메뉴 건너뛰기




Volumn 15, Issue 1, 2004, Pages 1-11

The transforming growth factor-β superfamily of receptors

Author keywords

Activin; BMP; GDF; Receptors; Signal transduction; Smads; TGF

Indexed keywords

ENDOGLIN; LIGAND; RECEPTOR SUBTYPE; SMAD PROTEIN; TRANSFORMING GROWTH FACTOR BETA; TRANSFORMING GROWTH FACTOR BETA RECEPTOR;

EID: 1642473157     PISSN: 13596101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cytogfr.2003.10.004     Document Type: Short Survey
Times cited : (402)

References (160)
  • 2
    • 0032979875 scopus 로고    scopus 로고
    • Molecular evolution of a developmental pathway: Phylogenetic analyses of transforming growth factor-beta family ligands
    • Newfeld S.J., Wisotzkey R.G., Kumar S. Molecular evolution of a developmental pathway: phylogenetic analyses of transforming growth factor-beta family ligands. Genetics. 152:1999;783-795.
    • (1999) Genetics , vol.152 , pp. 783-795
    • Newfeld, S.J.1    Wisotzkey, R.G.2    Kumar, S.3
  • 5
    • 0033545215 scopus 로고    scopus 로고
    • Regulation of bone morphogenetic protein activity by pro domains and proprotein convertases
    • Constam D.B., Robertson E.J. Regulation of bone morphogenetic protein activity by pro domains and proprotein convertases. J. Cell Biol. 144:1999;139-149.
    • (1999) J. Cell Biol. , vol.144 , pp. 139-149
    • Constam, D.B.1    Robertson, E.J.2
  • 6
    • 0027122245 scopus 로고
    • Crystal structure of transforming growth factor-beta 2: An unusual fold for the superfamily
    • Daopin S., Piez K.A., Ogawa Y., Davies D.R. Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily. Science. 257:1992;369-373.
    • (1992) Science , vol.257 , pp. 369-373
    • Daopin, S.1    Piez, K.A.2    Ogawa, Y.3    Davies, D.R.4
  • 7
    • 0029943464 scopus 로고    scopus 로고
    • The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: Implications for receptor binding
    • Mittl P.R., Priestle J.P., Cox D.A., McMaster G., Cerletti N., Grutter M.G. The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding. Protein Sci. 5:1996;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
  • 8
    • 8944220232 scopus 로고    scopus 로고
    • Transforming growth factor beta 1: Three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2
    • Hinck A.P., Archer S.J., Qian S.W., Roberts A.B., Sporn M.B., Weatherbee J.A.et al. Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2. Biochemistry. 35:1996;8517-8534.
    • (1996) Biochemistry , vol.35 , pp. 8517-8534
    • Hinck, A.P.1    Archer, S.J.2    Qian, S.W.3    Roberts, A.B.4    Sporn, M.B.5    Weatherbee, J.A.6
  • 9
    • 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., Carlson W.D. Three-dimensional structure of recombinant human osteogenic protein 1: structural paradigm for the transforming growth factor beta superfamily. Proc. Natl. Acad. Sci. USA. 93:1996;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
  • 10
    • 0033582942 scopus 로고    scopus 로고
    • Crystal structure of human bone morphogenetic protein-2 at 2.7 Å resolution
    • Scheufler C., Sebald W., Hulsmeyer M. Crystal structure of human bone morphogenetic protein-2 at 2.7 Å resolution. J. Mol. Biol. 287:1999;103-115.
    • (1999) J. Mol. Biol. , vol.287 , pp. 103-115
    • Scheufler, C.1    Sebald, W.2    Hulsmeyer, M.3
  • 11
    • 0345269804 scopus 로고    scopus 로고
    • Structures of an ActRIIB:activin a complex reveal a novel binding mode for TGF-beta ligand:receptor interactions
    • Thompson T.B., Woodruff T.K., Jardetzky T.S. Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-beta ligand:receptor interactions. EMBO J. 22:2003;1555-1566.
    • (2003) EMBO J. , vol.22 , pp. 1555-1566
    • Thompson, T.B.1    Woodruff, T.K.2    Jardetzky, T.S.3
  • 12
    • 0027401489 scopus 로고
    • GDF-3 and GDF-9: Two new members of the transforming growth factor-beta superfamily containing a novel pattern of cysteines
    • McPherron A.C., Lee S.J. GDF-3 and GDF-9: two new members of the transforming growth factor-beta superfamily containing a novel pattern of cysteines. J. Biol. Chem. 268:1993;3444-3449.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3444-3449
    • McPherron, A.C.1    Lee, S.J.2
  • 13
    • 0034043106 scopus 로고    scopus 로고
    • Crystal structure of the BMP-2-BRIA ectodomain complex
    • Kirsch T., Sebald W., Dreyer M.K. Crystal structure of the BMP-2-BRIA ectodomain complex. Nat. Struct. Biol. 7:2000;492-496.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 492-496
    • Kirsch, T.1    Sebald, W.2    Dreyer, M.K.3
  • 15
    • 0030908028 scopus 로고    scopus 로고
    • Latent transforming growth factor-beta: Structural features and mechanisms of activation
    • Munger J.S., Harpel J.G., Gleizes P.E., Mazzieri R., Nunes I., Rifkin D.B. Latent transforming growth factor-beta: structural features and mechanisms of activation. Kidney Int. 51:1997;1376-1382.
    • (1997) Kidney Int. , vol.51 , pp. 1376-1382
    • Munger, J.S.1    Harpel, J.G.2    Gleizes, P.E.3    Mazzieri, R.4    Nunes, I.5    Rifkin, D.B.6
  • 16
    • 0036399170 scopus 로고    scopus 로고
    • Extracellular regulation of BMP signaling in vertebrates: A cocktail of modulators
    • Balemans W., Van Hul W. Extracellular regulation of BMP signaling in vertebrates: a cocktail of modulators. Dev. Biol. 250:2002;231-250.
    • (2002) Dev. Biol. , vol.250 , pp. 231-250
    • Balemans, W.1    Van Hul, W.2
  • 17
    • 0027328191 scopus 로고
    • Activin receptor-like kinases: A novel subclass of cell-surface receptors with predicted serine/threonine kinase activity
    • ten Dijke P., Ichijo H., Franzen P., Schulz P., Saras J., Toyoshima H.et al. Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity. Oncogene. 8:1993;2879-2887.
    • (1993) Oncogene , vol.8 , pp. 2879-2887
    • Ten Dijke, P.1    Ichijo, H.2    Franzen, P.3    Schulz, P.4    Saras, J.5    Toyoshima, H.6
  • 18
    • 0028295762 scopus 로고
    • Characterization of type I receptors for transforming growth factor-beta and activin
    • ten Dijke P., Yamashita H., Ichijo H., Franzen P., Laiho M., Miyazono K.et al. Characterization of type I receptors for transforming growth factor-beta and activin. Science. 264:1994;101-104.
    • (1994) Science , vol.264 , pp. 101-104
    • Ten Dijke, P.1    Yamashita, H.2    Ichijo, H.3    Franzen, P.4    Laiho, M.5    Miyazono, K.6
  • 19
    • 0037250476 scopus 로고    scopus 로고
    • Consequences of knocking out BMP signaling in the mouse
    • Zhao G.Q. Consequences of knocking out BMP signaling in the mouse. Genesis. 35:2003;43-56.
    • (2003) Genesis , vol.35 , pp. 43-56
    • Zhao, G.Q.1
  • 20
    • 17144454645 scopus 로고    scopus 로고
    • TGF-beta superfamily signaling and left-right asymmetry
    • Whitman M., Mercola M. TGF-beta superfamily signaling and left-right asymmetry. Sci STKE. 2001:2001;RE1.
    • (2001) Sci STKE , vol.2001 , pp. 1
    • Whitman, M.1    Mercola, M.2
  • 21
    • 0035974428 scopus 로고    scopus 로고
    • Studying TGF-beta superfamily signaling by knockouts and knockins
    • Chang H., Lau A.L., Matzuk M.M. Studying TGF-beta superfamily signaling by knockouts and knockins. Mol. Cell Endocrinol. 180:2001;39-46.
    • (2001) Mol. Cell Endocrinol. , vol.180 , pp. 39-46
    • Chang, H.1    Lau, A.L.2    Matzuk, M.M.3
  • 22
    • 0034644472 scopus 로고    scopus 로고
    • TGFbeta signaling in growth control, cancer, and heritable disorders
    • [in process citation]
    • Massague J., Blain S.W., Lo R.S. TGFbeta signaling in growth control, cancer, and heritable disorders. Cell. 103:2000;295-309. [in process citation].
    • (2000) Cell , vol.103 , pp. 295-309
    • Massague, J.1    Blain, S.W.2    Lo, R.S.3
  • 23
  • 24
    • 0034972978 scopus 로고    scopus 로고
    • Germline mutations of the gene encoding bone morphogenetic protein receptor 1A in juvenile polyposis
    • Howe J.R., Bair J.L., Sayed M.G., Anderson M.E., Mitros F.A., Petersen G.M.et al. Germline mutations of the gene encoding bone morphogenetic protein receptor 1A in juvenile polyposis. Nat. Genet. 28:2001;184-187.
