메뉴 건너뛰기




Volumn , Issue , 2010, Pages

Eph receptors and ephrin ligands: Important players in angiogenesis and tumor angiogenesis

Author keywords

[No Author keywords available]

Indexed keywords

2,4 BIS ANILINOPYRIMIDINE; 2,5 DIMETHYLPYRROLYL BENZOIC ACID DERIVATIVE; ANTINEOPLASTIC AGENT; BEVACIZUMAB; DASATINIB; EPHRIN; EPHRIN RECEPTOR; EPHRIN RECEPTOR A1; EPHRIN RECEPTOR A7; EPHRIN RECEPTOR B6; HYPOXIA INDUCIBLE FACTOR 1ALPHA; N SUBSTITUTED 3 AMINO 4 METHYLBENZAMIDE; RHO KINASE; SORAFENIB; SUNITINIB; UNCLASSIFIED DRUG; VASCULOTROPIN;

EID: 77951677126     PISSN: 16878450     EISSN: 16878469     Source Type: Journal    
DOI: 10.1155/2010/135285     Document Type: Review
Times cited : (104)

References (140)
  • 1
    • 0023607638 scopus 로고
    • A novel putative tyrosine kinase receptor encoded by the eph gene
    • Hirai H., Maru Y., Hagiwara K., Nishida J., Takaku F., A novel putative tyrosine kinase receptor encoded by the eph gene Science 1987 238 4834 1717 1720
    • (1987) Science , vol.238 , Issue.4834 , pp. 1717-1720
    • Hirai, H.1    Maru, Y.2    Hagiwara, K.3    Nishida, J.4    Takaku, F.5
  • 2
    • 4644290521 scopus 로고    scopus 로고
    • Eph receptor tyrosine kinases in tumor and tumor microenvironment
    • DOI 10.2174/1381612043383160
    • Brantley-Sieders D., Schmidt S., Parker M., Chen J., Eph receptor tyrosine kinases in tumor and tumor microenvironment Current Pharmaceutical Design 2004 10 27 3431 3442 (Pubitemid 39276627)
    • (2004) Current Pharmaceutical Design , vol.10 , Issue.27 , pp. 3431-3442
    • Brantley-Sieders, D.1    Schmidt, S.2    Parker, M.3    Chen, J.4
  • 3
    • 0031919093 scopus 로고    scopus 로고
    • The Eph family receptors and ligands
    • DOI 10.1016/S0163-7258(97)00112-5, PII S0163725897001125
    • Zhou R., The Eph family receptors and ligands Pharmacology and Therapeutics 1998 77 3 151 181 (Pubitemid 28157319)
    • (1998) Pharmacology and Therapeutics , vol.77 , Issue.3 , pp. 151-181
    • Zhou, R.1
  • 4
    • 0036303033 scopus 로고    scopus 로고
    • Mechanisms and functions of Eph and ephrin signalling
    • DOI 10.1038/nrm856
    • Kullander K., Klein R., Mechanisms and functions of Eph and ephrin signalling Nature Reviews Molecular Cell Biology 2002 3 7 475 486 (Pubitemid 34733429)
    • (2002) Nature Reviews Molecular Cell Biology , vol.3 , Issue.7 , pp. 475-486
    • Kullander, K.1    Klein, R.2
  • 6
    • 2142764419 scopus 로고    scopus 로고
    • Eph-ephrin promiscuity is now crystal clear
    • Pasquale E. B., Eph-ephrin promiscuity is now crystal clear Nature Neuroscience 2004 7 5 417 418
    • (2004) Nature Neuroscience , vol.7 , Issue.5 , pp. 417-418
    • Pasquale, E.B.1
  • 7
    • 9244260551 scopus 로고    scopus 로고
    • The role of ephrins and Eph receptors in cancer
    • DOI 10.1016/j.cytogfr.2004.09.002, PII S1359610104000760
    • Surawska H., Ma P. C., Salgia R., The role of ephrins and Eph receptors in cancer Cytokine and Growth Factor Reviews 2004 15 6 419 433 (Pubitemid 39550453)
    • (2004) Cytokine and Growth Factor Reviews , vol.15 , Issue.6 , pp. 419-433
    • Surawska, H.1    Ma, P.C.2    Salgia, R.3
  • 9
    • 36048971979 scopus 로고    scopus 로고
    • Tissue transglutaminase clusters soluble A-type ephrins into functionally active high molecular weight oligomers
    • DOI 10.1016/j.yexcr.2007.07.019, PII S0014482707003564
    • Alford S. C., Bazowski J., Lorimer H., Elowe S., Howard P. L., Tissue transglutaminase clusters soluble A-type ephrins into functionally active high molecular weight oligomers Experimental Cell Research 2007 313 20 4170 4179 (Pubitemid 350087045)
    • (2007) Experimental Cell Research , vol.313 , Issue.20 , pp. 4170-4179
    • Alford, S.C.1    Bazowski, J.2    Lorimer, H.3    Elowe, S.4    Howard, P.L.5
  • 10
    • 57649123443 scopus 로고    scopus 로고
    • Soluble monomeric EphrinA1 is released from tumor cells and is a functional ligand for the EphA2 receptor
    • Wykosky J., Palma E., Gibo D. M., Ringler S., Turner C. P., Debinski W., Soluble monomeric EphrinA1 is released from tumor cells and is a functional ligand for the EphA2 receptor Oncogene 2008 27 58 7260 7273
    • (2008) Oncogene , vol.27 , Issue.58 , pp. 7260-7273
    • Wykosky, J.1    Palma, E.2    Gibo, D.M.3    Ringler, S.4    Turner, C.P.5    Debinski, W.6
  • 11
    • 0030891962 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of transmembrane ligands for Eph receptors
    • Brckner K., Pasquale E. B., Klein R., Tyrosine phosphorylation of transmembrane ligands for Eph receptors Science 1997 275 5306 1640 1643
    • (1997) Science , vol.275 , Issue.5306 , pp. 1640-1643
    • Brckner, K.1    Pasquale, E.B.2    Klein, R.3
  • 12
    • 0029851690 scopus 로고    scopus 로고
    • Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands
    • Holland S. J., Gale N. W., Mbamalu G., Yancopoulos G. D., Henkemeyer M., Pawson T., Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands Nature 1996 383 6602 722 725
    • (1996) Nature , vol.383 , Issue.6602 , pp. 722-725
    • Holland, S.J.1    Gale, N.W.2    Mbamalu, G.3    Yancopoulos, G.D.4    Henkemeyer, M.5    Pawson, T.6
  • 13
    • 41149084179 scopus 로고    scopus 로고
    • Eph-ephrin bidirectional signaling in physiology and disease
    • Pasquale E. B., Eph-ephrin bidirectional signaling in physiology and disease Cell 2008 133 1 38 52
    • (2008) Cell , vol.133 , Issue.1 , pp. 38-52
    • Pasquale, E.B.1
  • 14
    • 0034086061 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine residues in the kinase domain and juxtamembrane region regulates the biological and catalytic activities of Eph receptors
    • Binns K. L., Taylor P. P., Sicheri F., Pawson T., Holland S. J., Phosphorylation of tyrosine residues in the kinase domain and juxtamembrane region regulates the biological and catalytic activities of Eph receptors Molecular and Cellular Biology 2000 20 13 4791 4805
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.13 , pp. 4791-4805
    • Binns, K.L.1    Taylor, P.P.2    Sicheri, F.3    Pawson, T.4    Holland, S.J.5
  • 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., Pazzagli C., Freeman A. L., Replacing two conserved tyrosines of the EphB2 receptor with glutamic acid prevents binding of SH2 domains without abrogating kinase activity and biological responses Oncogene 2000 19 2 177 187
    • (2000) Oncogene , vol.19 , Issue.2 , pp. 177-187
    • Zisch, A.H.1    Pazzagli, C.2    Freeman, A.L.3
  • 16
    • 39449085234 scopus 로고    scopus 로고
    • Eph/ephrin signaling: Networks
    • Arvanitis D., Davy A., Eph/ephrin signaling: networks Genes and Development 2008 22 4 416 429
    • (2008) Genes and Development , vol.22 , Issue.4 , pp. 416-429
    • Arvanitis, D.1    Davy, A.2
  • 17
    • 0033016108 scopus 로고    scopus 로고
    • Eph receptors and ephrins: Effectors of morphogenesis
