메뉴 건너뛰기




Volumn 1840, Issue 1, 2014, Pages 454-463

The impact of the receptor binding profiles of the vascular endothelial growth factors on their angiogenic features

Author keywords

Angiogenesis; Neuropilin; Receptor activation; Vascular endothelial growth factor

Indexed keywords

NEUROPILIN; VASCULOTROPIN; VASCULOTROPIN RECEPTOR 2;

EID: 84886053524     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2013.10.005     Document Type: Article
Times cited : (25)

References (75)
  • 1
    • 0021111648 scopus 로고
    • Tumor cells secrete a vascular permeability factor that promotes accumulation of ascites fluid
    • D.R. Senger, S.J. Galli, A.M. Dvorak, C.A. Perruzzi, V.S. Harvey, and H.F. Dvorak Tumor cells secrete a vascular permeability factor that promotes accumulation of ascites fluid Science 219 1983 983 985
    • (1983) Science , vol.219 , pp. 983-985
    • Senger, D.R.1    Galli, S.J.2    Dvorak, A.M.3    Perruzzi, C.A.4    Harvey, V.S.5    Dvorak, H.F.6
  • 2
    • 0024818355 scopus 로고
    • Vascular endothelial growth factor is a secreted angiogenic mitogen
    • D.W. Leung, G. Cachianes, W.J. Kuang, D.V. Goeddel, and N. Ferrara Vascular endothelial growth factor is a secreted angiogenic mitogen Science 246 1989 1306 1309 (Pubitemid 20066716)
    • (1989) Science , vol.246 , Issue.4935 , pp. 1306-1309
    • Leung, D.W.1    Cachianes, G.2    Kuang, W.-J.3    Goeddel, D.V.4    Ferrara, N.5
  • 3
    • 12344274486 scopus 로고    scopus 로고
    • The biology of vascular endothelial growth factors
    • DOI 10.1016/j.cardiores.2004.12.002, PII S0008636304005498
    • T. Tammela, B. Enholm, K. Alitalo, and K. Paavonen The biology of vascular endothelial growth factors Cardiovasc. Res. 65 2005 550 563 (Pubitemid 40138976)
    • (2005) Cardiovascular Research , vol.65 , Issue.3 , pp. 550-563
    • Tammela, T.1    Enholm, B.2    Alitalo, K.3    Paavonen, K.4
  • 4
    • 0027979253 scopus 로고
    • Homologs of vascular endothelial growth factor are encoded by the poxvirus orf virus
    • D.J. Lyttle, K.M. Fraser, S.B. Fleming, A.A. Mercer, and A.J. Robinson Homologs of vascular endothelial growth factor are encoded by the poxvirus orf virus J. Virol. 68 1994 84 92
    • (1994) J. Virol. , vol.68 , pp. 84-92
    • Lyttle, D.J.1    Fraser, K.M.2    Fleming, S.B.3    Mercer, A.A.4    Robinson, A.J.5
  • 5
    • 65649109754 scopus 로고    scopus 로고
    • Snake venom vascular endothelial growth factors (VEGF-Fs) exclusively vary their structures and functions among species
    • Y. Yamazaki, Y. Matsunaga, Y. Tokunaga, S. Obayashi, M. Saito, and T. Morita Snake venom vascular endothelial growth factors (VEGF-Fs) exclusively vary their structures and functions among species J. Biol. Chem. 284 2009 9885 9891
    • (2009) J. Biol. Chem. , vol.284 , pp. 9885-9891
    • Yamazaki, Y.1    Matsunaga, Y.2    Tokunaga, Y.3    Obayashi, S.4    Saito, M.5    Morita, T.6
  • 7
    • 33847421319 scopus 로고    scopus 로고
    • Vascular endothelial growth factors. Biology and current status of clinical applications in cardiovascular medicine
    • DOI 10.1016/j.jacc.2006.09.053, PII S0735109706031147
    • S. Yla-Herttuala, T.T. Rissanen, I. Vajanto, and J. Hartikainen Vascular endothelial growth factors: biology and current status of clinical applications in cardiovascular medicine J. Am. Coll. Cardiol. 49 2007 1015 1026 (Pubitemid 46349500)
    • (2007) Journal of the American College of Cardiology , vol.49 , Issue.10 , pp. 1015-1026
    • Yla-Herttuala, S.1    Rissanen, T.T.2    Vajanto, I.3    Hartikainen, J.4
