메뉴 건너뛰기




Volumn 19, Issue 13, 2000, Pages 3314-3324

BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II

Author keywords

Binding epitope; Bone morphogenetic protein; Receptor signalling; TGF superfamily

Indexed keywords

ACTIVIN RECEPTOR; BONE MORPHOGENETIC PROTEIN 2; BONE MORPHOGENETIC PROTEIN RECEPTOR; EPITOPE; MUTANT PROTEIN; TRANSFORMING GROWTH FACTOR BETA;

EID: 0034600953     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.13.3314     Document Type: Article
Times cited : (225)

References (54)
  • 1
    • 0024396459 scopus 로고
    • Drugs from emasculated hormones: The principle of syntopic antagonism
    • Black, J. (1989) Drugs from emasculated hormones: the principle of syntopic antagonism. Science, 245, 486-493.
    • (1989) Science , vol.245 , pp. 486-493
    • Black, J.1
  • 2
    • 0029834634 scopus 로고    scopus 로고
    • Overexpression of bone morphogenetic protein-6 (BMP-6) in the epidermis of transgenic mice: Inhibition or stimulation of proliferation depending on the pattern of transgene expression and formation of psoriatic lesions
    • Blessing, M., Schirmacher, P. and Kaiser, S. (1996) Overexpression of bone morphogenetic protein-6 (BMP-6) in the epidermis of transgenic mice: inhibition or stimulation of proliferation depending on the pattern of transgene expression and formation of psoriatic lesions. J. Cell Biol., 135, 227-239.
    • (1996) J. Cell Biol. , vol.135 , pp. 227-239
    • Blessing, M.1    Schirmacher, P.2    Kaiser, S.3
  • 3
    • 2642609494 scopus 로고    scopus 로고
    • JunB is involved in the inhibition of myogenic differentiation by bone morphogenetic protein-2
    • Chalaux, E., Lopez Rovira, T., Rosa, J.L., Bartrons, R. and Ventura, F. (1998) JunB is involved in the inhibition of myogenic differentiation by bone morphogenetic protein-2. J. Biol. Chem., 273, 537-543.
    • (1998) J. Biol. Chem. , vol.273 , pp. 537-543
    • Chalaux, E.1    Lopez Rovira, T.2    Rosa, J.L.3    Bartrons, R.4    Ventura, F.5
  • 4
    • 0031860761 scopus 로고    scopus 로고
    • A genetic screen for modifiers of Drosophila decapentaplegic signaling identifies mutations in punt. Mothers against dpp and the BMP-7 homologue, 60A
    • Chen, Y., Riese, M.J., Killinger, M.A. and Hoffmann, F.M. (1998) A genetic screen for modifiers of Drosophila decapentaplegic signaling identifies mutations in punt. Mothers against dpp and the BMP-7 homologue, 60A. Development, 125, 1759-1768.
    • (1998) Development , vol.125 , pp. 1759-1768
    • Chen, Y.1    Riese, M.J.2    Killinger, M.A.3    Hoffmann, F.M.4
  • 5
    • 0027132013 scopus 로고
    • Comparison of a structural and a functional epitope
    • published erratum appears in J. Mol. Biol., 237, 513
    • Cunningham, B.C. and Wells, J.A. (1993) Comparison of a structural and a functional epitope [published erratum appears in J. Mol. Biol., 237, 513]. J. Mol. Biol., 234, 554-563.
    • (1993) J. Mol. Biol. , vol.234 , pp. 554-563
    • Cunningham, B.C.1    Wells, J.A.2
  • 6
    • 0027122245 scopus 로고
    • Crystal structure of transforming growth factor-β2: An unusual fold for the superfamily
    • Daopin, S., Piez, K.A., Ogawa, Y. and Davies, D.R. (1992) Crystal structure of transforming growth factor-β2: an unusual fold for the superfamily. Science, 257, 369-373.
