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Volumn 113, Issue 2, 2013, Pages 333-354

Targeting tumor micro-environment for design and development ofnovel anti-angiogenic agents arresting tumor growth

Author keywords

Angiogenesis; Angiogenic cytokines peptides; Antiangiogenic agents

Indexed keywords

ADENOSINE TRIPHOSPHATE; ANGIOGENESIS INHIBITOR; ANGIOGENIC PROTEIN; ANGIOGENIN; ANGIOPOIETIN 1; ANGIOPOIETIN 2; CALCITONIN GENE RELATED PEPTIDE; CALCITONIN RECEPTOR LIKE RECEPTOR; EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; FIBROBLAST GROWTH FACTOR; G PROTEIN COUPLED RECEPTOR; INTERLEUKIN 1; INTERLEUKIN 3; INTERLEUKIN 6; INTERLEUKIN 6 RECEPTOR; JANUS KINASE; LINOLENIC ACID; MACROPHAGE INFLAMMATORY PROTEIN; MONOCYTE CHEMOTACTIC PROTEIN; NERVE GROWTH FACTOR; PHORBOL DIBUTYRATE; PLACENTAL GROWTH FACTOR; PLATELET DERIVED GROWTH FACTOR; PLATELET DERIVED GROWTH FACTOR RECEPTOR; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROSTAGLANDIN F; RECEPTOR ACTIVITY MODIFYING PROTEIN; SCATTER FACTOR; SOMATOMEDIN; TUMOR NECROSIS FACTOR ALPHA; VASCULOTROPIN; VASCULOTROPIN RECEPTOR;

EID: 84887609331     PISSN: 00796107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pbiomolbio.2013.10.001     Document Type: Review
Times cited : (88)

References (261)
  • 1
    • 0032954241 scopus 로고    scopus 로고
    • Localization of VEGF-B in the mouse embryo suggests a paracrine role of the growth factor in the developing vasculature
    • Aase K., Lymboussaki A., Kaipainen A., Olofsson B., Alitalo K., Eriksson U. Localization of VEGF-B in the mouse embryo suggests a paracrine role of the growth factor in the developing vasculature. Dev. Dyn. 1999, 215:12-25.
    • (1999) Dev. Dyn. , vol.215 , pp. 12-25
    • Aase, K.1    Lymboussaki, A.2    Kaipainen, A.3    Olofsson, B.4    Alitalo, K.5    Eriksson, U.6
  • 5
    • 0029803552 scopus 로고    scopus 로고
    • An essential role for p300/CBP in the cellular response to hypoxia
    • Arany Z., Huang L.E., Eckner R. An essential role for p300/CBP in the cellular response to hypoxia. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:12969-12973.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 12969-12973
    • Arany, Z.1    Huang, L.E.2    Eckner, R.3
  • 7
    • 0027175177 scopus 로고
    • Binding of mutants of human insulin-like growth factor II to insulin-like growth factor binding proteins 1-6
    • Bach L.A., Hsieh S., Sakano K., Fujiwara H., Perdue J.F., Rechler M.M. Binding of mutants of human insulin-like growth factor II to insulin-like growth factor binding proteins 1-6. J.Biol. Chem. 1993, 268:9246-9254.
    • (1993) J.Biol. Chem. , vol.268 , pp. 9246-9254
    • Bach, L.A.1    Hsieh, S.2    Sakano, K.3    Fujiwara, H.4    Perdue, J.F.5    Rechler, M.M.6
  • 8
    • 0033025393 scopus 로고
    • Angiogenin, a potent mediator of angiogenesis. Biological, biochemical and structural properties
    • Badet J. Angiogenin, a potent mediator of angiogenesis. Biological, biochemical and structural properties. Pathol. Biol. (Paris) 1993, 47:345-351.
    • (1993) Pathol. Biol. (Paris) , vol.47 , pp. 345-351
    • Badet, J.1
  • 10
    • 0023241481 scopus 로고
    • On the tertiary structure of the extracellular domains of the epidermal growth factor and insulin receptors
    • Bajaj M., Waterfield M.D., Schlessinger J., Taylor W.R., Blundell T. On the tertiary structure of the extracellular domains of the epidermal growth factor and insulin receptors. Biochim. Biophys. Acta 1987, 16:220-226.
    • (1987) Biochim. Biophys. Acta , vol.16 , pp. 220-226
    • Bajaj, M.1    Waterfield, M.D.2    Schlessinger, J.3    Taylor, W.R.4    Blundell, T.5
  • 11
    • 0029965411 scopus 로고    scopus 로고
    • Epidermal growth factor related peptides activate distinct subsets of ErbB receptors and differ in their biological activities
    • Beerli R.R., Hynes N.E. Epidermal growth factor related peptides activate distinct subsets of ErbB receptors and differ in their biological activities. J.Biol. Chem. 1996, 271:6071-6076.
    • (1996) J.Biol. Chem. , vol.271 , pp. 6071-6076
    • Beerli, R.R.1    Hynes, N.E.2
  • 14
    • 0001603840 scopus 로고
    • Angiogenin stimulates endothelial cell prostacyclin secretion by activation of phospholipase A2
    • Bicknell R., Vallee B.L. Angiogenin stimulates endothelial cell prostacyclin secretion by activation of phospholipase A2. Proc. Natl. Acad. Sci. U. S. A. 1989, 86:1573-1577.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 1573-1577
    • Bicknell, R.1    Vallee, B.L.2
  • 18
    • 0036499988 scopus 로고    scopus 로고
    • Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur
    • Brown J., Esnouf R.M., Jones M.A., Linnell J., Harlos K., Hassan A.B., Jones E.Y. Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur. EMBO J. 2002, 21:1054-1062.
    • (2002) EMBO J. , vol.21 , pp. 1054-1062
    • Brown, J.1    Esnouf, R.M.2    Jones, M.A.3    Linnell, J.4    Harlos, K.5    Hassan, A.B.6    Jones, E.Y.7
  • 19
    • 0035834409 scopus 로고    scopus 로고
    • Aconserved family of prolyl-4-hydroxylases that modify HIF
    • Bruick R.K., McKnight S.L. Aconserved family of prolyl-4-hydroxylases that modify HIF. Science 2001, 294:1337-1340.
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 21
    • 77951233065 scopus 로고    scopus 로고
    • Selection of a novel and highly specific tumor necrosis factor-a (TNF-a) antagonist: insight from the crystal structure of the antagonist-TNF-a complex
    • Byla P., Andersen M.H., Holtet T.L., Jacobsen H., Munch M., Gad H.H., Thøgersen H.C., Hartmann R. Selection of a novel and highly specific tumor necrosis factor-a (TNF-a) antagonist: insight from the crystal structure of the antagonist-TNF-a complex. J.Biol. Chem. 2010, 285:12096-12100.
    • (2010) J.Biol. Chem. , vol.285 , pp. 12096-12100
    • Byla, P.1    Andersen, M.H.2    Holtet, T.L.3    Jacobsen, H.4    Munch, M.5    Gad, H.H.6    Thøgersen, H.C.7    Hartmann, R.8
  • 23
    • 0025134280 scopus 로고
    • Biochemical properties of site-directed mutants of human epidermal growth factor: importance of solvent-exposed hydrophobic residues of the amino-terminal domain in receptor binding
    • Campion S.R., Matsunami R.K., Engler D.A., Niyogi S.K. Biochemical properties of site-directed mutants of human epidermal growth factor: importance of solvent-exposed hydrophobic residues of the amino-terminal domain in receptor binding. Biochemistry 1990, 29:9988-9993.
    • (1990) Biochemistry , vol.29 , pp. 9988-9993
    • Campion, S.R.1    Matsunami, R.K.2    Engler, D.A.3    Niyogi, S.K.4
  • 25
    • 0025321157 scopus 로고
    • Epidermal growth factor
    • Carpenter G., Cohen S. Epidermal growth factor. J.Biol. Chem. 1990, 265:7709-7712.
    • (1990) J.Biol. Chem. , vol.265 , pp. 7709-7712
    • Carpenter, G.1    Cohen, S.2
  • 26
    • 0033986948 scopus 로고    scopus 로고
    • Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha
    • Carrero P., Okamoto K., Coumailleau P., O'Brien S., Tanaka H., Poellinger L. Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha. Mol. Cell Biol. 2000, 20:402-415.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 402-415
    • Carrero, P.1    Okamoto, K.2    Coumailleau, P.3    O'Brien, S.4    Tanaka, H.5    Poellinger, L.6
  • 27
    • 34547733023 scopus 로고    scopus 로고
    • The latest advances in kidney diseases and related disorders
    • Cases A. The latest advances in kidney diseases and related disorders. Drug News Perspect. 2007, 20:647-654.
    • (2007) Drug News Perspect. , vol.20 , pp. 647-654
    • Cases, A.1
  • 29
  • 30
    • 1642297115 scopus 로고    scopus 로고
    • The crystal structure of placental growth factor in complex with domain 2 of vascular endothelial growth factor receptor-1
    • Christinger H.W., Fuh G., de Vos A.M., Wiesmann C. The crystal structure of placental growth factor in complex with domain 2 of vascular endothelial growth factor receptor-1. J.Biol. Chem. 2004, 279:10382-10388.
    • (2004) J.Biol. Chem. , vol.279 , pp. 10382-10388
    • Christinger, H.W.1    Fuh, G.2    de Vos, A.M.3    Wiesmann, C.4
  • 32
    • 0030046481 scopus 로고    scopus 로고
    • Interleukin 6 induces the expression of vascular endothelial growth factor
    • Cohen T., Nahari D., Cerem L.W., Neufeld G., Levi B.Z. Interleukin 6 induces the expression of vascular endothelial growth factor. J.Biol. Chem. 1996, 271:736-741.
    • (1996) J.Biol. Chem. , vol.271 , pp. 736-741
    • Cohen, T.1    Nahari, D.2    Cerem, L.W.3    Neufeld, G.4    Levi, B.Z.5
  • 36
    • 0032499791 scopus 로고    scopus 로고
    • Crystal structure of chemically synthesized [N33A] stromal cell-derived factor 1a, a potent ligand for the HIV-1 "fusin" coreceptor
    • Dealwis C., Fernandez E.J., Thompson D.A., Simon R.J., Siani M.A., Lolis E. Crystal structure of chemically synthesized [N33A] stromal cell-derived factor 1a, a potent ligand for the HIV-1 "fusin" coreceptor. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:6941-6946.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6941-6946
    • Dealwis, C.1    Fernandez, E.J.2    Thompson, D.A.3    Simon, R.J.4    Siani, M.A.5    Lolis, E.6
  • 37
    • 1542344006 scopus 로고    scopus 로고
    • Expression, regulation and function of IGF-1, IGF-1R and IGF-1 binding proteins in blood vessels
    • Delafontaine P., Song Y., Li Y. Expression, regulation and function of IGF-1, IGF-1R and IGF-1 binding proteins in blood vessels. Arterioscler. Thromb. Vasc. Biol. 2004, 24:435-444.
    • (2004) Arterioscler. Thromb. Vasc. Biol. , vol.24 , pp. 435-444
    • Delafontaine, P.1    Song, Y.2    Li, Y.3
  • 41
    • 77953440123 scopus 로고    scopus 로고
    • Ahuman monoclonal antibody against insulin-like growth factor-II blocks the growth of human hepatocellular carcinoma cell lines invitro and invivo
    • Dransfield D.T., Cohen E.H., Chang Q. Ahuman monoclonal antibody against insulin-like growth factor-II blocks the growth of human hepatocellular carcinoma cell lines invitro and invivo. Mol. Cancer Ther. 2010, 9:1809-1819.
    • (2010) Mol. Cancer Ther. , vol.9 , pp. 1809-1819
    • Dransfield, D.T.1    Cohen, E.H.2    Chang, Q.3
  • 42
    • 65249122512 scopus 로고    scopus 로고
    • Novel therapeutic inhibitors of the c-Met signaling pathway in cancer
    • Eder J.P., VandeWoude G.F., Boerner S.A., LoRusso P.M. Novel therapeutic inhibitors of the c-Met signaling pathway in cancer. Clin. Cancer Res. 2009, 15:2207-2213.