  • 9
    • 33344474964 scopus 로고    scopus 로고
    • Signal transduction by VEGF receptors in regulation of angiogenesis and lymphangiogenesis
    • DOI 10.1016/j.yexcr.2005.11.012, PII S0014482705005215
    • M. Shibuya, and L. Claesson-Welsh Signal transduction by VEGF receptors in regulation of angiogenesis and lymphangiogenesis Exp. Cell Res. 312 2006 549 560 (Pubitemid 43290332)
    • (2006) Experimental Cell Research , vol.312 , Issue.5 , pp. 549-560
    • Shibuya, M.1    Claesson-Welsh, L.2
  • 10
    • 79957902010 scopus 로고    scopus 로고
    • Signal transduction by vascular endothelial growth factor receptors
    • S. Koch, S. Tugues, X. Li, L. Gualandi, and L. Claesson-Welsh Signal transduction by vascular endothelial growth factor receptors Biochem. J. 437 2011 169 183
    • (2011) Biochem. J. , vol.437 , pp. 169-183
    • Koch, S.1    Tugues, S.2    Li, X.3    Gualandi, L.4    Claesson-Welsh, L.5
  • 11
    • 0028170578 scopus 로고
    • Biological activity and phosphorylation sites of the bacterially expressed cytosolic domain of the KDR VEGF-receptor
    • M. Dougher-Vermazen, J.D. Hulmes, P. Bohlen, and B.I. Terman Biological activity and phosphorylation sites of the bacterially expressed cytosolic domain of the KDR VEGF-receptor Biochem. Biophys. Res. Commun. 205 1994 728 738
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 728-738
    • Dougher-Vermazen, M.1    Hulmes, J.D.2    Bohlen, P.3    Terman, B.I.4
  • 13
    • 0032515047 scopus 로고    scopus 로고
    • Vascular endothelial growth factor regulates endothelial cell survival through the phosphatidylinositol 3'-kinase/Akt signal transduction pathway: Requirement for Flk-1/KDR activation
    • DOI 10.1074/jbc.273.46.30336
    • H.P. Gerber, A. McMurtrey, J. Kowalski, M. Yan, B.A. Keyt, V. Dixit, and N. Ferrara Vascular endothelial growth factor regulates endothelial cell survival through the phosphatidylinositol 3′-kinase/Akt signal transduction pathway. Requirement for Flk-1/KDR activation J. Biol. Chem. 273 1998 30336 30343 (Pubitemid 28545503)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.46 , pp. 30336-30343
    • Gerber, H.-P.1    McMurtrey, A.2    Kowalski, J.3    Yan, M.4    Keyt, B.A.5    Dixit, V.6    Ferrara, N.7
  • 14
    • 0033542476 scopus 로고    scopus 로고
    • Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation
    • S. Dimmeler, I. Fleming, B. Fisslthaler, C. Hermann, R. Busse, and A.M. Zeiher Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation Nature 399 1999 601 605
    • (1999) Nature , vol.399 , pp. 601-605
    • Dimmeler, S.1    Fleming, I.2    Fisslthaler, B.3    Hermann, C.4    Busse, R.5    Zeiher, A.M.6
  • 16
    • 0035355472 scopus 로고    scopus 로고
    • A single autophosphorylation site on KDR/Flk-1 is essential for VEGF-A-dependent activation of PLC-γ and DNA synthesis in vascular endothelial cells
    • DOI 10.1093/emboj/20.11.2768
    • T. Takahashi, S. Yamaguchi, K. Chida, and M. Shibuya A single autophosphorylation site on KDR/Flk-1 is essential for VEGF-A-dependent activation of PLC-gamma and DNA synthesis in vascular endothelial cells EMBO J. 20 2001 2768 2778 (Pubitemid 32938560)
    • (2001) EMBO Journal , vol.20 , Issue.11 , pp. 2768-2778
    • Takahashi, T.1    Yamaguchi, S.2    Chida, K.3    Shibuya, M.4
  • 17
    • 33847050140 scopus 로고    scopus 로고
    • Src kinase phosphorylates vascular endothelial-cadherin in response to vascular endothelial growth factor: Identification of tyrosine 685 as the unique target site
