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Volumn 291, Issue 20, 2016, Pages 10792-10804

Transforming growth factor-β family ligands can function as antagonists by competing for type II receptor binding

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOPHAGES; EPITOPES; GLYCOPROTEINS; PHYSIOLOGICAL MODELS; PHYSIOLOGY; SIGNAL TRANSDUCTION; SIGNALING;

EID: 84969240504     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.713487     Document Type: Article
Times cited : (95)

References (74)
  • 1
    • 70450187617 scopus 로고    scopus 로고
    • The regulation of TGFβ signal transduction
    • Moustakas, A., and Heldin, C. H. (2009) The regulation of TGFβ signal transduction. Development 136, 3699-3714
    • (2009) Development , vol.136 , pp. 3699-3714
    • Moustakas, A.1    Heldin, C.H.2
  • 3
    • 0031685620 scopus 로고    scopus 로고
    • TGF-β signal transduction
    • Massagué, J. (1998) TGF-β signal transduction. Annu. Rev. Biochem. 67, 753-791
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 753-791
    • Massagué, J.1
  • 4
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-β signaling from cell membrane to the nucleus
    • Shi, Y., and Massagué, J. (2003) Mechanisms of TGF-β signaling from cell membrane to the nucleus. Cell 113, 685-700
    • (2003) Cell , vol.113 , pp. 685-700
    • Shi, Y.1    Massagué, J.2
  • 7
    • 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
  • 8
    • 38649088246 scopus 로고    scopus 로고
    • Cooperative assembly of TGF-β superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding
    • 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-β superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding. Mol. Cell 29, 157-168
    • (2008) Mol. Cell , vol.29 , 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
  • 10
    • 84866742560 scopus 로고    scopus 로고
    • TGFβ signalling in context
    • Massagué, J. (2012) TGFβ signalling in context. Nat. Rev. Mol. Cell Biol. 13, 616-630
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 616-630
    • Massagué, J.1
  • 11
    • 84866312611 scopus 로고    scopus 로고
    • Context-dependent action of transforming growth factor β family members on normal and cancer stem cells
    • Caja, L., Kahata, K., and Moustakas, A. (2012) Context-dependent action of transforming growth factor β family members on normal and cancer stem cells. Curr. Pharm. Des. 18, 4072-4086
    • (2012) Curr. Pharm. Des. , vol.18 , pp. 4072-4086
    • Caja, L.1    Kahata, K.2    Moustakas, A.3
  • 12
    • 84870875424 scopus 로고    scopus 로고
    • The harmonies played by TGF-β in stem cell biology
    • Oshimori, N., and Fuchs, E. (2012) The harmonies played by TGF-β in stem cell biology. Cell Stem Cell 11, 751-764
    • (2012) Cell Stem Cell , vol.11 , pp. 751-764
    • Oshimori, N.1    Fuchs, E.2
  • 13
    • 61749097816 scopus 로고    scopus 로고
    • Tgf-β superfamily signaling in embryonic development and homeostasis
    • Wu, M. Y., and Hill, C. S. (2009) Tgf-β superfamily signaling in embryonic development and homeostasis. Dev. Cell 16, 329-343
    • (2009) Dev. Cell , vol.16 , pp. 329-343
    • Wu, M.Y.1    Hill, C.S.2
  • 14
    • 63749105896 scopus 로고    scopus 로고
    • Mechanism of TGF-β signaling to growth arrest, apoptosis, and epithelial-mesenchymal transition
    • Heldin, C. H., Landström, M., and Moustakas, A. (2009) Mechanism of TGF-β signaling to growth arrest, apoptosis, and epithelial-mesenchymal transition. Curr. Opin. Cell Biol. 21, 166-176
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 166-176
    • Heldin, C.H.1    Landström, M.2    Moustakas, A.3
  • 15
    • 62649156796 scopus 로고    scopus 로고
    • Emergence, development and diversification of the TGF-β signalling pathway within the animal kingdom