    • (2009) Clin. Cancer Res. , vol.15 , pp. 2207-2213
    • Eder, J.P.1    VandeWoude, G.F.2    Boerner, S.A.3    LoRusso, P.M.4
  • 43
    • 77957241701 scopus 로고    scopus 로고
    • Dynamics of endothelial cell behavior in sprouting angiogenesis
    • Eilken H.M., Adams R.H. Dynamics of endothelial cell behavior in sprouting angiogenesis. Curr. Opin. Cell. Biol. 2010, 22:617-625.
    • (2010) Curr. Opin. Cell. Biol. , vol.22 , pp. 617-625
    • Eilken, H.M.1    Adams, R.H.2
  • 46
    • 5044236157 scopus 로고    scopus 로고
    • Epidermal growth factor receptor in tumor angiogenesis
    • Ellis L. Epidermal growth factor receptor in tumor angiogenesis. Hematol. Oncol. Clin. North. Am. 2004, 18:1007-1021.
    • (2004) Hematol. Oncol. Clin. North. Am. , vol.18 , pp. 1007-1021
    • Ellis, L.1
  • 47
    • 33745063095 scopus 로고    scopus 로고
    • The role of neuropilins in cancer
    • Ellis L.M. The role of neuropilins in cancer. Mol. Cancer Ther. 2006, 5:1099-1107.
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 1099-1107
    • Ellis, L.M.1
  • 48
    • 84894218473 scopus 로고    scopus 로고
    • Stromal cell-derived factor-1 stimulates cell recruitment, vascularization and osteogenic differentiation
    • Eman R.M., Oner F.C., Kruyt M., Dhert W., Alblas J. Stromal cell-derived factor-1 stimulates cell recruitment, vascularization and osteogenic differentiation. Tissue Eng. A 2013, 10.1089/ten.TEA.2012.0653.
    • (2013) Tissue Eng. A
    • Eman, R.M.1    Oner, F.C.2    Kruyt, M.3    Dhert, W.4    Alblas, J.5
  • 49
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. 2004, 60:2126-2132.
    • (2004) Acta Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 50
    • 0026787356 scopus 로고
    • Critical functional requirement for the guanidinium group of the arginine 41 side chain of human epidermal growth factor as revealed by mutagenic inactivation and chemical reactivation
    • Engler D.A., Campion S.R., Hauser M.R., Cook J.S., Niyogi S.K. Critical functional requirement for the guanidinium group of the arginine 41 side chain of human epidermal growth factor as revealed by mutagenic inactivation and chemical reactivation. J.Biol. Chem. 1992, 267:2274-2281.
    • (1992) J.Biol. Chem. , vol.267 , pp. 2274-2281
    • Engler, D.A.1    Campion, S.R.2    Hauser, M.R.3    Cook, J.S.4    Niyogi, S.K.5
  • 52
    • 8144225469 scopus 로고    scopus 로고
    • The CXCL12-CXCR4 chemotactic pathway as a target of adjuvant breast cancer therapies
    • Epstein R.J. The CXCL12-CXCR4 chemotactic pathway as a target of adjuvant breast cancer therapies. Nat. Rev. Cancer 2004, 4:901-909.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 901-909
    • Epstein, R.J.1
  • 55
    • 0037291769 scopus 로고    scopus 로고
    • EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization
    • Ferguson K.M., Berger M.B., Mendrola J.M., Cho H.S., Leahy D.J., Lemmon M.A. EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Mol. Cell 2003, 11:507-517.
    • (2003) Mol. Cell , vol.11 , pp. 507-517
    • Ferguson, K.M.1    Berger, M.B.2    Mendrola, J.M.3    Cho, H.S.4    Leahy, D.J.5    Lemmon, M.A.6
  • 57
    • 62149102642 scopus 로고    scopus 로고
    • Transforming growth factor-beta 1 (TGFbeta1) induces angiogenesis through vascular endothelial growth factor (VEGF)-mediated apoptosis
    • Ferrari G., Cook B.D., Terushkin V., Pintucci G., Mignatti P. Transforming growth factor-beta 1 (TGFbeta1) induces angiogenesis through vascular endothelial growth factor (VEGF)-mediated apoptosis. J.Cell. Physiol. 2009, 219:449-458.
    • (2009) J.Cell. Physiol. , vol.219 , pp. 449-458
    • Ferrari, G.1    Cook, B.D.2    Terushkin, V.3    Pintucci, G.4    Mignatti, P.5
  • 58
    • 0028232539 scopus 로고
    • Amonoclonal antibody to human angiogenin. Inhibition of ribonucleolytic and angiogenic activities and localization of the antigenic epitope
    • Fett J.W., Olson K.A., Rybak S.M. Amonoclonal antibody to human angiogenin. Inhibition of ribonucleolytic and angiogenic activities and localization of the antigenic epitope. Biochemistry 1994, 33:5421-5427.
    • (1994) Biochemistry , vol.33 , pp. 5421-5427
    • Fett, J.W.1    Olson, K.A.2    Rybak, S.M.3
  • 59
    • 0037449763 scopus 로고    scopus 로고
    • Angiopoietin-1 and angiopoietin-2 share the same binding domains in the Tie-2 receptor involving the first Ig-like loop and the epidermal growth factor-like repeats
    • Fiedler U., Krissl T., Koidl S., Weiss C., Koblizek T., Deutsch U., Martiny-Baron G., Marme D., Augustin H.G. Angiopoietin-1 and angiopoietin-2 share the same binding domains in the Tie-2 receptor involving the first Ig-like loop and the epidermal growth factor-like repeats. J.Biol. Chem. 2003, 278:1721-1727.
    • (2003) J.Biol. Chem. , vol.278 , pp. 1721-1727
    • Fiedler, U.1    Krissl, T.2    Koidl, S.3    Weiss, C.4    Koblizek, T.5    Deutsch, U.6    Martiny-Baron, G.7    Marme, D.8    Augustin, H.G.9
  • 60
    • 0026806781 scopus 로고
    • Analysis of human/mouse interleukin-6 hybrid proteins: both amino and carboxy termini of human interleukin-6 are required for invitro receptor binding
    • Fiorillo M.T., Cabibbo A., Iacopetti P., Fattori E., Ciliberto G. Analysis of human/mouse interleukin-6 hybrid proteins: both amino and carboxy termini of human interleukin-6 are required for invitro receptor binding. Eur. J. Immunol. 1992, 22:2609-2615.
    • (1992) Eur. J. Immunol. , vol.22 , pp. 2609-2615
    • Fiorillo, M.T.1    Cabibbo, A.2    Iacopetti, P.3    Fattori, E.4    Ciliberto, G.5
  • 64
    • 0034282885 scopus 로고    scopus 로고
    • The interaction of neuropilin-1 with vascular endothelial growth factor and its receptor flt-1
    • Fuh G., Garcia K.C., de Vos A.M. The interaction of neuropilin-1 with vascular endothelial growth factor and its receptor flt-1. J.Biol. Chem. 2000, 275:26690-26695.
    • (2000) J.Biol. Chem. , vol.275 , pp. 26690-26695
    • Fuh, G.1    Garcia, K.C.2    de Vos, A.M.3
  • 65
    • 0032080310 scopus 로고    scopus 로고
    • Requirements for binding and signaling of the kinase domain receptor for vascular endothelial growth factor
    • Fuh G., Li B., Crowley C., Cunningham B., Wells J.A. Requirements for binding and signaling of the kinase domain receptor for vascular endothelial growth factor. J.Biol. Chem. 1998, 273:11197-11204.
    • (1998) J.Biol. Chem. , vol.273 , pp. 11197-11204
    • Fuh, G.1    Li, B.2    Crowley, C.3    Cunningham, B.4    Wells, J.A.5
  • 66
    • 81155131029 scopus 로고    scopus 로고
    • Evaluation of selected flavonoids as antiangiogenic, anticancer, and radical scavenging agents: an experimental and in silico analysis
    • Gacche R.N., Shegokar H.D., Gond S.D., Yang Z., Jadhav A.D. Evaluation of selected flavonoids as antiangiogenic, anticancer, and radical scavenging agents: an experimental and in silico analysis. Cell. Biochem. Biophys. 2011, 61:651-663.
    • (2011) Cell. Biochem. Biophys. , vol.61 , pp. 651-663
    • Gacche, R.N.1    Shegokar, H.D.2    Gond, S.D.3    Yang, Z.4    Jadhav, A.D.5
  • 67
    • 73749086240 scopus 로고    scopus 로고
    • Effect of hydroxyl substitution of flavone on angiogenesis and free radical scavenging activities: a structure-activity relationship studies using computational tools
    • Gacche R.N., Shegokar H.D., Gond S.D., Jadhav A.D., Ghole V. Effect of hydroxyl substitution of flavone on angiogenesis and free radical scavenging activities: a structure-activity relationship studies using computational tools. Eur. J. Pharm. Sci. 2010, 39:37-44.
    • (2010) Eur. J. Pharm. Sci. , vol.39 , pp. 37-44
    • Gacche, R.N.1    Shegokar, H.D.2    Gond, S.D.3    Jadhav, A.D.4    Ghole, V.5
  • 69
    • 0027450356 scopus 로고
    • Clinical results with recombinant human interleukin-3
    • Ganser A. Clinical results with recombinant human interleukin-3. Cancer Invest 1993, 11:212-218.
    • (1993) Cancer Invest , vol.11 , pp. 212-218
    • Ganser, A.1
  • 71
    • 0008222162 scopus 로고
    • Purification of scatter factor, a fibroblast-derived basic protein that modulates epithelial interactions and movement
    • Gherardi E., Gray J., Stoker M., Perryman M., Furlong R. Purification of scatter factor, a fibroblast-derived basic protein that modulates epithelial interactions and movement. Proc. Natl. Acad. Sci. U. S. A. 1989, 86:5844-5848.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 5844-5848
    • Gherardi, E.1    Gray, J.2    Stoker, M.3    Perryman, M.4    Furlong, R.5
  • 72
    • 0025091556 scopus 로고
    • Asmall v-sis/platelet-derived growth factor (PDGF) B-protein domain in which subtle conformational changes abrogate PDGF receptor interaction and transforming activity
    • Giese N., LaRochelle W.J., May-Siroff M., Robbins K.C., Aaronson S.A. Asmall v-sis/platelet-derived growth factor (PDGF) B-protein domain in which subtle conformational changes abrogate PDGF receptor interaction and transforming activity. Mol. Cell Biol. 1990, 10:5496-5501.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 5496-5501
    • Giese, N.1    LaRochelle, W.J.2    May-Siroff, M.3    Robbins, K.C.4    Aaronson, S.A.5
  • 73
    • 34548843943 scopus 로고    scopus 로고
    • Acomparison of physicochemical property profiles of marketed oral drugs and orally bioavailable anti-cancer protein kinase inhibitors in clinical development
    • Gill A.L., Verdonk M., Boyle R.G., Taylor R. Acomparison of physicochemical property profiles of marketed oral drugs and orally bioavailable anti-cancer protein kinase inhibitors in clinical development. Curr. Top. Med. Chem. 2007, 7:1408-1422.
    • (2007) Curr. Top. Med. Chem. , vol.7 , pp. 1408-1422
    • Gill, A.L.1    Verdonk, M.2    Boyle, R.G.3    Taylor, R.4
  • 74
    • 79960096827 scopus 로고    scopus 로고
    • Normalization of the vasculature for treatment of cancer and other diseases
    • Goel S., Duda D.G., Xu L., Munn L.L., Boucher Y., Fukumura D., Jain R.K. Normalization of the vasculature for treatment of cancer and other diseases. Physiol. Rev. 2011, 91(3):1071-1121.