    • Y. Wallez, F. Cand, F. Cruzalegui, C. Wernstedt, S. Souchelnytskyi, I. Vilgrain, and P. Huber Src kinase phosphorylates vascular endothelial-cadherin in response to vascular endothelial growth factor: identification of tyrosine 685 as the unique target site Oncogene 26 2007 1067 1077
    • (2007) Oncogene , vol.26 , pp. 1067-1077
    • Wallez, Y.1    Cand, F.2    Cruzalegui, F.3    Wernstedt, C.4    Souchelnytskyi, S.5    Vilgrain, I.6    Huber, P.7
  • 19
    • 0029021660 scopus 로고
    • Role of the Flt-1 receptor tyrosine kinase in regulating the assembly of vascular endothelium
    • G.H. Fong, J. Rossant, M. Gertsenstein, and M.L. Breitman Role of the Flt-1 receptor tyrosine kinase in regulating the assembly of vascular endothelium Nature 376 1995 66 70
    • (1995) Nature , vol.376 , pp. 66-70
    • Fong, G.H.1    Rossant, J.2    Gertsenstein, M.3    Breitman, M.L.4
  • 24
    • 0142023866 scopus 로고    scopus 로고
    • Regional angiogenesis with vascular endothelial growth factor in peripheral arterial disease: A phase II randomized, double-blind, controlled study of adenoviral delivery of vascular endothelial growth factor 121 in patients with disabling intermittent claudication
    • DOI 10.1161/01.CIR.0000093398.16124.29
    • S. Rajagopalan, E.R. Mohler III, R.J. Lederman, F.O. Mendelsohn, J.F. Saucedo, C.K. Goldman, J. Blebea, J. Macko, P.D. Kessler, H.S. Rasmussen, and B.H. Annex Regional angiogenesis with vascular endothelial growth factor in peripheral arterial disease: a phase II randomized, double-blind, controlled study of adenoviral delivery of vascular endothelial growth factor 121 in patients with disabling intermittent claudication Circulation 108 2003 1933 1938 (Pubitemid 37296537)
    • (2003) Circulation , vol.108 , Issue.16 , pp. 1933-1938
    • Rajagopalan, S.1    Mohler III, E.R.2    Lederman, R.J.3    Mendelsohn, F.O.4    Saucedo, J.F.5    Goldman, C.K.6    Blebea, J.7    Macko, J.8    Kessler, P.D.9    Rasmussen, H.S.10    Annex, B.H.11
  • 26
    • 0028134936 scopus 로고
    • Placenta growth factor. Potentiation of vascular endothelial growth factor bioactivity, in vitro and in vivo, and high affinity binding to Flt-1 but not to Flk-1/KDR
    • J.E. Park, H.H. Chen, J. Winer, K.A. Houck, and N. Ferrara Placenta growth factor. Potentiation of vascular endothelial growth factor bioactivity, in vitro and in vivo, and high affinity binding to Flt-1 but not to Flk-1/KDR J. Biol. Chem. 269 1994 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
  • 28
    • 33846660840 scopus 로고    scopus 로고
    • Vascular permeability induced by VEGF family members in vivo: Role of endogenous PAF and NO synthesis
    • DOI 10.1002/jcb.21124
    • A. Brkovic, and M.G. Sirois Vascular permeability induced by VEGF family members in vivo: role of endogenous PAF and NO synthesis J. Cell. Biochem. 100 2007 727 737 (Pubitemid 46187709)
    • (2007) Journal of Cellular Biochemistry , vol.100 , Issue.3 , pp. 727-737
    • Brkovic, A.1    Sirois, M.G.2
  • 29
    • 0035793623 scopus 로고    scopus 로고
    • Analysis of biological effects and signaling properties of Flt-1 (VEGFR-1) and KDR (VEGFR-2). A reassessment using novel receptor-specific vascular endothelial growth factor mutants
    • H. Gille, J. Kowalski, B. Li, J. LeCouter, B. Moffat, T.F. Zioncheck, N. Pelletier, and N. Ferrara Analysis of biological effects and signaling properties of Flt-1 (VEGFR-1) and KDR (VEGFR-2). A reassessment using novel receptor-specific vascular endothelial growth factor mutants J. Biol. Chem. 276 2001 3222 3230
    • (2001) J. Biol. Chem. , vol.276 , pp. 3222-3230