    • (2001) Nat. Genet , vol.28 , pp. 184-187
    • Howe, J.R.1    Bair, J.L.2    Sayed, M.G.3    Anderson, M.E.4    Mitros, F.A.5    Petersen, G.M.6
  • 25
    • 0035721752 scopus 로고    scopus 로고
    • Bone morphogenetic proteins, genetics and the pathophysiology of primary pulmonary hypertension
    • de Caestecker M.P., Meyrick B. Bone morphogenetic proteins, genetics and the pathophysiology of primary pulmonary hypertension. Respir. Res. 2:2001;193.
    • (2001) Respir. Res. , vol.2 , pp. 193
    • De Caestecker, M.P.1    Meyrick, B.2
  • 26
    • 0034612789 scopus 로고    scopus 로고
    • Role of transforming growth factor-beta signaling in cancer
    • [in process citation]
    • de Caestecker M.P., Piek E., Roberts A.B. Role of transforming growth factor-beta signaling in cancer. J. Natl. Cancer Inst. 92:2000;1388-1402. [in process citation].
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 1388-1402
    • De Caestecker, M.P.1    Piek, E.2    Roberts, A.B.3
  • 27
    • 0027525105 scopus 로고
    • Identification of human activin and TGF beta type I receptors that form heteromeric kinase complexes with type II receptors
    • Attisano L., Carcamo J., Ventura F., Weis F.M., Massague J., Wrana J.L. Identification of human activin and TGF beta type I receptors that form heteromeric kinase complexes with type II receptors. Cell. 75:1993;671-680.
    • (1993) Cell , vol.75 , pp. 671-680
    • Attisano, L.1    Carcamo, J.2    Ventura, F.3    Weis, F.M.4    Massague, J.5    Wrana, J.L.6
  • 28
    • 12944273545 scopus 로고    scopus 로고
    • Activin receptor-like kinase 1 modulates transforming growth factor-beta 1 signaling in the regulation of angiogenesis
    • Oh S.P., Seki T., Goss K.A., Imamura T., Yi Y., Donahoe P.K.et al. Activin receptor-like kinase 1 modulates transforming growth factor-beta 1 signaling in the regulation of angiogenesis. Proc. Natl. Acad. Sci. USA. 97:2000;2626-2631.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2626-2631
    • Oh, S.P.1    Seki, T.2    Goss, K.A.3    Imamura, T.4    Yi, Y.5    Donahoe, P.K.6
  • 29
    • 0034982133 scopus 로고    scopus 로고
    • The serine/threonine transmembrane receptor ALK2 mediates Mullerian inhibiting substance signaling
    • Visser J.A., Olaso R., Verhoef-Post M., Kramer P., Themmen A.P., Ingraham H.A. The serine/threonine transmembrane receptor ALK2 mediates Mullerian inhibiting substance signaling. Mol Endocrinol. 15:2001;936-945.
    • (2001) Mol Endocrinol , vol.15 , pp. 936-945
    • Visser, J.A.1    Olaso, R.2    Verhoef-Post, M.3    Kramer, P.4    Themmen, A.P.5    Ingraham, H.A.6
  • 30
    • 0028603343 scopus 로고
    • TGF-beta induced transdifferentiation of mammary epithelial cells to mesenchymal cells: Involvement of type I receptors
    • Miettinen P.J., Ebner R., Lopez A.R., Derynck R. TGF-beta induced transdifferentiation of mammary epithelial cells to mesenchymal cells: involvement of type I receptors. J Cell Biol. 127:1994;2021-2036.
    • (1994) J Cell Biol , vol.127 , pp. 2021-2036
    • Miettinen, P.J.1    Ebner, R.2    Lopez, A.R.3    Derynck, R.4
  • 31
    • 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., Wrana J.L. Specific activation of Smad1 signaling pathways by the BMP7 type I receptor, ALK2. J Biol Chem. 273:1998;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
  • 32
    • 0029003377 scopus 로고
    • Osteogenic protein-1 binds to activin type II receptors and induces certain activin-like effects
    • Yamashita H., ten Dijke P., Huylebroeck D., Sampath T.K., Andries M., Smith J.C.et al. Osteogenic protein-1 binds to activin type II receptors and induces certain activin-like effects. J Cell Biol. 130:1995;217-226.
    • (1995) J Cell Biol , vol.130 , pp. 217-226
    • Yamashita, H.1    Ten Dijke, P.2    Huylebroeck, D.3    Sampath, T.K.4    Andries, M.5    Smith, J.C.6
  • 33
    • 0032754669 scopus 로고    scopus 로고
    • Characterization of bone morphogenetic protein-6 signaling pathways in osteoblast differentiation
    • Ebisawa T., Tada K., Kitajima I., Tojo K., Sampath T.K., Kawabata M.et al. Characterization of bone morphogenetic protein-6 signaling pathways in osteoblast differentiation. J Cell Sci. 112:1999;3519-3527.
    • (1999) J Cell Sci , vol.112 , pp. 3519-3527
    • Ebisawa, T.1    Tada, K.2    Kitajima, I.3    Tojo, K.4    Sampath, T.K.5    Kawabata, M.6
  • 34
    • 0028332818 scopus 로고
    • Identification of type I receptors for osteogenic protein-1 and bone morphogenetic protein-4
    • ten Dijke P., Yamashita H., Sampath T.K., Reddi A.H., Estevez M., Riddle D.L.et al. Identification of type I receptors for osteogenic protein-1 and bone morphogenetic protein-4. J Biol Chem. 269:1994;16985-16988.
    • (1994) J Biol Chem , vol.269 , pp. 16985-16988
    • Ten Dijke, P.1    Yamashita, H.2    Sampath, T.K.3    Reddi, A.H.4    Estevez, M.5    Riddle, D.L.6
  • 35
    • 0031918786 scopus 로고    scopus 로고
    • Cartilage-derived morphogenetic proteins and osteogenic protein-1 differentially regulate osteogenesis
    • Erlacher L., McCartney J., Piek E., ten Dijke P., Yanagishita M., Oppermann H.et al. Cartilage-derived morphogenetic proteins and osteogenic protein-1 differentially regulate osteogenesis. J Bone Miner Res. 13:1998;383-392.
    • (1998) J Bone Miner Res , vol.13 , pp. 383-392
    • Erlacher, L.1    McCartney, J.2    Piek, E.3    Ten Dijke, P.4    Yanagishita, M.5    Oppermann, H.6
  • 36
    • 0037414773 scopus 로고    scopus 로고
    • Molecular basis of bone morphogenetic protein-15 signaling in granulosa cells
    • Moore R.K., Otsuka F., Shimasaki S. Molecular basis of bone morphogenetic protein-15 signaling in granulosa cells. J Biol Chem. 278:2003;304-310.
    • (2003) J Biol Chem , vol.278 , pp. 304-310
    • Moore, R.K.1    Otsuka, F.2    Shimasaki, S.3
  • 37
    • 0034623238 scopus 로고    scopus 로고
    • Engagement of bone morphogenetic protein type IB receptor and Smad1 signaling by anti-Mullerian hormone and its type II receptor
    • Gouedard L., Chen Y.G., Thevenet L., Racine C., Borie S., Lamarre I.et al. Engagement of bone morphogenetic protein type IB receptor and Smad1 signaling by anti-Mullerian hormone and its type II receptor. J Biol Chem. 275:2000;27973-27978.
    • (2000) J Biol Chem , vol.275 , pp. 27973-27978
    • Gouedard, L.1    Chen, Y.G.2    Thevenet, L.3    Racine, C.4    Borie, S.5    Lamarre, I.6
  • 38
    • 0029831660 scopus 로고    scopus 로고
    • Identification of type I and type II serine/threonine kinase receptors for growth/differentiation factor-5
    • Nishitoh H., Ichijo H., Kimura M., Matsumoto T., Makishima F., Yamaguchi A.et al. Identification of type I and type II serine/threonine kinase receptors for growth/differentiation factor-5. J Biol Chem. 271:1996;21345-21352.
    • (1996) J Biol Chem , vol.271 , pp. 21345-21352
    • Nishitoh, H.1    Ichijo, H.2    Kimura, M.3    Matsumoto, T.4    Makishima, F.5    Yamaguchi, A.6
  • 39
    • 0035947301 scopus 로고    scopus 로고
    • Nodal signals to Smads through Cripto-dependent and Cripto-independent mechanisms
    • Yeo C., Whitman M. Nodal signals to Smads through Cripto-dependent and Cripto-independent mechanisms. Mol Cell. 7:2001;949-957.
    • (2001) Mol Cell , vol.7 , pp. 949-957
    • Yeo, C.1    Whitman, M.2
  • 40
    • 0036830490 scopus 로고    scopus 로고
    • Activin type IIA and IIB receptors mediate Gdf11 signaling in axial vertebral patterning
    • Oh S.P., Yeo C.Y., Lee Y., Schrewe H., Whitman M., Li E. Activin type IIA and IIB receptors mediate Gdf11 signaling in axial vertebral patterning. Genes Dev. 16:2002;2749-2754.