    • (2011) Physiol. Rev. , vol.91 , Issue.3 , pp. 1071-1121
    • Goel, S.1    Duda, D.G.2    Xu, L.3    Munn, L.L.4    Boucher, Y.5    Fukumura, D.6    Jain, R.K.7
  • 76
    • 0028618937 scopus 로고
    • Structure-function relationships for the EGF/TGF-family of mitogens
    • Groenen L.C., Nice E.C., Burgess A.W. Structure-function relationships for the EGF/TGF-family of mitogens. Growth Factors 1994, 11:235-257.
    • (1994) Growth Factors , vol.11 , pp. 235-257
    • Groenen, L.C.1    Nice, E.C.2    Burgess, A.W.3
  • 77
    • 0037124068 scopus 로고    scopus 로고
    • Characterization of neuropilin- 1 structural features that confer binding to semaphorin 3A and vascular endothelial growth factor 165
    • Gu C., Limberg B.J., Whitaker G.B., Perman B., Leahy D.J., Rosenbaum J.S., Ginty D.D., Kolodkin A.L. Characterization of neuropilin- 1 structural features that confer binding to semaphorin 3A and vascular endothelial growth factor 165. J.Biol. Chem. 2002, 277:18069-18076.
    • (2002) J.Biol. Chem. , vol.277 , pp. 18069-18076
    • Gu, C.1    Limberg, B.J.2    Whitaker, G.B.3    Perman, B.4    Leahy, D.J.5    Rosenbaum, J.S.6    Ginty, D.D.7    Kolodkin, A.L.8
  • 78
    • 73149099387 scopus 로고    scopus 로고
    • Molecular basis for the recognition and cleavages of IGF-II, TGF-alpha, and amylin by human insulin-degrading enzyme
    • Guo Q., Manolopoulou M., Bian Y., Schilling A.B., Tang W.J. Molecular basis for the recognition and cleavages of IGF-II, TGF-alpha, and amylin by human insulin-degrading enzyme. J.Mol. Biol. 2010, 395:430-443.
    • (2010) J.Mol. Biol. , vol.395 , pp. 430-443
    • Guo, Q.1    Manolopoulou, M.2    Bian, Y.3    Schilling, A.B.4    Tang, W.J.5
  • 79
    • 0033928332 scopus 로고    scopus 로고
    • Expression of the hypoxically regulated angiogenic factor adrenomedullin correlates with uterine leiomyoma vascular density
    • Hague S., Zhang L., Oehler M.K., Manek S., MacKenzie I.Z., Bicknell R., Rees M.C. Expression of the hypoxically regulated angiogenic factor adrenomedullin correlates with uterine leiomyoma vascular density. Clin. Cancer Res. 2000, 3:2808-2814.
    • (2000) Clin. Cancer Res. , vol.3 , pp. 2808-2814
    • Hague, S.1    Zhang, L.2    Oehler, M.K.3    Manek, S.4    MacKenzie, I.Z.5    Bicknell, R.6    Rees, M.C.7
  • 80
    • 0038636392 scopus 로고    scopus 로고
    • Stromal cell-derived factor 1, a novel target of estrogen receptor action, mediates the mitogenic effects of estradiol in ovarian and breast cancer cells
    • Hall J.M., Korach K.S. Stromal cell-derived factor 1, a novel target of estrogen receptor action, mediates the mitogenic effects of estradiol in ovarian and breast cancer cells. Mol. Endocrinol. 2003, 17:792-803.
    • (2003) Mol. Endocrinol. , vol.17 , pp. 792-803
    • Hall, J.M.1    Korach, K.S.2
  • 81
    • 0026656238 scopus 로고
    • Importance of asparagine-61 and asparagine-109 to the angiogenic activity of human angiogenin
    • Hallahan T.W., Shapiro R., Strydom D.J., Vallee B.L. Importance of asparagine-61 and asparagine-109 to the angiogenic activity of human angiogenin. Biochemistry 1992, 31:8022-8029.
    • (1992) Biochemistry , vol.31 , pp. 8022-8029
    • Hallahan, T.W.1    Shapiro, R.2    Strydom, D.J.3    Vallee, B.L.4
  • 83
    • 0030576517 scopus 로고    scopus 로고
    • Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis
    • Hanahan D., Folkman J. Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis. Cell 1996, 86:353-364.
    • (1996) Cell , vol.86 , pp. 353-364
    • Hanahan, D.1    Folkman, J.2
  • 84
    • 0028361540 scopus 로고
    • Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains
    • Harpaz Y., Chothia C. Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains. J.Mol. Biol. 1994, 238:528-539.
    • (1994) J.Mol. Biol. , vol.238 , pp. 528-539
    • Harpaz, Y.1    Chothia, C.2
  • 85
    • 0027745824 scopus 로고
    • Aheparin-binding form of placenta growth factor (PlGF-2) is expressed in human umbilical vein endothelial cells and in placenta
    • Hauser S., Weich H.A. Aheparin-binding form of placenta growth factor (PlGF-2) is expressed in human umbilical vein endothelial cells and in placenta. Growth Factors 1993, 9:259-268.
    • (1993) Growth Factors , vol.9 , pp. 259-268
    • Hauser, S.1    Weich, H.A.2
  • 87
    • 26244459598 scopus 로고    scopus 로고
    • FGF-1 and S100A13 possibly contribute to angiogenesis in endometriosis
    • Hayrabedyan S., Kyurkchiev S., Kehayov I. FGF-1 and S100A13 possibly contribute to angiogenesis in endometriosis. J.Reprod. Immunol. 2005, 67:87-101.
    • (2005) J.Reprod. Immunol. , vol.67 , pp. 87-101
    • Hayrabedyan, S.1    Kyurkchiev, S.2    Kehayov, I.3
  • 88
    • 0026005126 scopus 로고
    • Scanning mutagenesis of IL-8 identifies a cluster of residues required for receptor binding
    • Hébert C.A., Vitangcol R.V., Baker J.B. Scanning mutagenesis of IL-8 identifies a cluster of residues required for receptor binding. J.Biol. Chem. 1991, 266:18989-18994.
    • (1991) J.Biol. Chem. , vol.266 , pp. 18989-18994
    • Hébert, C.A.1    Vitangcol, R.V.2    Baker, J.B.3
  • 94
    • 0033016887 scopus 로고    scopus 로고
    • Effect of thiazinotrienomycin B, an ansamycin antibiotic, on the function of epidermal growth factor receptor in human stomach tumor cells
    • Hosokawa N., Yamamoto S., Uehara Y., Hori M., Tsuchiya K.S. Effect of thiazinotrienomycin B, an ansamycin antibiotic, on the function of epidermal growth factor receptor in human stomach tumor cells. J.Antibiot. (Tokyo) 1999, 52:485-490.
    • (1999) J.Antibiot. (Tokyo) , vol.52 , pp. 485-490
    • Hosokawa, N.1    Yamamoto, S.2    Uehara, Y.3    Hori, M.4    Tsuchiya, K.S.5
  • 95
    • 0030975693 scopus 로고    scopus 로고
    • Aputative angiogenin receptor in angiogenin-responsive human endothelial cells
    • Hu G.F., Riordan J.F., Vallee B.L. Aputative angiogenin receptor in angiogenin-responsive human endothelial cells. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:2204-2209.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 2204-2209
    • Hu, G.F.1    Riordan, J.F.2    Vallee, B.L.3
  • 97
    • 0036310021 scopus 로고    scopus 로고
    • Fully humanized neutralizing antibodies to interleukin-8 (ABX-IL8) inhibit angiogenesis, tumor growth, and metastasis of human melanoma
    • Huang S., Mills L., Mian B., Tellez C., McCarty M., Yang X.D., Gudas J.M., Bar-Eli M. Fully humanized neutralizing antibodies to interleukin-8 (ABX-IL8) inhibit angiogenesis, tumor growth, and metastasis of human melanoma. Am. J. Pathol. 2002, 161:125-134.
    • (2002) Am. J. Pathol. , vol.161 , pp. 125-134
    • Huang, S.1    Mills, L.2    Mian, B.3    Tellez, C.4    McCarty, M.5    Yang, X.D.6    Gudas, J.M.7    Bar-Eli, M.8
  • 99
    • 0034508480 scopus 로고    scopus 로고
    • Extracellular matrix tenascin-X in combination with vascular endothelial growth factor B enhances endothelial cell proliferation
    • Ikuta T., Ariga H., Matsumoto K. Extracellular matrix tenascin-X in combination with vascular endothelial growth factor B enhances endothelial cell proliferation. Genes Cells 2000, 5:913-927.
    • (2000) Genes Cells , vol.5 , pp. 913-927
    • Ikuta, T.1    Ariga, H.2    Matsumoto, K.3
  • 102
    • 34447618418 scopus 로고    scopus 로고
    • Drug evaluation: Nilotinib - a novel Bcr-Abl tyrosine kinase inhibitor for the treatment of chronic myelocytic leukemia and beyond
    • Jabbour E., Cortes J., Giles F., O'Brien S., Kantarijan H. Drug evaluation: Nilotinib - a novel Bcr-Abl tyrosine kinase inhibitor for the treatment of chronic myelocytic leukemia and beyond. IDrugs 2007, 10:468-479.
    • (2007) IDrugs , vol.10 , pp. 468-479
    • Jabbour, E.1    Cortes, J.2    Giles, F.3    O'Brien, S.4    Kantarijan, H.5
  • 103
    • 0030986951 scopus 로고    scopus 로고
    • Structural changes in insulin-like growth factor IGF I mutant proteins affecting binding kinetic rates to IGF binding protein 1 and IGF-I receptor
    • Jansson M., Uhlen M., Nilsson B. Structural changes in insulin-like growth factor IGF I mutant proteins affecting binding kinetic rates to IGF binding protein 1 and IGF-I receptor. Biochemistry 1997, 36:4108-4117.
    • (1997) Biochemistry , vol.36 , pp. 4108-4117
    • Jansson, M.1    Uhlen, M.2    Nilsson, B.3
  • 105
    • 0026649742 scopus 로고
    • Fibroblast growth factor receptor tyrosine kinases: molecular analysis and signal transduction
    • Jaye M., Schlessinger J., Dionne C.A. Fibroblast growth factor receptor tyrosine kinases: molecular analysis and signal transduction. Biochim. Biophys. Acta 1992, 1135:185-199.
    • (1992) Biochim. Biophys. Acta , vol.1135 , pp. 185-199
    • Jaye, M.1    Schlessinger, J.2    Dionne, C.A.3
  • 107
    • 0030787469 scopus 로고    scopus 로고
    • Transactivation and inhibitory domains of hypoxia-inducible factor 1alpha. Modulation of transcriptional activity by oxygen tension
    • Jiang B.H., Zheng J.Z., Leung S.W., Roe R., Semenza G.L. Transactivation and inhibitory domains of hypoxia-inducible factor 1alpha. Modulation of transcriptional activity by oxygen tension. J.Biol. Chem. 1997, 272:19253-19260.
    • (1997) J.Biol. Chem. , vol.272 , pp. 19253-19260
    • Jiang, B.H.1    Zheng, J.Z.2    Leung, S.W.3    Roe, R.4    Semenza, G.L.5
  • 108
    • 0027344852 scopus 로고
    • Structural and functional diversity in the FGF receptor multigene family
    • Johnson D.E., Williams L.T. Structural and functional diversity in the FGF receptor multigene family. Adv. Cancer Res. 1993, 60:1-41.
    • (1993) Adv. Cancer Res. , vol.60 , pp. 1-41
    • Johnson, D.E.1    Williams, L.T.2
  • 109
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: structural basis for regulation
    • Johnson L.N., Noble M.E.M., Owen D.J. Active and inactive protein kinases: structural basis for regulation. Cell 1996, 85:149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.M.2    Owen, D.J.3
  • 110
    • 0030026897 scopus 로고    scopus 로고
    • Anovel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGFR-3) and KDR (VEGFR-2) receptor tyrosine kinases
    • Joukov V., Pajusola K., Kaipainen A., Chilov D., Lahtinen I., Kukk E., Saksela O., Kalkkinen N., Alitalo K. Anovel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGFR-3) and KDR (VEGFR-2) receptor tyrosine kinases. EMBO J. 1996, 15:290-298.
