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Volumn 51, Issue 32, 2012, Pages 6328-6341

Structure of the Alk1 extracellular domain and characterization of its bone morphogenetic protein (BMP) binding properties

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROPERTIES; BONE MORPHOGENETIC PROTEINS; EXTRACELLULAR DOMAINS; HYDROPHOBIC INTERFACE; MUTATIONAL ANALYSIS; N-TERMINALS; SIGNALING PROTEINS; TYPE II;

EID: 84865124878     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300942x     Document Type: Article
Times cited : (31)

References (58)
  • 1
    • 0029737070 scopus 로고    scopus 로고
    • Bone morphogenetic proteins: Multifunctional regulators of vertebrate development
    • Hogan, B. L. (1996) Bone morphogenetic proteins: multifunctional regulators of vertebrate development Genes Dev. 10, 1580-1594 (Pubitemid 26268864)
    • (1996) Genes and Development , vol.10 , Issue.13 , pp. 1580-1594
    • Hogan, B.L.M.1
  • 2
    • 0031685620 scopus 로고    scopus 로고
    • TGF-beta signal transduction
    • Massague, J. (1998) TGF-beta signal transduction Annu. Rev. Biochem. 67, 753-791
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 753-791
    • Massague, J.1
  • 3
    • 21344434155 scopus 로고    scopus 로고
    • BMPs: From bone morphogenetic proteins to body morphogenetic proteins
    • DOI 10.1016/j.cytogfr.2005.04.003, PII S1359610105000547
    • Reddi, A. H. (2005) BMPs: from bone morphogenetic proteins to body morphogenetic proteins Cytokine Growth Factor Rev. 16, 249-250 (Pubitemid 40910314)
    • (2005) Cytokine and Growth Factor Reviews , vol.16 , Issue.3 , pp. 249-250
    • Reddi, A.H.1
  • 4
    • 0028180315 scopus 로고
    • The TGF-beta superfamily: New members, new receptors, and new genetic tests of function in different organisms
    • Kingsley, D. M. (1994) The TGF-beta superfamily: new members, new receptors, and new genetic tests of function in different organisms Genes Dev. 8, 133-146
    • (1994) Genes Dev. , vol.8 , pp. 133-146
    • Kingsley, D.M.1
  • 5
    • 0028173316 scopus 로고
    • TGF-beta-receptor-mediated signaling
    • Derynck, R. (1994) TGF-beta-receptor-mediated signaling Trends Biochem. Sci. 19, 548-553
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 548-553
    • Derynck, R.1
  • 6
    • 0028170226 scopus 로고
    • Mechanism of activation of the TGF-beta receptor
    • DOI 10.1038/370341a0
    • Wrana, J. L., Attisano, L., Wieser, R., Ventura, F., and Massague, J. (1994) Mechanism of activation of the TGF-beta receptor Nature 370, 341-347 (Pubitemid 2110860)
    • (1994) Nature , vol.370 , Issue.6488 , pp. 341-347
    • Wrana, J.L.1    Attisano, L.2    Wieser, R.3    Ventura, F.4    Massague, J.5
  • 7
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF- signaling from cell membrane to the nucleus
    • DOI 10.1016/S0092-8674(03)00432-X
    • Shi, Y. and Massague, J. (2003) Mechanisms of TGF-beta signaling from cell membrane to the nucleus Cell 113, 685-700 (Pubitemid 36724933)
    • (2003) Cell , vol.113 , Issue.6 , pp. 685-700
    • Shi, Y.1    Massague, J.2
  • 8
    • 0034678908 scopus 로고    scopus 로고
    • Transcriptional control by the TGF-/Smad signaling system
    • Massague, J. and Wotton, D. (2000) Transcriptional control by the TGF-beta/Smad signaling system EMBO J. 19, 1745-1754 (Pubitemid 30204386)
    • (2000) EMBO Journal , vol.19 , Issue.8 , pp. 1745-1754
    • Massague, J.1    Wotton, D.2
  • 12
    • 34548595361 scopus 로고    scopus 로고