    • (2002) Genes Dev , vol.16 , pp. 2749-2754
    • Oh, S.P.1    Yeo, C.Y.2    Lee, Y.3    Schrewe, H.4    Whitman, M.5    Li, E.6
  • 41
    • 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., Vale W.W. 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. 17:1997;1682-1691.
    • (1997) Mol Cell Biol , vol.17 , pp. 1682-1691
    • Lebrun, J.J.1    Vale, W.W.2
  • 42
    • 0030060831 scopus 로고    scopus 로고
    • Activation of signalling by the activin receptor complex
    • Attisano L., Wrana J.L., Montalvo E., Massague J. Activation of signalling by the activin receptor complex. Mol Cell Biol. 16:1996;1066-1073.
    • (1996) Mol Cell Biol , vol.16 , pp. 1066-1073
    • Attisano, L.1    Wrana, J.L.2    Montalvo, E.3    Massague, J.4
  • 43
    • 0037229696 scopus 로고    scopus 로고
    • EGF-CFC proteins are essential coreceptors for the TGF-beta signals Vg1 and GDF1
    • Cheng S.K., Olale F., Bennett J.T., Brivanlou A.H., Schier A.F. EGF-CFC proteins are essential coreceptors for the TGF-beta signals Vg1 and GDF1. Genes Dev. 17:2003;31-36.
    • (2003) Genes Dev , vol.17 , pp. 31-36
    • Cheng, S.K.1    Olale, F.2    Bennett, J.T.3    Brivanlou, A.H.4    Schier, A.F.5
  • 44
    • 0026496172 scopus 로고
    • TGF beta signals through a heteromeric protein kinase receptor complex
    • Wrana J.L., Attisano L., Carcamo J., Zentella A., Doody J., Laiho M.et al. TGF beta signals through a heteromeric protein kinase receptor complex. Cell. 71:1992;1003-1014.
    • (1992) Cell , vol.71 , pp. 1003-1014
    • Wrana, J.L.1    Attisano, L.2    Carcamo, J.3    Zentella, A.4    Doody, J.5    Laiho, M.6
  • 45
    • 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.et al. Cloning of a TGF beta type I receptor that forms a heteromeric complex with the TGF beta type II receptor. Cell. 75:1993;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
  • 46
    • 0035425463 scopus 로고    scopus 로고
    • The orphan receptor ALK7 and the Activin receptor ALK4 mediate signaling by Nodal proteins during vertebrate development
    • Reissmann E., Jornvall H., Blokzijl A., Andersson O., Chang C., Minchiotti G.et al. The orphan receptor ALK7 and the Activin receptor ALK4 mediate signaling by Nodal proteins during vertebrate development. Genes Dev. 15:2001;2010-2022.
    • (2001) Genes Dev , vol.15 , pp. 2010-2022
    • Reissmann, E.1    Jornvall, H.2    Blokzijl, A.3    Andersson, O.4    Chang, C.5    Minchiotti, G.6
  • 48
    • 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., Massague J. Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs. Mol Cell Biol. 15:1995;3479-3486.
    • (1995) Mol Cell Biol , vol.15 , pp. 3479-3486
    • Liu, F.1    Ventura, F.2    Doody, J.3    Massague, J.4
  • 49
    • 0037424231 scopus 로고    scopus 로고
    • Inhibin is an antagonist of bone morphogenetic protein signaling
    • Wiater E., Vale W. Inhibin is an antagonist of bone morphogenetic protein signaling. J Biol Chem. 278:2003;7934-7941.
    • (2003) J Biol Chem , vol.278 , pp. 7934-7941
    • Wiater, E.1    Vale, W.2
  • 50
    • 0035979253 scopus 로고    scopus 로고
    • Regulation of myostatin activity and muscle growth
    • Lee S.J., McPherron A.C. Regulation of myostatin activity and muscle growth. Proc Natl Acad Sci USA. 98:2001;9306-9311.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9306-9311
    • Lee, S.J.1    McPherron, A.C.2
  • 51
    • 0037206410 scopus 로고    scopus 로고
    • Properties of inhibin binding to betaglycan, InhBP/p120 and the activin type II receptors
    • Chapman S.C., Bernard D.J., Jelen J., Woodruff T.K. Properties of inhibin binding to betaglycan, InhBP/p120 and the activin type II receptors. Mol Cell Endocrinol. 196:2002;79-93.
    • (2002) Mol Cell Endocrinol , vol.196 , pp. 79-93
    • Chapman, S.C.1    Bernard, D.J.2    Jelen, J.3    Woodruff, T.K.4
  • 53
    • 0029985652 scopus 로고    scopus 로고
    • Formation and activation by phosphorylation of activin receptor complexes
    • Willis S.A., Zimmerman C.M., Li L.I., Mathews L.S. Formation and activation by phosphorylation of activin receptor complexes. Mol Endocrinol. 10:1996;367-379.
    • (1996) Mol Endocrinol , vol.10 , pp. 367-379
    • Willis, S.A.1    Zimmerman, C.M.2    Li, L.I.3    Mathews, L.S.4
  • 54
    • 0028142801 scopus 로고
    • Characterization and cloning of a receptor for BMP-2 and BMP-4 from NIH 3T3 cells
    • Koenig B.B., Cook J.S., Wolsing D.H., Ting J., Tiesman J.P., Correa P.E.et al. Characterization and cloning of a receptor for BMP-2 and BMP-4 from NIH 3T3 cells. Mol Cell Biol. 14:1994;5961-5974.
    • (1994) Mol Cell Biol , vol.14 , pp. 5961-5974
    • Koenig, B.B.1    Cook, J.S.2    Wolsing, D.H.3    Ting, J.4    Tiesman, J.P.5    Correa, P.E.6
  • 55
    • 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.et al. The BMP7/ActRII extracellular domain complex provides new insights into the cooperative nature of receptor assembly. Mol Cell. 11:2003;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
  • 56
    • 0033813903 scopus 로고    scopus 로고
    • Connective tissue growth factor: What's in a name?
    • Moussad E.E., Brigstock D.R. Connective tissue growth factor: what's in a name? Mol Genet Metab. 71:2000;276-292.
    • (2000) Mol Genet Metab , vol.71 , pp. 276-292
    • Moussad, E.E.1    Brigstock, D.R.2
  • 57
    • 0036051343 scopus 로고    scopus 로고
    • Connective-tissue growth factor (CTGF) modulates cell signalling by BMP and TGF-beta
    • Abreu J.G., Ketpura N.I., Reversade B., De Robertis E.M. Connective-tissue growth factor (CTGF) modulates cell signalling by BMP and TGF-beta. Nat Cell Biol. 4:2002;599-604.
    • (2002) Nat Cell Biol , vol.4 , pp. 599-604
    • Abreu, J.G.1    Ketpura, N.I.2    Reversade, B.3    De Robertis, E.M.4
  • 59
    • 0033537831 scopus 로고    scopus 로고
    • Assignment of transforming growth factor beta1 and beta3 and a third new ligand to the type I receptor ALK-1
    • Lux A., Attisano L., Marchuk D.A. Assignment of transforming growth factor beta1 and beta3 and a third new ligand to the type I receptor ALK-1. J Biol Chem. 274:1999;9984-9992.
    • (1999) J Biol Chem , vol.274 , pp. 9984-9992
    • Lux, A.1    Attisano, L.2    Marchuk, D.A.3
  • 60
    • 0027739933 scopus 로고
    • Determination of type I receptor specificity by the type II receptors for TGF-beta or activin
    • Ebner R., Chen R.H., Lawler S., Zioncheck T., Derynck R. Determination of type I receptor specificity by the type II receptors for TGF-beta or activin. Science. 262:1993;900-902.
    • (1993) Science , vol.262 , pp. 900-902
    • Ebner, R.1    Chen, R.H.2    Lawler, S.3    Zioncheck, T.4    Derynck, R.5
  • 61
    • 0037085287 scopus 로고    scopus 로고
    • The mode of bone morphogenetic protein (BMP) receptor oligomerization determines different BMP-2 signaling pathways
    • Nohe A., Hassel S., Ehrlich M., Neubauer F., Sebald W., Henis Y.I.et al. The mode of bone morphogenetic protein (BMP) receptor oligomerization determines different BMP-2 signaling pathways. J Biol Chem. 277:2002;5330-5338.
    • (2002) J Biol Chem , vol.277 , pp. 5330-5338
    • Nohe, A.1    Hassel, S.2    Ehrlich, M.3    Neubauer, F.4    Sebald, W.5    Henis, Y.I.6
  • 62
    • 0033605117 scopus 로고    scopus 로고
    • Transforming growth factor-beta induces formation of a dithiothreitol-resistant type I/type II receptor complex in live cells
    • Wells R.G., Gilboa L., Sun Y., Liu X., Henis Y.I., Lodish H.F. Transforming growth factor-beta induces formation of a dithiothreitol-resistant type I/type II receptor complex in live cells. J Biol Chem. 274:1999;5716-5722.