    • Holder N., Klein R., Eph receptors and ephrins: effectors of morphogenesis Development 1999 126 10 2033 2044
    • (1999) Development , vol.126 , Issue.10 , pp. 2033-2044
    • Holder, N.1    Klein, R.2
  • 18
    • 0032968502 scopus 로고    scopus 로고
    • An early developmental role for Eph-ephrin interaction during vertebrate gastrulation
    • Oates A. C., Lackmann M., Power M.-A., An early developmental role for Eph-ephrin interaction during vertebrate gastrulation Mechanisms of Development 1999 83 1-2 77 94
    • (1999) Mechanisms of Development , vol.83 , Issue.12 , pp. 77-94
    • Oates, A.C.1    Lackmann, M.2    Power, M.-A.3
  • 19
    • 51349144056 scopus 로고    scopus 로고
    • Eph/ephrin signalling and function in oncogenesis: Lessons from embryonic development
    • Janes P. W., Adikari S., Lackmann M., Eph/ephrin signalling and function in oncogenesis: lessons from embryonic development Current Cancer Drug Targets 2008 8 6 473 489
    • (2008) Current Cancer Drug Targets , vol.8 , Issue.6 , pp. 473-489
    • Janes, P.W.1    Adikari, S.2    Lackmann, M.3
  • 20
    • 0033598224 scopus 로고    scopus 로고
    • Neural development: Bidirectional signals establish boundaries
    • Klein R., Neural development: bidirectional signals establish boundaries Current Biology 1999 9 18 R691 R694
    • (1999) Current Biology , vol.9 , Issue.18
    • Klein, R.1
  • 21
    • 0033168047 scopus 로고    scopus 로고
    • Eph receptors and ephrins restrict cell intermingling and communication
    • Mellitzer G., Xu Q., Wilkinson D. G., Eph receptors and ephrins restrict cell intermingling and communication Nature 1999 400 6739 77 81
    • (1999) Nature , vol.400 , Issue.6739 , pp. 77-81
    • Mellitzer, G.1    Xu, Q.2    Wilkinson, D.G.3
  • 23
    • 0035137449 scopus 로고    scopus 로고
    • Kinase-dependent and kinase-independent functions of EphA4 receptors in major axon tract formation in vivo
    • Kullander K., Mather N. K., Diella F., Dottori M., Boyd A. W., Klein R., Kinase-dependent and kinase-independent functions of EphA4 receptors in major axon tract formation in vivo Neuron 2001 29 1 73 84
    • (2001) Neuron , vol.29 , Issue.1 , pp. 73-84
    • Kullander, K.1    Mather, N.K.2    Diella, F.3    Dottori, M.4    Boyd, A.W.5    Klein, R.6
  • 24
    • 0033119320 scopus 로고    scopus 로고
    • Modulation of EphA receptor function by coexpressed EphrinA ligands on retinal ganglion cell axons
    • Hornberger M. R., Dtting D., Ciossek T., Modulation of EphA receptor function by coexpressed EphrinA ligands on retinal ganglion cell axons Neuron 1999 22 4 731 742
    • (1999) Neuron , vol.22 , Issue.4 , pp. 731-742
    • Hornberger, M.R.1    Dtting, D.2    Ciossek, T.3
  • 25
    • 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 2000 127 6 1231 1241
    • (2000) Development , vol.127 , Issue.6 , pp. 1231-1241
    • Birgbauer, E.1    Cowan, C.A.2    Sretavan, D.W.3    Henkemeyer, M.4
  • 26
    • 70449713824 scopus 로고    scopus 로고
    • Bidirectional signaling of ErbB and Eph receptors at synapses
    • Chen Y., Fu A. K. Y., Ip N. Y., Bidirectional signaling of ErbB and Eph receptors at synapses Neuron Glia Biology 2008 4 3 211 221
    • (2008) Neuron Glia Biology , vol.4 , Issue.3 , pp. 211-221
    • Chen, Y.1    Fu, A.K.Y.2    Ip, N.Y.3
  • 27
    • 58149138860 scopus 로고    scopus 로고
    • Bidirectional modulation of synaptic functions by Eph/ephrin signaling
    • Klein R., Bidirectional modulation of synaptic functions by Eph/ephrin signaling Nature Neuroscience 2009 12 1 15 20
    • (2009) Nature Neuroscience , vol.12 , Issue.1 , pp. 15-20
    • Klein, R.1
  • 28
    • 0035924602 scopus 로고    scopus 로고
    • The receptor tyrosine kinase EphB2 regulates NMDA-dependent synaptic function
    • Henderson J. T., Georgiou J., Jia Z., The receptor tyrosine kinase EphB2 regulates NMDA-dependent synaptic function Neuron 2001 32 6 1041 1056
    • (2001) Neuron , vol.32 , Issue.6 , pp. 1041-1056
    • Henderson, J.T.1    Georgiou, J.2    Jia, Z.3
  • 29
    • 0034693857 scopus 로고    scopus 로고
    • Eph receptors and ephrin ligands: Embryogenesis to tumorigenesis
    • Dodelet V. C., Pasquale E. B., Eph receptors and ephrin ligands: embryogenesis to tumorigenesis Oncogene 2000 19 49 5614 5619
    • (2000) Oncogene , vol.19 , Issue.49 , pp. 5614-5619
    • Dodelet, V.C.1    Pasquale, E.B.2
  • 31
    • 23044435769 scopus 로고    scopus 로고
    • Eph-modulated cell morphology, adhesion and motility in carcinogenesis
    • Wimmer-Kleikamp S. H., Lackmann M., Eph-modulated cell morphology, adhesion and motility in carcinogenesis IUBMB Life 2005 57 6 421 431
    • (2005) IUBMB Life , vol.57 , Issue.6 , pp. 421-431
    • Wimmer-Kleikamp, S.H.1    Lackmann, M.2
  • 32
    • 58149174073 scopus 로고    scopus 로고
    • Downregulation of EphA1 in colorectal carcinomas correlates with invasion and metastasis
    • Dong Y., Wang J., Sheng Z., Downregulation of EphA1 in colorectal carcinomas correlates with invasion and metastasis Modern Pathology 2009 22 1 151 160
    • (2009) Modern Pathology , vol.22 , Issue.1 , pp. 151-160
    • Dong, Y.1    Wang, J.2    Sheng, Z.3
  • 33
    • 58149402919 scopus 로고    scopus 로고
    • Aberrant methylation of EphA7 in human prostate cancer and its relation to clinicopathologic features
    • Guan M., Xu C., Zhang F., Ye C., Aberrant methylation of EphA7 in human prostate cancer and its relation to clinicopathologic features International Journal of Cancer 2009 124 1 88 94
    • (2009) International Journal of Cancer , vol.124 , Issue.1 , pp. 88-94
    • Guan, M.1    Xu, C.2    Zhang, F.3    Ye, C.4
  • 35
    • 0025373765 scopus 로고
    • Overexpression confers an oncogenic potential upon the eph gene
    • Maru Y., Hirai H., Takaku F., Overexpression confers an oncogenic potential upon the eph gene Oncogene 1990 5 3 445 447
    • (1990) Oncogene , vol.5 , Issue.3 , pp. 445-447
    • Maru, Y.1    Hirai, H.2    Takaku, F.3
  • 37
    • 0033785409 scopus 로고    scopus 로고
    • Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation
    • Miao H., Burnett E., Kinch M., Simon E., Wang B., Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation Nature Cell Biology 2000 2 2 62 69
    • (2000) Nature Cell Biology , vol.2 , Issue.2 , pp. 62-69
    • Miao, H.1    Burnett, E.2    Kinch, M.3    Simon, E.4    Wang, B.5
  • 40
    • 50649111592 scopus 로고    scopus 로고
    • Comparative 3′ UTR analysis allows identification of regulatory clusters that drive Eph/ephrin expression in cancer cell lines
    • article e2780
    • Winter J., Roepcke S., Krause S., Comparative 3′ UTR analysis allows identification of regulatory clusters that drive Eph/ephrin expression in cancer cell lines PLoS ONE 2008 3 7, article e2780
    • (2008) PLoS ONE , vol.3 , pp. 7
    • Winter, J.1    Roepcke, S.2    Krause, S.3