    • (1992) Science , vol.257 , pp. 369-373
    • Daopin, S.1    Piez, K.A.2    Ogawa, Y.3    Davies, D.R.4
  • 7
    • 0033022235 scopus 로고    scopus 로고
    • Activin and inhibin binding to the soluble extracellular domain of activin receptor II
    • Donaldson, C.J., Vaughan, J.M., Corrigan, A.Z., Fischer, W.H. and Vale, W.W. (1999) Activin and inhibin binding to the soluble extracellular domain of activin receptor II. Endocrinology, 140, 1760-1766.
    • (1999) Endocrinology , vol.140 , pp. 1760-1766
    • Donaldson, C.J.1    Vaughan, J.M.2    Corrigan, A.Z.3    Fischer, W.H.4    Vale, W.W.5
  • 8
    • 0344423815 scopus 로고    scopus 로고
    • Distinct structural elements in GDNF mediate binding to GFRα1 and activation of the GFRα1-c-Ret receptor complex
    • Eketjall, S., Fainzilber, M., Murray Rust, J. and Ibanez, C.F. (1999) Distinct structural elements in GDNF mediate binding to GFRα1 and activation of the GFRα1-c-Ret receptor complex. EMBO J., 18, 5901-5910.
    • (1999) EMBO J. , vol.18 , pp. 5901-5910
    • Eketjall, S.1    Fainzilber, M.2    Murray Rust, J.3    Ibanez, C.F.4
  • 9
    • 0034021776 scopus 로고    scopus 로고
    • BMP receptor complexes on the surface of live cells: A new oligomerization mode for serine/threonine kinase receptors
    • Gilboa, L., Nohe, A., Geissendörfer, T., Sebald, W., Henis, Y.I. and Knaus, P. (2000) BMP receptor complexes on the surface of live cells: a new oligomerization mode for serine/threonine kinase receptors. Mol. Biol. Cell, 11, 1023-1035.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1023-1035
    • Gilboa, L.1    Nohe, A.2    Geissendörfer, T.3    Sebald, W.4    Henis, Y.I.5    Knaus, P.6
  • 10
    • 0032899751 scopus 로고    scopus 로고
    • Three-finger toxin fold for the extracellular ligand-binding domain of the type II activin receptor serine kinase
    • Greenwald, J., Fischer, W.H., Vale, W.W. and Choe, S. (1999) Three-finger toxin fold for the extracellular ligand-binding domain of the type II activin receptor serine kinase. Nature Struct. Biol., 6, 18-22.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 18-22
    • Greenwald, J.1    Fischer, W.H.2    Vale, W.W.3    Choe, S.4
  • 11
    • 0030042590 scopus 로고    scopus 로고
    • Three-dimensional structure of recombinant human osteogenic protein 1: Structural paradigm for the transforming growth factor beta superfamily
    • Griffith, D.L., Keck, P.C., Sampath, T.K., Rueger, D.C. and Carlson, W.D. (1996) Three-dimensional structure of recombinant human osteogenic protein 1: structural paradigm for the transforming growth factor beta superfamily. Proc. Natl Acad. Sci. USA, 93, 878-883.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 878-883
    • Griffith, D.L.1    Keck, P.C.2    Sampath, T.K.3    Rueger, D.C.4    Carlson, W.D.5
  • 12
    • 0029802904 scopus 로고    scopus 로고
    • Genetic analysis of dorsoventral pattern formation in the zebrafish: Requirement of a BMP-like ventralizing activity and its dorsal repressor
    • Hammerschmidt, M., Serbedzija, G.N. and McMahon, A.P. (1996) Genetic analysis of dorsoventral pattern formation in the zebrafish: requirement of a BMP-like ventralizing activity and its dorsal repressor. Genes Dev., 10, 2452-2461.
    • (1996) Genes Dev. , vol.10 , pp. 2452-2461
    • Hammerschmidt, M.1    Serbedzija, G.N.2    McMahon, A.P.3
  • 13
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin, C.H. (1995) Dimerization of cell surface receptors in signal transduction. Cell, 80, 213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 14
    • 0031438047 scopus 로고    scopus 로고
    • TGF-β signalling from cell membrane to nucleus through SMAD proteins
    • Heldin, C.H., Miyazono, K. and ten Dijke, P. (1997) TGF-β signalling from cell membrane to nucleus through SMAD proteins. Nature, 390, 465-471.