    • Gille, H.1    Kowalski, J.2    Li, B.3    Lecouter, J.4    Moffat, B.5    Zioncheck, T.F.6    Pelletier, N.7    Ferrara, N.8
  • 30
    • 0032549572 scopus 로고    scopus 로고
    • A recombinant mutant vascular endothelial growth factor-C that has lost vascular endothelial growth factor receptor-2 binding, activation, and vascular permeability activities
    • DOI 10.1074/jbc.273.12.6599
    • V. Joukov, V. Kumar, T. Sorsa, E. Arighi, H. Weich, O. Saksela, and K. Alitalo A recombinant mutant vascular endothelial growth factor-C that has lost vascular endothelial growth factor receptor-2 binding, activation, and vascular permeability activities J. Biol. Chem. 273 1998 6599 6602 (Pubitemid 28160314)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.12 , pp. 6599-6602
    • Joukov, V.1    Kumar, V.2    Sorsa, T.3    Arighi, E.4    Weich, H.5    Saksela, O.6    Alitalo, K.7
  • 31
    • 0033520916 scopus 로고    scopus 로고
    • A mutant form of vascular endothelial growth factor (VEGF) that lacks VEGF receptor-2 activation retains the ability to induce vascular permeability
    • S.A. Stacker, A. Vitali, C. Caesar, T. Domagala, L.C. Groenen, E. Nice, M.G. Achen, and A.F. Wilks A mutant form of vascular endothelial growth factor (VEGF) that lacks VEGF receptor-2 activation retains the ability to induce vascular permeability J. Biol. Chem. 274 1999 34884 34892 (Pubitemid 129509535)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.49 , pp. 34884-34892
    • Stacker, S.A.1    Vitali, A.2    Caesar, C.3    Domagala, T.4    Groenen, L.C.5    Nice, E.6    Achen, M.G.7    Wilks, A.F.8
  • 32
    • 8544262237 scopus 로고    scopus 로고
    • A novel snake venom vascular endothelial growth factor (VEGF) predominantly induces vascular permeability through preferential signaling via VEGF receptor-1
    • DOI 10.1074/jbc.M403687200
    • H. Takahashi, S. Hattori, A. Iwamatsu, H. Takizawa, and M. Shibuya A novel snake venom vascular endothelial growth factor (VEGF) predominantly induces vascular permeability through preferential signaling via VEGF receptor-1 J. Biol. Chem. 279 2004 46304 46314 (Pubitemid 39491626)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.44 , pp. 46304-46314
    • Takahashi, H.1    Hattori, S.2    Iwamatsu, A.3    Takizawa, H.4    Shibuya, M.5
  • 35
    • 33845678052 scopus 로고    scopus 로고
    • C terminus of RGS-GAIP-interacting protein conveys neuropilin-1-mediated signaling during angiogenesis
    • L. Wang, D. Mukhopadhyay, and X. Xu C terminus of RGS-GAIP-interacting protein conveys neuropilin-1-mediated signaling during angiogenesis FASEB J. 20 2006 1513 1515
    • (2006) FASEB J. , vol.20 , pp. 1513-1515
    • Wang, L.1    Mukhopadhyay, D.2    Xu, X.3
  • 36
    • 33745441066 scopus 로고    scopus 로고
    • The role of heparan sulphate proteoglycans in angiogenesis
    • DOI 10.1042/BST0340451
    • S.E. Stringer The role of heparan sulphate proteoglycans in angiogenesis Biochem. Soc. Trans. 34 2006 451 453 (Pubitemid 43954009)
    • (2006) Biochemical Society Transactions , vol.34 , Issue.3 , pp. 451-453
    • Stringer, S.E.1
  • 37
    • 75349091269 scopus 로고    scopus 로고
    • Structure-function analysis of VEGF receptor activation and the role of coreceptors in angiogenic signaling
    • F.S. Grunewald, A.E. Prota, A. Giese, and K. Ballmer-Hofer Structure-function analysis of VEGF receptor activation and the role of coreceptors in angiogenic signaling Biochim. Biophys. Acta 1804 2010 567 580
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 567-580