  • 41
    • 70249128037 scopus 로고    scopus 로고
    • Over-expression of EphB3 enhances cell-cell contacts and suppresses tumor growth in HT-29 human colon cancer cells
    • Chiu S.-T., Chang K.-J., Ting C.-H., Shen H.-C., Li H., Hsieh F.-J., Over-expression of EphB3 enhances cell-cell contacts and suppresses tumor growth in HT-29 human colon cancer cells Carcinogenesis 2009 30 9 1475 1486
    • (2009) Carcinogenesis , vol.30 , Issue.9 , pp. 1475-1486
    • Chiu, S.-T.1    Chang, K.-J.2    Ting, C.-H.3    Shen, H.-C.4    Li, H.5    Hsieh, F.-J.6
  • 45
    • 0034678363 scopus 로고    scopus 로고
    • Ephrin-A5 induces collapse of growth cones by activating Rho and Rho kinase
    • DOI 10.1083/jcb.149.2.263
    • Wahl S., Barth H., Ciossek T., Aktories K., Mueller B. K., Ephrin-A5 induces collapse of growth cones by activating Rho and Rho kinase Journal of Cell Biology 2000 149 2 263 270 (Pubitemid 30227145)
    • (2000) Journal of Cell Biology , vol.149 , Issue.2 , pp. 263-270
    • Wahl, S.1    Barth, H.2    Ciossek, T.3    Aktories, K.4    Mueller, B.K.5
  • 46
    • 57149102284 scopus 로고    scopus 로고
    • The EphA3 receptor is expressed in a subset of rhabdomyosarcoma cell lines and suppresses cell adhesion and migration
    • Clifford N., Smith L. M., Powell J., Gattenlhner S., Marx A., OConnor R., The EphA3 receptor is expressed in a subset of rhabdomyosarcoma cell lines and suppresses cell adhesion and migration Journal of Cellular Biochemistry 2008 105 5 1250 1259
    • (2008) Journal of Cellular Biochemistry , vol.105 , Issue.5 , pp. 1250-1259
    • Clifford, N.1    Smith, L.M.2    Powell, J.3    Gattenlhner, S.4    Marx, A.5    Oconnor, R.6
  • 47
    • 75449087524 scopus 로고    scopus 로고
    • Liver cancer: EphrinA2 promotes tumorigenicity through Rac1/Akt/NF- B signaling pathway
    • Feng Y.-X., Zhao J.-S., Li J.-J., Liver cancer: EphrinA2 promotes tumorigenicity through Rac1/Akt/NF- B signaling pathway Hepatology 2010 51 2 535 544
    • (2010) Hepatology , vol.51 , Issue.2 , pp. 535-544
    • Feng, Y.-X.1    Zhao, J.-S.2    Li, J.-J.3
  • 48
    • 54249084591 scopus 로고    scopus 로고
    • Signaling through ephrin-A ligand leads to activation of Src-family kinases, Akt phosphorylation, and inhibition of antigen receptor-induced apoptosis
    • Holen H. L., Shadidi M., Narvhus K., Kjsnes O., Tierens A., Aasheim H.-C., Signaling through ephrin-A ligand leads to activation of Src-family kinases, Akt phosphorylation, and inhibition of antigen receptor-induced apoptosis Journal of Leukocyte Biology 2008 84 4 1183 1191
    • (2008) Journal of Leukocyte Biology , vol.84 , Issue.4 , pp. 1183-1191
    • Holen, H.L.1    Shadidi, M.2    Narvhus, K.3    Kjsnes, O.4    Tierens, A.5    Aasheim, H.-C.6
  • 51
    • 0030576517 scopus 로고    scopus 로고
    • Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis
    • DOI 10.1016/S0092-8674(00)80108-7
    • Hanahan D., Folkman J., Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis Cell 1996 86 3 353 364 (Pubitemid 26272076)
    • (1996) Cell , vol.86 , Issue.3 , pp. 353-364
    • Hanahan, D.1    Folkman, J.2
  • 52
    • 0030758704 scopus 로고    scopus 로고
    • Angiogenesis: A dynamic balance of stimulators and inhibitors
    • Iruela-Arispe M. L., Dvorak H. F., Angiogenesis: a dynamic balance of stimulators and inhibitors Thrombosis and Haemostasis 1997 78 1 672 677
    • (1997) Thrombosis and Haemostasis , vol.78 , Issue.1 , pp. 672-677
    • Iruela-Arispe, M.L.1    Dvorak, H.F.2
  • 53
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D., Weinberg R. A., The hallmarks of cancer Cell 2000 100 1 57 70 (Pubitemid 30046295)
    • (2000) Cell , vol.100 , Issue.1 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 55
    • 4344679183 scopus 로고    scopus 로고
    • Eph receptor tyrosine kinases in angiogenesis: From development to disease
    • DOI 10.1023/B:AGEN.0000037340.33788.87
    • Brantley-Sieders D. M., Chen J., Eph receptor tyrosine kinases in angiogenesis: from development to disease Angiogenesis 2004 7 1 17 28 (Pubitemid 39127767)
    • (2004) Angiogenesis , vol.7 , Issue.1 , pp. 17-28
    • Brantley-Sieders, D.M.1    Chen, J.2
  • 56
    • 59149089644 scopus 로고    scopus 로고
    • Artery and vein size is balanced by Notch and ephrin B2/EphB4 during angiogenesis
    • Kim Y. H., Hu H., Guevara-Gallardo S., Lam M. T. Y., Fong S.-Y., Wang R. A., Artery and vein size is balanced by Notch and ephrin B2/EphB4 during angiogenesis Development 2008 135 22 3755 3764
    • (2008) Development , vol.135 , Issue.22 , pp. 3755-3764
    • Kim, Y.H.1    Hu, H.2    Guevara-Gallardo, S.3    Lam, M.T.Y.4    Fong, S.-Y.5    Wang, R.A.6
  • 57
    • 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 1998 93 5 741 753
    • (1998) Cell , vol.93 , Issue.5 , pp. 741-753
    • Wang, H.U.1    Chen, Z.-F.2    Anderson, D.J.3
  • 58
    • 0035865227 scopus 로고    scopus 로고
    • Ephrin-B2 selectively marks arterial vessels and neovascularization sites in the adult, with expression in both endothelial and smooth-muscle cells
    • DOI 10.1006/dbio.2000.0112
    • Gale N. W., Baluk P., Pan L., Ephrin-B2 selectively marks arterial vessels and neovascularization sites in the adult, with expression in both endothelial and smooth-muscle cells Developmental Biology 2001 230 2 151 160 (Pubitemid 32171414)
    • (2001) Developmental Biology , vol.230 , Issue.2 , pp. 151-160
    • Gale, N.W.1    Baluk, P.2    Pan, L.3    Kwan, M.4    Holash, J.5    DeChiara, T.M.6    McDonald, D.M.7    Yancopoulos, G.D.8
  • 59
    • 30344440869 scopus 로고    scopus 로고
    • Ephrin-B2 controls cell motility and adhesion during blood-vessel-wall assembly
    • Foo S. S., Turner C. J., Adams S., Ephrin-B2 controls cell motility and adhesion during blood-vessel-wall assembly Cell 2006 124 1 161 173
    • (2006) Cell , vol.124 , Issue.1 , pp. 161-173
    • Foo, S.S.1    Turner, C.J.2    Adams, S.3
  • 60
    • 0037103260 scopus 로고    scopus 로고
    • Regulation of vasculogenesis and angiogenesis by EphB/ephrin-B2 signaling between endothelial cells and surrounding mesenchymal cells
    • Oike Y., Ito Y., Hamada K., Regulation of vasculogenesis and angiogenesis by EphB/ephrin-B2 signaling between endothelial cells and surrounding mesenchymal cells Blood 2002 100 4 1326 1333
    • (2002) Blood , vol.100 , Issue.4 , pp. 1326-1333
    • Oike, Y.1    Ito, Y.2    Hamada, K.3
  • 61
    • 0038497941 scopus 로고    scopus 로고
    • Forward EphB4 signaling in endothelial cells controls cellular repulsion and segregation from ephrinB2 positive cells
    • Fller 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 Journal of Cell Science 2003 116 12 2461 2470
    • (2003) Journal of Cell Science , vol.116 , Issue.12 , pp. 2461-2470
    • Fller, T.1    Korff, T.2    Kilian, A.3    Dandekar, G.4    Augustin, H.G.5
  • 62