    • (1999) J Biol Chem , vol.274 , pp. 5716-5722
    • Wells, R.G.1    Gilboa, L.2    Sun, Y.3    Liu, X.4    Henis, Y.I.5    Lodish, H.F.6
  • 63
    • 0027930903 scopus 로고
    • Formation of hetero-oligomeric complexes of type I and type II receptors for transforming growth factor-beta
    • Yamashita H., ten Dijke P., Franzen P., Miyazono K., Heldin C.H. Formation of hetero-oligomeric complexes of type I and type II receptors for transforming growth factor-beta. J Biol Chem. 269:1994;20172-20178.
    • (1994) J Biol Chem , vol.269 , pp. 20172-20178
    • Yamashita, H.1    Ten Dijke, P.2    Franzen, P.3    Miyazono, K.4    Heldin, C.H.5
  • 64
    • 0025323376 scopus 로고
    • Bovine osteogenic protein is composed of dimers of OP-1 and BMP-2A, two members of the transforming growth factor-beta superfamily
    • Sampath T.K., Coughlin J.E., Whetstone R.M., Banach D., Corbett C., Ridge R.J.et al. Bovine osteogenic protein is composed of dimers of OP-1 and BMP-2A, two members of the transforming growth factor-beta superfamily. J Biol Chem. 265:1990;13198-13205.
    • (1990) J Biol Chem , vol.265 , pp. 13198-13205
    • Sampath, T.K.1    Coughlin, J.E.2    Whetstone, R.M.3    Banach, D.4    Corbett, C.5    Ridge, R.J.6
  • 65
    • 0029862206 scopus 로고    scopus 로고
    • Heterodimeric bone morphogenetic proteins show enhanced activity in vitro and in vivo
    • Israel D.I., Nove J., Kerns K.M., Kaufman R.J., Rosen V., Cox K.A.et al. Heterodimeric bone morphogenetic proteins show enhanced activity in vitro and in vivo. Growth Factors. 13:1996;291-300.
    • (1996) Growth Factors , vol.13 , pp. 291-300
    • Israel, D.I.1    Nove, J.2    Kerns, K.M.3    Kaufman, R.J.4    Rosen, V.5    Cox, K.A.6
  • 66
    • 0032102668 scopus 로고    scopus 로고
    • Ventral mesoderm induction and patterning by bone morphogenetic protein heterodimers in Xenopus embryos
    • Nishimatsu S., Thomsen G.H. Ventral mesoderm induction and patterning by bone morphogenetic protein heterodimers in Xenopus embryos. Mech Dev. 74:1998;75-88.
    • (1998) Mech Dev , vol.74 , pp. 75-88
    • Nishimatsu, S.1    Thomsen, G.H.2
  • 67
    • 0034704753 scopus 로고    scopus 로고
    • Betaglycan binds inhibin and can mediate functional antagonism of activin signalling
    • Lewis K.A., Gray P.C., Blount A.L., MacConell L.A., Wiater E., Bilezikjian L.M.et al. Betaglycan binds inhibin and can mediate functional antagonism of activin signalling. Nature. 404:2000;411-414.
    • (2000) Nature , vol.404 , pp. 411-414
    • Lewis, K.A.1    Gray, P.C.2    Blount, A.L.3    MacConell, L.A.4    Wiater, E.5    Bilezikjian, L.M.6
  • 68
    • 0036240683 scopus 로고    scopus 로고
    • Inhibition of Nodal signalling by Lefty mediated through interaction with common receptors and efficient diffusion
    • Sakuma R., Ohnishi Yi Y., Meno C., Fujii H., Juan H., Takeuchi J.et al. Inhibition of Nodal signalling by Lefty mediated through interaction with common receptors and efficient diffusion. Genes Cells. 7:2002;401-412.
    • (2002) Genes Cells , vol.7 , pp. 401-412
    • Sakuma, R.1    Ohnishi Yi, Y.2    Meno, C.3    Fujii, H.4    Juan, H.5    Takeuchi, J.6
  • 69
    • 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., ten Dijke P. Functional antagonism between activin and osteogenic protein-1 in human embryonal carcinoma cells. J Cell Physiol. 180:1999;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
  • 70
    • 0026713747 scopus 로고
    • Transforming growth factor beta (TGF-beta) type V receptor has a TGF-beta-stimulated serine/threonine-specific autophosphorylation activity
    • O'Grady P., Liu Q., Huang S.S., Huang J.S. Transforming growth factor beta (TGF-beta) type V receptor has a TGF-beta-stimulated serine/threonine- specific autophosphorylation activity. J Biol Chem. 267:1992;21033-21037.
    • (1992) J Biol Chem , vol.267 , pp. 21033-21037
    • O'Grady, P.1    Liu, Q.2    Huang, S.S.3    Huang, J.S.4
  • 71
    • 0030856858 scopus 로고    scopus 로고
    • Characterization of a 60-kDa cell surface-associated transforming growth factor-beta binding protein that can interfere with transforming growth factor-beta receptor binding
    • Piek E., Franzen P., Heldin C.H., ten Dijke P. Characterization of a 60-kDa cell surface-associated transforming growth factor-beta binding protein that can interfere with transforming growth factor-beta receptor binding. J Cell Physiol. 173:1997;447-459.
    • (1997) J Cell Physiol , vol.173 , pp. 447-459
    • Piek, E.1    Franzen, P.2    Heldin, C.H.3    Ten Dijke, P.4
  • 72
    • 0034753206 scopus 로고    scopus 로고
    • Characterization of a 150 kDa accessory receptor for TGF-beta 1 on keratinocytes: Direct evidence for a GPI anchor and ligand binding of the released form
    • Tam B.Y., Larouche D., Germain L., Hooper N.M., Philip A. Characterization of a 150 kDa accessory receptor for TGF-beta 1 on keratinocytes: direct evidence for a GPI anchor and ligand binding of the released form. J Cell Biochem. 83:2001;494-507.
    • (2001) J Cell Biochem , vol.83 , pp. 494-507
    • Tam, B.Y.1    Larouche, D.2    Germain, L.3    Hooper, N.M.4    Philip, A.5
  • 73
    • 0025987832 scopus 로고
    • Structure and expression of the membrane proteoglycan betaglycan, a component of the TGF-beta receptor system
    • Lopez-Casillas F., Cheifetz S., Doody J., Andres J.L., Lane W.S., Massague J. Structure and expression of the membrane proteoglycan betaglycan, a component of the TGF-beta receptor system. Cell. 67:1991;785-795.
    • (1991) Cell , vol.67 , pp. 785-795
    • Lopez-Casillas, F.1    Cheifetz, S.2    Doody, J.3    Andres, J.L.4    Lane, W.S.5    Massague, J.6
  • 74
    • 0027276765 scopus 로고
    • Betaglycan presents ligand to the TGF beta signaling receptor
    • Lopez-Casillas F., Wrana J.L., Massague J. Betaglycan presents ligand to the TGF beta signaling receptor. Cell. 73:1993;1435-1444.
    • (1993) Cell , vol.73 , pp. 1435-1444
    • Lopez-Casillas, F.1    Wrana, J.L.2    Massague, J.3
  • 75
    • 0029066003 scopus 로고
    • Expression of transforming growth factor type III receptor in vascular endothelial cells increases their responsiveness to transforming growth factor beta 2
    • Sankar S., Mahooti-Brooks N., Centrella M., McCarthy T.L., Madri J.A. Expression of transforming growth factor type III receptor in vascular endothelial cells increases their responsiveness to transforming growth factor beta 2. J Biol Chem. 270:1995;13567-13572.
    • (1995) J Biol Chem , vol.270 , pp. 13567-13572
    • Sankar, S.1    Mahooti-Brooks, N.2    Centrella, M.3    McCarthy, T.L.4    Madri, J.A.5
  • 76
    • 0035816662 scopus 로고    scopus 로고
    • Functional roles for the cytoplasmic domain of the type III transforming growth factor beta receptor in regulating transforming growth factor beta signaling
    • Blobe G.C., Schiemann W.P., Pepin M.C., Beauchemin M., Moustakas A., Lodish H.F.et al. Functional roles for the cytoplasmic domain of the type III transforming growth factor beta receptor in regulating transforming growth factor beta signaling. J Biol Chem. 276:2001;24627-24637.
    • (2001) J Biol Chem , vol.276 , pp. 24627-24637
    • Blobe, G.C.1    Schiemann, W.P.2    Pepin, M.C.3    Beauchemin, M.4    Moustakas, A.5    Lodish, H.F.6
  • 77
    • 0035955713 scopus 로고    scopus 로고
    • A novel mechanism for regulating transforming growth factor beta (TGF-beta) signaling. Functional modulation of type III TGF-beta receptor expression through interaction with the PDZ domain protein, GIPC
    • Blobe G.C., Liu X., Fang S.J., How T., Lodish H.F. A novel mechanism for regulating transforming growth factor beta (TGF-beta) signaling. Functional modulation of type III TGF-beta receptor expression through interaction with the PDZ domain protein, GIPC. J Biol Chem. 276:2001;39608-39617.