    • Grunewald, F.S.1    Prota, A.E.2    Giese, A.3    Ballmer-Hofer, K.4
  • 39
    • 84859488831 scopus 로고    scopus 로고
    • Structural basis for the selective vascular endothelial growth factor-A (VEGF-A) binding to neuropilin-1
    • M.W. Parker, P. Xu, X. Li, and C.W. Vander Kooi Structural basis for the selective vascular endothelial growth factor-A (VEGF-A) binding to neuropilin-1 J. Biol. Chem. 287 2012 11082 11089
    • (2012) J. Biol. Chem. , vol.287 , pp. 11082-11089
    • Parker, M.W.1    Xu, P.2    Li, X.3    Vander Kooi, C.W.4
  • 43
    • 33744951970 scopus 로고    scopus 로고
    • Vascular endothelial growth factor (VEGF)/VEGF-C mosaic molecules reveal specificity determinants and feature novel receptor binding patterns
    • DOI 10.1074/jbc.M511593200
    • M. Jeltsch, T. Karpanen, T. Strandin, K. Aho, H. Lankinen, and K. Alitalo Vascular endothelial growth factor (VEGF)/VEGF-C mosaic molecules reveal specificity determinants and feature novel receptor binding patterns J. Biol. Chem. 281 2006 12187 12195 (Pubitemid 43855483)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.17 , pp. 12187-12195
    • Jeltsch, M.1    Karpanen, T.2    Strandin, T.3    Aho, K.4    Lankinen, H.5    Alitalo, K.6
  • 44
    • 0027997863 scopus 로고
    • Different signal transduction properties of KDR and Flt1, two receptors for vascular endothelial growth factor
    • J. Waltenberger, L. Claesson-Welsh, A. Siegbahn, M. Shibuya, and C.H. Heldin Different signal transduction properties of KDR and Flt1, two receptors for vascular endothelial growth factor J. Biol. Chem. 269 1994 26988 26995 (Pubitemid 24332901)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.43 , pp. 26988-26995
    • Waltenberger, J.1    Claesson-Welsh, L.2    Siegbahn, A.3    Shibuya, M.4    Heldin, C.-H.5
  • 46
    • 0026572345 scopus 로고
    • The fms-like tyrosine kinase, a receptor for vascular endothelial growth factor
    • C. de Vries, J.A. Escobedo, H. Ueno, K. Houck, N. Ferrara, and L.T. Williams The fms-like tyrosine kinase, a receptor for vascular endothelial growth factor Science 255 1992 989 991
    • (1992) Science , vol.255 , pp. 989-991
    • De Vries, C.1    Escobedo, J.A.2    Ueno, H.3    Houck, K.4    Ferrara, N.5    Williams, L.T.6
  • 49
    • 0027064888 scopus 로고
    • Dual regulation of vascular endothelial growth factor bioavailability by genetic and proteolytic mechanisms
    • K.A. Houck, D.W. Leung, A.M. Rowland, J. Winer, and N. Ferrara Dual regulation of vascular endothelial growth factor bioavailability by genetic and proteolytic mechanisms J. Biol. Chem. 267 1992 26031 26037 (Pubitemid 23014012)
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.36 , pp. 26031-26037
    • Houck, K.A.1    Leung, D.W.2    Rowland, A.M.3    Winer, J.4    Ferrara, N.5
  • 51
    • 0037631338 scopus 로고    scopus 로고
    • NZ-7, is essential for the activation of VEGFR-2 signaling
    • DOI 10.1074/jbc.M210931200
    • A. Kiba, N. Yabana, and M. Shibuya A set of loop-1 and -3 structures in the novel vascular endothelial growth factor (VEGF) family member, VEGF-ENZ-7, is essential for the activation of VEGFR-2 signaling J. Biol. Chem. 278 2003 13453 13461 (Pubitemid 36800119)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.15 , pp. 13453-13461
    • Kiba, A.1    Yabana, N.2    Shibuya, M.3
  • 52
    • 0346101800 scopus 로고    scopus 로고
    • Snake Venom Vascular Endothelial Growth Factors (VEGFs) Exhibit Potent Activity through Their Specific Recognition of KDR (VEGF Receptor 2)
    • DOI 10.1074/jbc.C300454200