    • Huminiecki, L., Goldovsky, L., Freilich, S., Moustakas, A., Ouzounis, C., and Heldin, C. H. (2009) Emergence, development and diversification of the TGF-β signalling pathway within the animal kingdom.BMCEvol. Biol. 9, 28
    • (2009) BMCEvol. Biol. , vol.9 , pp. 28
    • Huminiecki, L.1    Goldovsky, L.2    Freilich, S.3    Moustakas, A.4    Ouzounis, C.5    Heldin, C.H.6
  • 17
    • 69849113284 scopus 로고    scopus 로고
    • The structure of myostatin:follistatin 288: Insights into receptor utilization and heparin binding
    • Cash, J. N., Rejon, C. A., McPherron, A. C., Bernard, D. J., and Thompson, T. B. (2009) The structure of myostatin:follistatin 288: insights into receptor utilization and heparin binding. EMBO J. 28, 2662-2676
    • (2009) EMBO J. , vol.28 , pp. 2662-2676
    • Cash, J.N.1    Rejon, C.A.2    McPherron, A.C.3    Bernard, D.J.4    Thompson, T.B.5
  • 18
    • 84929501032 scopus 로고    scopus 로고
    • Human cerberus prevents nodal-receptor binding, inhibits nodal signaling, and suppresses nodal-mediated phenotypes
    • Aykul, S., Ni, W., Mutatu, W., and Martinez-Hackert, E. (2015) Human cerberus prevents nodal-receptor binding, inhibits nodal signaling, and suppresses nodal-mediated phenotypes. PLoS ONE 10, e0114954
    • (2015) PLoS ONE , vol.10
    • Aykul, S.1    Ni, W.2    Mutatu, W.3    Martinez-Hackert, E.4
  • 19
    • 4544286802 scopus 로고    scopus 로고
    • Molecular recognition in bone morphogenetic protein (BMP)/receptor interaction
    • Sebald, W., Nickel, J., Zhang, J. L., and Mueller, T. D. (2004) Molecular recognition in bone morphogenetic protein (BMP)/receptor interaction. Biol. Chem. 385, 697-710
    • (2004) Biol. Chem. , vol.385 , pp. 697-710
    • Sebald, W.1    Nickel, J.2    Zhang, J.L.3    Mueller, T.D.4
  • 21
    • 0030060831 scopus 로고    scopus 로고
    • Activation of signalling by the activin receptor complex
    • Attisano, L., Wrana, J. L., Montalvo, E., and Massagué, J. (1996) Activation of signalling by the activin receptor complex. Mol. Cell. Biol. 16, 1066-1073
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1066-1073
    • Attisano, L.1    Wrana, J.L.2    Montalvo, E.3    Massagué, J.4
  • 22
    • 0034043106 scopus 로고    scopus 로고
    • Crystal structure of the BMP-2-BRIA ectodomain complex
    • Kirsch, T., Sebald, W., and Dreyer, M. K. (2000) Crystal structure of the BMP-2-BRIA ectodomain complex. Nat. Struct. Biol. 7, 492-496
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 492-496
    • Kirsch, T.1    Sebald, W.2    Dreyer, M.K.3
  • 23
    • 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
    • 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
    • (2007) Blood , vol.109 , pp. 1953-1961
    • David, L.1    Mallet, C.2    Mazerbourg, S.3    Feige, J.J.4    Bailly, S.5
  • 26
    • 0037351880 scopus 로고    scopus 로고
    • The BMP7/ActRII extracellular domain complex provides new insights into the cooperative nature of receptor assembly
    • 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
    • (2003) Mol. Cell , vol.11 , pp. 605-617
    • Greenwald, J.1    Groppe, J.2    Gray, P.3    Wiater, E.4    Kwiatkowski, W.5    Vale, W.6    Choe, S.7
  • 27
    • 84862752910 scopus 로고    scopus 로고
    • Structural studies of the TGF-βs and their receptors-insights into evolution of the TGF-β superfamily
    • Hinck, A. P. (2012) Structural studies of the TGF-βs and their receptors-insights into evolution of the TGF-β superfamily. FEBS Lett. 586, 1860-1870
    • (2012) FEBS Lett. , vol.586 , pp. 1860-1870
    • Hinck, A.P.1
  • 28
    • 84884538870 scopus 로고    scopus 로고
    • Activins bind and signal via bone morphogenetic protein receptor type II (BMPR2) in immortalized gonadotrope-like cells