    • (1996) EMBO J. , vol.15 , pp. 290-298
    • Joukov, V.1    Pajusola, K.2    Kaipainen, A.3    Chilov, D.4    Lahtinen, I.5    Kukk, E.6    Saksela, O.7    Kalkkinen, N.8    Alitalo, K.9
  • 111
    • 38949167600 scopus 로고    scopus 로고
    • Therapeutic applications of aptamers
    • Kaur G., Roy I. Therapeutic applications of aptamers. Expert Opin. Investig. Drugs 2008, 17:43-60.
    • (2008) Expert Opin. Investig. Drugs , vol.17 , pp. 43-60
    • Kaur, G.1    Roy, I.2
  • 114
    • 0034453098 scopus 로고    scopus 로고
    • The effects of insulin-like growth factors on tumorigenesis and neoplastic growth
    • Khandwala H.M., McCutcheon I.E., Flyvbjerg A., Friend K.E. The effects of insulin-like growth factors on tumorigenesis and neoplastic growth. Endocr. Rev. 2000, 21:215-244.
    • (2000) Endocr. Rev. , vol.21 , pp. 215-244
    • Khandwala, H.M.1    McCutcheon, I.E.2    Flyvbjerg, A.3    Friend, K.E.4
  • 115
    • 0036093854 scopus 로고    scopus 로고
    • Chimeric receptor analyses of the interactions of the ectodomains of ErbB-1 with epidermal growth factor and of those of ErbB-4 with neuregulin
    • Kim J.H., Saito K., Yokoyama S. Chimeric receptor analyses of the interactions of the ectodomains of ErbB-1 with epidermal growth factor and of those of ErbB-4 with neuregulin. Eur. J. Biochem. 2002, 269:2323-2329.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2323-2329
    • Kim, J.H.1    Saito, K.2    Yokoyama, S.3
  • 116
    • 2642529116 scopus 로고    scopus 로고
    • Angiogenic role of adrenomedullin through activation of Akt, mitogenactivated protein kinase, and focal adhesion kinase in endothelial cells
    • Kim W., Moon S.O., Sung M.J., Kim S.H., Lee S., So J.N., Park S.K. Angiogenic role of adrenomedullin through activation of Akt, mitogenactivated protein kinase, and focal adhesion kinase in endothelial cells. FASEB. J. 2003, 17:1937-1939.
    • (2003) FASEB. J. , vol.17 , pp. 1937-1939
    • Kim, W.1    Moon, S.O.2    Sung, M.J.3    Kim, S.H.4    Lee, S.5    So, J.N.6    Park, S.K.7
  • 118
    • 84870545783 scopus 로고    scopus 로고
    • Are epsins a therapeutic target for tumor angiogenesis?
    • Klauber-DeMore N. Are epsins a therapeutic target for tumor angiogenesis?. J.Clin. Invest. 2012, 122(12):4341-4343.
    • (2012) J.Clin. Invest. , vol.122 , Issue.12 , pp. 4341-4343
    • Klauber-DeMore, N.1
  • 122
    • 17644444217 scopus 로고
    • Recognition of an antiparallel beta-sheet structure of human epidermal growth factor by its receptor. Site-directed mutagenesis studies of Ala-30 and Asn-32
    • Koide H., Muto Y., Kasai H., Hoshi K., Takusari H., Kohri K., Takahashi S., Sasaki T., Tsukumo K., Miyake T. Recognition of an antiparallel beta-sheet structure of human epidermal growth factor by its receptor. Site-directed mutagenesis studies of Ala-30 and Asn-32. FEBS. Lett. 1992, 302:39-42.
    • (1992) FEBS. Lett. , vol.302 , pp. 39-42
    • Koide, H.1    Muto, Y.2    Kasai, H.3    Hoshi, K.4    Takusari, H.5    Kohri, K.6    Takahashi, S.7    Sasaki, T.8    Tsukumo, K.9    Miyake, T.10
  • 123
    • 0027337146 scopus 로고
    • Proteolytic processing of the hepatocyte growth factor/scatter factor receptor by furin
    • Komada M., Hatsuzawa K., Shibamoto S., Ito F., Nakayama K., Kitamura N. Proteolytic processing of the hepatocyte growth factor/scatter factor receptor by furin. FEBS. Lett. 1993, 328:25-29.
    • (1993) FEBS. Lett. , vol.328 , pp. 25-29
    • Komada, M.1    Hatsuzawa, K.2    Shibamoto, S.3    Ito, F.4    Nakayama, K.5    Kitamura, N.6
  • 124
    • 3142619403 scopus 로고    scopus 로고
    • The Sema domain of Met is necessary for receptor dimerization and activation
    • Kong B.M., Stamos J., Wickramasinghe D. The Sema domain of Met is necessary for receptor dimerization and activation. Cancer Cell. 2004, 6:75-84.
    • (2004) Cancer Cell. , vol.6 , pp. 75-84
    • Kong, B.M.1    Stamos, J.2    Wickramasinghe, D.3
  • 125
    • 24344465796 scopus 로고    scopus 로고
    • Dose-finding study of the multitargeted tyrosine kinase inhibitor SU6668 in patients with advanced malignancies
    • Kuenen B.C., Giaccone G., Ruijter R., Kok A., Schalkwijk C., Hoekman K., Pinedo H.M. Dose-finding study of the multitargeted tyrosine kinase inhibitor SU6668 in patients with advanced malignancies. Clin. Cancer Res. 2005, 11:6240-6246.
    • (2005) Clin. Cancer Res. , vol.11 , pp. 6240-6246
    • Kuenen, B.C.1    Giaccone, G.2    Ruijter, R.3    Kok, A.4    Schalkwijk, C.5    Hoekman, K.6    Pinedo, H.M.7
  • 126
    • 0034529914 scopus 로고    scopus 로고
    • Suppression of tumor growth through disruption of hypoxia-inducible transcription
    • Kung A.L., Wang S., Klco J.M., Kaelin W.G., Livingston D.M. Suppression of tumor growth through disruption of hypoxia-inducible transcription. Nat. Med. 2000, 6:1335-1340.
    • (2000) Nat. Med. , vol.6 , pp. 1335-1340
    • Kung, A.L.1    Wang, S.2    Klco, J.M.3    Kaelin, W.G.4    Livingston, D.M.5
  • 127
    • 0037097861 scopus 로고    scopus 로고
    • FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
    • Lando D., Peet D.J., Gorman J.J., Whelan D.A., Whitelaw M.L., Bruick R.K. FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes. Dev. 2002, 16:1466-1471.
    • (2002) Genes. Dev. , vol.16 , pp. 1466-1471
    • Lando, D.1    Peet, D.J.2    Gorman, J.J.3    Whelan, D.A.4    Whitelaw, M.L.5    Bruick, R.K.6
  • 128
    • 0025367994 scopus 로고
    • Molecular localization of the transforming and secretory properties of PDGF A and PDGF B
    • LaRochelle W.J., Giese N., May-Siroff M., Robbins K.C., Aaronson S.A. Molecular localization of the transforming and secretory properties of PDGF A and PDGF B. Science 1990, 248:1541-1544.
    • (1990) Science , vol.248 , pp. 1541-1544
    • LaRochelle, W.J.1    Giese, N.2    May-Siroff, M.3    Robbins, K.C.4    Aaronson, S.A.5
  • 129
    • 29144484059 scopus 로고    scopus 로고
    • Combined inhibition of vascular endothelial growth factor (VEGF), fibroblast growth factor and platelet-derived growth factor, but not inhibition of VEGF alone, effectively suppress angiogenesis and vessel maturation in endometriotic lesions
    • Laschke M.W., Elitzsch A., Vollmer B., Vajkoczy P., Menger M.D. Combined inhibition of vascular endothelial growth factor (VEGF), fibroblast growth factor and platelet-derived growth factor, but not inhibition of VEGF alone, effectively suppress angiogenesis and vessel maturation in endometriotic lesions. Hum. Reprod. 2006, 21:262-268.
    • (2006) Hum. Reprod. , vol.21 , pp. 262-268
    • Laschke, M.W.1    Elitzsch, A.2    Vollmer, B.3    Vajkoczy, P.4    Menger, M.D.5
  • 130
  • 131
    • 70349230744 scopus 로고    scopus 로고
    • The interaction between thermodynamic stability and buried free cysteines in regulating the functional half-life of fibroblast growth factor-1
    • Lee J., Blaber M. The interaction between thermodynamic stability and buried free cysteines in regulating the functional half-life of fibroblast growth factor-1. J.Mol. Biol. 2009, 393:113-127.
    • (2009) J.Mol. Biol. , vol.393 , pp. 113-127
    • Lee, J.1    Blaber, M.2
  • 132
    • 0028104202 scopus 로고
    • Regulation of signal transduction and signal diversity by receptor oligomerization
    • Lemmon M.A., Schlessinger J. Regulation of signal transduction and signal diversity by receptor oligomerization. Trends. Biochem. Sci. 1994, 19:459-463.
    • (1994) Trends. Biochem. Sci. , vol.19 , pp. 459-463
    • Lemmon, M.A.1    Schlessinger, J.2
  • 133
    • 0033593472 scopus 로고    scopus 로고
    • Refined crystal structures of native human angiogenin and two active site variants: implications for the unique functional properties of an enzyme involved in neovascularisation during tumour growth
    • Leonidas D.D., Shapiro R., Allen S.C., Subbarao G.V., Veluraja K., Acharya K.R. Refined crystal structures of native human angiogenin and two active site variants: implications for the unique functional properties of an enzyme involved in neovascularisation during tumour growth. J.Mol. Biol. 1999, 285:1209-1233.
    • (1999) J.Mol. Biol. , vol.285 , pp. 1209-1233
    • Leonidas, D.D.1    Shapiro, R.2    Allen, S.C.3    Subbarao, G.V.4    Veluraja, K.5    Acharya, K.R.6
  • 134
    • 0037176894 scopus 로고    scopus 로고
    • Crystallographic studies on the role of the C-terminal segment of human angiogenin in defining enzymatic potency
    • Leonidas D.D., Shapiro R., Subbarao G.V., Russo A., Acharya K.R. Crystallographic studies on the role of the C-terminal segment of human angiogenin in defining enzymatic potency. Biochemistry 2002, 41:2552-2562.
    • (2002) Biochemistry , vol.41 , pp. 2552-2562
    • Leonidas, D.D.1    Shapiro, R.2    Subbarao, G.V.3    Russo, A.4    Acharya, K.R.5
  • 137
    • 0037443760 scopus 로고    scopus 로고
    • IL-8 directly enhanced endothelial cell survival, proliferation, and matrix metalloproteinases production and regulated angiogenesis
    • Li A., Dubey S., Varney M.L., Dave B.J., Singh R.K. IL-8 directly enhanced endothelial cell survival, proliferation, and matrix metalloproteinases production and regulated angiogenesis. J.Immunol. 2003, 170:3369-3376.
    • (2003) J.Immunol. , vol.170 , pp. 3369-3376
    • Li, A.1    Dubey, S.2    Varney, M.L.3    Dave, B.J.4    Singh, R.K.5
  • 138
    • 58249117625 scopus 로고    scopus 로고
    • Low levels of tumor necrosis factor a increase tumor growth by inducing an endothelial phenotype of monocytes recruited to the tumor site
    • Li B., Vincent A., Cates J., Brantley-Sieders D.M., Polk D.B., Young P.P. Low levels of tumor necrosis factor a increase tumor growth by inducing an endothelial phenotype of monocytes recruited to the tumor site. Cancer Res. 2009, 69:338-348.
    • (2009) Cancer Res. , vol.69 , pp. 338-348
    • Li, B.1    Vincent, A.2    Cates, J.3    Brantley-Sieders, D.M.4    Polk, D.B.5    Young, P.P.6
  • 140
    • 33947541141 scopus 로고    scopus 로고
    • Erlotinib effectively inhibits JAK2V617F activity and polycythemia vera cell growth
    • Li Z., Xu M., Xing S., Ho W.T., Ishii T., Li Q., Fu X., Zhao Z.J. Erlotinib effectively inhibits JAK2V617F activity and polycythemia vera cell growth. J.Biol. Chem. 2007, 282:3428-3432.
