메뉴 건너뛰기




Volumn 383, Issue 4, 2009, Pages 386-391

Structural and functional characterization of soluble endoglin receptor

Author keywords

Endoglin; Reporter assay; Small angle X ray scattering; TGF

Indexed keywords

DIMER; ENDOGLIN; HUMAN GROWTH HORMONE; LUCIFERASE; MEMBRANE RECEPTOR; OLIGOMER; TETRAMER; TRANSFORMING GROWTH FACTOR BETA RECEPTOR 1; TRANSFORMING GROWTH FACTOR BETA RECEPTOR 2; TRANSFORMING GROWTH FACTOR BETA1;

EID: 65549108692     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.02.162     Document Type: Article
Times cited : (16)

References (26)
  • 1
    • 0025222517 scopus 로고
    • The transforming growth factor β family
    • Massagué J. The transforming growth factor β family. Annu. Rev. Cell Biol. 6 (1990) 597-641
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 597-641
    • Massagué, J.1
  • 2
    • 0031685620 scopus 로고    scopus 로고
    • TGF-β signal transduction
    • Massagué J. TGF-β signal transduction. Annu. Rev. Biochem. 67 (1998) 753-791
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 753-791
    • Massagué, J.1
  • 3
    • 0034104591 scopus 로고    scopus 로고
    • Smads as transcriptional co-modulators
    • Attisano L., and Wrana J.L. Smads as transcriptional co-modulators. Curr. Opin. Cell Biol. 12 (2000) 235-243
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 235-243
    • Attisano, L.1    Wrana, J.L.2
  • 4
    • 0026646785 scopus 로고
    • Endoglin is a component of the transforming growth factor β receptor system in human endothelial cells
    • Cheifetz S., Bellon T., Cales C., Vera S., Bernabeu C., Massagué J., and Letarte M. Endoglin is a component of the transforming growth factor β receptor system in human endothelial cells. J. Biol. Chem. 267 (1992) 19027-19030
    • (1992) J. Biol. Chem. , vol.267 , pp. 19027-19030
    • Cheifetz, S.1    Bellon, T.2    Cales, C.3    Vera, S.4    Bernabeu, C.5    Massagué, J.6    Letarte, M.7
  • 5
    • 21644452716 scopus 로고    scopus 로고
    • Interaction and functional interplay between endoglin and ALK-1, two components of the endothelial transforming growth factor-β receptor complex
    • Blanco F.J., Santibanez J.F., Guerrero-esteo M., Langa C., Vary C.P., and Bernabeu C. Interaction and functional interplay between endoglin and ALK-1, two components of the endothelial transforming growth factor-β receptor complex. J. Cell Physiol. 204 (2005) 574-584
    • (2005) J. Cell Physiol. , vol.204 , pp. 574-584
    • Blanco, F.J.1    Santibanez, J.F.2    Guerrero-esteo, M.3    Langa, C.4    Vary, C.P.5    Bernabeu, C.6
  • 7
    • 0028171579 scopus 로고
    • Endoglin, a TGF-β binding protein of endothelial cells, is the gene for hereditary haemorrhagic telangiectasia type 1
    • McAllister K.A., et al. Endoglin, a TGF-β binding protein of endothelial cells, is the gene for hereditary haemorrhagic telangiectasia type 1. Nat. Genet. 8 (1994) 345-351
    • (1994) Nat. Genet. , vol.8 , pp. 345-351
    • McAllister, K.A.1
  • 10
    • 0034648765 scopus 로고    scopus 로고
    • Angiogenesis in cancer and other diseases
    • Carmeliet P., and Jain R.K. Angiogenesis in cancer and other diseases. Nature 407 (2000) 249-257
    • (2000) Nature , vol.407 , pp. 249-257
    • Carmeliet, P.1    Jain, R.K.2
  • 11
    • 0242708765 scopus 로고    scopus 로고
    • Endoglin (CD105): a powerful therapeutic target on tumor-associated angiogenetic blood vessels
    • Fonsatti E., Altomonte M., Nicotra M.R., Natali P.G., and Maio M. Endoglin (CD105): a powerful therapeutic target on tumor-associated angiogenetic blood vessels. Oncogene 22 (2003) 6557-6563
    • (2003) Oncogene , vol.22 , pp. 6557-6563
    • Fonsatti, E.1    Altomonte, M.2    Nicotra, M.R.3    Natali, P.G.4    Maio, M.5
  • 13
    • 85080845781 scopus 로고    scopus 로고
    • Structural model of human endoglin, a transmembrane receptor responsible for hereditary hemorrhagic telangiectasia