    • Rejon, C. A., Hancock, M. A., Li, Y. N., Thompson, T. B., Hébert, T. E., and Bernard, D. J. (2013) activins bind and signal via bone morphogenetic protein receptor type II (BMPR2) in immortalized gonadotrope-like cells. Cell. Signal. 25, 2717-2726
    • (2013) Cell Signal. , vol.25 , pp. 2717-2726
    • Rejon, C.A.1    Hancock, M.A.2    Li, Y.N.3    Thompson, T.B.4    Hébert, T.E.5    Bernard, D.J.6
  • 29
    • 84959037027 scopus 로고    scopus 로고
    • New ligand binding function of human Cerberus and the role of proteolytic processing in regulating ligand-receptor interactions and antagonist activity
    • Aykul, S., and Martinez-Hackert, E. (2016) New ligand binding function of human Cerberus and the role of proteolytic processing in regulating ligand-receptor interactions and antagonist activity. J. Mol. Biol. 428, 590-602
    • (2016) J. Mol. Biol. , vol.428 , pp. 590-602
    • Aykul, S.1    Martinez-Hackert, E.2
  • 30
    • 0032990886 scopus 로고    scopus 로고
    • Functional antagonism between activin and osteogenic protein-1 in human embryonal carcinoma cells
    • Piek, E., Afrakhte, M., Sampath, K., van Zoelen, E. J., Heldin, C. H., and ten Dijke, P. (1999) Functional antagonism between activin and osteogenic protein-1 in human embryonal carcinoma cells. J. Cell. Physiol. 180, 141-149
    • (1999) J. Cell. Physiol. , vol.180 , pp. 141-149
    • Piek, E.1    Afrakhte, M.2    Sampath, K.3    Van Zoelen, E.J.4    Heldin, C.H.5    Ten Dijke, P.6
  • 31
    • 24144438593 scopus 로고    scopus 로고
    • BMP-3 is a novel inhibitor of both activin and BMP-4 signaling in Xenopus embryos
    • Gamer, L. W., Nove, J., Levin, M., and Rosen, V. (2005) BMP-3 is a novel inhibitor of both activin and BMP-4 signaling in Xenopus embryos. Dev. Biol. 285, 156-168
    • (2005) Dev. Biol. , vol.285 , pp. 156-168
    • Gamer, L.W.1    Nove, J.2    Levin, M.3    Rosen, V.4
  • 35
    • 0037424231 scopus 로고    scopus 로고
    • Inhibin is an antagonist of bone morphogenetic protein signaling
    • Wiater, E., and Vale, W. (2003) Inhibin is an antagonist of bone morphogenetic protein signaling. J. Biol. Chem. 278, 7934-7941
    • (2003) J. Biol. Chem. , vol.278 , pp. 7934-7941
    • Wiater, E.1    Vale, W.2
  • 36
    • 0030920284 scopus 로고    scopus 로고
    • Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells
    • Martens, J. W., de Winter, J. P., Timmerman, M. A., McLuskey, A., van Schaik, R. H., Themmen, A. P., and de Jong, F. H. (1997) Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells. Endocrinology 138, 2928-2936
    • (1997) Endocrinology , vol.138 , pp. 2928-2936
    • Martens, J.W.1    De Winter, J.P.2    Timmerman, M.A.3    McLuskey, A.4    Van Schaik, R.H.5    Themmen, A.P.6    De Jong, F.H.7
  • 37
    • 0031018483 scopus 로고    scopus 로고
    • Activin and inhibin have antagonistic effects on ligand-dependent heteromerization of the type i and type II activin receptors and human erythroid differentiation
    • Lebrun, J. J., and Vale, W. W. (1997) activin and inhibin have antagonistic effects on ligand-dependent heteromerization of the type I and type II activin receptors and human erythroid differentiation. Mol. Cell. Biol. 17, 1682-1691
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1682-1691
    • Lebrun, J.J.1    Vale, W.W.2
  • 38
    • 0038676258 scopus 로고    scopus 로고
    • Regulation of wound healing by growth factors and cytokines
    • Werner, S., and Grose, R. (2003) Regulation of wound healing by growth factors and cytokines. Physiol. Rev. 83, 835-870
    • (2003) Physiol. Rev. , vol.83 , pp. 835-870
    • Werner, S.1    Grose, R.2
  • 41
    • 84901931429 scopus 로고    scopus 로고
    • High-throughput functional screening using a homemade dual-glow luciferase assay
    • Baker, J. M., and Boyce, F. M. (2014) High-throughput functional screening using a homemade dual-glow luciferase assay. J. Vis. Exp. 10.3791/50282
    • (2014) J. Vis. Exp.