    • (2001) J Biol Chem , vol.276 , pp. 39608-39617
    • Blobe, G.C.1    Liu, X.2    Fang, S.J.3    How, T.4    Lodish, H.F.5
  • 78
    • 0026646785 scopus 로고
    • Endoglin is a component of the transforming growth factor-beta receptor system in human endothelial cells
    • Cheifetz S., Bellon T., Cales C., Vera S., Bernabeu C., Massague J.et al. Endoglin is a component of the transforming growth factor-beta 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    Massague, J.6
  • 79
    • 0033534572 scopus 로고    scopus 로고
    • Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily
    • Barbara N.P., Wrana J.L., Letarte M. Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily. J Biol Chem. 274:1999;584-594.
    • (1999) J Biol Chem , vol.274 , pp. 584-594
    • Barbara, N.P.1    Wrana, J.L.2    Letarte, M.3
  • 80
    • 0028023647 scopus 로고
    • Localization of endoglin, a transforming growth factor-beta binding protein, and of CD44 and integrins in placenta during the first trimester of pregnancy
    • St-Jacques S., Forte M., Lye S.J., Letarte M. Localization of endoglin, a transforming growth factor-beta binding protein, and of CD44 and integrins in placenta during the first trimester of pregnancy. Biol Reprod. 51:1994;405-413.
    • (1994) Biol Reprod , vol.51 , pp. 405-413
    • St-Jacques, S.1    Forte, M.2    Lye, S.J.3    Letarte, M.4
  • 82
    • 0031981468 scopus 로고    scopus 로고
    • Distribution of endoglin in early human development reveals high levels on endocardial cushion tissue mesenchyme during valve formation
    • Qu R., Silver M.M., Letarte M. Distribution of endoglin in early human development reveals high levels on endocardial cushion tissue mesenchyme during valve formation. Cell Tissue Res. 292:1998;333-343.
    • (1998) Cell Tissue Res , vol.292 , pp. 333-343
    • Qu, R.1    Silver, M.M.2    Letarte, M.3
  • 83
    • 0032484022 scopus 로고    scopus 로고
    • Role of endoglin in cellular responses to transforming growth factor-beta. A comparative study with betaglycan
    • Letamendia A., Lastres P., Botella L.M., Raab U., Langa C., Velasco B.et al. Role of endoglin in cellular responses to transforming growth factor-beta. A comparative study with betaglycan. J Biol Chem. 273:1998;33011-33019.
    • (1998) J Biol Chem , vol.273 , pp. 33011-33019
    • Letamendia, A.1    Lastres, P.2    Botella, L.M.3    Raab, U.4    Langa, C.5    Velasco, B.6
  • 84
    • 0033851028 scopus 로고    scopus 로고
    • Endoglin expression on human microvascular endothelial cells association with betaglycan and formation of higher order complexes with TGF-beta signalling receptors
    • Wong S.H., Hamel L., Chevalier S., Philip A. Endoglin expression on human microvascular endothelial cells association with betaglycan and formation of higher order complexes with TGF-beta signalling receptors. Eur J Biochem. 267:2000;5550-5560.
    • (2000) Eur J Biochem , vol.267 , pp. 5550-5560
    • Wong, S.H.1    Hamel, L.2    Chevalier, S.3    Philip, A.4
  • 85
    • 0034237708 scopus 로고    scopus 로고
    • The EGF-CFC gene family in vertebrate development
    • Shen M.M., Schier A.F. The EGF-CFC gene family in vertebrate development. Trends Genet. 16:2000;303-309.
    • (2000) Trends Genet , vol.16 , pp. 303-309
    • Shen, M.M.1    Schier, A.F.2
  • 86
    • 0038642113 scopus 로고    scopus 로고
    • Cripto forms a complex with activin and type II activin receptors and can block activin signaling
    • Gray P.C., Harrison C.A., Vale W. Cripto forms a complex with activin and type II activin receptors and can block activin signaling. Proc Natl Acad Sci USA. 100:2003;5193-5198.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5193-5198
    • Gray, P.C.1    Harrison, C.A.2    Vale, W.3
  • 87
    • 0029882492 scopus 로고    scopus 로고
    • Expression of nma, a novel gene, inversely correlates with the metastatic potential of human melanoma cell lines and xenografts
    • Degen W.G., Weterman M.A., van Groningen J.J., Cornelissen I.M., Lemmers J.P., Agterbos M.A.et al. Expression of nma, a novel gene, inversely correlates with the metastatic potential of human melanoma cell lines and xenografts. Int J Cancer. 65:1996;460-465.
    • (1996) Int J Cancer , vol.65 , pp. 460-465
    • Degen, W.G.1    Weterman, M.A.2    Van Groningen, J.J.3    Cornelissen, I.M.4    Lemmers, J.P.5    Agterbos, M.A.6
  • 90
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson L.N., Noble M.E., Owen D.J. Active and inactive protein kinases: structural basis for regulation. Cell. 85:1996;149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.2    Owen, D.J.3
  • 91
    • 0033524943 scopus 로고    scopus 로고
    • Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12
    • Huse M., Chen Y.G., Massague J., Kuriyan J. Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12. Cell. 96:1999;425-436.
    • (1999) Cell , vol.96 , pp. 425-436
    • Huse, M.1    Chen, Y.G.2    Massague, J.3    Kuriyan, J.4
  • 92
    • 0034796457 scopus 로고    scopus 로고
    • The TGF beta receptor activation process: An inhibitor- to substrate-binding switch
    • Huse M., Muir T.W., Xu L., Chen Y.G., Kuriyan J., Massague J. The TGF beta receptor activation process: an inhibitor- to substrate-binding switch. Mol Cell. 8:2001;671-682.
    • (2001) Mol Cell , vol.8 , pp. 671-682
    • Huse, M.1    Muir, T.W.2    Xu, L.3    Chen, Y.G.4    Kuriyan, J.5    Massague, J.6
  • 93
    • 0030576525 scopus 로고    scopus 로고
    • The immunophilin FKBP12 functions as a common inhibitor of the TGF beta family type I receptors
    • Wang T., Li B.Y., Danielson P.D., Shah P.C., Rockwell S., Lechleider R.J.et al. The immunophilin FKBP12 functions as a common inhibitor of the TGF beta family type I receptors. Cell. 86:1996;435-444.
    • (1996) Cell , vol.86 , pp. 435-444
    • Wang, T.1    Li, B.Y.2    Danielson, P.D.3    Shah, P.C.4    Rockwell, S.5    Lechleider, R.J.6
  • 94
    • 0037157147 scopus 로고    scopus 로고
    • Phosphorylation regulation of the interaction between Smad7 and activin type I receptor
    • Liu X., Nagarajan R.P., Vale W., Chen Y. Phosphorylation regulation of the interaction between Smad7 and activin type I receptor. FEBS Lett. 519:2002;93-98.
    • (2002) FEBS Lett , vol.519 , pp. 93-98
    • Liu, X.1    Nagarajan, R.P.2    Vale, W.3    Chen, Y.4
  • 95
    • 0033602101 scopus 로고    scopus 로고
    • Inhibition of transforming growth factor-beta/SMAD signalling by the interferon-gamma/STAT pathway
    • Ulloa L., Doody J., Massague J. Inhibition of transforming growth factor-beta/SMAD signalling by the interferon-gamma/STAT pathway. Nature. 397:1999;710-713.
    • (1999) Nature , vol.397 , pp. 710-713
    • Ulloa, L.1    Doody, J.2    Massague, J.3
  • 97
    • 0030611757 scopus 로고    scopus 로고
    • Identification of Smad7, a TGFbeta-inducible antagonist of TGF-beta signalling
    • Nakao A., Afrakhte M., Moren A., Nakayama T., Christian J.L., Heuchel R.et al. Identification of Smad7, a TGFbeta-inducible antagonist of TGF-beta signalling. Nature. 389:1997;631-635.
    • (1997) Nature , vol.389 , pp. 631-635
    • Nakao, A.1    Afrakhte, M.2    Moren, A.3    Nakayama, T.4    Christian, J.L.5    Heuchel, R.6
  • 99
    • 12644260471 scopus 로고    scopus 로고
    • Vascular MADs: Two novel MAD-related genes selectively inducible by flow in human vascular endothelium
    • Topper J.N., Cai J., Qiu Y., Anderson K.R., Xu Y.Y., Deeds J.D.et al. Vascular MADs: two novel MAD-related genes selectively inducible by flow in human vascular endothelium. Proc Natl Acad Sci USA. 94:1997;9314-9319.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9314-9319
    • Topper, J.N.1    Cai, J.2    Qiu, Y.3    Anderson, K.R.4    Xu, Y.Y.5    Deeds, J.D.6
  • 100
    • 0034104591 scopus 로고    scopus 로고
    • Smads as transcriptional co-modulators
    • Attisano L., Wrana andJ.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
  • 101
    • 0034678908 scopus 로고    scopus 로고
    • Transcriptional control by the TGF-beta/Smad signaling system
    • Massague J., Wotton D. Transcriptional control by the TGF-beta/Smad signaling system. EMBO J. 19:2000;1745-1754.