    • Endoglin is required for hemangioblast and early hematopoietic development
    • DOI 10.1242/dev.002907
    • Perlingeiro, R. C. (2007) Endoglin is required for hemangioblast and early hematopoietic development Development 134, 3041-3048 (Pubitemid 47386915)
    • (2007) Development , vol.134 , Issue.16 , pp. 3041-3048
    • Perlingeiro, R.C.R.1
  • 13
    • 67449146883 scopus 로고    scopus 로고
    • Emerging role of bone morphogenetic proteins in angiogenesis
    • David, L., Feige, J. J., and Bailly, S. (2009) Emerging role of bone morphogenetic proteins in angiogenesis Cytokine Growth Factor Rev. 20, 203-212
    • (2009) Cytokine Growth Factor Rev. , vol.20 , pp. 203-212
    • David, L.1    Feige, J.J.2    Bailly, S.3
  • 14
    • 33847369980 scopus 로고    scopus 로고
    • Identification of BMP9 and BMP10 as functional activators of the orphan activin receptor-like kinase 1 (ALK1) in endothelial cells
    • DOI 10.1182/blood-2006-07-034124
    • David, L., Mallet, C., Mazerbourg, S., Feige, J. J., and Bailly, S. (2007) Identification of BMP9 and BMP10 as functional activators of the orphan activin receptor-like kinase 1 (ALK1) in endothelial cells Blood 109, 1953-1961 (Pubitemid 46348192)
    • (2007) Blood , vol.109 , Issue.5 , pp. 1953-1961
    • David, L.1    Mallet, C.2    Mazerbourg, S.3    Feige, J.-J.4    Bailly, S.5
  • 19
    • 0034043106 scopus 로고    scopus 로고
    • Crystal structure of the BMP-2-BRIA ectodomain complex
    • DOI 10.1038/75903
    • Kirsch, T., Sebald, W., and Dreyer, M. K. (2000) Crystal structure of the BMP-2-BRIA ectodomain complex Nat. Struct. Biol. 7, 492-496 (Pubitemid 30414472)
    • (2000) Nature Structural Biology , vol.7 , Issue.6 , pp. 492-496
    • Kirsch, T.1    Sebald, W.2    Dreyer, M.K.3
  • 20
    • 56249097214 scopus 로고    scopus 로고
    • The solution structure of BMPR-IA reveals a local disorder-to-order transition upon BMP-2 binding
    • Klages, J., Kotzsch, A., Coles, M., Sebald, W., Nickel, J., Muller, T., and Kessler, H. (2008) The solution structure of BMPR-IA reveals a local disorder-to-order transition upon BMP-2 binding Biochemistry 47, 11930-11939
    • (2008) Biochemistry , vol.47 , pp. 11930-11939
    • Klages, J.1    Kotzsch, A.2    Coles, M.3    Sebald, W.4    Nickel, J.5    Muller, T.6    Kessler, H.7
  • 22
    • 0027332995 scopus 로고
    • Cloning of a TGF beta type i receptor that forms a heteromeric complex with the TGF beta type II receptor
    • Franzen, P., ten Dijke, P., Ichijo, H., Yamashita, H., Schulz, P., Heldin, C. H., and Miyazono, K. (1993) Cloning of a TGF beta type I receptor that forms a heteromeric complex with the TGF beta type II receptor Cell 75, 681-692
    • (1993) Cell , vol.75 , pp. 681-692
    • Franzen, P.1    Ten Dijke, P.2    Ichijo, H.3    Yamashita, H.4    Schulz, P.5    Heldin, C.H.6    Miyazono, K.7
  • 23
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3-D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha-carbon and beta-carbon resonances in proteins
    • Wittekind, M. and Mueller, L. (1993) HNCACB, a high-sensitivity 3-D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha-carbon and beta-carbon resonances in proteins J. Magn. Reson. Ser. B 101, 201-205
    • (1993) J. Magn. Reson. Ser. B , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 24
    • 0027569483 scopus 로고
    • Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins
    • Grzesiek, S. and Bax, A. (1993) Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins J. Biomol. NMR 3, 185-204
    • (1993) J. Biomol. NMR , vol.3 , pp. 185-204
    • Grzesiek, S.1    Bax, A.2
  • 25
    • 43949175202 scopus 로고
    • Correlation of backbone amide and aliphatic side-chain resonances in C-13/N-15-enriched proteins by isotropic mixing of C-13 magnetization
    • Grzesiek, S., Anglister, J., and Bax, A. (1993) Correlation of backbone amide and aliphatic side-chain resonances in C-13/N-15-enriched proteins by isotropic mixing of C-13 magnetization J. Magn. Reson. Ser. B 101, 114-119
    • (1993) J. Magn. Reson. Ser. B , vol.101 , pp. 114-119
    • Grzesiek, S.1    Anglister, J.2    Bax, A.3
  • 26
    • 44949291986 scopus 로고
    • 3-Dimensional triple-resonance NMR-spectroscopy of isotopically enriched proteins
    • Kay, L. E., Ikura, M., Tschudin, R., and Bax, A. (1990) 3-Dimensional triple-resonance NMR-spectroscopy of isotopically enriched proteins J. Magn. Reson. 89, 496-514
    • (1990) J. Magn. Reson. , vol.89 , pp. 496-514
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 27
    • 0002848358 scopus 로고
    • A constant-time 3-dimensional triple-resonance pulse scheme to correlate intraresidue H-1(N), N-15, and C-13(') chemical-shifts in N-15-C-13-labeled proteins
    • Clubb, R. T., Thanabal, V., and Wagner, G. (1992) A constant-time 3-dimensional triple-resonance pulse scheme to correlate intraresidue H-1(N), N-15, and C-13(') chemical-shifts in N-15-C-13-labeled proteins J. Magn. Reson. 97, 213-217
    • (1992) J. Magn. Reson. , vol.97 , pp. 213-217
    • Clubb, R.T.1    Thanabal, V.2    Wagner, G.3
  • 29
    • 0024449503 scopus 로고
    • 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease Biochemistry 28, 8972-8979 (Pubitemid 19283459)
    • (1989) Biochemistry , vol.28 , Issue.23 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 30
    • 0036147844 scopus 로고    scopus 로고
    • Rapid structural fluctuations of the free HIV protease flaps in solution: Relationship to crystal structures and comparison with predictions of dynamics calculations
    • DOI 10.1110/ps.33202
    • Freedberg, D. I., Ishima, R., Jacob, J., Wang, Y. X., Kustanovich, I., Louis, J. M., and Torchia, D. A. (2002) Rapid structural fluctuations of the free HIV protease flaps in solution: relationship to crystal structures and comparison with predictions of dynamics calculations Protein Sci. 11, 221-232 (Pubitemid 34075785)
    • (2002) Protein Science , vol.11 , Issue.2 , pp. 221-232
    • Freedberg, D.I.1    Ishima, R.2    Jacob, J.3    Wang, Y.-X.4    Kustanovich, I.5    Louis, J.M.6    Torchia, D.A.7
  • 31
    • 0026748968 scopus 로고
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible Biochemistry 31, 5269-5278
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 32
    • 0025046144 scopus 로고
    • Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins
    • DOI 10.1021/ja00168a070
    • Clore, G. M., Szabo, A., Bax, A., Kay, L. E., Driscoll, P. C., and Gronenborn, A. M. (1990) Deviations from the simple 2-parameter model-free approach to the interpretation of N-15 nulcear magnetic -relaxation of protein J. Am. Chem. Soc. 112, 4989-4991 (Pubitemid 20285925)
    • (1990) Journal of the American Chemical Society , vol.112 , Issue.12 , pp. 4989-4991
    • Clore, G.M.1    Szabo, A.2    Bax, A.3    Kay, L.E.4    Driscoll, P.C.5    Gronenborn, A.M.6
  • 33
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance in macromolecules. 1. Theory and range of validity