    • Baker, J.M.1    Boyce, F.M.2
  • 44
    • 0030776705 scopus 로고    scopus 로고
    • Immunological measurement of transforming growth factor-β1 (TGF-β1) in blood; Assay development and comparison
    • Kropf, J., Schurek, J. O., Wollner, A., and Gressner, A. M. (1997) Immunological measurement of transforming growth factor-β1 (TGF-β1) in blood; assay development and comparison. Clin. Chem. 43, 1965-1974
    • (1997) Clin. Chem. , vol.43 , pp. 1965-1974
    • Kropf, J.1    Schurek, J.O.2    Wollner, A.3    Gressner, A.M.4
  • 45
    • 0242684423 scopus 로고    scopus 로고
    • Transforming growth factor-β (TGF-β) binding to the extracellular domain of the type II TGF-β receptor: Receptor capture on a biosensor surface using a new coiled-coil capture system demonstrates that avidity contributes significantly to high affinity binding
    • De Crescenzo, G., Pham, P. L., Durocher, Y., and O'Connor-McCourt, M. D. (2003) Transforming growth factor-β (TGF-β) binding to the extracellular domain of the type II TGF-β receptor: receptor capture on a biosensor surface using a new coiled-coil capture system demonstrates that avidity contributes significantly to high affinity binding. J. Mol. Biol. 328, 1173-1183
    • (2003) J. Mol. Biol. , vol.328 , pp. 1173-1183
    • De Crescenzo, G.1    Pham, P.L.2    Durocher, Y.3    O'Connor-McCourt, M.D.4
  • 46
    • 64349095268 scopus 로고    scopus 로고
    • TβR-II discriminates the high-and low-affinity TGF-β isoforms via two hydrogen-bonded ion pairs
    • Baardsnes, J., Hinck, C. S., Hinck, A. P., and O'Connor-McCourt, M. D. (2009) TβR-II discriminates the high-and low-affinity TGF-β isoforms via two hydrogen-bonded ion pairs. Biochemistry 48, 2146-2155
    • (2009) Biochemistry , vol.48 , pp. 2146-2155
    • Baardsnes, J.1    Hinck, C.S.2    Hinck, A.P.3    O'Connor-McCourt, M.D.4
  • 47
    • 36448936383 scopus 로고    scopus 로고
    • TGFβ-SMAD signal transduction: Molecular specificity and functional flexibility
    • Schmierer, B., and Hill, C. S. (2007) TGFβ-SMAD signal transduction: molecular specificity and functional flexibility. Nat. Rev. Mol. Cell Biol. 8, 970-982
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 970-982
    • Schmierer, B.1    Hill, C.S.2
  • 48
    • 0037085441 scopus 로고    scopus 로고
    • Identification and functional characterization of distinct critically important bone morphogenetic protein-specific response elements in the Id1 promoter
    • Korchynskyi, O., and ten Dijke, P. (2002) Identification and functional characterization of distinct critically important bone morphogenetic protein-specific response elements in the Id1 promoter. J. Biol. Chem. 277, 4883-4891
    • (2002) J. Biol. Chem. , vol.277 , pp. 4883-4891
    • Korchynskyi, O.1    Ten Dijke, P.2
  • 50
    • 58749089988 scopus 로고    scopus 로고
    • TGFβ-stimulated Smad1/5 phosphorylation requires the ALK5 L45 loop and mediates the pro-migratory TGFβ switch
    • Liu, I. M., Schilling, S. H., Knouse, K. A., Choy, L., Derynck, R., and Wang, X. F. (2009) TGFβ-stimulated Smad1/5 phosphorylation requires the ALK5 L45 loop and mediates the pro-migratory TGFβ switch. EMBO J. 28, 88-98
    • (2009) EMBO J. , vol.28 , pp. 88-98
    • Liu, I.M.1    Schilling, S.H.2    Knouse, K.A.3    Choy, L.4    Derynck, R.5    Wang, X.F.6
  • 51
    • 55849145475 scopus 로고    scopus 로고
    • Transforming growth factor β-induced Smad1/5 phosphorylation in epithelial cells is mediated by novel receptor complexes and is essential for anchorage-independent growth
    • Daly, A. C., Randall, R. A., and Hill, C. S. (2008) Transforming growth factor β-induced Smad1/5 phosphorylation in epithelial cells is mediated by novel receptor complexes and is essential for anchorage-independent growth. Mol. Cell. Biol. 28, 6889-6902
