive effects, and the ephrin-A molecules by mediating attractive effects.
    • (2005) Cell , vol.121 , pp. 127-139
    • Marquardt, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.