    • Y. Yamazaki, K. Takani, H. Atoda, and T. Morita Snake venom vascular endothelial growth factors (VEGFs) exhibit potent activity through their specific recognition of KDR (VEGF receptor 2) J. Biol. Chem. 278 2003 51985 51988 (Pubitemid 38035782)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.52 , pp. 51985-51988
    • Yamazaki, Y.1    Takani, K.2    Atoda, H.3    Morita, T.4
  • 57
    • 12544258730 scopus 로고    scopus 로고
    • Crystal structures of novel vascular endothelial growth factors (VEGF) from snake venoms: Insight into selective VEGF binding to kinase insert domain-containing receptor but not to fms-like tyrosine kinase-1
    • K. Suto, Y. Yamazaki, T. Morita, and H. Mizuno Crystal structures of novel vascular endothelial growth factors (VEGF) from snake venoms: insight into selective VEGF binding to kinase insert domain-containing receptor but not to fms-like tyrosine kinase-1 J. Biol. Chem. 280 2005 2126 2131
    • (2005) J. Biol. Chem. , vol.280 , pp. 2126-2131
    • Suto, K.1    Yamazaki, Y.2    Morita, T.3    Mizuno, H.4
  • 61
    • 0034282885 scopus 로고    scopus 로고
    • The interaction of neuropilin-1 with vascular endothelial growth factor and its receptor flt-1
    • G. Fuh, K.C. Garcia, and A.M. de Vos The interaction of neuropilin-1 with vascular endothelial growth factor and its receptor flt-1 J. Biol. Chem. 275 2000 26690 26695
    • (2000) J. Biol. Chem. , vol.275 , pp. 26690-26695
    • Fuh, G.1    Garcia, K.C.2    De Vos, A.M.3
  • 62
    • 79960690759 scopus 로고    scopus 로고
    • Neuropilin-1 promotes VEGFR-2 trafficking through Rab11 vesicles thereby specifying signal output
    • K. Ballmer-Hofer, A.E. Andersson, L.E. Ratcliffe, and P. Berger Neuropilin-1 promotes VEGFR-2 trafficking through Rab11 vesicles thereby specifying signal output Blood 118 2011 816 826
    • (2011) Blood , vol.118 , pp. 816-826
    • Ballmer-Hofer, K.1    Andersson, A.E.2    Ratcliffe, L.E.3    Berger, P.4
  • 63
    • 33746936677 scopus 로고    scopus 로고
    • Intrinsic tyrosine kinase activity is required for vascular endothelial growth factor receptor 2 ubiquitination, sorting and degradation in endothelial cells
    • DOI 10.1111/j.1600-0854.2006.00462.x
    • L.C. Ewan, H.M. Jopling, H. Jia, S. Mittar, A. Bagherzadeh, G.J. Howell, J.H. Walker, I.C. Zachary, and S. Ponnambalam Intrinsic tyrosine kinase activity is required for vascular endothelial growth factor receptor 2 ubiquitination, sorting and degradation in endothelial cells Traffic 7 2006 1270 1282 (Pubitemid 44204001)
    • (2006) Traffic , vol.7 , Issue.9 , pp. 1270-1282
    • Ewan, L.C.1    Jopling, H.M.2    Jia, H.3    Mittar, S.4    Bagherzadeh, A.5    Howell, G.J.6    Walker, J.H.7    Zachary, I.C.8    Ponnambalam, S.9
  • 64
    • 0029103274 scopus 로고
    • Hypoxia regulates vascular endothelial growth factor gene expression in endothelial cells. Identification of a 5′ enhancer
    • Y. Liu, S.R. Cox, T. Morita, and S. Kourembanas Hypoxia regulates vascular endothelial growth factor gene expression in endothelial cells. Identification of a 5′ enhancer Circ. Res. 77 1995 638 643
    • (1995) Circ. Res. , vol.77 , pp. 638-643
    • Liu, Y.1    Cox, S.R.2    Morita, T.3    Kourembanas, S.4
  • 67
    • 0030782410 scopus 로고    scopus 로고
    • Crystal structure at 1.7 A resolution f VEGF in complex with domain 2 of the Fit-1 receptor
    • C. Wiesmann, G. Fuh, H.W. Christinger, C. Eigenbrot, J.A. Wells, and A.M. de Vos Crystal structure at 1.7 A resolution of VEGF in complex with domain 2 of the Flt-1 receptor Cell 91 1997 695 704 (Pubitemid 27513660)