    • (2007) J.Biol. Chem. , vol.282 , pp. 3428-3432
    • Li, Z.1    Xu, M.2    Xing, S.3    Ho, W.T.4    Ishii, T.5    Li, Q.6    Fu, X.7    Zhao, Z.J.8
  • 141
    • 0035887033 scopus 로고    scopus 로고
    • Crystal structures of NK1-heparin complexes reveal the basis of NK1 activity and enable engineering of potent agonists of the MET receptor
    • Lietha D., Chirgadze D.Y., Mulloy B., Blundell T.L., Gherardi E. Crystal structures of NK1-heparin complexes reveal the basis of NK1 activity and enable engineering of potent agonists of the MET receptor. EMBO J. 2001, 20:5543-5555.
    • (2001) EMBO J. , vol.20 , pp. 5543-5555
    • Lietha, D.1    Chirgadze, D.Y.2    Mulloy, B.3    Blundell, T.L.4    Gherardi, E.5
  • 142
    • 0035968216 scopus 로고    scopus 로고
    • Real, time kinetics of insulin like growth factor II (IGF-II) interaction with the IGF-II/mannose 6-phosphate receptor: the effects of domain 13 and pH
    • Linnell J., Groeger G., Hassan A.B. Real, time kinetics of insulin like growth factor II (IGF-II) interaction with the IGF-II/mannose 6-phosphate receptor: the effects of domain 13 and pH. J.Biol. Chem. 2001, 276:23986-23991.
    • (2001) J.Biol. Chem. , vol.276 , pp. 23986-23991
    • Linnell, J.1    Groeger, G.2    Hassan, A.B.3
  • 143
    • 17844396959 scopus 로고    scopus 로고
    • Interleukin-6 induces transcriptional activation of vascular endothelial growth factor (VEGF) in astrocytes invivo and regulates VEGF promoter activity in glioblastoma cells via direct interaction between STAT3 and Sp1
    • Loeffler S., Fayard B., Weis J., Weissenberger J. Interleukin-6 induces transcriptional activation of vascular endothelial growth factor (VEGF) in astrocytes invivo and regulates VEGF promoter activity in glioblastoma cells via direct interaction between STAT3 and Sp1. Int. J. Cancer 2005, 115:202-213.
    • (2005) Int. J. Cancer , vol.115 , pp. 202-213
    • Loeffler, S.1    Fayard, B.2    Weis, J.3    Weissenberger, J.4
  • 144
    • 0026734672 scopus 로고
    • Structure-function analysis of hepatocyte growth factor: identification of variants that lack mitogenic activity yet retain high affinity receptor binding
    • Lokker N.A., Mark M.R., Luis E.A., Bennett G.L., Robbins K.A., Baker J.B., Godowski P.J. Structure-function analysis of hepatocyte growth factor: identification of variants that lack mitogenic activity yet retain high affinity receptor binding. EMBO J. 1992, 11:2503-2510.
    • (1992) EMBO J. , vol.11 , pp. 2503-2510
    • Lokker, N.A.1    Mark, M.R.2    Luis, E.A.3    Bennett, G.L.4    Robbins, K.A.5    Baker, J.B.6    Godowski, P.J.7
  • 145
    • 0030891853 scopus 로고    scopus 로고
    • Monomeric variants of IL-8: effects of sidechain substitutions and solution conditions upon dimer formation
    • Lowman H.B., Fairbrother W.J., Slagle P.H., Kabakoff R., Liu J., Shire S., Hébert C.A. Monomeric variants of IL-8: effects of sidechain substitutions and solution conditions upon dimer formation. Protein Sci. 1997, 6:598-608.
    • (1997) Protein Sci. , vol.6 , pp. 598-608
    • Lowman, H.B.1    Fairbrother, W.J.2    Slagle, P.H.3    Kabakoff, R.4    Liu, J.5    Shire, S.6    Hébert, C.A.7
  • 146
    • 0032483474 scopus 로고    scopus 로고
    • Solution structure of acidic fibroblast growth factor bound to 1,3, 6-naphthalenetrisulfonate: a minimal model for the anti-tumoral action of suramins and suradistas
    • Lozano R.M., Jiménez M., Santoro J., Rico M., Giménez-Gallego G. Solution structure of acidic fibroblast growth factor bound to 1,3, 6-naphthalenetrisulfonate: a minimal model for the anti-tumoral action of suramins and suradistas. J.Mol. Biol. 1998, 281:899-915.
    • (1998) J.Mol. Biol. , vol.281 , pp. 899-915
    • Lozano, R.M.1    Jiménez, M.2    Santoro, J.3    Rico, M.4    Giménez-Gallego, G.5
  • 147
    • 78649548465 scopus 로고    scopus 로고
    • Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor
    • Lu C., Mi L.Z., Grey M.J., Zhu J., Graef E., Yokoyama S., Timothy A. Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor. Mol. Cell Biol. 2010, 30:5432-5443.
    • (2010) Mol. Cell Biol. , vol.30 , pp. 5432-5443
    • Lu, C.1    Mi, L.Z.2    Grey, M.J.3    Zhu, J.4    Graef, E.5    Yokoyama, S.6    Timothy, A.7
  • 148
    • 0035860766 scopus 로고    scopus 로고
    • Crystal structure of human epidermal growth factor and its dimerization
    • Lu H.S., Chai J.J., Li M., Huang B.R., He C.H., Bi R.C. Crystal structure of human epidermal growth factor and its dimerization. J.Biol. Chem. 2001, 276:34913-34917.
    • (2001) J.Biol. Chem. , vol.276 , pp. 34913-34917
    • Lu, H.S.1    Chai, J.J.2    Li, M.3    Huang, B.R.4    He, C.H.5    Bi, R.C.6
  • 149
    • 33645077056 scopus 로고    scopus 로고
    • NMR conformational analysis of proadrenomedullin N-terminal 20 peptide, a proangiogenic factor involved in tumor growth
    • Lucyk S., Taha H., Yamamoto H., Miskolzie M., Kotovych G. NMR conformational analysis of proadrenomedullin N-terminal 20 peptide, a proangiogenic factor involved in tumor growth. Biopolymers 2006, 81:295-308.
    • (2006) Biopolymers , vol.81 , pp. 295-308
    • Lucyk, S.1    Taha, H.2    Yamamoto, H.3    Miskolzie, M.4    Kotovych, G.5
  • 151
    • 33746868899 scopus 로고    scopus 로고
    • Functions of CXCL12 and CXCR4 in breast cancer
    • Luker K.E., Luker G.D. Functions of CXCL12 and CXCR4 in breast cancer. Cancer Lett. 2006, 238:30-41.
    • (2006) Cancer Lett. , vol.238 , pp. 30-41
    • Luker, K.E.1    Luker, G.D.2
  • 152
    • 6344284887 scopus 로고    scopus 로고
    • The interactions of hepatocyte growth factor/scatter factor and its NK1 and NK2 variants with glycosaminoglycans using a modified gel mobility shift assay
    • Lyon M., Deakin J.A., Lietha D., Gherardi E., Gallagher J.T. The interactions of hepatocyte growth factor/scatter factor and its NK1 and NK2 variants with glycosaminoglycans using a modified gel mobility shift assay. J.Biol. Chem. 2004, 42:43560-43567.
    • (2004) J.Biol. Chem. , vol.42 , pp. 43560-43567
    • Lyon, M.1    Deakin, J.A.2    Lietha, D.3    Gherardi, E.4    Gallagher, J.T.5
  • 155
    • 55049111537 scopus 로고    scopus 로고
    • Design and development of antisense drugs
    • Malik R., Roy I. Design and development of antisense drugs. Expert Opin. Drug Discov. 2008, 3:1189-1207.
    • (2008) Expert Opin. Drug Discov. , vol.3 , pp. 1189-1207
    • Malik, R.1    Roy, I.2
  • 156
    • 0037025311 scopus 로고    scopus 로고
    • Neuropilin-1 binds vascular endothelial growth factor 165, placenta growth factor-2, and heparin via its b1b2 domain
    • Mamluk R., Gechtman Z., Kutcher M.E., Gasiunas N., Gallagher J., Klagsbrun M. Neuropilin-1 binds vascular endothelial growth factor 165, placenta growth factor-2, and heparin via its b1b2 domain. J.Biol. Chem. 2002, 277:24818-24825.
    • (2002) J.Biol. Chem. , vol.277 , pp. 24818-24825
    • Mamluk, R.1    Gechtman, Z.2    Kutcher, M.E.3    Gasiunas, N.4    Gallagher, J.5    Klagsbrun, M.6
  • 159
    • 0021013896 scopus 로고
    • Epidermal growth factor-like transforming growth factor 11. Interaction with epidermal growth factor receptors in human placenta membranes and A431 cells
    • Massague J. Epidermal growth factor-like transforming growth factor 11. Interaction with epidermal growth factor receptors in human placenta membranes and A431 cells. J.Biol. Chem. 1983, 258:13614-13620.
    • (1983) J.Biol. Chem. , vol.258 , pp. 13614-13620
    • Massague, J.1
  • 160
    • 0035479234 scopus 로고    scopus 로고
    • Tumor angiogenesis as a therapeutic target
    • Matter A. Tumor angiogenesis as a therapeutic target. Drug Discov. Today 2001, 6:1005-1024.
    • (2001) Drug Discov. Today , vol.6 , pp. 1005-1024
    • Matter, A.1
  • 161
    • 0033922217 scopus 로고    scopus 로고
    • The pleiotropic effects of fibroblast growth factor receptors in mammalian development
    • McIntosh I., Bellus G.A., Jab E.W. The pleiotropic effects of fibroblast growth factor receptors in mammalian development. Cell. Struct. Funct. 2000, 25:85-96.
    • (2000) Cell. Struct. Funct. , vol.25 , pp. 85-96
    • McIntosh, I.1    Bellus, G.A.2    Jab, E.W.3
  • 163
    • 77952044402 scopus 로고    scopus 로고
    • The heterohexameric complex structure, a component in the non-classical pathway for fibroblast growth factor 1 (FGF1) secretion
    • Mohan S.K., Rani S.G., Yu C. The heterohexameric complex structure, a component in the non-classical pathway for fibroblast growth factor 1 (FGF1) secretion. J.Biol. Chem. 2010, 285:15464-15475.
    • (2010) J.Biol. Chem. , vol.285 , pp. 15464-15475
    • Mohan, S.K.1    Rani, S.G.2    Yu, C.3
  • 164
    • 0027941844 scopus 로고
    • Identification of the nucleolar targeting signal of human angiogenin
    • Moroianu J., Riordan J.F. Identification of the nucleolar targeting signal of human angiogenin. Biochem. Biophys. Res. Commun. 1994, 203:1765-1772.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 1765-1772
    • Moroianu, J.1    Riordan, J.F.2
  • 165
    • 0028262977 scopus 로고
    • Nuclear translocation of angiogenin in proliferating endothelial cells is essential to its angiogenic activity
    • Moroianu J., Riordan J.F. Nuclear translocation of angiogenin in proliferating endothelial cells is essential to its angiogenic activity. Proc. Natl. Acad. Sci. U. S. A. 1994, 91:1677-1681.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 1677-1681
    • Moroianu, J.1    Riordan, J.F.2
  • 166
    • 0032530717 scopus 로고    scopus 로고
    • VEGF and the Fab fragment of a humanized neutralizing antibody: crystal structure of the complex at 2.4 A resolution and mutational analysis of the interface
    • Muller Y.A., Chen Y., Christinger H.W., Li B., Cunningham B.C., Lowman H.B., de Vos A.M. VEGF and the Fab fragment of a humanized neutralizing antibody: crystal structure of the complex at 2.4 A resolution and mutational analysis of the interface. Structure 1998, 6:1153-1167.