    • (2000) EMBO J , vol.19 , pp. 1745-1754
    • Massague, J.1    Wotton, D.2
  • 102
    • 0035032914 scopus 로고    scopus 로고
    • Divergence and convergence of TGF-beta/BMP signaling
    • Miyazono K., Kusanagi K., Inoue H. Divergence and convergence of TGF-beta/BMP signaling. J Cell Physiol. 187:2001;265-276.
    • (2001) J Cell Physiol , vol.187 , pp. 265-276
    • Miyazono, K.1    Kusanagi, K.2    Inoue, H.3
  • 103
    • 0032428684 scopus 로고    scopus 로고
    • SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor
    • Tsukazaki T., Chiang T.A., Davison A.F., Attisano L., Wrana J.L. SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor. Cell. 95:1998;779-791.
    • (1998) Cell , vol.95 , pp. 779-791
    • Tsukazaki, T.1    Chiang, T.A.2    Davison, A.F.3    Attisano, L.4    Wrana, J.L.5
  • 104
    • 0035355473 scopus 로고    scopus 로고
    • The adaptor molecule disabled-2 links the transforming growth factor beta receptors to the Smad pathway
    • Hocevar B.A., Smine A., Xu X.X., Howe P.H. The adaptor molecule disabled-2 links the transforming growth factor beta receptors to the Smad pathway. EMBO J. 20:2001;2789-2801.
    • (2001) EMBO J , vol.20 , pp. 2789-2801
    • Hocevar, B.A.1    Smine, A.2    Xu, X.X.3    Howe, P.H.4
  • 105
    • 0042738094 scopus 로고    scopus 로고
    • TLP, a novel modulator of TGF-beta signaling, has opposite effects on Smad2- and Smad3-dependent signaling
    • Felici A., Wurthner J.U., Parks W.T., Giam L.R., Reiss M., Karpova T.S. et al. TLP, a novel modulator of TGF-beta signaling, has opposite effects on Smad2- and Smad3-dependent signaling. EMBO J. 22:2003;4465-4477.
    • (2003) EMBO J , vol.22 , pp. 4465-4477
    • Felici, A.1    Wurthner, J.U.2    Parks, W.T.3    Giam, L.R.4    Reiss, M.5    Karpova, T.S.6
  • 106
    • 0035379649 scopus 로고    scopus 로고
    • Transforming growth factor-beta receptor-associated protein 1 is a Smad4 chaperone
    • Wurthner J.U., Frank D.B., Felici A., Green H.M., Cao Z., Schneider M.D.et al. Transforming growth factor-beta receptor-associated protein 1 is a Smad4 chaperone. J Biol Chem. 276:2001;19495-19502.
    • (2001) J Biol Chem , vol.276 , pp. 19495-19502
    • Wurthner, J.U.1    Frank, D.B.2    Felici, A.3    Green, H.M.4    Cao, Z.5    Schneider, M.D.6
  • 107
    • 0347927630 scopus 로고    scopus 로고
    • SANE, a novel LEM domain protein, regulates bone morphogenetic protein signaling through interaction with Smad1
    • Raju G.P., Dimova N., Klein P.S., Huang H.C. SANE, a novel LEM domain protein, regulates bone morphogenetic protein signaling through interaction with Smad1. J Biol Chem. 278:2003;428-437.
    • (2003) J Biol Chem , vol.278 , pp. 428-437
    • Raju, G.P.1    Dimova, N.2    Klein, P.S.3    Huang, H.C.4
  • 108
    • 0034462833 scopus 로고    scopus 로고
    • Hgs (Hrs), a FYVE domain protein, is involved in Smad signaling through cooperation with SARA
    • Miura S., Takeshita T., Asao H., Kimura Y., Murata K., Sasaki Y.et al. Hgs (Hrs), a FYVE domain protein, is involved in Smad signaling through cooperation with SARA. Mol Cell Biol. 20:2000;9346-9355.
    • (2000) Mol Cell Biol , vol.20 , pp. 9346-9355
    • Miura, S.1    Takeshita, T.2    Asao, H.3    Kimura, Y.4    Murata, K.5    Sasaki, Y.6
  • 109
    • 0034947962 scopus 로고    scopus 로고
    • Axin facilitates Smad3 activation in the transforming growth factor beta signaling pathway
    • Furuhashi M., Yagi K., Yamamoto H., Furukawa Y., Shimada S., Nakamura Y.et al. Axin facilitates Smad3 activation in the transforming growth factor beta signaling pathway. Mol Cell Biol. 21:2001;5132-5141.
    • (2001) Mol Cell Biol , vol.21 , pp. 5132-5141
    • Furuhashi, M.1    Yagi, K.2    Yamamoto, H.3    Furukawa, Y.4    Shimada, S.5    Nakamura, Y.6
  • 110
    • 0037462502 scopus 로고    scopus 로고
    • Disruption of transforming growth factor-beta signaling in ELF beta-spectrin-deficient mice
    • Tang Y., Katuri V., Dillner A., Mishra B., Deng C.X., Mishra L. Disruption of transforming growth factor-beta signaling in ELF beta-spectrin-deficient mice. Science. 299:2003;574-577.
    • (2003) Science , vol.299 , pp. 574-577
    • Tang, Y.1    Katuri, V.2    Dillner, A.3    Mishra, B.4    Deng, C.X.5    Mishra, L.6
  • 111
    • 0034614708 scopus 로고    scopus 로고
    • Structural basis of Smad2 recognition by the Smad anchor for receptor activation
    • Wu G., Chen Y.G., Ozdamar B., Gyuricza C.A., Chong P.A., Wrana J.L.et al. Structural basis of Smad2 recognition by the Smad anchor for receptor activation. Science. 287:2000;92-97.
    • (2000) Science , vol.287 , pp. 92-97
    • Wu, G.1    Chen, Y.G.2    Ozdamar, B.3    Gyuricza, C.A.4    Chong, P.A.5    Wrana, J.L.6
  • 112
    • 0033524945 scopus 로고    scopus 로고
    • Smad1 recognition and activation by the ALK1 group of transforming growth factor-beta family receptors
    • Chen Y.G., Massague J. Smad1 recognition and activation by the ALK1 group of transforming growth factor-beta family receptors. J Biol Chem. 274:1999;3672-3677.
    • (1999) J Biol Chem , vol.274 , pp. 3672-3677
    • Chen, Y.G.1    Massague, J.2
  • 113
    • 0032528055 scopus 로고    scopus 로고
    • Determinants of specificity in TGF-beta signal transduction
    • Chen Y.G., Hata A., Lo R.S., Wotton D., Shi Y., Pavletich N.et al. Determinants of specificity in TGF-beta signal transduction. Genes Dev. 12:1998;2144-2152.
    • (1998) Genes Dev , vol.12 , pp. 2144-2152
    • Chen, Y.G.1    Hata, A.2    Lo, R.S.3    Wotton, D.4    Shi, Y.5    Pavletich, N.6
  • 114
    • 0037007226 scopus 로고    scopus 로고
    • Balancing the activation state of the endothelium via two distinct TGF-beta type I receptors
    • Goumans M.J., Valdimarsdottir G., Itoh S., Rosendahl A., Sideras P., ten Dijke P. Balancing the activation state of the endothelium via two distinct TGF-beta type I receptors. EMBO J. 21:2002;1743-1753.
    • (2002) EMBO J , vol.21 , pp. 1743-1753
    • Goumans, M.J.1    Valdimarsdottir, G.2    Itoh, S.3    Rosendahl, A.4    Sideras, P.5    Ten Dijke, P.6
  • 115
    • 0036888627 scopus 로고    scopus 로고
    • Targets of transcriptional regulation by two distinct type I receptors for transforming growth factor-beta in human umbilical vein endothelial cells
    • Ota T., Fujii M., Sugizaki T., Ishii M., Miyazawa K., Aburatani H.et al. Targets of transcriptional regulation by two distinct type I receptors for transforming growth factor-beta in human umbilical vein endothelial cells. J Cell Physiol. 193:2002;299-318.
    • (2002) J Cell Physiol , vol.193 , pp. 299-318
    • Ota, T.1    Fujii, M.2    Sugizaki, T.3    Ishii, M.4    Miyazawa, K.5    Aburatani, H.6
  • 116
    • 0034011765 scopus 로고    scopus 로고
    • Regulation of signal transduction by endocytosis
    • Ceresa B.P., Schmid S.L. Regulation of signal transduction by endocytosis. Curr Opin Cell Biol. 12:2000;204-210.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 204-210
    • Ceresa, B.P.1    Schmid, S.L.2
  • 117
    • 0037598870 scopus 로고    scopus 로고
    • Distinct endocytic pathways regulate TGF-beta receptor signalling and turnover
    • Di Guglielmo G.M., Le Roy C., Goodfellow A.F., Wrana J.L. Distinct endocytic pathways regulate TGF-beta receptor signalling and turnover. Nat Cell Biol. 5:2003;410-421.
    • (2003) Nat Cell Biol , vol.5 , pp. 410-421
    • Di Guglielmo, G.M.1    Le Roy, C.2    Goodfellow, A.F.3    Wrana, J.L.4
  • 118
    • 0036272313 scopus 로고    scopus 로고
    • Internalization-dependent and -independent requirements for transforming growth factor beta receptor signaling via the Smad pathway
    • Penheiter S.G., Mitchell H., Garamszegi N., Edens M., Dore J.J. Jr., Leof E.B. Internalization-dependent and -independent requirements for transforming growth factor beta receptor signaling via the Smad pathway. Mol Cell Biol. 22:2002;4750-4759.