    • Lipari, G. and Szabo, A. (1982) Model-free approach to the interpretation of nuclear magnetic resonance in macromolecules. 1. Theory and range of validity J. Am. Chem. Soc. 104, 4546-4559
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 34
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis and experimental results
    • Lipari, G. and Szabo, A. (1982) Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis and experimental results J. Am. Chem. Soc. 104, 4559-4570
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 35
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
    • Mandel, A. M., Akke, M., and Palmer, A. G., (1995) Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme J. Mol. Biol. 246, 144-163
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 36
    • 0038161052 scopus 로고    scopus 로고
    • Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations
    • DOI 10.1016/S0022-2836(03)00670-3
    • Gray, J. J., Moughon, S., Wang, C., Schueler-Furman, O., Kuhlman, B., Rohl, C. A., and Baker, D. (2003) Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations J. Mol. Biol. 331, 281-299 (Pubitemid 36870793)
    • (2003) Journal of Molecular Biology , vol.331 , Issue.1 , pp. 281-299
    • Gray, J.J.1    Moughon, S.2    Wang, C.3    Schueler-Furman, O.4    Kuhlman, B.5    Rohl, C.A.6    Baker, D.7
  • 37
    • 48449105393 scopus 로고    scopus 로고
    • The RosettaDock server for local protein-protein docking
    • Lyskov, S. and Gray, J. J. (2008) The RosettaDock server for local protein-protein docking Nucleic Acids Res. 36, W233-238
    • (2008) Nucleic Acids Res. , vol.36 , pp. 233-238
    • Lyskov, S.1    Gray, J.J.2
  • 38
    • 17744364070 scopus 로고    scopus 로고
    • Improved side-chain modeling for protein-protein docking
    • DOI 10.1110/ps.041222905
    • Wang, C., Schueler-Furman, O., and Baker, D. (2005) Improved side-chain modeling for protein-protein docking Protein Sci. 14, 1328-1339 (Pubitemid 40577812)
    • (2005) Protein Science , vol.14 , Issue.5 , pp. 1328-1339
    • Wang, C.1    Schueler-Furman, O.2    Baker, D.3
  • 39
    • 38649088246 scopus 로고    scopus 로고
    • Cooperative Assembly of TGF- Superfamily Signaling Complexes Is Mediated by Two Disparate Mechanisms and Distinct Modes of Receptor Binding
    • DOI 10.1016/j.molcel.2007.11.039, PII S1097276508000166
    • Groppe, J., Hinck, C. S., Samavarchi-Tehrani, P., Zubieta, C., Schuermann, J. P., Taylor, A. B., Schwarz, P. M., Wrana, J. L., and Hinck, A. P. (2008) Cooperative assembly of TGF-beta superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding Mol. Cell 29, 157-168 (Pubitemid 351172827)
    • (2008) Molecular Cell , vol.29 , Issue.2 , pp. 157-168
    • Groppe, J.1    Hinck, C.S.2    Samavarchi-Tehrani, P.3    Zubieta, C.4    Schuermann, J.P.5    Taylor, A.B.6    Schwarz, P.M.7    Wrana, J.L.8    Hinck, A.P.9
  • 40
    • 80052970306 scopus 로고    scopus 로고
    • The TbetaR-I pre-helix extension is structurally ordered in the unbound form and its flanking prolines are essential for binding
    • Zuniga, J. E., Ilangovan, U., Mahlawat, P., Hinck, C. S., Huang, T., Groppe, J. C., McEwen, D. G., and Hinck, A. P. (2011) The TbetaR-I pre-helix extension is structurally ordered in the unbound form and its flanking prolines are essential for binding J. Mol. Biol. 412, 601-618
    • (2011) J. Mol. Biol. , vol.412 , pp. 601-618