    • 0035846911 scopus 로고    scopus 로고
    • The cytoplasmic domain of the ligand EphrinB2 is required for vascular morphogenesis but not cranial neural crest migration
    • Adams R. H., Diella F., Hennig S., Helmbacher F., Deutsch U., Klein R., The cytoplasmic domain of the ligand EphrinB2 is required for vascular morphogenesis but not cranial neural crest migration Cell 2001 104 1 57 69
    • (2001) Cell , vol.104 , Issue.1 , pp. 57-69
    • Adams, R.H.1    Diella, F.2    Hennig, S.3    Helmbacher, F.4    Deutsch, U.5    Klein, R.6
  • 63
    • 70349569570 scopus 로고    scopus 로고
    • EphrinB reverse signaling contributes to endothelial and mural cell assembly into vascular structures
    • Salvucci O., Maric D., Economopoulou M., EphrinB reverse signaling contributes to endothelial and mural cell assembly into vascular structures Blood 2009 114 8 1707 1716
    • (2009) Blood , vol.114 , Issue.8 , pp. 1707-1716
    • Salvucci, O.1    Maric, D.2    Economopoulou, M.3
  • 64
    • 0037113915 scopus 로고    scopus 로고
    • Eph B4 receptor signaling mediates endothelial cell migration and proliferation via the phosphatidylinositol 3-kinase pathway
    • Steinle J. J., Meininger C. J., Forough R., Wu G., Wu M. H., Granger H. J., Eph B4 receptor signaling mediates endothelial cell migration and proliferation via the phosphatidylinositol 3-kinase pathway Journal of Biological Chemistry 2002 277 46 43830 43835
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.46 , pp. 43830-43835
    • Steinle, J.J.1    Meininger, C.J.2    Forough, R.3    Wu, G.4    Wu, M.H.5    Granger, H.J.6
  • 65
    • 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., Wilkinson G. A., Weiss C., Roles of ephrinB ligands and EphB receptors in cardiovascular development: demarcation of arterial/venous domains, vascular morphogenesis, and sprouting angiogenesis Genes and Development 1999 13 3 295 306
    • (1999) Genes and Development , vol.13 , Issue.3 , pp. 295-306
    • Adams, R.H.1    Wilkinson, G.A.2    Weiss, C.3
  • 66
    • 0037154999 scopus 로고    scopus 로고
    • Trophoblast functions, angiogenesis and remodeling of the maternal vasculature in the placenta
    • Cross J., Hemberger M., Lu Y., Trophoblast functions, angiogenesis and remodeling of the maternal vasculature in the placenta Molecular and Cellular Endocrinology 2002 187 1-2 207 212
    • (2002) Molecular and Cellular Endocrinology , vol.187 , Issue.12 , pp. 207-212
    • Cross, J.1    Hemberger, M.2    Lu, Y.3
  • 67
    • 0141453017 scopus 로고    scopus 로고
    • Ephrin B1 is expressed on human luteinizing granulosa cells in corpora lutea of the early luteal phase: The possible involvement of the B class Eph-ephrin system during corpus luteum formation
    • Egawa M., Yoshioka S., Higuchi T., Ephrin B1 is expressed on human luteinizing granulosa cells in corpora lutea of the early luteal phase: the possible involvement of the B class Eph-ephrin system during corpus luteum formation Journal of Clinical Endocrinology and Metabolism 2003 88 9 4384 4392
    • (2003) Journal of Clinical Endocrinology and Metabolism , vol.88 , Issue.9 , pp. 4384-4392
    • Egawa, M.1    Yoshioka, S.2    Higuchi, T.3
  • 68
    • 0033560751 scopus 로고    scopus 로고
    • Surface densities of ephrin-B1 determine EphB1-coupled activation of cell attachment through v3 and 51 integrins
    • Huynh-Do U., Stein E., Lane A. A., Liu H., Cerretti D. P., Daniel T. O., Surface densities of ephrin-B1 determine EphB1-coupled activation of cell attachment through v3 and 51 integrins EMBO Journal 1999 18 8 2165 2173
    • (1999) EMBO Journal , vol.18 , Issue.8 , pp. 2165-2173
    • Huynh-Do, U.1    Stein, E.2    Lane, A.A.3    Liu, H.4    Cerretti, D.P.5    Daniel, T.O.6
  • 69
    • 0031787110 scopus 로고    scopus 로고
    • Ephrin-A1 is expressed at sites of vascular development in the mouse
    • McBride J. L., Ruiz J. C., Ephrin-A1 is expressed at sites of vascular development in the mouse Mechanisms of Development 1998 77 2 201 204
    • (1998) Mechanisms of Development , vol.77 , Issue.2 , pp. 201-204
    • McBride, J.L.1    Ruiz, J.C.2
  • 70
    • 0345269144 scopus 로고    scopus 로고
    • Blockade of EphA receptor tyrosine kinase activation inhibits vascular endothelial cell growth factor-induced angiogenesis
    • Cheng N., Brantley D. M., Liu H., Blockade of EphA receptor tyrosine kinase activation inhibits vascular endothelial cell growth factor-induced angiogenesis Molecular Cancer Research 2002 1 1 2 11
    • (2002) Molecular Cancer Research , vol.1 , Issue.1 , pp. 2-11
    • Cheng, N.1    Brantley, D.M.2    Liu, H.3
  • 72
    • 2942605976 scopus 로고    scopus 로고
    • EphA2 receptor tyrosine kinase regulates endothelial cell migration and vascular assembly through phosphoinositide 3-kinase-mediated Rac1 GTPase activation
    • Brantley-Sieders D. M., Caughron J., Hicks D., Pozzi A., Ruiz J. C., Chen J., EphA2 receptor tyrosine kinase regulates endothelial cell migration and vascular assembly through phosphoinositide 3-kinase-mediated Rac1 GTPase activation Journal of Cell Science 2004 117 10 2037 2049
    • (2004) Journal of Cell Science , vol.117 , Issue.10 , pp. 2037-2049
    • Brantley-Sieders, D.M.1    Caughron, J.2    Hicks, D.3    Pozzi, A.4    Ruiz, J.C.5    Chen, J.6
  • 74
    • 0842282623 scopus 로고    scopus 로고
    • Antiangiogenic and antitumor efficacy of EphA2 receptor antagonist
    • Dobrzanski P., Hunter K., Jones-Bolin S., Antiangiogenic and antitumor efficacy of EphA2 receptor antagonist Cancer Research 2004 64 3 910 919
    • (2004) Cancer Research , vol.64 , Issue.3 , pp. 910-919
    • Dobrzanski, P.1    Hunter, K.2    Jones-Bolin, S.3
  • 75
    • 0030242225 scopus 로고    scopus 로고
    • Fighting cancer by attacking its blood supply
    • Folkman J., Fighting cancer by attacking its blood supply Scientific American 1996 275 3 150 154
    • (1996) Scientific American , vol.275 , Issue.3 , pp. 150-154
    • Folkman, J.1
  • 77
    • 0037143102 scopus 로고    scopus 로고
    • Retinoic acid modulates the ability of macrophages to participate in the induction of the angiogenic phenotype in head and neck squamous cell carcinoma
    • Liss C., Fekete M. J., Hasina R., Lingen M. W., Retinoic acid modulates the ability of macrophages to participate in the induction of the angiogenic phenotype in head and neck squamous cell carcinoma International Journal of Cancer 2002 100 3 283 289
    • (2002) International Journal of Cancer , vol.100 , Issue.3 , pp. 283-289
    • Liss, C.1    Fekete, M.J.2    Hasina, R.3    Lingen, M.W.4
  • 78
    • 0023095122 scopus 로고
    • Fibroblast growth factors are present in the extracellular matrix produced by endothelial cells in vitro: Implications for a role of heparinase-like enzymes in the neovascular response