    • (1997) Cell , vol.91 , Issue.5 , pp. 695-704
    • Wiesmann, C.1    Fuh, G.2    Christinger, H.W.3    Eigenbrot, C.4    Wells, J.A.5    De Vos, A.M.6
  • 69
    • 79952255709 scopus 로고    scopus 로고
    • Neuropilin-1 signaling through p130Cas tyrosine phosphorylation is essential for growth factor-dependent migration of glioma and endothelial cells
    • I.M. Evans, M. Yamaji, G. Britton, C. Pellet-Many, C. Lockie, I.C. Zachary, and P. Frankel Neuropilin-1 signaling through p130Cas tyrosine phosphorylation is essential for growth factor-dependent migration of glioma and endothelial cells Mol. Cell. Biol. 31 2011 1174 1185
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 1174-1185
    • Evans, I.M.1    Yamaji, M.2    Britton, G.3    Pellet-Many, C.4    Lockie, C.5    Zachary, I.C.6    Frankel, P.7
  • 70
    • 79961042374 scopus 로고    scopus 로고
    • VEGF binding to NRP1 is essential for VEGF stimulation of endothelial cell migration, complex formation between NRP1 and VEGFR2, and signaling via FAK Tyr407 phosphorylation
    • B. Herzog, C. Pellet-Many, G. Britton, B. Hartzoulakis, and I.C. Zachary VEGF binding to NRP1 is essential for VEGF stimulation of endothelial cell migration, complex formation between NRP1 and VEGFR2, and signaling via FAK Tyr407 phosphorylation Mol. Biol. Cell 22 2011 2766 2776
    • (2011) Mol. Biol. Cell , vol.22 , pp. 2766-2776
    • Herzog, B.1    Pellet-Many, C.2    Britton, G.3    Hartzoulakis, B.4    Zachary, I.C.5
  • 71
    • 0029920944 scopus 로고    scopus 로고
    • Identification of vascular endothelial growth factor determinants for binding KDR and FLT-1 receptors. Generation of receptor-selective VEGF variants by site-directed mutagenesis
    • B.A. Keyt, H.V. Nguyen, L.T. Berleau, C.M. Duarte, J. Park, H. Chen, and N. Ferrara Identification of vascular endothelial growth factor determinants for binding KDR and FLT-1 receptors. Generation of receptor-selective VEGF variants by site-directed mutagenesis J. Biol. Chem. 271 1996 5638 5646
    • (1996) J. Biol. Chem. , vol.271 , pp. 5638-5646
    • Keyt, B.A.1    Nguyen, H.V.2    Berleau, L.T.3    Duarte, C.M.4    Park, J.5    Chen, H.6    Ferrara, N.7
  • 72
    • 0032553299 scopus 로고    scopus 로고
    • A novel type of vascular endothelial growth factor, VEGF-E (NZ-7 VEGF), preferentially utilizes KDR/Flk-1 receptor and carries a potent mitotic activity without heparin-binding domain
    • DOI 10.1074/jbc.273.47.31273
    • S. Ogawa, A. Oku, A. Sawano, S. Yamaguchi, Y. Yazaki, and M. Shibuya A novel type of vascular endothelial growth factor, VEGF-E (NZ-7 VEGF), preferentially utilizes KDR/Flk-1 receptor and carries a potent mitotic activity without heparin-binding domain J. Biol. Chem. 273 1998 31273 31282 (Pubitemid 28533143)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.47 , pp. 31273-31282
    • Ogawa, S.1    Oku, A.2    Sawano, A.3    Yamaguchi, S.4    Yazaki, Y.5    Shibuya, M.6
  • 75
    • 0031572858 scopus 로고    scopus 로고
    • The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93 A resolution: Multiple copy flexibility and receptor binding
    • Y.A. Muller, H.W. Christinger, B.A. Keyt, and A.M. de Vos The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93 A resolution: multiple copy flexibility and receptor binding Structure 5 1997 1325 1338 (Pubitemid 27484475)
    • (1997) Structure , vol.5 , Issue.10 , pp. 1325-1338
    • Muller, Y.A.1    Christinger, H.W.2    Keyt, B.A.3    De Vos, A.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.