    • Zuniga, J.E.1    Ilangovan, U.2    Mahlawat, P.3    Hinck, C.S.4    Huang, T.5    Groppe, J.C.6    McEwen, D.G.7    Hinck, A.P.8
  • 41
    • 65449189690 scopus 로고    scopus 로고
    • Crystal structure analysis reveals a spring-loaded latch as molecular mechanism for GDF-5-type i receptor specificity
    • Kotzsch, A., Nickel, J., Seher, A., Sebald, W., and Muller, T. D. (2009) Crystal structure analysis reveals a spring-loaded latch as molecular mechanism for GDF-5-type I receptor specificity EMBO J. 28, 937-947
    • (2009) EMBO J. , vol.28 , pp. 937-947
    • Kotzsch, A.1    Nickel, J.2    Seher, A.3    Sebald, W.4    Muller, T.D.5
  • 44
    • 0033975972 scopus 로고    scopus 로고
    • Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2
    • DOI 10.1016/S0014-5793(00)01214-X, PII S001457930001214X
    • Kirsch, T., Nickel, J., and Sebald, W. (2000) Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2 FEBS Lett. 468, 215-219 (Pubitemid 30110798)
    • (2000) FEBS Letters , vol.468 , Issue.2-3 , pp. 215-219
    • Kirsch, T.1    Nickel, J.2    Sebald, W.3
  • 45
    • 0032525922 scopus 로고    scopus 로고
    • Chimeric extracellular domain of type II transforming growth factor (TGF)- receptor fused to the Fc region of human immunoglobulin as a TGF- antagonist
    • DOI 10.1046/j.1432-1327.1998.2540505.x
    • Komesli, S., Vivien, D., and Dutartre, P. (1998) Chimeric extracellular domain type II transforming growth factor (TGF)-beta receptor fused to the Fc region of human immunoglobulin as a TGF-beta antagonist Eur. J. Biochem. 254, 505-513 (Pubitemid 28308100)
    • (1998) European Journal of Biochemistry , vol.254 , Issue.3 , pp. 505-513
    • Komesli, S.1    Vivien, D.2    Dutartre, P.3
  • 46
    • 70350037984 scopus 로고    scopus 로고
    • Receptor oligomerization and beyond: A case study in bone morphogenetic proteins
    • Heinecke, K., Seher, A., Schmitz, W., Mueller, T. D., Sebald, W., and Nickel, J. (2009) Receptor oligomerization and beyond: a case study in bone morphogenetic proteins BMC Biol. 7, 59
    • (2009) BMC Biol. , vol.7 , pp. 59
    • Heinecke, K.1    Seher, A.2    Schmitz, W.3    Mueller, T.D.4    Sebald, W.5    Nickel, J.6
  • 47
    • 23144437542 scopus 로고    scopus 로고
    • Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its use in determining secondary structural elements
    • DOI 10.1007/s10858-005-5705-1
    • Eghbalnia, H. R., Wang, L., Bahrami, A., Assadi, A., and Markley, J. L. (2005) Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its use in determining secondary structural elements J. Biomol. NMR 32, 71-81 (Pubitemid 41086469)
    • (2005) Journal of Biomolecular NMR , vol.32 , Issue.1 , pp. 71-81
    • Eghbalnia, H.R.1    Wang, L.2    Bahrami, A.3    Assadi, A.4    Markley, J.L.5
  • 48
    • 0037316363 scopus 로고    scopus 로고
    • ARIA: Automated NOE assignment and NMR structure calculation
    • DOI 10.1093/bioinformatics/19.2.315
    • Linge, J. P., Habeck, M., Rieping, W., and Nilges, M. (2003) ARIA: automated NOE assignment and NMR structure calculation Bioinformatics 19, 315-316 (Pubitemid 36181930)
    • (2003) Bioinformatics , vol.19 , Issue.2 , pp. 315-316
    • Linge, J.P.1    Habeck, M.2    Rieping, W.3    Nilges, M.4
  • 49
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • DOI 10.1023/A:1008392405740
    • Cornilescu, G., Delaglio, F., and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology J. Biomol. NMR 13, 289-302 (Pubitemid 29143535)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.3 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 51
