메뉴 건너뛰기




Volumn 32, Issue 19, 2012, Pages 3802-3813

Targeting extracellular domains D4 and D7 of vascular endothelial growth factor receptor 2 reveals allosteric receptor regulatory sites

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; IMMUNOGLOBULIN D; VASCULOTROPIN RECEPTOR 2;

EID: 84868699474     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.06787-11     Document Type: Article
Times cited : (40)

References (32)
  • 1
    • 24144469768 scopus 로고    scopus 로고
    • MCP-1-stimulated chemotaxis of monocytic and endothelial cells is dependent on activation of different signaling cascades
    • Arefieva TI, Kukhtina NB, Antonova OA, Krasnikova TL. 2005. MCP-1-stimulated chemotaxis of monocytic and endothelial cells is dependent on activation of different signaling cascades. Cytokine 31:439-446.
    • (2005) Cytokine , vol.31 , pp. 439-446
    • Arefieva, T.I.1    Kukhtina, N.B.2    Antonova, O.A.3    Krasnikova, T.L.4
  • 2
    • 33745912405 scopus 로고    scopus 로고
    • A time- and cost-efficient system for high-level protein production in mammalian cells
    • Aricescu AR, Lu W, Jones EY. 2006. A time- and cost-efficient system for high-level protein production in mammalian cells. Acta Crystallogr. D Biol. Crystallogr. 62:1243-1250.
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 1243-1250
    • Aricescu, A.R.1    Lu, W.2    Jones, E.Y.3
  • 3
    • 0030932842 scopus 로고    scopus 로고
    • Mapping of the sites for ligand binding and receptor dimerization at the extracellular domain of the vascular endothelial growth factor receptor FLT-1
    • Barleon B, et al. 1997. Mapping of the sites for ligand binding and receptor dimerization at the extracellular domain of the vascular endothelial growth factor receptor FLT-1. J. Biol. Chem. 272:10382-10388.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10382-10388
    • Barleon, B.1
  • 4
    • 73449122689 scopus 로고    scopus 로고
    • VEGF autoregulates its proliferative and migratory ERK1/2 and p38 cascades by enhancing the expression of DUSP1 and DUSP5 phosphatases in endothelial cells
    • Bellou S, et al. 2009. VEGF autoregulates its proliferative and migratory ERK1/2 and p38 cascades by enhancing the expression of DUSP1 and DUSP5 phosphatases in endothelial cells. Am. J. Physiol. Cell Physiol. 297:C1477-C1489.
    • (2009) Am. J. Physiol. Cell Physiol. , vol.297
    • Bellou, S.1
  • 5
    • 2342624119 scopus 로고    scopus 로고
    • High-affinity binders selected from designed ankyrin repeat protein libraries
    • Binz HK, et al. 2004. High-affinity binders selected from designed ankyrin repeat protein libraries. Nat. Biotechnol. 22:575-582.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 575-582
    • Binz, H.K.1
  • 6
    • 84857466204 scopus 로고    scopus 로고
    • Thermodynamic and structural description of allosterically regulated VEGF receptor 2 dimerization
    • Brozzo MS, et al. 2012. Thermodynamic and structural description of allosterically regulated VEGF receptor 2 dimerization. Blood 119:1781-1788.
    • (2012) Blood , vol.119 , pp. 1781-1788
    • Brozzo, M.S.1
  • 7
    • 75149176738 scopus 로고    scopus 로고
    • Transmembrane domainmediated orientation of receptor monomers in active VEGFR-2 dimers
    • Dell'Era Dosch D, Ballmer-Hofer K. 2010. Transmembrane domainmediated orientation of receptor monomers in active VEGFR-2 dimers. FASEB J. 24:32-38.
    • (2010) FASEB J , vol.24 , pp. 32-38
    • Dell'Era Dosch, D.1    Ballmer-Hofer, K.2
  • 8
    • 0037465790 scopus 로고    scopus 로고
    • Small GTP-binding protein Rac is an essential mediator of vascular endothelial growth factor-induced endothelial fenestrations and vascular permeability
    • Eriksson A, et al. 2003. Small GTP-binding protein Rac is an essential mediator of vascular endothelial growth factor-induced endothelial fenestrations and vascular permeability. Circulation 107:1532-1538. 8a
    • (2003) Circulation , vol.107 , Issue.1532-1538
    • Eriksson, A.1
  • 9
    • 1842605531 scopus 로고    scopus 로고
    • Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex
    • Franklin MC, et al. 2004. Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex. Cancer Cell 5:317-328.
    • (2004) Cancer Cell , vol.5 , pp. 317-328
    • Franklin, M.C.1
  • 10
    • 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 JA. 1998. Requirements for binding and signaling of the kinase domain receptor for vascular endothelial growth factor. J. Biol. Chem. 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
  • 11
    • 0034947940 scopus 로고    scopus 로고