    • (1998) Structure , vol.6 , pp. 1153-1167
    • Muller, Y.A.1    Chen, Y.2    Christinger, H.W.3    Li, B.4    Cunningham, B.C.5    Lowman, H.B.6    de Vos, A.M.7
  • 167
    • 0032842680 scopus 로고    scopus 로고
    • CXC chemokine receptor expression on human endothelial cells
    • Murdoch C., Monk P.N., Finn A. CXC chemokine receptor expression on human endothelial cells. Cytokine 1999, 11:704-712.
    • (1999) Cytokine , vol.11 , pp. 704-712
    • Murdoch, C.1    Monk, P.N.2    Finn, A.3
  • 168
    • 77951245615 scopus 로고    scopus 로고
    • Heterologous quaternary structure of CXCL12 and its relationship to the CC chemokine family
    • Murphy J.W., Yuan H., Kong Y., Xiong Y., Lolis E.J. Heterologous quaternary structure of CXCL12 and its relationship to the CC chemokine family. Proteins 2010, 78:1331-1337.
    • (2010) Proteins , vol.78 , pp. 1331-1337
    • Murphy, J.W.1    Yuan, H.2    Kong, Y.3    Xiong, Y.4    Lolis, E.J.5
  • 169
    • 0026691284 scopus 로고
    • Stimulatory effects of insulin and insulin-like growth factor I on migration and tube formation by vascular endothelial cells
    • Nakao-Hayashi J., Ito H., Kanayasu T., Morita I., Murota S. Stimulatory effects of insulin and insulin-like growth factor I on migration and tube formation by vascular endothelial cells. Atherosclerosis 1992, 92:141-149.
    • (1992) Atherosclerosis , vol.92 , pp. 141-149
    • Nakao-Hayashi, J.1    Ito, H.2    Kanayasu, T.3    Morita, I.4    Murota, S.5
  • 170
    • 33644973673 scopus 로고    scopus 로고
    • FGF signaling in skeletal development
    • Naski M.C., Ornitz D.M. FGF signaling in skeletal development. Front. Biosci. 1998, 3:D781-D794.
    • (1998) Front. Biosci. , vol.3
    • Naski, M.C.1    Ornitz, D.M.2
  • 171
    • 33144481305 scopus 로고    scopus 로고
    • Lapatinib: a novel dual tyrosine kinase inhibitor with activity in solid tumors
    • Nelson M.H., Dolder C.R. Lapatinib: a novel dual tyrosine kinase inhibitor with activity in solid tumors. Ann. Pharmacother. 2006, 40:261-269.
    • (2006) Ann. Pharmacother. , vol.40 , pp. 261-269
    • Nelson, M.H.1    Dolder, C.R.2
  • 173
    • 0033841052 scopus 로고    scopus 로고
    • Adrenomedullin is an autocrine regulator of endothelial growth in human endometrium
    • Nikitenko L.L., MacKenzie I.Z., Rees M.C.P., Bicknell R. Adrenomedullin is an autocrine regulator of endothelial growth in human endometrium. Mol. Hum. Reprod. 2000, 6:811-819.
    • (2000) Mol. Hum. Reprod. , vol.6 , pp. 811-819
    • Nikitenko, L.L.1    MacKenzie, I.Z.2    Rees, M.C.P.3    Bicknell, R.4
  • 174
    • 0042203519 scopus 로고    scopus 로고
    • Transcriptional regulation of the CRLR gene in human microvascular endothelial cells by hypoxia
    • Nikitenko L.L., Smith D.M., Bicknell R., Rees M.C.P. Transcriptional regulation of the CRLR gene in human microvascular endothelial cells by hypoxia. FASEB. J. 2003, 17:1499-1501.
    • (2003) FASEB. J. , vol.17 , pp. 1499-1501
    • Nikitenko, L.L.1    Smith, D.M.2    Bicknell, R.3    Rees, M.C.P.4
  • 175
    • 0037171952 scopus 로고    scopus 로고
    • Adrenomedullin promotes formation of xenografted endometrial tumors by stimulation of autocrine growth and angiogenesis
    • Oehler M.K., Hague S., Rees M.C., Bicknell R. Adrenomedullin promotes formation of xenografted endometrial tumors by stimulation of autocrine growth and angiogenesis. Oncogene 2002, 21:2815-2821.
    • (2002) Oncogene , vol.21 , pp. 2815-2821
    • Oehler, M.K.1    Hague, S.2    Rees, M.C.3    Bicknell, R.4
  • 177
    • 0037140086 scopus 로고    scopus 로고
    • Inhibition of prostate carcinoma establishment and metastatic growth in mice by an antiangiogenin monoclonal antibody
    • Olson K.A., Byers H.R., Key M.E., Fett J.W. Inhibition of prostate carcinoma establishment and metastatic growth in mice by an antiangiogenin monoclonal antibody. Int. J. Cancer 2002, 98:923-929.
    • (2002) Int. J. Cancer , vol.98 , pp. 923-929
    • Olson, K.A.1    Byers, H.R.2    Key, M.E.3    Fett, J.W.4
  • 179
    • 18844428327 scopus 로고    scopus 로고
    • Stromal fibroblasts present in invasive human breast carcinomas promote tumor growth and angiogenesis through elevated SDF-1/CXCL12 secretion
    • Orimo A., Gupta P.B., Sgroi D.C., Arenzana-Seisdedos F., Delaunay T., Naeem R., Carey V.J., Richardson A.L., Weinberg R.A. Stromal fibroblasts present in invasive human breast carcinomas promote tumor growth and angiogenesis through elevated SDF-1/CXCL12 secretion. Cell 2005, 121:335-348.
    • (2005) Cell , vol.121 , pp. 335-348
    • Orimo, A.1    Gupta, P.B.2    Sgroi, D.C.3    Arenzana-Seisdedos, F.4    Delaunay, T.5    Naeem, R.6    Carey, V.J.7    Richardson, A.L.8    Weinberg, R.A.9
  • 182
    • 0033999314 scopus 로고    scopus 로고
    • Disassociation of met-mediated biological responses invivo: the natural hepatocyte growth factor/scatter factor splice variant NK2 antagonizes growth but facilitates metastasis
    • Otsuka T., Jakubczak J., Vieira W., Bottaro D.P., Breckenridge D., Larochelle W.J., Merlino G. Disassociation of met-mediated biological responses invivo: the natural hepatocyte growth factor/scatter factor splice variant NK2 antagonizes growth but facilitates metastasis. Mol. Cell Biol. 2000, 20:2055-2065.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 2055-2065
    • Otsuka, T.1    Jakubczak, J.2    Vieira, W.3    Bottaro, D.P.4    Breckenridge, D.5    Larochelle, W.J.6    Merlino, G.7
  • 184
    • 0030811908 scopus 로고    scopus 로고
    • Distinct but overlapping epitopes for the interaction of RANTES with CCR1, CCR3 and CCR5
    • Pakianathan D., Kuta E., Skelton N.J., Artis D.R., Hébert C.A. Distinct but overlapping epitopes for the interaction of RANTES with CCR1, CCR3 and CCR5. Biochemistry 1997, 36:9642-9648.
    • (1997) Biochemistry , vol.36 , pp. 9642-9648
    • Pakianathan, D.1    Kuta, E.2    Skelton, N.J.3    Artis, D.R.4    Hébert, C.A.5
  • 185
    • 0028134936 scopus 로고
    • Placenta growth factor. Potentiation of vascular endothelial growth factor bioactivity, invitro and invivo, and high affinity binding to Flt-1 but not to Flk-1/KDR
    • Park J.E., Chen H.H., Winer J., Houck K.A., Ferrara N. Placenta growth factor. Potentiation of vascular endothelial growth factor bioactivity, invitro and invivo, and high affinity binding to Flt-1 but not to Flk-1/KDR. J.Biol. Chem. 1994, 269:25646-25654.
    • (1994) J.Biol. Chem. , vol.269 , pp. 25646-25654
    • Park, J.E.1    Chen, H.H.2    Winer, J.3    Houck, K.A.4    Ferrara, N.5
  • 186
    • 0034741607 scopus 로고    scopus 로고
    • Angiogenin: involvement in angiogenesis and tumour growth
    • Pavlov N., Badet J. Angiogenin: involvement in angiogenesis and tumour growth. Bull Cancer 2001, 88:725-732.
    • (2001) Bull Cancer , vol.88 , pp. 725-732
    • Pavlov, N.1    Badet, J.2
  • 189
    • 0030598354 scopus 로고    scopus 로고
    • Three-dimensional structure of acidic fibroblast growth factor in solution: effects of binding to a heparin functional analog
    • Pineda-Lucena A., Jiménez M.A., Lozano R.M., Nieto J.L., Santoro J., Rico M., Giménez-Gallego G. Three-dimensional structure of acidic fibroblast growth factor in solution: effects of binding to a heparin functional analog. J.Mol. Biol. 1996, 264:162-178.
    • (1996) J.Mol. Biol. , vol.264 , pp. 162-178
    • Pineda-Lucena, A.1    Jiménez, M.A.2    Lozano, R.M.3    Nieto, J.L.4    Santoro, J.5    Rico, M.6    Giménez-Gallego, G.7
  • 191
    • 0036266044 scopus 로고    scopus 로고
    • International Union of Pharmacology. XXXII. The mammalian calcitonin gene-related peptides, adrenomedullin, amylin, and calcitonin receptors
    • Poyner D.R., Sexton P.M., Marshall I., Smith D.M., Quirion R., Born W., Muff R., Fischer J.A., Foord S.M. International Union of Pharmacology. XXXII. The mammalian calcitonin gene-related peptides, adrenomedullin, amylin, and calcitonin receptors. Pharmacol. Rev. 2002, 54:233-246.
    • (2002) Pharmacol. Rev. , vol.54 , pp. 233-246
    • Poyner, D.R.1    Sexton, P.M.2    Marshall, I.3    Smith, D.M.4    Quirion, R.5    Born, W.6    Muff, R.7    Fischer, J.A.8    Foord, S.M.9
  • 192
    • 0030937718 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible factor-1, definition of regulatory domains within the alpha subunit
    • Pugh C.W., O'Rourke J.F., Nagao M., Gleadle J.M., Ratcliffe P.J. Activation of hypoxia-inducible factor-1, definition of regulatory domains within the alpha subunit. J.Biol. Chem. 1997, 272:11205-11214.
    • (1997) J.Biol. Chem. , vol.272 , pp. 11205-11214
    • Pugh, C.W.1    O'Rourke, J.F.2    Nagao, M.3    Gleadle, J.M.4    Ratcliffe, P.J.5
  • 193
    • 1842554921 scopus 로고    scopus 로고
    • The multifunctional role of IGF-1 in peripheral nerve regeneration
    • Rabinovsky E. The multifunctional role of IGF-1 in peripheral nerve regeneration. Neurol. Res. 2004, 26:204-210.
    • (2004) Neurol. Res. , vol.26 , pp. 204-210
    • Rabinovsky, E.1
  • 194
    • 0037931815 scopus 로고    scopus 로고
    • Platelet-derived growth factor (PDGF)-C, a PDGF family member with a vascular endothelial growth factor-like structure
    • Reigstad L.J., Sande H.M., Fluge Ø., Bruland O., Muga A., Varhaug J.E., Martinez A., Lillehaug J.R. Platelet-derived growth factor (PDGF)-C, a PDGF family member with a vascular endothelial growth factor-like structure. J.Biol. Chem. 2003, 278:17114-17120.
    • (2003) J.Biol. Chem. , vol.278 , pp. 17114-17120
    • Reigstad, L.J.1    Sande, H.M.2    Fluge, Ø.3    Bruland, O.4    Muga, A.5    Varhaug, J.E.6    Martinez, A.7    Lillehaug, J.R.8
  • 195
    • 77951698149 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1-dependent mechanisms of vascularization and vascular remodelling
    • Rey S., Semenza G.L. Hypoxia-inducible factor-1-dependent mechanisms of vascularization and vascular remodelling. Cardiovasc. Res. 2010, 86:236-242.