    • (1997) Nature , vol.390 , pp. 465-471
    • Heldin, C.H.1    Miyazono, K.2    Ten Dijke, P.3
  • 15
    • 0030218004 scopus 로고    scopus 로고
    • Bone morphogenetic proteins in development
    • Hogan, B.L. (1996) Bone morphogenetic proteins in development. Curr. Opin. Genet. Dev., 6, 432-438.
    • (1996) Curr. Opin. Genet. Dev. , vol.6 , pp. 432-438
    • Hogan, B.L.1
  • 16
    • 0001138870 scopus 로고    scopus 로고
    • An active site of transforming growth factor-β1 for growth inhibition and stimulation
    • Huang, S.S., Zhou, M., Johnson, F.E., Shieh, H.S. and Huang, J.S. (1999) An active site of transforming growth factor-β1 for growth inhibition and stimulation. J. Biol. Chem., 274, 27754-27758.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27754-27758
    • Huang, S.S.1    Zhou, M.2    Johnson, F.E.3    Shieh, H.S.4    Huang, J.S.5
  • 17
    • 0031000759 scopus 로고    scopus 로고
    • Cloning of human bone morphogenetic protein type IB receptor (BMPR-IB) and its expression in prostate cancer in comparison with other BMPRs
    • published erratum appears in Oncogene, 15, 1121
    • Ide, H., Katoh, M., Sasaki H., Yoshida, T., Aoki, K., Nawa, Y., Osada, Y., Sugimura, T. and Terada, M. (1997) Cloning of human bone morphogenetic protein type IB receptor (BMPR-IB) and its expression in prostate cancer in comparison with other BMPRs [published erratum appears in Oncogene, 15, 1121]. Oncogene, 14, 1377-1382.
    • (1997) Oncogene , vol.14 , pp. 1377-1382
    • Ide, H.1    Katoh, M.2    Sasaki, H.3    Yoshida, T.4    Aoki, K.5    Nawa, Y.6    Osada, Y.7    Sugimura, T.8    Terada, M.9
  • 18
    • 0032482928 scopus 로고    scopus 로고
    • Direct binding of follistatin to a complex of bone-morphogenetic protein and its receptor inhibits ventral and epidermal cell fates in early xenopus embryo
    • Iemura, S., Yamamoto, T.S., Takagi, C., Uchiyama, H., Natsume, T., Shimasaki, S., Sugino, H. and Ueno, N. (1998) Direct binding of follistatin to a complex of bone-morphogenetic protein and its receptor inhibits ventral and epidermal cell fates in early Xenopus embryo. Proc. Natl Acad. Sci. USA, 95, 9337-9342.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 9337-9342
    • Iemura, S.1    Yamamoto, T.S.2    Takagi, C.3    Uchiyama, H.4    Natsume, T.5    Shimasaki, S.6    Sugino, H.7    Ueno, N.8
  • 19
    • 0027946689 scopus 로고
    • Bone morphogenetic protein-2 converts the differentiation pathway of C2C12 myoblasts into the osteoblast lineage
    • published erratum appears in J. Cell Biol., 128, following 713
    • Katagiri, T. et al. (1994) Bone morphogenetic protein-2 converts the differentiation pathway of C2C12 myoblasts into the osteoblast lineage [published erratum appears in J. Cell Biol., 128, following 713]. J. Cell Biol., 127, 1755-1766.
    • (1994) J. Cell Biol. , vol.127 , pp. 1755-1766
    • Katagiri, T.1
  • 20
    • 0028931238 scopus 로고
    • Cloning of a novel type II serine/threonine kinase receptor through interaction with the type I transforming growth factor-β receptor
    • Kawabata, M., Chytil, A. and Moses, H.L. (1995) Cloning of a novel type II serine/threonine kinase receptor through interaction with the type I transforming growth factor-β receptor. J. Biol. Chem., 270, 5625-5630.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5625-5630
    • Kawabata, M.1    Chytil, A.2    Moses, H.L.3
  • 21
    • 0033975972 scopus 로고    scopus 로고
    • Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2
    • 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.