    • Integration of PCR fragments at any specific site within cloning vectors without the use of restriction enzymes and DNA ligase
    • Geiser M, Cébe R, Drewello D, Schmitz R. 2001. Integration of PCR fragments at any specific site within cloning vectors without the use of restriction enzymes and DNA ligase. Biotechniques 31:88-90, 92.
    • (2001) Biotechniques , vol.31 , Issue.88-90 , pp. 92
    • Geiser, M.1    Cébe, R.2    Drewello, D.3    Schmitz, R.4
  • 12
    • 0017710978 scopus 로고
    • Characteristics of a human cell line transformed by DNA from human adenovirus type 5
    • Graham FL, Smiley J, Russell WC, Nairn R. 1977. Characteristics of a human cell line transformed by DNA from human adenovirus type 5. J. Gen. Virol. 36:59-74.
    • (1977) J. Gen. Virol. , vol.36 , pp. 59-74
    • Graham, F.L.1    Smiley, J.2    Russell, W.C.3    Nairn, R.4
  • 13
    • 0023732047 scopus 로고
    • Use of simian virus 40 replication to amplify Epstein-Barr virus shuttle vectors in human cells
    • Heinzel SS, Krysan PJ, Calos MP, DuBridge RB. 1988. Use of simian virus 40 replication to amplify Epstein-Barr virus shuttle vectors in human cells. J. Virol. 62:3738-3746.
    • (1988) J. Virol. , vol.62 , pp. 3738-3746
    • Heinzel, S.S.1    Krysan, P.J.2    Calos, M.P.3    DuBridge, R.B.4
  • 14
    • 79955987184 scopus 로고    scopus 로고
    • An antibody targetted to VEGFR-2 Ig domains 4-7 inhibits VEGFR-2 activation and VEGFR-2 dependent angiogenesis without affecting ligand binding
    • Kendrew J, et al. 2011. An antibody targetted to VEGFR-2 Ig domains 4-7 inhibits VEGFR-2 activation and VEGFR-2 dependent angiogenesis without affecting ligand binding. Mol. Cancer Ther. 10:770-783.
    • (2011) Mol. Cancer Ther. , vol.10 , pp. 770-783
    • Kendrew, J.1
  • 15
    • 80052675879 scopus 로고    scopus 로고
    • Structural analysis of vascular endothelial growth factor receptor-2/ligand complexes by small-angle X-ray solution scattering
    • Kisko K, et al. 2011. Structural analysis of vascular endothelial growth factor receptor-2/ligand complexes by small-angle X-ray solution scattering. FASEB J. 25:2980-2986.
    • (2011) FASEB J , vol.25 , pp. 2980-2986
    • Kisko, K.1
  • 16
    • 79957902010 scopus 로고    scopus 로고
    • Signal transduction by vascular endothelial growth factor receptors
    • Koch S, Tugues S, Li X, Gualandi L, Claesson-Welsh L. 2011. Signal transduction by vascular endothelial growth factor receptors. Biochem. J. 437:169-183.
    • (2011) Biochem. J. , vol.437 , pp. 169-183
    • Koch, S.1    Tugues, S.2    Li, X.3    Gualandi, L.4    Claesson-Welsh, L.5
  • 17
    • 2942716714 scopus 로고    scopus 로고
    • Three-dimensional spheroidal culture of cytotrophoblast cells mimics the phenotype and differentiation of cytotrophoblasts from normal and preeclamptic pregnancies
    • Korff T, Krauss T, Augustin HG. 2004. Three-dimensional spheroidal culture of cytotrophoblast cells mimics the phenotype and differentiation of cytotrophoblasts from normal and preeclamptic pregnancies. Exp. Cell Res. 297:415-423.
    • (2004) Exp. Cell Res. , vol.297 , pp. 415-423
    • Korff, T.1    Krauss, T.2    Augustin, H.G.3
  • 18
    • 77249148863 scopus 로고    scopus 로고
    • Structural determinants of growth factor binding and specificity by VEGF receptor 2
    • Leppänen VM, et al. 2010. Structural determinants of growth factor binding and specificity by VEGF receptor 2. Proc. Natl. Acad. Sci. U. S. A. 107:2425-2430.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 2425-2430
    • Leppänen, V.M.1
  • 19
    • 34347218991 scopus 로고    scopus 로고
    • In vitro scratch assay, a convenient and inexpensive method for analysis of cell migration in vitro
    • Liang CC, Park AY, Guan JL. 2007. In vitro scratch assay: a convenient and inexpensive method for analysis of cell migration in vitro. Nat. Protoc. 2:329-333.
    • (2007) Nat. Protoc. , vol.2 , pp. 329-333
    • Liang, C.C.1    Park, A.Y.2    Guan, J.L.3
  • 20
    • 0034974903 scopus 로고    scopus 로고
    • Differential regulation of sphingosine-1-phosphate- and VEGF-induced endothelial cell chemotaxis Involvement of G(ialpha2)-linked Rho kinase activity
    • Liu F, et al. 2001. Differential regulation of sphingosine-1-phosphate- and VEGF-induced endothelial cell chemotaxis. Involvement of G(ialpha2)-linked Rho kinase activity. Am. J. Respir. Cell Mol. Biol. 24:711-719.
    • (2001) Am. J. Respir. Cell Mol. Biol. , vol.24 , pp. 711-719
    • Liu, F.1
  • 21
    • 20444385832 scopus 로고    scopus 로고