    • (2010) Cardiovasc. Res. , vol.86 , pp. 236-242
    • Rey, S.1    Semenza, G.L.2
  • 196
    • 84874613534 scopus 로고    scopus 로고
    • The role of angiogenesis in human non-Hodgkin lymphomas
    • Ribatti D., Nico B., Ranieri G., Specchia G., Vacca A. The role of angiogenesis in human non-Hodgkin lymphomas. Neoplasia 2013, 15(3):231-238.
    • (2013) Neoplasia , vol.15 , Issue.3 , pp. 231-238
    • Ribatti, D.1    Nico, B.2    Ranieri, G.3    Specchia, G.4    Vacca, A.5
  • 198
    • 0028909329 scopus 로고
    • Contribution of the transforming growth factor alpha B-loop beta-sheet to binding and activation of the epidermal growth factor receptor
    • Richter A., Drummond D.R., MacGarvie J., Puddicombe S.M., Chamberlin S.G., Davies D.E. Contribution of the transforming growth factor alpha B-loop beta-sheet to binding and activation of the epidermal growth factor receptor. J.Biol. Chem. 1995, 270:1612-1616.
    • (1995) J.Biol. Chem. , vol.270 , pp. 1612-1616
    • Richter, A.1    Drummond, D.R.2    MacGarvie, J.3    Puddicombe, S.M.4    Chamberlin, S.G.5    Davies, D.E.6
  • 199
    • 33947370773 scopus 로고    scopus 로고
    • Vascular endothelial growth factor (VEGF) signaling in tumor progression
    • Roskoski R. Vascular endothelial growth factor (VEGF) signaling in tumor progression. Crit. Rev. Oncol. Hematol. 2007, 62:179-213.
    • (2007) Crit. Rev. Oncol. Hematol. , vol.62 , pp. 179-213
    • Roskoski, R.1
  • 200
    • 0022457822 scopus 로고
    • The biology of platelet-derived growth factor
    • Ross R., Raines E.W., Bowen-Pope D.F. The biology of platelet-derived growth factor. Cell 1986, 46:155-169.
    • (1986) Cell , vol.46 , pp. 155-169
    • Ross, R.1    Raines, E.W.2    Bowen-Pope, D.F.3
  • 201
    • 80053495098 scopus 로고    scopus 로고
    • Targeting angiogenesis for controlling neuroblastoma
    • Roy Choudhury S., Karmakar S., Banik N.L., Ray S.K. Targeting angiogenesis for controlling neuroblastoma. J.Oncol. 2012, 2012:782020.
    • (2012) J.Oncol. , vol.2012 , pp. 782020
    • Roy Choudhury, S.1    Karmakar, S.2    Banik, N.L.3    Ray, S.K.4
  • 202
    • 0036152493 scopus 로고    scopus 로고
    • The chemopreventive agent oltipraz possesses potent antiangiogenic activity invitro, exvivo, and invivo and inhibits tumor xenograft growth
    • Ruggeri B.A., Robinson C., Angeles T., Wilkinson J., Clapper M.L. The chemopreventive agent oltipraz possesses potent antiangiogenic activity invitro, exvivo, and invivo and inhibits tumor xenograft growth. Clin. Cancer Res. 2002, 8:267-274.
    • (2002) Clin. Cancer Res. , vol.8 , pp. 267-274
    • Ruggeri, B.A.1    Robinson, C.2    Angeles, T.3    Wilkinson, J.4    Clapper, M.L.5
  • 203
    • 34248577928 scopus 로고    scopus 로고
    • Crystal structure of recombinant human stromal cell-derived factor-1a
    • Ryu E.K., Kim T.G., Kwon T.H. Crystal structure of recombinant human stromal cell-derived factor-1a. Proteins 2007, 67:1193-1197.
    • (2007) Proteins , vol.67 , pp. 1193-1197
    • Ryu, E.K.1    Kim, T.G.2    Kwon, T.H.3
  • 205
    • 6344284808 scopus 로고    scopus 로고
    • Heparan sulfate/heparin oligosaccharides protect stromal cell-derived factor-1 (SDF-1)/CXCL12 against proteolysis induced by CD26/dipeptidyl peptidase IV
    • Sadir R., Imberty A., Baleux F., Lortat-Jacob H. Heparan sulfate/heparin oligosaccharides protect stromal cell-derived factor-1 (SDF-1)/CXCL12 against proteolysis induced by CD26/dipeptidyl peptidase IV. J.Biol. Chem. 2004, 279:43854-43860.
    • (2004) J.Biol. Chem. , vol.279 , pp. 43854-43860
    • Sadir, R.1    Imberty, A.2    Baleux, F.3    Lortat-Jacob, H.4
  • 206
    • 0036644713 scopus 로고    scopus 로고
    • Proinflammatory cytokine IL-1 beta promotes tumor growth of Lewis lung carcinoma by induction of angiogenic factors: invivo analysis of tumor-stromal interaction
    • Saijo Y., Tanaka M., Miki M., Usui K., Suzuki T., Maemondo M., Hong X., Tazawa R., Kikuchi T., Matsushima K., Nukiwa T. Proinflammatory cytokine IL-1 beta promotes tumor growth of Lewis lung carcinoma by induction of angiogenic factors: invivo analysis of tumor-stromal interaction. J.Immunol. 2002, 169:469-475.
    • (2002) J.Immunol. , vol.169 , pp. 469-475
    • Saijo, Y.1    Tanaka, M.2    Miki, M.3    Usui, K.4    Suzuki, T.5    Maemondo, M.6    Hong, X.7    Tazawa, R.8    Kikuchi, T.9    Matsushima, K.10    Nukiwa, T.11
  • 207
    • 0027511809 scopus 로고
    • High-resolution three-dimensional structure of ribonuclease A in solution by nuclear magnetic resonance spectroscopy
    • Santoro J., Gonzalez C., Bruix M., Neira J.L., Nieto J.L., Herranz J., Rico M. High-resolution three-dimensional structure of ribonuclease A in solution by nuclear magnetic resonance spectroscopy. J.Mol. Biol. 1993, 229:722-734.
    • (1993) J.Mol. Biol. , vol.229 , pp. 722-734
    • Santoro, J.1    Gonzalez, C.2    Bruix, M.3    Neira, J.L.4    Nieto, J.L.5    Herranz, J.6    Rico, M.7
  • 209
    • 0027157426 scopus 로고
    • Indispensable role of tissue-type plasminogen activator in growth factor-dependent tube formation of human microvascular endothelial cells invitro
    • Sato Y., Okamura K., Morimoto A., Hamanaka R., Hamaguchi K., Shimada T., Ono M., Kohno K., Sakata T., Kuwano M. Indispensable role of tissue-type plasminogen activator in growth factor-dependent tube formation of human microvascular endothelial cells invitro. Exp. Cell. Res. 1993, 204:223-229.
    • (1993) Exp. Cell. Res. , vol.204 , pp. 223-229
    • Sato, Y.1    Okamura, K.2    Morimoto, A.3    Hamanaka, R.4    Hamaguchi, K.5    Shimada, T.6    Ono, M.7    Kohno, K.8    Sakata, T.9    Kuwano, M.10
  • 210
    • 0028825543 scopus 로고
    • Regulation of growth factor activation by proteoglycans: what is the role of the low affinity receptors?
    • Schlessinger J., Lax I., Lemmon M. Regulation of growth factor activation by proteoglycans: what is the role of the low affinity receptors?. Cell 1995, 83:357-360.
    • (1995) Cell , vol.83 , pp. 357-360
    • Schlessinger, J.1    Lax, I.2    Lemmon, M.3
  • 212
    • 0041440927 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 (FGF-2) induces vascular endothelial growth factor (VEGF) expression in the endothelial cells of forming capillaries: an autocrine mechanism contributing to angiogenesis
    • Seghezzi G., Patel S., Ren C.J., Gualandris A., Pintucci G., Robbins E.S., Shapiro R.L., Galloway A.C., Rifkin D.B., Mignatti P. Fibroblast growth factor-2 (FGF-2) induces vascular endothelial growth factor (VEGF) expression in the endothelial cells of forming capillaries: an autocrine mechanism contributing to angiogenesis. J.Cell. Biol. 1998, 141:1659-1673.
    • (1998) J.Cell. Biol. , vol.141 , pp. 1659-1673
    • Seghezzi, G.1    Patel, S.2    Ren, C.J.3    Gualandris, A.4    Pintucci, G.5    Robbins, E.S.6    Shapiro, R.L.7    Galloway, A.C.8    Rifkin, D.B.9    Mignatti, P.10
  • 213
    • 76349095132 scopus 로고    scopus 로고
    • Defining the role of hypoxia-inducible factor 1 in cancer biology and therapeutics
    • Semenza G.L. Defining the role of hypoxia-inducible factor 1 in cancer biology and therapeutics. Oncogene 2010, 29:625-634.
    • (2010) Oncogene , vol.29 , pp. 625-634
    • Semenza, G.L.1
  • 214
    • 0022497178 scopus 로고
    • Characteristic ribonucleolytic activity of human angiogenin
    • Shapiro R., Riordan J.F., Vallee B.L. Characteristic ribonucleolytic activity of human angiogenin. Biochemistry 1986, 25:3527-3532.
    • (1986) Biochemistry , vol.25 , pp. 3527-3532
    • Shapiro, R.1    Riordan, J.F.2    Vallee, B.L.3
  • 216
    • 0024435026 scopus 로고
    • Site-directed mutagenesis of histidine-13 and histidine-1 14 of human angiogenin. Alanine derivatives inhibit angiogenin-induced angiogenesis
    • Shapiro R., Vallee B.L. Site-directed mutagenesis of histidine-13 and histidine-1 14 of human angiogenin. Alanine derivatives inhibit angiogenin-induced angiogenesis. Biochemistry 1989, 28:7401-7408.
    • (1989) Biochemistry , vol.28 , pp. 7401-7408
    • Shapiro, R.1    Vallee, B.L.2
  • 217
    • 77954911810 scopus 로고    scopus 로고
    • Structures of a platelet-derived growth factor/propeptide complex and a platelet-derived growth factor/receptor complex
    • Shima A.H., Liua H., Fociaa P.J., Chena X., Linb P.C., Hea X. Structures of a platelet-derived growth factor/propeptide complex and a platelet-derived growth factor/receptor complex. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:11307-11312.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 11307-11312
    • Shima, A.H.1    Liua, H.2    Fociaa, P.J.3    Chena, X.4    Linb, P.C.5    Hea, X.6
  • 221
    • 0032549799 scopus 로고    scopus 로고
    • Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor
    • Soker S., Takashima S., Miao H.Q., Neufeld G., Klagsbrun M. Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor. Cell 1998, 92:735-745.
    • (1998) Cell , vol.92 , pp. 735-745
    • Soker, S.1    Takashima, S.2    Miao, H.Q.3    Neufeld, G.4    Klagsbrun, M.5
  • 222
    • 0026589835 scopus 로고
    • Angiogenin supports endothelial and fibroblast cell adhesion
    • Soncin F. Angiogenin supports endothelial and fibroblast cell adhesion. Proc. Natl. Acad. Sci. U. S. A. 1992, 89:2232-2236.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 2232-2236
    • Soncin, F.1
  • 226
    • 0027157416 scopus 로고
    • The functional importance of hydrophobicity of the tyrosine at position 13 of human epidermal growth factor in receptor binding
    • Tadaki D.K., Niyogi S.K. The functional importance of hydrophobicity of the tyrosine at position 13 of human epidermal growth factor in receptor binding. J.Biol. Chem. 1993, 268:10114-10119.
    • (1993) J.Biol. Chem. , vol.268 , pp. 10114-10119
    • Tadaki, D.K.1    Niyogi, S.K.2
  • 227
    • 0033025858 scopus 로고    scopus 로고
    • Hepatocyte growth factor is an invasion/migration factor of rat urothelial carcinoma cells invitro
    • Tamatani T., Hattori K., Iyer A., Tamatani K., Oyasu R. Hepatocyte growth factor is an invasion/migration factor of rat urothelial carcinoma cells invitro. Carcinogenesis 1999, 20:957-962.