    • (2000) FEBS Lett. , vol.468 , pp. 215-219
    • Kirsch, T.1    Nickel, J.2    Sebald, W.3
  • 22
    • 0034043106 scopus 로고    scopus 로고
    • Crystal structure of the BMP-2-BRIA ectodomain complex
    • Kirsch, T., Sebald, W. and Dreyer, M. (2000b) Crystal structure of the BMP-2-BRIA ectodomain complex. Nature Struct. Biol., 7, 492-496.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 492-496
    • Kirsch, T.1    Sebald, W.2    Dreyer, M.3
  • 23
    • 0028142801 scopus 로고
    • Characterization and cloning of a receptor for BMP-2 and BMP-4 from NIH 3T3 cells
    • Koenig, B.B. et al. (1994) Characterization and cloning of a receptor for BMP-2 and BMP-4 from NIH 3T3 cells. Mol. Cell. Biol., 14, 5961-5974.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5961-5974
    • Koenig, B.B.1
  • 25
    • 0029742706 scopus 로고    scopus 로고
    • Transforming growth factor-β: A general review
    • Lawrence, D.A. (1996) Transforming growth factor-β: a general review. Eur. Cytokine Network, 7, 363-374.
    • (1996) Eur. Cytokine Network , vol.7 , pp. 363-374
    • Lawrence, D.A.1
  • 26
    • 0029008597 scopus 로고
    • Human type II receptor for bone morphogenic proteins (BMPs): Extension of the two-kinase receptor model to the BMPs
    • Liu, F., Ventura, F., Doody, J. and Massague, J. (1995) Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs. Mol. Cell. Biol., 15, 3479-3486.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3479-3486
    • Liu, F.1    Ventura, F.2    Doody, J.3    Massague, J.4
  • 27
    • 0029792338 scopus 로고    scopus 로고
    • Signaling by chimeric erythropoietin-TGF-β receptors: Homodimerization of the cytoplasmic domain of the type I TGF-β receptor and heterodimerization with the type II receptor are both required for intracellular signal transduction
    • Luo, K. and Lodish, H.F. (1996) Signaling by chimeric erythropoietin-TGF-β receptors: homodimerization of the cytoplasmic domain of the type I TGF-β receptor and heterodimerization with the type II receptor are both required for intracellular signal transduction. EMBO J., 15, 4485-4496.
    • (1996) EMBO J. , vol.15 , pp. 4485-4496
    • Luo, K.1    Lodish, H.F.2
  • 28
    • 0030972496 scopus 로고    scopus 로고
    • Positive and negative regulation of type II TGF-β receptor signal transduction by autophosphorylation on multiple serine residues
    • Luo, K. and Lodish, H.F. (1997) Positive and negative regulation of type II TGF-β receptor signal transduction by autophosphorylation on multiple serine residues. EMBO J., 16, 1970-1981.
    • (1997) EMBO J. , vol.16 , pp. 1970-1981
    • Luo, K.1    Lodish, H.F.2
  • 29
    • 0032475884 scopus 로고    scopus 로고
    • Specific activation of Smad1 signaling pathways by the BMP7 type I receptor, ALK2
    • Macias-Silva, M., Hoodless, P.A., Tang, S.J., Buchwald, M. and Wrana, J.L. (1998) Specific activation of Smad1 signaling pathways by the BMP7 type I receptor, ALK2. J. Biol. Chem., 273, 25628-25636.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25628-25636
    • Macias-Silva, M.1    Hoodless, P.A.2    Tang, S.J.3    Buchwald, M.4    Wrana, J.L.5
  • 30
    • 0031685620 scopus 로고    scopus 로고
    • TGF-β signal transduction
    • Massague, J. (1998) TGF-β signal transduction. Annu. Rev. Biochem., 67, 753-791.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 753-791
    • Massague, J.1
  • 31
    • 0026502619 scopus 로고
    • Cloning of the human activin receptor cDNA reveals high evolutionary conservation
    • published erratum appears in Biochim. Biophys. Acta, 1131, 243
    • Matzuk, M.M. and Bradley, A. (1992) Cloning of the human activin receptor cDNA reveals high evolutionary conservation [published erratum appears in Biochim. Biophys. Acta, 1131, 243]. Biochim. Biophys. Acta, 1130, 105-108.