    • Baird A., Ling N., Fibroblast growth factors are present in the extracellular matrix produced by endothelial cells in vitro: implications for a role of heparinase-like enzymes in the neovascular response Biochemical and Biophysical Research Communications 1987 142 2 428 435
    • (1987) Biochemical and Biophysical Research Communications , vol.142 , Issue.2 , pp. 428-435
    • Baird, A.1    Ling, N.2
  • 79
    • 0022252997 scopus 로고
    • Heparin-binding fragments of fibronectin are potent inhibitors of endothelial cell growth
    • Homandberg G. A., Williams J. E., Grant D., Heparin-binding fragments of fibronectin are potent inhibitors of endothelial cell growth American Journal of Pathology 1985 120 3 327 332
    • (1985) American Journal of Pathology , vol.120 , Issue.3 , pp. 327-332
    • Homandberg, G.A.1    Williams, J.E.2    Grant, D.3
  • 80
    • 0027236943 scopus 로고
    • The 16-kilodalton N-terminal fragment of human prolactin is a potent inhibitor of angiogenesis
    • Clapp C., Martial J. A., Guzman R. C., Rentier-Delrue F., Weiner R. I., The 16-kilodalton N-terminal fragment of human prolactin is a potent inhibitor of angiogenesis Endocrinology 1993 133 3 1292 1299
    • (1993) Endocrinology , vol.133 , Issue.3 , pp. 1292-1299
    • Clapp, C.1    Martial, J.A.2    Guzman, R.C.3    Rentier-Delrue, F.4    Weiner, R.I.5
  • 81
    • 0025949596 scopus 로고
    • The 16K fragment of prolactin specifically inhibits basal or fibroblast growth factor stimulated growth of capillary endothelial cells
    • Ferrara N., Clapp C., Weiner R., The 16K fragment of prolactin specifically inhibits basal or fibroblast growth factor stimulated growth of capillary endothelial cells Endocrinology 1991 129 2 896 900
    • (1991) Endocrinology , vol.129 , Issue.2 , pp. 896-900
    • Ferrara, N.1    Clapp, C.2    Weiner, R.3
  • 82
    • 0027970092 scopus 로고
    • Angiostatin: A novel angiogenesis inhibitor that mediates the suppression of metastases by a Lewis lung carcinoma
    • OReilly M. S., Holmgren L., Shing Y., Angiostatin: a novel angiogenesis inhibitor that mediates the suppression of metastases by a Lewis lung carcinoma Cell 1994 79 2 315 328
    • (1994) Cell , vol.79 , Issue.2 , pp. 315-328
    • Oreilly, M.S.1    Holmgren, L.2    Shing, Y.3
  • 84
    • 0027290714 scopus 로고
    • Peptides derived from two separate domains of the matrix protein thrombospondin-1 have anti-angiogenic activity
    • Tolsma S. S., Volpert O. V., Good D. J., Frazier W. A., Polverini P. J., Bouck N., Peptides derived from two separate domains of the matrix protein thrombospondin-1 have anti-angiogenic activity Journal of Cell Biology 1993 122 2 497 511
    • (1993) Journal of Cell Biology , vol.122 , Issue.2 , pp. 497-511
    • Tolsma, S.S.1    Volpert, O.V.2    Good, D.J.3    Frazier, W.A.4    Polverini, P.J.5    Bouck, N.6
  • 85
    • 0029094212 scopus 로고
    • Murine epidermal growth factor (EGF) fragment (3342) inhibits both EGF- and laminin-dependent endothelial cell motility and angiogenesis
    • Nelson J., Allen W. E., Scott W. N., Murine epidermal growth factor (EGF) fragment (3342) inhibits both EGF- and laminin-dependent endothelial cell motility and angiogenesis Cancer Research 1995 55 17 3772 3776
    • (1995) Cancer Research , vol.55 , Issue.17 , pp. 3772-3776
    • Nelson, J.1    Allen, W.E.2    Scott, W.N.3
  • 86
    • 0032886829 scopus 로고    scopus 로고
    • Tumor plasticity allows vasculogenic mimicry, a novel form of angiogenic switch: A rose by any other name?
    • Bissell M. J., Tumor plasticity allows vasculogenic mimicry, a novel form of angiogenic switch: a rose by any other name? American Journal of Pathology 1999 155 3 675 679
    • (1999) American Journal of Pathology , vol.155 , Issue.3 , pp. 675-679
    • Bissell, M.J.1
  • 87
    • 0032887340 scopus 로고    scopus 로고
    • Vascular channel formation by human melanoma cells in vivo and in vitro: Vasculogenic mimicry
    • Maniotis A. J., Folberg R., Hess A., Vascular channel formation by human melanoma cells in vivo and in vitro: vasculogenic mimicry American Journal of Pathology 1999 155 3 739 752
    • (1999) American Journal of Pathology , vol.155 , Issue.3 , pp. 739-752
    • Maniotis, A.J.1    Folberg, R.2    Hess, A.3
  • 88
    • 0035870251 scopus 로고    scopus 로고
    • Molecular regulation of tumor cell vasculogenic mimicry by tyrosine phosphorylation: Role of epithelial cell kinase (Eck/EphA2)
    • Hess A. R., Seftor E. A., Gardner L. M. G., Molecular regulation of tumor cell vasculogenic mimicry by tyrosine phosphorylation: role of epithelial cell kinase (Eck/EphA2) Cancer Research 2001 61 8 3250 3255
    • (2001) Cancer Research , vol.61 , Issue.8 , pp. 3250-3255
    • Hess, A.R.1    Seftor, E.A.2    Gardner, L.M.G.3
  • 89
    • 0036943687 scopus 로고    scopus 로고
    • Role of receptor tyrosine kinase in the angiogenesis
    • Meyer S., Hafner C., Vogt T., Role of receptor tyrosine kinase in the angiogenesis Hautarzt 2002 53 9 629 642
    • (2002) Hautarzt , vol.53 , Issue.9 , pp. 629-642
    • Meyer, S.1    Hafner, C.2    Vogt, T.3
  • 90
    • 33644645280 scopus 로고    scopus 로고
    • VE-cadherin regulates EphA2 in aggressive melanoma cells through a novel signaling pathway: Implications for vasculogenic mimicry
    • Hess A. R., Seftor E. A., Gruman L. M., Kinch M. S., Seftor R. E. B., Hendrix M. J. C., VE-cadherin regulates EphA2 in aggressive melanoma cells through a novel signaling pathway: implications for vasculogenic mimicry Cancer Biology and Therapy 2006 5 2 228 233
    • (2006) Cancer Biology and Therapy , vol.5 , Issue.2 , pp. 228-233
    • Hess, A.R.1    Seftor, E.A.2    Gruman, L.M.3    Kinch, M.S.4    Seftor, R.E.B.5    Hendrix, M.J.C.6
  • 91
    • 0031786126 scopus 로고    scopus 로고
    • Cell-type specific and estrogen dependent expression of the receptor tyrosine kinase EphB4 and its ligand ephrin-B2 during mammary gland morphogenesis
    • Nikolova Z., Djonov V., Zuercher G., Andres A.-C., Ziemiecki A., Cell-type specific and estrogen dependent expression of the receptor tyrosine kinase EphB4 and its ligand ephrin-B2 during mammary gland morphogenesis Journal of Cell Science 1998 111 18 2741 2751
    • (1998) Journal of Cell Science , vol.111 , Issue.18 , pp. 2741-2751
    • Nikolova, Z.1    Djonov, V.2    Zuercher, G.3    Andres, A.-C.4    Ziemiecki, A.5
  • 92
    • 64549133471 scopus 로고    scopus 로고
    • Soluble form of ephrinB2 inhibits xenograft growth of squamous cell carcinoma of the Head and neck
    • Kimura M., Kato Y., Sano D., Soluble form of ephrinB2 inhibits xenograft growth of squamous cell carcinoma of the Head and neck International Journal of Oncology 2009 34 2 321 327
    • (2009) International Journal of Oncology , vol.34 , Issue.2 , pp. 321-327
    • Kimura, M.1    Kato, Y.2    Sano, D.3
  • 93
    • 33745700696 scopus 로고    scopus 로고