    • (1999) Carcinogenesis , vol.20 , pp. 957-962
    • Tamatani, T.1    Hattori, K.2    Iyer, A.3    Tamatani, K.4    Oyasu, R.5
  • 228
    • 76749083490 scopus 로고    scopus 로고
    • Lymphangiogenesis: molecular mechanisms and future promise
    • Tammela T., Alitalo K. Lymphangiogenesis: molecular mechanisms and future promise. Cell 2010, 140:460-476.
    • (2010) Cell , vol.140 , pp. 460-476
    • Tammela, T.1    Alitalo, K.2
  • 230
    • 0037431536 scopus 로고    scopus 로고
    • Altered tumor vessel maturation and proliferation in placenta growth factor-producing tumors: potential relationship to post-therapy tumor angiogenesis and recurrence
    • Taylor A.P., Rodriguez M., Adams K., Goldenberg D.M., Blumenthal R.D. Altered tumor vessel maturation and proliferation in placenta growth factor-producing tumors: potential relationship to post-therapy tumor angiogenesis and recurrence. Int. J. Cancer 2003, 105:158-164.
    • (2003) Int. J. Cancer , vol.105 , pp. 158-164
    • Taylor, A.P.1    Rodriguez, M.2    Adams, K.3    Goldenberg, D.M.4    Blumenthal, R.D.5
  • 232
    • 38349077239 scopus 로고    scopus 로고
    • Gas phase reaction of substituted isoquinolines to carboxylic acids in ion trap and triple quadrupole mass spectrometers after electrospray ionization and collision-induced dissociation
    • Thevis M., Kohler M., Schlörer N., Schänzer W. Gas phase reaction of substituted isoquinolines to carboxylic acids in ion trap and triple quadrupole mass spectrometers after electrospray ionization and collision-induced dissociation. J.Am. Soc. Mass. Spectrom. 2008, 19:151-158.
    • (2008) J.Am. Soc. Mass. Spectrom. , vol.19 , pp. 151-158
    • Thevis, M.1    Kohler, M.2    Schlörer, N.3    Schänzer, W.4
  • 234
    • 0028045937 scopus 로고
    • Inhibition of degranulation of polymorphonuclear leukocytes by angiogenin and its tryptic fragment
    • Tschesche H., Kopp C., Horl W.H., Hempelmann U. Inhibition of degranulation of polymorphonuclear leukocytes by angiogenin and its tryptic fragment. J.Biol. Chem. 1994, 269:30274-30280.
    • (1994) J.Biol. Chem. , vol.269 , pp. 30274-30280
    • Tschesche, H.1    Kopp, C.2    Horl, W.H.3    Hempelmann, U.4
  • 235
    • 0029814271 scopus 로고    scopus 로고
    • Ahierarchical network of interreceptor interactions determines signal transduction by neu differentiation factor/neuregulin and epidermal growth factor
    • Tzahar E., Waterman H., Chen X., Levkowitz G., Karunagaran D., Lavi S., Ratzkin B.J., Yarden Y.A. Ahierarchical network of interreceptor interactions determines signal transduction by neu differentiation factor/neuregulin and epidermal growth factor. Mol. Cell Biol. 1996, 16:5276-5287.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 5276-5287
    • Tzahar, E.1    Waterman, H.2    Chen, X.3    Levkowitz, G.4    Karunagaran, D.5    Lavi, S.6    Ratzkin, B.J.7    Yarden, Y.A.8
  • 236
    • 0030900908 scopus 로고    scopus 로고
    • Insertion of Argos sequences into the B-loop of epidermal growth factor results in a low-affinity ligand with strong agonistic activity
    • Van de Poll M.L., Van Vugt M.J., Lenferink A.E., Van Zoelen E.J. Insertion of Argos sequences into the B-loop of epidermal growth factor results in a low-affinity ligand with strong agonistic activity. Biochemistry 1997, 36:7425-7431.
    • (1997) Biochemistry , vol.36 , pp. 7425-7431
    • Van de Poll, M.L.1    Van Vugt, M.J.2    Lenferink, A.E.3    Van Zoelen, E.J.4
  • 240
  • 241
    • 33745173829 scopus 로고    scopus 로고
    • Recognition of a CXCR4 sulfotyrosine by the chemokine stromal cell-derived factor-1[alpha] (SDF-1[alpha]/CXCL12)
    • Veldkamp C.T., Seibert C., Peterson F.C., Sakmar T.P., Volkman B.F. Recognition of a CXCR4 sulfotyrosine by the chemokine stromal cell-derived factor-1[alpha] (SDF-1[alpha]/CXCL12). J.Mol. Biol. 2006, 359:1400-1409.
    • (2006) J.Mol. Biol. , vol.359 , pp. 1400-1409
    • Veldkamp, C.T.1    Seibert, C.2    Peterson, F.C.3    Sakmar, T.P.4    Volkman, B.F.5
  • 242
    • 0030998098 scopus 로고    scopus 로고
    • Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta
    • Vigers G.P., Anderson L.J., Caffes P., Brandhuber B.J. Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta. Nature 1997, 386:190-194.
    • (1997) Nature , vol.386 , pp. 190-194
    • Vigers, G.P.1    Anderson, L.J.2    Caffes, P.3    Brandhuber, B.J.4
  • 244
    • 0029060529 scopus 로고
    • Insulin and epidermal growth factor receptors contain the cysteine repeat motif found in the tumor necrosis factor receptor
    • Ward C.W., Hoyne P.A., Flegg R.H. Insulin and epidermal growth factor receptors contain the cysteine repeat motif found in the tumor necrosis factor receptor. Proteins 1995, 22:141-153.
    • (1995) Proteins , vol.22 , pp. 141-153
    • Ward, C.W.1    Hoyne, P.A.2    Flegg, R.H.3
  • 245
    • 0037435011 scopus 로고    scopus 로고
    • Interleukin-6 promotes cervical tumor growth by VEGF dependent angiogenesis via a STAT3 pathway
    • Wei L.H., Kuo M.L., Chen C.A., Chou C.H., Lai K.B., Lee C.N., Hsieh C.Y. Interleukin-6 promotes cervical tumor growth by VEGF dependent angiogenesis via a STAT3 pathway. Oncogene 2003, 22:1517-1527.
    • (2003) Oncogene , vol.22 , pp. 1517-1527
    • Wei, L.H.1    Kuo, M.L.2    Chen, C.A.3    Chou, C.H.4    Lai, K.B.5    Lee, C.N.6    Hsieh, C.Y.7
  • 247
    • 70450274968 scopus 로고    scopus 로고
    • High resolution NMR-based model for the structure of a scFv-IL-1beta complex potential for NMR as a key tool in therapeutic antibody design and development
    • Wilkinson I.C., Hall C.J., Veverka V., Shi J.Y., Muskett F.W., Stephens P.E., Taylor R.J., Henry A.J., Carr M.D. High resolution NMR-based model for the structure of a scFv-IL-1beta complex potential for NMR as a key tool in therapeutic antibody design and development. J.Biol. Chem. 2009, 284:31928-31935.
    • (2009) J.Biol. Chem. , vol.284 , pp. 31928-31935
    • Wilkinson, I.C.1    Hall, C.J.2    Veverka, V.3    Shi, J.Y.4    Muskett, F.W.5    Stephens, P.E.6    Taylor, R.J.7    Henry, A.J.8    Carr, M.D.9
  • 249
    • 0141996267 scopus 로고    scopus 로고
    • Structural analysis of an epidermal growth factor/transforming growth factor-alpha chimera with unique ErbB binding specificity
    • Wingens M., Walma T., van Ingen H., Stortelers C., van Leeuwen J.E., van Zoelen E.J., Vuister G.W. Structural analysis of an epidermal growth factor/transforming growth factor-alpha chimera with unique ErbB binding specificity. J.Biol. Chem. 2003, 278:39114-39123.
    • (2003) J.Biol. Chem. , vol.278 , pp. 39114-39123
    • Wingens, M.1    Walma, T.2    van Ingen, H.3    Stortelers, C.4    van Leeuwen, J.E.5    van Zoelen, E.J.6    Vuister, G.W.7
  • 250
    • 0032541165 scopus 로고    scopus 로고
    • Chemotactic properties of angiopoietin-1 and -2, ligands for the endothelial-specific receptor tyrosine kinase Tie2
    • Witzenbichler B., Maisonpierre P.C., Jones P., Yancopoulos G.D., Isner J.M. Chemotactic properties of angiopoietin-1 and -2, ligands for the endothelial-specific receptor tyrosine kinase Tie2. J.Biol. Chem. 1998, 273:18514-18521.
    • (1998) J.Biol. Chem. , vol.273 , pp. 18514-18521
    • Witzenbichler, B.1    Maisonpierre, P.C.2    Jones, P.3    Yancopoulos, G.D.4    Isner, J.M.5
  • 251
    • 0024291642 scopus 로고
    • Structure of phosphate-free ribonuclease A refined at 1.26 A
    • Wlodawer A., Svensson L.A., Sjolin L., Gilliland G.L. Structure of phosphate-free ribonuclease A refined at 1.26 A. Biochemistry 1988, 27:2705-2717.
    • (1988) Biochemistry , vol.27 , pp. 2705-2717
    • Wlodawer, A.1    Svensson, L.A.2    Sjolin, L.3    Gilliland, G.L.4
  • 253
    • 45349097237 scopus 로고    scopus 로고
    • Panitumumab: human monoclonal antibody against epidermal growth factor receptors for the treatment of metastatic colorectal cancer
    • Wu M., Rivkin A., Pham T. Panitumumab: human monoclonal antibody against epidermal growth factor receptors for the treatment of metastatic colorectal cancer. Clin. Ther. 2008, 30:14-30.
    • (2008) Clin. Ther. , vol.30 , pp. 14-30
    • Wu, M.1    Rivkin, A.2    Pham, T.3
  • 257
    • 0032556955 scopus 로고    scopus 로고
    • PCR display identifies tamoxifen induction of the novel angiogenic factor adrenomedullin by a non estrogenic mechanism in the human endometrium
    • Zhao Y., Hague S., Manek S., Zhang L., Bicknell R., Rees M.C.P. PCR display identifies tamoxifen induction of the novel angiogenic factor adrenomedullin by a non estrogenic mechanism in the human endometrium. Oncogene 1998, 16:409-415.
    • (1998) Oncogene , vol.16 , pp. 409-415
    • Zhao, Y.1    Hague, S.2    Manek, S.3    Zhang, L.4    Bicknell, R.5    Rees, M.C.P.6
  • 259
    • 0031026055 scopus 로고    scopus 로고
    • Potent and selective inhibitors of the Abl-kinase: phenylamino-pyrimidine (PAP) derivatives
    • Zimmermann J., Buchdunger E., Mett H., Meyer T., Lydon N.B. Potent and selective inhibitors of the Abl-kinase: phenylamino-pyrimidine (PAP) derivatives. Bioorg. Med. Chem. Lett. 1997, 7:187-192.
    • (1997) Bioorg. Med. Chem. Lett. , vol.7 , pp. 187-192
    • Zimmermann, J.1    Buchdunger, E.2    Mett, H.3    Meyer, T.4    Lydon, N.B.5
  • 260
    • 0029951570 scopus 로고    scopus 로고
    • Phenylamino-pyrimidine (PAP) derivatives: a new class of potent and highly selective PDGF-receptor autophosphorylation inhibitors
    • Zimmermann J., Caravatti G., Mett H., Meyer T., Müller M., Lydon N.B., Fabbro D. Phenylamino-pyrimidine (PAP) derivatives: a new class of potent and highly selective PDGF-receptor autophosphorylation inhibitors. Med. Chem. Let 1996, 6:1221-1226.
    • (1996) Med. Chem. Let , vol.6 , pp. 1221-1226
    • Zimmermann, J.1    Caravatti, G.2    Mett, H.3    Meyer, T.4    Müller, M.5    Lydon, N.B.6    Fabbro, D.7


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