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 6889-6902
    • Daly, A.C.1    Randall, R.A.2    Hill, C.S.3
  • 52
    • 65649105437 scopus 로고    scopus 로고
    • Transforming growth factor β can stimulate smad1 phosphorylation independently of bone morphogenic protein receptors
    • Wrighton, K. H., Lin, X., Yu, P. B., and Feng, X. H. (2009) Transforming growth factor β can stimulate smad1 phosphorylation independently of bone morphogenic protein receptors. J. Biol. Chem. 284, 9755-9763
    • (2009) J. Biol. Chem. , vol.284 , pp. 9755-9763
    • Wrighton, K.H.1    Lin, X.2    Yu, P.B.3    Feng, X.H.4
  • 53
    • 43149095145 scopus 로고    scopus 로고
    • Bone morphogenetic proteins signal through the transforming growth factor-β type III receptor
    • Kirkbride, K. C., Townsend, T. A., Bruinsma, M. W., Barnett, J. V., and Blobe, G. C. (2008) Bone morphogenetic proteins signal through the transforming growth factor-β type III receptor. J. Biol. Chem. 283, 7628-7637
    • (2008) J. Biol. Chem. , vol.283 , pp. 7628-7637
    • Kirkbride, K.C.1    Townsend, T.A.2    Bruinsma, M.W.3    Barnett, J.V.4    Blobe, G.C.5
  • 54
    • 0027276765 scopus 로고
    • β-Glycan presents ligand to the TGFβ signaling receptor
    • López-Casillas, F., Wrana, J. L., and Massagué, J. (1993) β-Glycan presents ligand to the TGFβ signaling receptor. Cell 73, 1435-1444
    • (1993) Cell , vol.73 , pp. 1435-1444
    • López-Casillas, F.1    Wrana, J.L.2    Massagué, J.3
  • 57
    • 0036085920 scopus 로고    scopus 로고
    • SB-431542 is a potent and specific inhibitor of transforming growth factor-β superfamily type i activin receptor-like kinase (ALK) receptors ALK4, ALK5, and ALK7
    • Inman, G. J., Nicolás, F. J., Callahan, J. F., Harling, J. D., Gaster, L. M., Reith, A. D., Laping, N. J., and Hill, C. S. (2002) SB-431542 is a potent and specific inhibitor of transforming growth factor-β superfamily type I activin receptor-like kinase (ALK) receptors ALK4, ALK5, and ALK7. Mol. Pharmacol. 62, 65-74
    • (2002) Mol. Pharmacol. , vol.62 , pp. 65-74
    • Inman, G.J.1    Nicolás, F.J.2    Callahan, J.F.3    Harling, J.D.4    Gaster, L.M.5    Reith, A.D.6    Laping, N.J.7    Hill, C.S.8
  • 58
    • 0036499549 scopus 로고    scopus 로고
    • Follistatin regulates bone morphogenetic protein-7 (BMP-7) activity to stimulate embryonic muscle growth
    • Amthor, H., Christ, B., Rashid-Doubell, F., Kemp, C. F., Lang, E., and Patel, K. (2002) Follistatin regulates bone morphogenetic protein-7 (BMP-7) activity to stimulate embryonic muscle growth. Dev. Biol. 243, 115-127
    • (2002) Dev. Biol. , vol.243 , pp. 115-127
    • Amthor, H.1    Christ, B.2    Rashid-Doubell, F.3    Kemp, C.F.4    Lang, E.5    Patel, K.6
  • 59
    • 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. U.S.A. 95, 9337-9342
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 60
    • 0034574298 scopus 로고    scopus 로고
    • How cells read TGF-β signals
    • Massagué, J. (2000) How cells read TGF-β signals. Nat. Rev. Mol. Cell Biol. 1, 169-178
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 169-178
    • Massagué, J.1
  • 61
    • 84861653647 scopus 로고    scopus 로고
    • The roles of activin A and its binding protein, follistatin, in inflammation and tissue repair
    • de Kretser, D. M., O'Hehir, R. E., Hardy, C. L., and Hedger, M. P. (2012) The roles of activin A and its binding protein, follistatin, in inflammation and tissue repair. Mol. Cell. Endocrinol. 359, 101-106
    • (2012) Mol. Cell. Endocrinol. , vol.359 , pp. 101-106
    • De Kretser, D.M.1    O'Hehir, R.E.2    Hardy, C.L.3    Hedger, M.P.4