    • Receptor tyrosine kinase EphB4 is a survival factor in breast cancer
    • Kumar S. R., Singh J., Xia G., Receptor tyrosine kinase EphB4 is a survival factor in breast cancer American Journal of Pathology 2006 169 1 279 293
    • (2006) American Journal of Pathology , vol.169 , Issue.1 , pp. 279-293
    • Kumar, S.R.1    Singh, J.2    Xia, G.3
  • 94
    • 33747475699 scopus 로고    scopus 로고
    • EphB4 provides survival advantage to squamous cell carcinoma of the head and neck
    • Masood R., Ram Kumar S., Sinha U. K., EphB4 provides survival advantage to squamous cell carcinoma of the head and neck International Journal of Cancer 2006 119 6 1236 1248
    • (2006) International Journal of Cancer , vol.119 , Issue.6 , pp. 1236-1248
    • Masood, R.1    Ram Kumar, S.2    Sinha, U.K.3
  • 95
    • 0034619758 scopus 로고    scopus 로고
    • The ephrin-A1 ligand and its receptor, EphA2, are expressed during tumor neovascularization
    • Ogawa K., Pasqualini R., Lindberg R. A., Kain R., Freeman A. L., Pasquale E. B., The ephrin-A1 ligand and its receptor, EphA2, are expressed during tumor neovascularization Oncogene 2000 19 52 6043 6052
    • (2000) Oncogene , vol.19 , Issue.52 , pp. 6043-6052
    • Ogawa, K.1    Pasqualini, R.2    Lindberg, R.A.3    Kain, R.4    Freeman, A.L.5    Pasquale, E.B.6
  • 96
    • 56249088261 scopus 로고    scopus 로고
    • Expression of EphA2 and VEGF in squamous cell carcinoma of the tongue: Correlation with the angiogenesis and clinical outcome
    • Shao Z., Zhang W.-F., Chen X.-M., Shang Z.-J., Expression of EphA2 and VEGF in squamous cell carcinoma of the tongue: correlation with the angiogenesis and clinical outcome Oral Oncology 2008 44 12 1110 1117
    • (2008) Oral Oncology , vol.44 , Issue.12 , pp. 1110-1117
    • Shao, Z.1    Zhang, W.-F.2    Chen, X.-M.3    Shang, Z.-J.4
  • 97
    • 18644379904 scopus 로고    scopus 로고
    • Soluble Eph A receptors inhibit tumor angiogenesis and progression in vivo
    • Brantley D. M., Cheng N., Thompson E. J., Soluble Eph A receptors inhibit tumor angiogenesis and progression in vivo Oncogene 2002 21 46 7011 7026
    • (2002) Oncogene , vol.21 , Issue.46 , pp. 7011-7026
    • Brantley, D.M.1    Cheng, N.2    Thompson, E.J.3
  • 98
    • 10744223603 scopus 로고    scopus 로고
    • Inhibition of VEGF-dependent multistage carcinogenesis by soluble EphA receptors
    • Cheng N., Brantley D., Fang W. B., Inhibition of VEGF-dependent multistage carcinogenesis by soluble EphA receptors Neoplasia 2003 5 5 445 456
    • (2003) Neoplasia , vol.5 , Issue.5 , pp. 445-456
    • Cheng, N.1    Brantley, D.2    Fang, W.B.3
  • 99
    • 27744597086 scopus 로고    scopus 로고
    • Impaired tumor microenvironment in EphA2-deficient mice inhibits tumor angiogenesis and metastatic progression
    • Brantley-Sieders D. M., Fang W. B., Hicks D. J., Zhuang G., Shyr Y., Chen J., Impaired tumor microenvironment in EphA2-deficient mice inhibits tumor angiogenesis and metastatic progression FASEB Journal 2005 19 13 1884 1886
    • (2005) FASEB Journal , vol.19 , Issue.13 , pp. 1884-1886
    • Brantley-Sieders, D.M.1    Fang, W.B.2    Hicks, D.J.3    Zhuang, G.4    Shyr, Y.5    Chen, J.6
  • 100
    • 47949133687 scopus 로고    scopus 로고
    • EphA2 overexpression promotes ovarian cancer growth
    • Lu C., Shahzad M. M. K., Wang H., EphA2 overexpression promotes ovarian cancer growth Cancer Biology and Therapy 2008 7 7 1098 1103
    • (2008) Cancer Biology and Therapy , vol.7 , Issue.7 , pp. 1098-1103
    • Lu, C.1    Shahzad, M.M.K.2    Wang, H.3
  • 102
    • 32544436614 scopus 로고    scopus 로고
    • EphB4 controls blood vascular morphogenesis during postnatal angiogenesis
    • Erber R., Eichelsbacher U., Powajbo V., EphB4 controls blood vascular morphogenesis during postnatal angiogenesis EMBO Journal 2006 25 3 628 641
    • (2006) EMBO Journal , vol.25 , Issue.3 , pp. 628-641
    • Erber, R.1    Eichelsbacher, U.2    Powajbo, V.3
  • 103
    • 59149083473 scopus 로고    scopus 로고
    • Transcriptional switch of dormant tumors to fast-growing angiogenic phenotype
    • Almog N., Ma L., Raychowdhury R., Transcriptional switch of dormant tumors to fast-growing angiogenic phenotype Cancer Research 2009 69 3 836 844
    • (2009) Cancer Research , vol.69 , Issue.3 , pp. 836-844
    • Almog, N.1    Ma, L.2    Raychowdhury, R.3
  • 104
    • 26444553595 scopus 로고    scopus 로고
    • Hypoxia up-regulates expression of Eph receptors and ephrins in mouse skin
    • Vihanto M. M., Plock J., Erni D., Frey B. M., Frey F. J., Huynh-Do U., Hypoxia up-regulates expression of Eph receptors and ephrins in mouse skin FASEB Journal 2005 19 12 1689 1691
    • (2005) FASEB Journal , vol.19 , Issue.12 , pp. 1689-1691
    • Vihanto, M.M.1    Plock, J.2    Erni, D.3    Frey, B.M.4    Frey, F.J.5    Huynh-Do, U.6
  • 105
    • 34147144960 scopus 로고    scopus 로고
    • Transcriptional profiling of human cord blood CD133+ and cultured bone marrow mesenchymal stem cells in response to hypoxia
    • Martin-Rendon E., Hale S. J. M., Ryan D., Transcriptional profiling of human cord blood CD133+ and cultured bone marrow mesenchymal stem cells in response to hypoxia Stem Cells 2007 25 4 1003 1012
    • (2007) Stem Cells , vol.25 , Issue.4 , pp. 1003-1012
    • Martin-Rendon, E.1    Hale, S.J.M.2    Ryan, D.3
  • 106
    • 49649115935 scopus 로고    scopus 로고
    • Hypoxia-inducible transcription factor- 2 in endothelial cells regulates tumor neovascularization through activation of ephrin A1
    • Yamashita T., Ohneda K., Nagano M., Hypoxia-inducible transcription factor- 2 in endothelial cells regulates tumor neovascularization through activation of ephrin A1 Journal of Biological Chemistry 2008 283 27 18926 18936
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.27 , pp. 18926-18936
    • Yamashita, T.1    Ohneda, K.2    Nagano, M.3
  • 107
    • 49849085256 scopus 로고    scopus 로고
    • Chronic hypoxia and rat lung development: Analysis by morphometry and directed microarray
    • Truog W. E., Xu D., Ekekezie I. I., Chronic hypoxia and rat lung development: analysis by morphometry and directed microarray Pediatric Research 2008 64 1 56 62
    • (2008) Pediatric Research , vol.64 , Issue.1 , pp. 56-62
    • Truog, W.E.1    Xu, D.2    Ekekezie, I.I.3
  • 108
    • 0344874638 scopus 로고    scopus 로고
    • The impact of anti-angiogenic agents on cancer therapy
    • Marme D., The impact of anti-angiogenic agents on cancer therapy Journal of Cancer Research and Clinical Oncology 2003 129 11 607 620
    • (2003) Journal of Cancer Research and Clinical Oncology , vol.129 , Issue.11 , pp. 607-620
    • Marme, D.1
  • 109
    • 43249114710 scopus 로고    scopus 로고
    • Vascular endothelial growth factor-dependent and -independent regulation of angiogenesis