    • (2002) Mol Cell Biol , vol.22 , pp. 4750-4759
    • Penheiter, S.G.1    Mitchell, H.2    Garamszegi, N.3    Edens, M.4    Dore Jr., J.J.5    Leof, E.B.6
  • 119
    • 0035794218 scopus 로고    scopus 로고
    • Caveolin-1 regulates transforming growth factor (TGF)-beta/SMAD signaling through an interaction with the TGF-beta type I receptor
    • Razani B., Zhang X.L., Bitzer M., von Gersdorff G., Bottinger E.P., Lisanti M.P. Caveolin-1 regulates transforming growth factor (TGF)-beta/SMAD signaling through an interaction with the TGF-beta type I receptor. J Biol Chem. 276:2001;6727-6738.
    • (2001) J Biol Chem , vol.276 , pp. 6727-6738
    • Razani, B.1    Zhang, X.L.2    Bitzer, M.3    Von Gersdorff, G.4    Bottinger, E.P.5    Lisanti, M.P.6
  • 120
    • 0034517389 scopus 로고    scopus 로고
    • Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation
    • Kavsak P., Rasmussen R.K., Causing C.G., Bonni S., Zhu H., Thomsen G.H. et al. Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation. Mol Cell. 6:2000;1365-1375.
    • (2000) Mol Cell , vol.6 , pp. 1365-1375
    • Kavsak, P.1    Rasmussen, R.K.2    Causing, C.G.3    Bonni, S.4    Zhu, H.5    Thomsen, G.H.6
  • 121
    • 0035374391 scopus 로고    scopus 로고
    • Sorting nexin 6, a novel SNX, interacts with the transforming growth factor-beta family of receptor serine-threonine kinases
    • Parks W.T., Frank D.B., Huff C., Renfrew Haft C., Martin J., Meng X.et al. Sorting nexin 6, a novel SNX, interacts with the transforming growth factor-beta family of receptor serine-threonine kinases. J Biol Chem. 276:2001;19332-19339.
    • (2001) J Biol Chem , vol.276 , pp. 19332-19339
    • Parks, W.T.1    Frank, D.B.2    Huff, C.3    Renfrew Haft, C.4    Martin, J.5    Meng, X.6
  • 122
    • 0037131283 scopus 로고    scopus 로고
    • Smurf1 regulates the inhibitory activity of Smad7 by targeting Smad7 to the plasma membrane
    • Suzuki C., Murakami G., Fukuchi M., Shimanuki T., Shikauchi Y., Imamura T.et al. Smurf1 regulates the inhibitory activity of Smad7 by targeting Smad7 to the plasma membrane. J Biol Chem. 277:2002;39919-39925.
    • (2002) J Biol Chem , vol.277 , pp. 39919-39925
    • Suzuki, C.1    Murakami, G.2    Fukuchi, M.3    Shimanuki, T.4    Shikauchi, Y.5    Imamura, T.6
  • 123
    • 0035918274 scopus 로고    scopus 로고
    • Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation
    • Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T.et al. Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation. J Biol Chem. 276:2001;12477-12480.
    • (2001) J Biol Chem , vol.276 , pp. 12477-12480
    • Ebisawa, T.1    Fukuchi, M.2    Murakami, G.3    Chiba, T.4    Tanaka, K.5    Imamura, T.6
  • 124
    • 0030609939 scopus 로고    scopus 로고
    • TGFbeta regulation of mitogen-activated protein kinases in human breast cancer cells
    • Frey R.S., Mulder K.M. TGFbeta regulation of mitogen-activated protein kinases in human breast cancer cells. Cancer Lett. 117:1997;41-50.
    • (1997) Cancer Lett , vol.117 , pp. 41-50
    • Frey, R.S.1    Mulder, K.M.2
  • 125
    • 0035957924 scopus 로고    scopus 로고
    • Transcriptional cross-talk between Smad, ERK1/2, and p38 mitogen-activated protein kinase pathways regulates transforming growth factor-beta-induced aggrecan gene expression in chondrogenic ATDC5 cells
    • Watanabe H., de Caestecker M.P., Yamada Y. Transcriptional cross-talk between Smad, ERK1/2, and p38 mitogen-activated protein kinase pathways regulates transforming growth factor-beta-induced aggrecan gene expression in chondrogenic ATDC5 cells. J Biol Chem. 276:2001;14466-14473.
    • (2001) J Biol Chem , vol.276 , pp. 14466-14473
    • Watanabe, H.1    De Caestecker, M.P.2    Yamada, Y.3
  • 126
    • 0042704734 scopus 로고    scopus 로고
    • Cross-talk between ERK MAP kinase and Smad signaling pathways enhances TGF-beta-dependent responses in human mesangial cells
    • Hayashida T., de caestecker M., Schnaper H.W. Cross-talk between ERK MAP kinase and Smad signaling pathways enhances TGF-beta-dependent responses in human mesangial cells. FASEB J. 17:2003;1576-1578.
    • (2003) FASEB J , vol.17 , pp. 1576-1578
    • Hayashida, T.1    De Caestecker, M.2    Schnaper, H.W.3
  • 127
    • 0028937610 scopus 로고
    • Transforming growth factor beta activation of p44mapk in proliferating cultures of epithelial cells
    • Hartsough M.T., Mulder K.M. Transforming growth factor beta activation of p44mapk in proliferating cultures of epithelial cells. J Biol Chem. 270:1995;7117-7124.
    • (1995) J Biol Chem , vol.270 , pp. 7117-7124
    • Hartsough, M.T.1    Mulder, K.M.2
  • 128
    • 0033601179 scopus 로고    scopus 로고
    • Interdependent SMAD and JNK signaling in transforming growth factor-beta-mediated transcription
    • Engel M.E., McDonnell M.A., Law B.K., Moses H.L. Interdependent SMAD and JNK signaling in transforming growth factor-beta-mediated transcription. J Biol Chem. 274:1999;37413-37420.
    • (1999) J Biol Chem , vol.274 , pp. 37413-37420
    • Engel, M.E.1    McDonnell, M.A.2    Law, B.K.3    Moses, H.L.4
  • 129
    • 0033104505 scopus 로고    scopus 로고
    • TGF-beta induces fibronectin synthesis through a c-Jun N-terminal kinase-dependent, Smad4-independent pathway
    • Hocevar B.A., Brown T.L., Howe P.H. TGF-beta induces fibronectin synthesis through a c-Jun N-terminal kinase-dependent, Smad4-independent pathway. EMBO J. 18:1999;1345-1356.
    • (1999) EMBO J , vol.18 , pp. 1345-1356
    • Hocevar, B.A.1    Brown, T.L.2    Howe, P.H.3
  • 130
    • 0031035582 scopus 로고    scopus 로고
    • Evidence for a role of Rho-like GTPases and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) in transforming growth factor beta-mediated signaling
    • Atfi A., Djelloul S., Chastre E., Davis R., Gespach C. Evidence for a role of Rho-like GTPases and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) in transforming growth factor beta-mediated signaling. J Biol Chem. 272:1997;1429-1432.
    • (1997) J Biol Chem , vol.272 , pp. 1429-1432
    • Atfi, A.1    Djelloul, S.2    Chastre, E.3    Davis, R.4    Gespach, C.5
  • 131
    • 0037849935 scopus 로고    scopus 로고
    • Transforming growth factor-beta1 potentiates renal tubular epithelial cell death by a mechanism independent of Smad signaling
    • Dai C., Yang J., Liu Y. Transforming growth factor-beta1 potentiates renal tubular epithelial cell death by a mechanism independent of Smad signaling. J Biol Chem. 278:2003;12537-12545.
    • (2003) J Biol Chem , vol.278 , pp. 12537-12545
    • Dai, C.1    Yang, J.2    Liu, Y.3
  • 132
    • 0037099745 scopus 로고    scopus 로고
    • TGF-beta receptor-activated p38 MAP kinase mediates Smad-independent TGF-beta responses
    • Yu L., Hebert M.C., Zhang Y.E. TGF-beta receptor-activated p38 MAP kinase mediates Smad-independent TGF-beta responses. EMBO J. 21:2002;3749-3759.
    • (2002) EMBO J , vol.21 , pp. 3749-3759
    • Yu, L.1    Hebert, M.C.2    Zhang, Y.E.3
  • 133
    • 0034711307 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase function is required for transforming growth factor beta-mediated epithelial to mesenchymal transition and cell migration
    • Bakin A.V., Tomlinson A.K., Bhowmick N.A., Moses H.L., Arteaga C.L. Phosphatidylinositol 3-kinase function is required for transforming growth factor beta-mediated epithelial to mesenchymal transition and cell migration. J Biol Chem. 275:2000;36803-36810.