  • 62
    • 63749105935 scopus 로고    scopus 로고
    • Activin and related proteins in inflammation: Not just interested bystanders
    • Phillips, D. J., de Kretser, D. M., and Hedger, M. P. (2009) activin and related proteins in inflammation: not just interested bystanders. Cytokine Growth Factor Rev. 20, 153-164
    • (2009) Cytokine Growth Factor Rev. , vol.20 , pp. 153-164
    • Phillips, D.J.1    De Kretser, D.M.2    Hedger, M.P.3
  • 63
    • 84883240109 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of bone morphogenetic proteins and activins in the skin: Potential benefits for wound healing
    • Moura, J., da Silva, L., Cruz, M. T., and Carvalho, E. (2013) Molecular and cellular mechanisms of bone morphogenetic proteins and activins in the skin: potential benefits for wound healing. Arch. Dermatol. Res. 305, 557-569
    • (2013) Arch. Dermatol. Res. , vol.305 , pp. 557-569
    • Moura, J.1    Da Silva, L.2    Cruz, M.T.3    Carvalho, E.4
  • 64
    • 33744515391 scopus 로고    scopus 로고
    • Roles of activin in tissue repair, fibrosis, and inflammatory disease
    • Werner, S., and Alzheimer, C. (2006) Roles of activin in tissue repair, fibrosis, and inflammatory disease. Cytokine Growth Factor Rev. 17, 157-171
    • (2006) Cytokine Growth Factor Rev. , vol.17 , pp. 157-171
    • Werner, S.1    Alzheimer, C.2
  • 66
    • 0036486076 scopus 로고    scopus 로고
    • Regulation of cell proliferation, apoptosis, and carcinogenesis by activin
    • Chen, Y. G., Lui, H. M., Lin, S. L., Lee, J. M., and Ying, S. Y. (2002) Regulation of cell proliferation, apoptosis, and carcinogenesis by activin. Exp. Biol. Med. 227, 75-87
    • (2002) Exp. Biol. Med. , vol.227 , pp. 75-87
    • Chen, Y.G.1    Lui, H.M.2    Lin, S.L.3    Lee, J.M.4    Ying, S.Y.5
  • 67
    • 26444515002 scopus 로고    scopus 로고
    • The structure of the follistatin:activin complex reveals antagonism of both type i and type II receptor binding
    • Thompson, T. B., Lerch, T. F., Cook, R. W., Woodruff, T. K., and Jardetzky, T. S. (2005) The structure of the follistatin:activin complex reveals antagonism of both type I and type II receptor binding. Dev. Cell 9, 535-543
    • (2005) Dev. Cell , vol.9 , pp. 535-543
    • Thompson, T.B.1    Lerch, T.F.2    Cook, R.W.3    Woodruff, T.K.4    Jardetzky, T.S.5
  • 68
    • 0141864365 scopus 로고    scopus 로고
    • Myostatin signals through a transforming growth factor β-like signaling pathway to block adipogenesis
    • Rebbapragada, A., Benchabane, H., Wrana, J. L., Celeste, A. J., and Attisano, L. (2003) Myostatin signals through a transforming growth factor β-like signaling pathway to block adipogenesis. Mol. Cell. Biol. 23, 7230-7242
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7230-7242
    • Rebbapragada, A.1    Benchabane, H.2    Wrana, J.L.3    Celeste, A.J.4    Attisano, L.5
  • 73
    • 84869140926 scopus 로고    scopus 로고
    • The bright and the dark sides of activin in wound healing and cancer
    • Antsiferova, M., and Werner, S. (2012) The bright and the dark sides of activin in wound healing and cancer. J. Cell Sci. 125, 3929-3937
    • (2012) J. Cell Sci. , vol.125 , pp. 3929-3937
    • Antsiferova, M.1    Werner, S.2
  • 74
    • 0345269804 scopus 로고    scopus 로고
    • Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-β ligand:receptor interactions
    • Thompson, T. B., Woodruff, T. K., and Jardetzky, T. S. (2003) Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-β ligand:receptor interactions. EMBO J. 22, 1555-1566
    • (2003) EMBO J. , vol.22 , pp. 1555-1566
    • Thompson, T.B.1    Woodruff, T.K.2    Jardetzky, T.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.