    • Activation of p38 has opposing effects on the proliferation and migration of endothelial cells
    • McMullen ME, Bryant PW, Glembotski CC, Vincent PA, Pumiglia KM. 2005. Activation of p38 has opposing effects on the proliferation and migration of endothelial cells. J. Biol. Chem. 280:20995-21003.
    • (2005) J. Biol. Chem. , vol.280 , pp. 20995-21003
    • McMullen, M.E.1    Bryant, P.W.2    Glembotski, C.C.3    Vincent, P.A.4    Pumiglia, K.M.5
  • 22
    • 0026682934 scopus 로고
    • Coupling and connexin 43 expression in microvascular and large vessel endothelial cells
    • Pepper MS, et al. 1992. Coupling and connexin 43 expression in microvascular and large vessel endothelial cells. Am. J. Physiol. 262:C1246-C1257.
    • (1992) Am. J. Physiol. , vol.262
    • Pepper, M.S.1
  • 25
    • 0032553425 scopus 로고    scopus 로고
    • Mapping of the sites involved in ligand association and dissociation at the extracellular domain of the kinase insert domaincontaining receptor for vascular endothelial growth factor
    • Shinkai A, et al. 1998. Mapping of the sites involved in ligand association and dissociation at the extracellular domain of the kinase insert domaincontaining receptor for vascular endothelial growth factor. J. Biol. Chem. 273:31283-31288.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31283-31288
    • Shinkai, A.1
  • 26
    • 70350780365 scopus 로고    scopus 로고
    • Structure and function of VEGF receptors
    • Stuttfeld E, Ballmer-Hofer K. 2009. Structure and function of VEGF receptors. IUBMB Life 61:915-922.
    • (2009) IUBMB Life , vol.61 , pp. 915-922
    • Stuttfeld, E.1    Ballmer-Hofer, K.2
  • 27
    • 0035877708 scopus 로고    scopus 로고
    • Kinase insert domain receptor (kdr) extracellular immunoglobulin-like domains 4-7 contain structural features that block receptor dimerization and vascular endothelial growth factor-induced signaling
    • Tao Q, Backer MV, Backer JM, Terman BI. 2001. Kinase insert domain receptor (kdr) extracellular immunoglobulin-like domains 4-7 contain structural features that block receptor dimerization and vascular endothelial growth factor-induced signaling. J. Biol. Chem. 276:21916-21923.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21916-21923
    • Tao, Q.1    Backer, M.V.2    Backer, J.M.3    Terman, B.I.4
  • 28
    • 78649992510 scopus 로고    scopus 로고
    • Effective suppression of vascular network formation by combination of antibodies blocking VEGFR ligand binding and receptor dimerization
    • Tvorogov D, et al. 2010. Effective suppression of vascular network formation by combination of antibodies blocking VEGFR ligand binding and receptor dimerization. Cancer Cell 18:630-640.
    • (2010) Cancer Cell , vol.18 , pp. 630-640
    • Tvorogov, D.1
  • 29
    • 76649105135 scopus 로고    scopus 로고
    • Direct contacts between extracellular membrane-proximal domains are required for VEGF receptor activation and cell signaling
    • Yang Y, Xie P, Opatowsky Y, Schlessinger J. 2010. Direct contacts between extracellular membrane-proximal domains are required for VEGF receptor activation and cell signaling. Proc. Natl. Acad. Sci. U. S. A. 107:1906-1911.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 1906-1911
    • Yang, Y.1    Xie, P.2    Opatowsky, Y.3    Schlessinger, J.4
  • 30
    • 45549109855 scopus 로고    scopus 로고
    • Contacts between membrane proximal regions of the PDGF receptor ectodomain are required for receptor activation but not for receptor dimerization
    • Yang Y, Yuzawa S, Schlessinger J. 2008. Contacts between membrane proximal regions of the PDGF receptor ectodomain are required for receptor activation but not for receptor dimerization. Proc. Natl. Acad. Sci. U. S. A. 105:7681-7686.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 7681-7686
    • Yang, Y.1    Yuzawa, S.2    Schlessinger, J.3
  • 31
    • 34447531743 scopus 로고    scopus 로고
    • Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor
    • Yuzawa S, et al. 2007. Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor. Cell 130:323-334.
    • (2007) Cell , vol.130 , pp. 323-334
    • Yuzawa, S.1
  • 32
    • 33847634290 scopus 로고    scopus 로고
    • Ribosome display, selecting and evolving proteins in vitro that specifically bind to a target
    • Zahnd C, Amstutz P, Pluckthun A. 2007. Ribosome display: selecting and evolving proteins in vitro that specifically bind to a target. Nat. Methods 4:269-279.
    • (2007) Nat. Methods , vol.4 , pp. 269-279
    • Zahnd, C.1    Amstutz, P.2    Pluckthun, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.