    • Llorca O., Trujillo A., Blanco F.J., and Bernabeu C. Structural model of human endoglin, a transmembrane receptor responsible for hereditary hemorrhagic telangiectasia. J. Mol. Biol. 365 (2006) 4726-4739
    • (2006) J. Mol. Biol. , vol.365 , pp. 4726-4739
    • Llorca, O.1    Trujillo, A.2    Blanco, F.J.3    Bernabeu, C.4
  • 14
    • 0033662957 scopus 로고    scopus 로고
    • A mammalian expression vector for expression and purification of secreted proteins for structural studies
    • Leahy D.J., Dann C.E., Longo P., Perman B., and Ramyar K.X. A mammalian expression vector for expression and purification of secreted proteins for structural studies. Protein Expr. Purif. 20 (2000) 500-506
    • (2000) Protein Expr. Purif. , vol.20 , pp. 500-506
    • Leahy, D.J.1    Dann, C.E.2    Longo, P.3    Perman, B.4    Ramyar, K.X.5
  • 16
    • 34248347847 scopus 로고    scopus 로고
    • Upgrade of the small-angle X-ray scattering beamline X33 at the European Molecular Biology Laboratory, Hamburg
    • Roessle M.W., Klaering R., Ristau U., Robrahn B., Jahn D., Gehrmann T., et al. Upgrade of the small-angle X-ray scattering beamline X33 at the European Molecular Biology Laboratory, Hamburg. J. Appl. Crystallogr. 40 (2007) s190-s194
    • (2007) J. Appl. Crystallogr. , vol.40
    • Roessle, M.W.1    Klaering, R.2    Ristau, U.3    Robrahn, B.4    Jahn, D.5    Gehrmann, T.6
  • 18
    • 0001498978 scopus 로고
    • La diffraction des rayons X aux tres petits angles; application a l'etude de phenomenes ultramicroscopiques
    • Guinier A. La diffraction des rayons X aux tres petits angles; application a l'etude de phenomenes ultramicroscopiques. Ann. Phys. (Paris) 12 (1939) 161-237
    • (1939) Ann. Phys. (Paris) , vol.12 , pp. 161-237
    • Guinier, A.1
  • 19
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun D.I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25 (1992) 495-503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 20
    • 0002720864 scopus 로고
    • General theory
    • Glatter O., and Kratky O. (Eds), Academic Press, London
    • Porod G. General theory. In: Glatter O., and Kratky O. (Eds). Small-angle X-ray Scattering (1982), Academic Press, London 17-51
    • (1982) Small-angle X-ray Scattering , pp. 17-51
    • Porod, G.1
  • 21
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun D.I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76 (1999) 2879-2886
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 22
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small angle scattering
    • Volkov V.V., and Svergun D.I. Uniqueness of ab initio shape determination in small angle scattering. J. Appl. Crystallogr. 36 (2003) 860-864
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 23
    • 0029185933 scopus 로고
    • CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D.I., Barberato C., and Koch M.H.J. CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28 (1995) 768-773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 24
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov M.V., and Svergun D.I. Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys. J. 89 (2005) 1237-1250
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 25
    • 0037047426 scopus 로고    scopus 로고
    • Extracellular and cytoplasmic domains of endoglin interact with the transforming growth factor-β receptors I and II
    • Guerrero-Esteo M., Sanchez-Elsner T., Letamendia A., and Bernabeu C. Extracellular and cytoplasmic domains of endoglin interact with the transforming growth factor-β receptors I and II. J. Biol. Chem. 277 (2002) 29197-29209
    • (2002) J. Biol. Chem. , vol.277 , pp. 29197-29209
    • Guerrero-Esteo, M.1    Sanchez-Elsner, T.2    Letamendia, A.3    Bernabeu, C.4
  • 26
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin M.B., and Svergun D.I. Automated matching of high- and low-resolution structural models. J. Appl. Crystallogr. 34 (2001) 33-41
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.