    • Shibuya M., Vascular endothelial growth factor-dependent and -independent regulation of angiogenesis Journal of Biochemistry and Molecular Biology 2008 41 4 278 286
    • (2008) Journal of Biochemistry and Molecular Biology , vol.41 , Issue.4 , pp. 278-286
    • Shibuya, M.1
  • 110
    • 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 Research 2002 62 10 2840 2847
    • (2002) Cancer Research , vol.62 , Issue.10 , pp. 2840-2847
    • Carles-Kinch, K.1    Kilpatrick, K.E.2    Stewart, J.C.3    Kinch, M.S.4
  • 111
    • 10744228315 scopus 로고    scopus 로고
    • Differential EphA2 epitope display on normal versus malignant cells
    • Coffman K. T., Hu M., Carles-Kinch K., Differential EphA2 epitope display on normal versus malignant cells Cancer Research 2003 63 22 7907 7912
    • (2003) Cancer Research , vol.63 , Issue.22 , pp. 7907-7912
    • Coffman, K.T.1    Hu, M.2    Carles-Kinch, K.3
  • 112
    • 10744222441 scopus 로고    scopus 로고
    • EphB2 as a therapeutic antibody drug target for the treatment of colorectal cancer
    • Mao W., Luis E., Ross S., EphB2 as a therapeutic antibody drug target for the treatment of colorectal cancer Cancer Research 2004 64 3 781 788
    • (2004) Cancer Research , vol.64 , Issue.3 , pp. 781-788
    • Mao, W.1    Luis, E.2    Ross, S.3
  • 113
    • 23044497596 scopus 로고    scopus 로고
    • Concurrent binding of anti-EphA3 antibody and ephrin-A5 amplifies EphA3 signaling and downstream responses: Potential as EphA3-specific tumor-targeting reagents
    • Vearing C., Lee F.-T., Wimmer-Kleikamp S., Concurrent binding of anti-EphA3 antibody and ephrin-A5 amplifies EphA3 signaling and downstream responses: potential as EphA3-specific tumor-targeting reagents Cancer Research 2005 65 15 6745 6754
    • (2005) Cancer Research , vol.65 , Issue.15 , pp. 6745-6754
    • Vearing, C.1    Lee, F.-T.2    Wimmer-Kleikamp, S.3
  • 114
    • 33644783643 scopus 로고    scopus 로고
    • The soluble extracellular domain of EphB4 (sEphB4) antagonizes EphB4-EphrinB2 interaction, modulates angiogenesis, and inhibits tumor growth
    • Kertesz N., Krasnoperov V., Reddy R., The soluble extracellular domain of EphB4 (sEphB4) antagonizes EphB4-EphrinB2 interaction, modulates angiogenesis, and inhibits tumor growth Blood 2006 107 6 2330 2338
    • (2006) Blood , vol.107 , Issue.6 , pp. 2330-2338
    • Kertesz, N.1    Krasnoperov, V.2    Reddy, R.3
  • 115
    • 2442706421 scopus 로고    scopus 로고
    • Inhibition of tumor growth and angiogenesis by soluble EphB4
    • Martiny-Baron G., Korff T., Schaffner F., Inhibition of tumor growth and angiogenesis by soluble EphB4 Neoplasia 2004 6 3 248 257
    • (2004) Neoplasia , vol.6 , Issue.3 , pp. 248-257
    • Martiny-Baron, G.1    Korff, T.2    Schaffner, F.3
  • 116
    • 59449103839 scopus 로고    scopus 로고
    • The role of Ephs, Ephrins, and growth factors in Kaposi sarcoma and implications of EphrinB2 blockade
    • Scehnet J. S., Ley E. J., Krasnoperov V., The role of Ephs, Ephrins, and growth factors in Kaposi sarcoma and implications of EphrinB2 blockade Blood 2009 113 1 254 263
    • (2009) Blood , vol.113 , Issue.1 , pp. 254-263
    • Scehnet, J.S.1    Ley, E.J.2    Krasnoperov, V.3
  • 117
    • 64049096339 scopus 로고    scopus 로고
    • Soluble ephrin-B2 mediates apoptosis in retinal neovascularization and in endothelial cells
    • Davies M. H., Zamora D. O., Smith J. R., Powers M. R., Soluble ephrin-B2 mediates apoptosis in retinal neovascularization and in endothelial cells Microvascular Research 2009 77 3 382 386
    • (2009) Microvascular Research , vol.77 , Issue.3 , pp. 382-386
    • Davies, M.H.1    Zamora, D.O.2    Smith, J.R.3    Powers, M.R.4
  • 119
    • 58149277085 scopus 로고    scopus 로고
    • Ephrin A1-targeted nanoshells for photothermal ablation of prostate cancer cells
    • Gobin A. M., Moon J. J., West J. L., Ephrin A1-targeted nanoshells for photothermal ablation of prostate cancer cells International Journal of Nanomedicine 2008 3 3 351 358
    • (2008) International Journal of Nanomedicine , vol.3 , Issue.3 , pp. 351-358
    • Gobin, A.M.1    Moon, J.J.2    West, J.L.3
  • 120
    • 32044470909 scopus 로고    scopus 로고
    • Structure and thermodynamic characterization of the EphB4/Ephrin-B2 antagonist peptide complex reveals the determinants for receptor specificity
    • Chrencik J. E., Brooun A., Recht M. I., Structure and thermodynamic characterization of the EphB4/Ephrin-B2 antagonist peptide complex reveals the determinants for receptor specificity Structure 2006 14 2 321 330
    • (2006) Structure , vol.14 , Issue.2 , pp. 321-330
    • Chrencik, J.E.1    Brooun, A.2    Recht, M.I.3
  • 121
    • 37549017344 scopus 로고    scopus 로고
    • Three-dimensional structure of the EphB2 receptor in complex with an antagonistic peptide reveals a novel mode of inhibition
    • Chrencik J. E., Brooun A., Recht M. I., Three-dimensional structure of the EphB2 receptor in complex with an antagonistic peptide reveals a novel mode of inhibition Journal of Biological Chemistry 2007 282 50 36505 36513
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.50 , pp. 36505-36513
    • Chrencik, J.E.1    Brooun, A.2    Recht, M.I.3
  • 122
    • 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 Journal of Biological Chemistry 2005 280 17 17301 17311
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 17301-17311
    • Koolpe, M.1    Burgess, R.2    Dail, M.3    Pasquale, E.B.4
  • 123
    • 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 Journal of Biological Chemistry 2002 277 49 46974 46979
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.49 , pp. 46974-46979
    • Koolpe, M.1    Dail, M.2    Pasquale, E.B.3
  • 124
    • 34648834393 scopus 로고    scopus 로고
    • Immunotherapy of murine colon cancer using receptor tyrosine kinase EphA2-derived peptide-pulsed dendritic cell vaccines
    • Yamaguchi S., Tatsumi T., Takehara T., Immunotherapy of murine colon cancer using receptor tyrosine kinase EphA2-derived peptide-pulsed dendritic cell vaccines Cancer 2007 110 7 1469 1477
    • (2007) Cancer , vol.110 , Issue.7 , pp. 1469-1477
    • Yamaguchi, S.1    Tatsumi, T.2    Takehara, T.3
  • 125
    • 54049137918 scopus 로고    scopus 로고
    • Inhibitors of the tyrosine kinase EphB4. Part 2: Structure-based discovery and optimisation of 3,5-bis substituted anilinopyrimidines
    • Bardelle C., Coleman T., Cross D., Inhibitors of the tyrosine kinase EphB4. Part 2: structure-based discovery and optimisation of 3,5-bis substituted anilinopyrimidines Bioorganic and Medicinal Chemistry Letters 2008 18 21 5717 5721
    • (2008) Bioorganic and Medicinal Chemistry Letters , vol.18 , Issue.21 , pp. 5717-5721
    • Bardelle, C.1    Coleman, T.2    Cross, D.3
  • 126
    • 43049114977 scopus 로고    scopus 로고
    • Inhibitors of the tyrosine kinase EphB4. Part 1: Structure-based design and optimization of a series of 2,4-bis-anilinopyrimidines