    • (1992) Biochim. Biophys. Acta , vol.1130 , pp. 105-108
    • Matzuk, M.M.1    Bradley, A.2
  • 33
    • 0031010050 scopus 로고    scopus 로고
    • Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member
    • McPherron, A.C., Lawler, A.M. and Lee, S.J. (1997) Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member. Nature, 387, 83-90.
    • (1997) Nature , vol.387 , pp. 83-90
    • McPherron, A.C.1    Lawler, A.M.2    Lee, S.J.3
  • 34
    • 0029943464 scopus 로고    scopus 로고
    • The crystal structure of TGF-β 3 and comparison to TGF-β 2: Implications for receptor binding
    • Mittl, P.R., Priestle, J.P., Cox, D.A., McMaster, G., Cerletti, N. and Grutter, M.G. (1996) The crystal structure of TGF-β 3 and comparison to TGF-β 2: implications for receptor binding. Protein Sci., 5, 1261-1271.
    • (1996) Protein Sci. , vol.5 , pp. 1261-1271
    • Mittl, P.R.1    Priestle, J.P.2    Cox, D.A.3    McMaster, G.4    Cerletti, N.5    Grutter, M.G.6
  • 35
    • 0030826702 scopus 로고    scopus 로고
    • A kinase domain-truncated type I receptor blocks bone morphogenetic protein-2-induced signal transduction in C2C12 myoblasts
    • Namiki, M., Akiyama, S., Katagiri, T., Suzuki, A., Ueno, N., Yamaji, N., Rosen, V., Wozney, J.M. and Suda, T. (1997) A kinase domain-truncated type I receptor blocks bone morphogenetic protein-2-induced signal transduction in C2C12 myoblasts. J. Biol. Chem., 272, 22046-22052.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22046-22052
    • Namiki, M.1    Akiyama, S.2    Katagiri, T.3    Suzuki, A.4    Ueno, N.5    Yamaji, N.6    Rosen, V.7    Wozney, J.M.8    Suda, T.9
  • 36
    • 0031939744 scopus 로고    scopus 로고
    • Smad5 and DPC4 are key molecules in mediating BMP-2-induced osteoblastic differentiation of the pluripotent mesenchymal precursor cell line C2C12
    • Nishimura, R., Kato, Y., Chen, D., Harris, S.E., Mundy, G.R. and Yoneda, T. (1998) Smad5 and DPC4 are key molecules in mediating BMP-2-induced osteoblastic differentiation of the pluripotent mesenchymal precursor cell line C2C12. J. Biol. Chem., 273, 1872-1879.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1872-1879
    • Nishimura, R.1    Kato, Y.2    Chen, D.3    Harris, S.E.4    Mundy, G.R.5    Yoneda, T.6
  • 38
    • 0029153741 scopus 로고
    • Identification of a human type II receptor for bone morphogenetic protein-4 that forms differential heteromeric complexes with bone morphogenetic protein type I receptors
    • Nohno, T., Ishikawa, T., Saito, T., Hosokawa, K., Noji, S., Wolsing, D.H. and Rosenbaum, J.S. (1995) Identification of a human type II receptor for bone morphogenetic protein-4 that forms differential heteromeric complexes with bone morphogenetic protein type I receptors. J Biol. Chem., 270, 22522-22526.
    • (1995) J Biol. Chem. , vol.270 , pp. 22522-22526
    • Nohno, T.1    Ishikawa, T.2    Saito, T.3    Hosokawa, K.4    Noji, S.5    Wolsing, D.H.6    Rosenbaum, J.S.7
  • 39
    • 0026607545 scopus 로고
    • Kinetics of protein-protein association explained by Brownian dynamics computer simulation
    • Northrup, S.H. and Erickson, H.P. (1992) Kinetics of protein-protein association explained by Brownian dynamics computer simulation. Proc. Natl Acad. Sci. USA. 89, 3338-3342.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 3338-3342
    • Northrup, S.H.1    Erickson, H.P.2
  • 40
    • 0028097108 scopus 로고
    • Bone and cartilage differentiation
    • Reddi, A.H. (1994) Bone and cartilage differentiation. Curr. Opin. Genet. Dev., 4, 737-744.