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. and Sander, C. (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22, 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 52
    • 33646749327 scopus 로고    scopus 로고
    • Structure of the ternary signaling complex of a TGF-beta superfamily member
    • Allendorph, G. P., Vale, W. W., and Choe, S. (2006) Structure of the ternary signaling complex of a TGF-beta superfamily member Proc. Natl. Acad. Sci. U. S. A. 103, 7643-7648
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 7643-7648
    • Allendorph, G.P.1    Vale, W.W.2    Choe, S.3
  • 53
    • 33847118974 scopus 로고    scopus 로고
    • A silent H-bond can be mutationally activated for high-affinity interaction of BMP-2 and activin type IIB receptor
    • Weber, D., Kotzsch, A., Nickel, J., Harth, S., Seher, A., Mueller, U., Sebald, W., and Mueller, T. D. (2007) A silent H-bond can be mutationally activated for high-affinity interaction of BMP-2 and activin type IIB receptor BMC Struct. Biol. 7, 6
    • (2007) BMC Struct. Biol. , vol.7 , pp. 6
    • Weber, D.1    Kotzsch, A.2    Nickel, J.3    Harth, S.4    Seher, A.5    Mueller, U.6    Sebald, W.7    Mueller, T.D.8
  • 54
    • 77952005098 scopus 로고    scopus 로고
    • Ternary complex of transforming growth factor-beta1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily
    • Radaev, S., Zou, Z., Huang, T., Lafer, E. M., Hinck, A. P., and Sun, P. D. (2010) Ternary complex of transforming growth factor-beta1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily J. Biol. Chem. 285, 14806-14814
    • (2010) J. Biol. Chem. , vol.285 , pp. 14806-14814
    • Radaev, S.1    Zou, Z.2    Huang, T.3    Lafer, E.M.4    Hinck, A.P.5    Sun, P.D.6
  • 55
    • 0037351880 scopus 로고    scopus 로고
    • The BMP7/ActRII extracellular domain complex provides new insights into the cooperative nature of receptor assembly
    • DOI 10.1016/S1097-2765(03)00094-7
    • Greenwald, J., Groppe, J., Gray, P., Wiater, E., Kwiatkowski, W., Vale, W., and Choe, S. (2003) The BMP7/ActRII extracellular domain complex provides new insights into the cooperative nature of receptor assembly Mol. Cell 11, 605-617 (Pubitemid 36385117)
    • (2003) Molecular Cell , vol.11 , Issue.3 , pp. 605-617
    • Greenwald, J.1    Groppe, J.2    Gray, P.3    Wiater, E.4    Kwiatkowski, W.5    Vale, W.6    Choe, S.7
  • 56
    • 67449146883 scopus 로고    scopus 로고
    • Emerging role of bone morphogenetic proteins in angiogenesis
    • David, L., Feige, J. J., and Bailly, S. (2009) Emerging role of bone morphogenetic proteins in angiogenesis Cytokine Growth Factor Rev. 20, 203-212
    • (2009) Cytokine Growth Factor Rev. , vol.20 , pp. 203-212
    • David, L.1    Feige, J.J.2    Bailly, S.3
  • 57
    • 77956563351 scopus 로고    scopus 로고
    • Functional analysis of the BMP9 response of ALK1 mutants from HHT2 patients: A diagnostic tool for novel ACVRL1 mutations
    • Ricard, N., Bidart, M., Mallet, C., Lesca, G., Giraud, S., Prudent, R., Feige, J. J., and Bailly, S. (2010) Functional analysis of the BMP9 response of ALK1 mutants from HHT2 patients: a diagnostic tool for novel ACVRL1 mutations Blood 116, 1604-1612
    • (2010) Blood , vol.116 , pp. 1604-1612
    • Ricard, N.1    Bidart, M.2    Mallet, C.3    Lesca, G.4    Giraud, S.5    Prudent, R.6    Feige, J.J.7    Bailly, S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.