    • Bardelle C., Cross D., Davenport S., Inhibitors of the tyrosine kinase EphB4. Part 1: structure-based design and optimization of a series of 2,4-bis-anilinopyrimidines Bioorganic and Medicinal Chemistry Letters 2008 18 9 2776 2780
    • (2008) Bioorganic and Medicinal Chemistry Letters , vol.18 , Issue.9 , pp. 2776-2780
    • Bardelle, C.1    Cross, D.2    Davenport, S.3
  • 127
    • 57649178194 scopus 로고    scopus 로고
    • Small molecules can selectively inhibit ephrin binding to the EphA4 and EphA2 receptors
    • Noberini R., Koolpe M., Peddibhotla S., Small molecules can selectively inhibit ephrin binding to the EphA4 and EphA2 receptors Journal of Biological Chemistry 2008 283 43 29461 29472
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.43 , pp. 29461-29472
    • Noberini, R.1    Koolpe, M.2    Peddibhotla, S.3
  • 128
    • 67649996707 scopus 로고    scopus 로고
    • Discovery and structural analysis of Eph receptor tyrosine kinase inhibitors
    • Choi Y., Syeda F., Walker J. R., Discovery and structural analysis of Eph receptor tyrosine kinase inhibitors Bioorganic and Medicinal Chemistry Letters 2009 19 15 4467 4470
    • (2009) Bioorganic and Medicinal Chemistry Letters , vol.19 , Issue.15 , pp. 4467-4470
    • Choi, Y.1    Syeda, F.2    Walker, J.R.3
  • 129
    • 38549168926 scopus 로고    scopus 로고
    • Dasatinib: In chronic myeloid leukemia and Philadelphia chromosome-positive acute lymphoblastic leukemia
    • Keam S. J., Dasatinib: in chronic myeloid leukemia and Philadelphia chromosome-positive acute lymphoblastic leukemia BioDrugs 2008 22 1 59 69
    • (2008) BioDrugs , vol.22 , Issue.1 , pp. 59-69
    • Keam, S.J.1
  • 130
    • 56449100212 scopus 로고    scopus 로고
    • Inhibition of Src family kinases with dasatinib blocks migration and invasion of human melanoma cells
    • Buettner R., Mesa T., Vultur A., Lee F., Jove R., Inhibition of Src family kinases with dasatinib blocks migration and invasion of human melanoma cells Molecular Cancer Research 2008 6 11 1766 1774
    • (2008) Molecular Cancer Research , vol.6 , Issue.11 , pp. 1766-1774
    • Buettner, R.1    Mesa, T.2    Vultur, A.3    Lee, F.4    Jove, R.5
  • 131
    • 67649846431 scopus 로고    scopus 로고
    • Dasatinib synergizes with doxorubicin to block growth, migration, and invasion of breast cancer cells
    • Pichot C. S., Hartig S. M., Xia L., Dasatinib synergizes with doxorubicin to block growth, migration, and invasion of breast cancer cells British Journal of Cancer 2009 101 1 38 47
    • (2009) British Journal of Cancer , vol.101 , Issue.1 , pp. 38-47
    • Pichot, C.S.1    Hartig, S.M.2    Xia, L.3
  • 132
    • 70449533848 scopus 로고    scopus 로고
    • Activity of the multikinase inhibitor dasatinib against ovarian cancer cells
    • Konecny G. E., Glas R., Dering J., Activity of the multikinase inhibitor dasatinib against ovarian cancer cells British Journal of Cancer 2009 101 10 1699 1708
    • (2009) British Journal of Cancer , vol.101 , Issue.10 , pp. 1699-1708
    • Konecny, G.E.1    Glas, R.2    Dering, J.3
  • 133
    • 53049104807 scopus 로고    scopus 로고
    • Effects of dasatinib on EphA2 receptor tyrosine kinase activity and downstream signalling in pancreatic cancer
    • Chang Q., Jorgensen C., Pawson T., Hedley D. W., Effects of dasatinib on EphA2 receptor tyrosine kinase activity and downstream signalling in pancreatic cancer British Journal of Cancer 2008 99 7 1074 1082
    • (2008) British Journal of Cancer , vol.99 , Issue.7 , pp. 1074-1082
    • Chang, Q.1    Jorgensen, C.2    Pawson, T.3    Hedley, D.W.4
  • 134
    • 56949094399 scopus 로고    scopus 로고
    • RNA interference targeting EphA2 inhibits proliferation, induces apoptosis, and cooperates with cytotoxic drugs in human glioma cells
    • Zhou Z., Yuan X., Li Z., RNA interference targeting EphA2 inhibits proliferation, induces apoptosis, and cooperates with cytotoxic drugs in human glioma cells Surgical Neurology 2008 70 6 562 568
    • (2008) Surgical Neurology , vol.70 , Issue.6 , pp. 562-568
    • Zhou, Z.1    Yuan, X.2    Li, Z.3
  • 135
    • 63849221730 scopus 로고    scopus 로고
    • Eph receptors in breast cancer: Roles in tumor promotion and tumor suppression
    • Vaught D., Brantley-Sieders D. M., Chen J., Eph receptors in breast cancer: roles in tumor promotion and tumor suppression Breast Cancer Research 2008 10 6 217
    • (2008) Breast Cancer Research , vol.10 , Issue.6 , pp. 217
    • Vaught, D.1    Brantley-Sieders, D.M.2    Chen, J.3
  • 136
    • 34249329249 scopus 로고    scopus 로고
    • Paradoxes of the EphB4 receptor in cancer
    • Noren N. K., Pasquale E. B., Paradoxes of the EphB4 receptor in cancer Cancer Research 2007 67 9 3994 3997
    • (2007) Cancer Research , vol.67 , Issue.9 , pp. 3994-3997
    • Noren, N.K.1    Pasquale, E.B.2
  • 137
    • 57749121465 scopus 로고    scopus 로고
    • The EphA2 receptor and EphrinA1 ligand in solid tumors: Function and therapeutic targeting
    • Wykosky J., Debinski W., The EphA2 receptor and EphrinA1 ligand in solid tumors: function and therapeutic targeting Molecular Cancer Research 2008 6 12 1795 1806
    • (2008) Molecular Cancer Research , vol.6 , Issue.12 , pp. 1795-1806
    • Wykosky, J.1    Debinski, W.2
  • 138
    • 33646434790 scopus 로고    scopus 로고
    • Anti-EphA2 antibodies decrease EphA2 protein levels in murine CT26 colorectal and human MDA-231 breast tumors but do not inhibit tumor growth
    • Kiewlich D., Zhang J., Gross C., Anti-EphA2 antibodies decrease EphA2 protein levels in murine CT26 colorectal and human MDA-231 breast tumors but do not inhibit tumor growth Neoplasia 2006 8 1 18 30
    • (2006) Neoplasia , vol.8 , Issue.1 , pp. 18-30
    • Kiewlich, D.1    Zhang, J.2    Gross, C.3
  • 139
    • 38149137411 scopus 로고    scopus 로고
    • The receptor tyrosine kinase EphA2 promotes mammary adenocarcinoma tumorigenesis and metastatic progression in mice by amplifying ErbB2 signaling
    • Brantley-Sieders D. M., Zhuang G., Hicks D., The receptor tyrosine kinase EphA2 promotes mammary adenocarcinoma tumorigenesis and metastatic progression in mice by amplifying ErbB2 signaling Journal of Clinical Investigation 2008 118 1 64 78
    • (2008) Journal of Clinical Investigation , vol.118 , Issue.1 , pp. 64-78
    • Brantley-Sieders, D.M.1    Zhuang, G.2    Hicks, D.3
  • 140
    • 57749101164 scopus 로고    scopus 로고
    • Eph receptors and ephrins in cancer: Common themes and controversies
    • Chen J., Zhuang G., Frieden L., Debinski W., Eph receptors and ephrins in cancer: common themes and controversies Cancer Research 2008 68 24 10031 10033
    • (2008) Cancer Research , vol.68 , Issue.24 , pp. 10031-10033
    • Chen, J.1    Zhuang, G.2    Frieden, L.3    Debinski, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.