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 737-744
    • Reddi, A.H.1
  • 41
    • 0031105160 scopus 로고    scopus 로고
    • Bone morphogenetic proteins: An unconventional approach to isolation of first mammalian morphogens
    • Reddi, A.H. (1997) Bone morphogenetic proteins: an unconventional approach to isolation of first mammalian morphogens. Cytokine Growth Factor Rev., 8, 11-20.
    • (1997) Cytokine Growth Factor Rev. , vol.8 , pp. 11-20
    • Reddi, A.H.1
  • 42
    • 0031909665 scopus 로고    scopus 로고
    • Role of morphogenetic proteins in skeletal tissue engineering and regeneration
    • Reddi, A.H. (1998) Role of morphogenetic proteins in skeletal tissue engineering and regeneration. Nature Biotechnol., 16, 247-252.
    • (1998) Nature Biotechnol. , vol.16 , pp. 247-252
    • Reddi, A.H.1
  • 44
    • 0029985256 scopus 로고    scopus 로고
    • Human bone morphogenetic protein 2 contains a heparin-binding site which modifies its biological activity
    • Ruppert, R., Hoffmann, E. and Sebald, W. (1996) Human bone morphogenetic protein 2 contains a heparin-binding site which modifies its biological activity. Eur. J. Biochem., 237, 295-302.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 295-302
    • Ruppert, R.1    Hoffmann, E.2    Sebald, W.3
  • 45
    • 0033582942 scopus 로고    scopus 로고
    • Crystal structure of human bone morphogenetic protein-2 at 2.7 Å resolution
    • Scheufler, C., Sebald, W. and Hulsmeyer, M. (1999) Crystal structure of human bone morphogenetic protein-2 at 2.7 Å resolution. J. Mol. Biol., 287, 103-115.
    • (1999) J. Mol. Biol. , vol.287 , pp. 103-115
    • Scheufler, C.1    Hulsmeyer, M.2
  • 46
    • 0026633842 scopus 로고
    • An unusual feature revealed by the crystal structure at 2.2 Å resolution of human transforming growth factor-β2
    • Schlunegger, M.P. and Grutter, M.G. (1992) An unusual feature revealed by the crystal structure at 2.2 Å resolution of human transforming growth factor-β2. Nature, 358, 430-434.
    • (1992) Nature , vol.358 , pp. 430-434
    • Schlunegger, M.P.1    Grutter, M.G.2
  • 47
    • 0029818648 scopus 로고    scopus 로고
    • Global and local determinants for the kinetics of interleukin-4/interleukin-4 receptor α chain interaction. A biosensor study employing recombinant interleukin-4-binding protein
    • Shen, B.J., Hage, T. and Sebald, W. (1996) Global and local determinants for the kinetics of interleukin-4/interleukin-4 receptor α chain interaction. A biosensor study employing recombinant interleukin-4-binding protein. Eur. J. Biochem., 240, 252-261.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 252-261
    • Shen, B.J.1    Hage, T.2    Sebald, W.3
  • 50
    • 0030030373 scopus 로고    scopus 로고
    • Complementation between kinase-defective and activation-defective TGF-β receptors reveals a novel form of receptor cooperatively essential for signaling
    • Weis Garcia, F. and Massague, J. (1996) Complementation between kinase-defective and activation-defective TGF-β receptors reveals a novel form of receptor cooperatively essential for signaling. EMBO J., 15, 276-289.
    • (1996) EMBO J. , vol.15 , pp. 276-289
    • Weis Garcia, F.1    Massague, J.2
  • 53
    • 0033515443 scopus 로고    scopus 로고
    • Identification of two amino acids in activin A that are important for biological activity and binding to the activin type II receptors
    • Wuytens, G. et al. (1999) Identification of two amino acids in activin A that are important for biological activity and binding to the activin type II receptors. J. Biol. Chem., 274, 9821-9827.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9821-9827
    • Wuytens, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.