    • (2000) J Biol Chem , vol.275 , pp. 36803-36810
    • Bakin, A.V.1    Tomlinson, A.K.2    Bhowmick, N.A.3    Moses, H.L.4    Arteaga, C.L.5
  • 134
    • 0031417544 scopus 로고    scopus 로고
    • TGF-beta 1 modulates EGF-stimulated phosphatidylinositol 3-kinase activity in human airway smooth muscle cells
    • Krymskaya V.P., Hoffman R., Eszterhas A., Ciocca V., Panettieri R.A. Jr. TGF-beta 1 modulates EGF-stimulated phosphatidylinositol 3-kinase activity in human airway smooth muscle cells. Am J Physiol. 273:1997;L1220-1227.
    • (1997) Am J Physiol , vol.273 , pp. 1220-1227
    • Krymskaya, V.P.1    Hoffman, R.2    Eszterhas, A.3    Ciocca, V.4    Panettieri Jr., R.A.5
  • 135
    • 0037031854 scopus 로고    scopus 로고
    • Requirement of BMP-2-induced phosphatidylinositol 3-kinase and Akt serine/threonine kinase in osteoblast differentiation and Smad- dependent BMP-2 gene transcription
    • Ghosh-Choudhury N., Abboud S.L., Nishimura R., Celeste A., Mahimainathan L., Choudhury G.G. Requirement of BMP-2-induced phosphatidylinositol 3-kinase and Akt serine/threonine kinase in osteoblast differentiation and Smad- dependent BMP-2 gene transcription. J Biol Chem. 277:2002;33361-33368.
    • (2002) J Biol Chem , vol.277 , pp. 33361-33368
    • Ghosh-Choudhury, N.1    Abboud, S.L.2    Nishimura, R.3    Celeste, A.4    Mahimainathan, L.5    Choudhury, G.G.6
  • 136
    • 0041883785 scopus 로고    scopus 로고
    • Smad3 and PKC{delta} mediate TGF-{beta}1-induced collagen I expression in human mesangial cells
    • Runyan C.E., Schnaper H.W., Poncelet A.C. Smad3 and PKC{delta} mediate TGF-{beta}1-induced collagen I expression in human mesangial cells. Am J Physiol Renal Physiol. 285:2003;F413-F422.
    • (2003) Am J Physiol Renal Physiol , vol.285
    • Runyan, C.E.1    Schnaper, H.W.2    Poncelet, A.C.3
  • 137
    • 0035800764 scopus 로고    scopus 로고
    • Bone morphogenetic protein-2 promotes osteoblast apoptosis through a Smad-independent, protein kinase C-dependent signaling pathway
    • Hay E., Lemonnier J., Fromigue O., Marie P.J. Bone morphogenetic protein-2 promotes osteoblast apoptosis through a Smad-independent, protein kinase C-dependent signaling pathway. J Biol Chem. 276:2001;29028-29036.
    • (2001) J Biol Chem , vol.276 , pp. 29028-29036
    • Hay, E.1    Lemonnier, J.2    Fromigue, O.3    Marie, P.J.4
  • 138
    • 0037005903 scopus 로고    scopus 로고
    • Inhibition of PI3K/p70 S6K and p38 MAPK cascades increases osteoblastic differentiation induced by BMP-2
    • Vinals F., Lopez-Rovira T., Rosa J.L., Ventura F. Inhibition of PI3K/p70 S6K and p38 MAPK cascades increases osteoblastic differentiation induced by BMP-2. FEBS Lett. 510:2002;99-104.
    • (2002) FEBS Lett , vol.510 , pp. 99-104
    • Vinals, F.1    Lopez-Rovira, T.2    Rosa, J.L.3    Ventura, F.4
  • 139
    • 0034671578 scopus 로고    scopus 로고
    • TGF-beta inhibits p70 S6 kinase via protein phosphatase 2A to induce G(1) arrest
    • Petritsch C., Beug H., Balmain A., Oft M. TGF-beta inhibits p70 S6 kinase via protein phosphatase 2A to induce G(1) arrest. Genes Dev. 14:2000;3093-3101.
    • (2000) Genes Dev , vol.14 , pp. 3093-3101
    • Petritsch, C.1    Beug, H.2    Balmain, A.3    Oft, M.4
  • 140
    • 0037126380 scopus 로고    scopus 로고
    • Both the Smad and p38 MAPK pathways play a crucial role in Runx2 expression following induction by transforming growth factor-beta and bone morphogenetic protein
    • Lee K.S., Hong S.H., Bae S.C. Both the Smad and p38 MAPK pathways play a crucial role in Runx2 expression following induction by transforming growth factor-beta and bone morphogenetic protein. Oncogene. 21:2002;7156-7163.
    • (2002) Oncogene , vol.21 , pp. 7156-7163
    • Lee, K.S.1    Hong, S.H.2    Bae, S.C.3
  • 141
    • 0034906821 scopus 로고    scopus 로고
    • TGF-beta-induced apoptosis is mediated by the adapter protein Daxx that facilitates JNK activation
    • Perlman R., Schiemann W.P., Brooks M.W., Lodish H.F., Weinberg R.A. TGF-beta-induced apoptosis is mediated by the adapter protein Daxx that facilitates JNK activation. Nat Cell Biol. 3:2001;708-714.
    • (2001) Nat Cell Biol , vol.3 , pp. 708-714
    • Perlman, R.1    Schiemann, W.P.2    Brooks, M.W.3    Lodish, H.F.4    Weinberg, R.A.5
  • 142
    • 0037423374 scopus 로고    scopus 로고
    • Elucidation of Smad requirement in transforming growth factor-beta type I receptor-induced responses
    • Itoh S., Thorikay M., Kowanetz M., Moustakas A., Itoh F., Heldin C.H.et al. Elucidation of Smad requirement in transforming growth factor-beta type I receptor-induced responses. J Biol Chem. 278:2003;3751-3761.
    • (2003) J Biol Chem , vol.278 , pp. 3751-3761
    • Itoh, S.1    Thorikay, M.2    Kowanetz, M.3    Moustakas, A.4    Itoh, F.5    Heldin, C.H.6
  • 143
    • 0042847362 scopus 로고    scopus 로고
    • Transforming growth factor-beta-Smad signaling pathway negatively regulates nontypeable Haemophilus influenzae-induced MUC5AC mucin transcription via mitogen-activated protein kinase (MAPK) phosphatase-1-dependent inhibition of p38 MAPK
    • Jono H., Xu H., Kai H., Lim D.J., Kim Y.S., Feng X.H.et al. Transforming growth factor-beta-Smad signaling pathway negatively regulates nontypeable Haemophilus influenzae-induced MUC5AC mucin transcription via mitogen-activated protein kinase (MAPK) phosphatase-1-dependent inhibition of p38 MAPK. J Biol Chem. 278:2003;27811-27819.
    • (2003) J Biol Chem , vol.278 , pp. 27811-27819
    • Jono, H.1    Xu, H.2    Kai, H.3    Lim, D.J.4    Kim, Y.S.5    Feng, X.H.6
  • 144
    • 0030961008 scopus 로고    scopus 로고
    • Activation of the hematopoietic progenitor kinase-1 (HPK1)-dependent, stress-activated c-Jun N-terminal kinase (JNK) pathway by transforming growth factor beta (TGF-beta)-activated kinase (TAK1), a kinase mediator of TGF beta signal transduction
    • Wang W., Zhou G., Hu M.C., Yao Z., Tan T.H. Activation of the hematopoietic progenitor kinase-1 (HPK1)-dependent, stress-activated c-Jun N-terminal kinase (JNK) pathway by transforming growth factor beta (TGF-beta)-activated kinase (TAK1), a kinase mediator of TGF beta signal transduction. J Biol Chem. 272:1997;22771-22775.
    • (1997) J Biol Chem , vol.272 , pp. 22771-22775
    • Wang, W.1    Zhou, G.2    Hu, M.C.3    Yao, Z.4    Tan, T.H.5
  • 145
    • 0033531954 scopus 로고    scopus 로고
    • Hematopoietic progenitor kinase 1 is a component of transforming growth factor beta-induced c-Jun N-terminal kinase signaling cascade
    • Zhou G., Lee S.C., Yao Z., Tan T.H. Hematopoietic progenitor kinase 1 is a component of transforming growth factor beta-induced c-Jun N-terminal kinase signaling cascade. J Biol Chem. 274:1999;13133-13138.
    • (1999) J Biol Chem , vol.274 , pp. 13133-13138
    • Zhou, G.1    Lee, S.C.2    Yao, Z.3    Tan, T.H.4
  • 146
    • 0029788015 scopus 로고    scopus 로고
    • Altered transforming growth factor signaling in epithelial cells when ras activation is blocked
    • Hartsough M.T., Frey R.S., Zipfel P.A., Buard A., Cook S.J., McCormick F., Mulder K.M. Altered transforming growth factor signaling in epithelial cells when ras activation is blocked. J Biol Chem. 271:1996;22368-22375.
    • (1996) J Biol Chem , vol.271 , pp. 22368-22375
    • Hartsough, M.T.1    Frey, R.S.2    Zipfel, P.A.3    Buard, A.4    Cook, S.J.5    McCormick, F.6    Mulder, K.M.7
  • 147
    • 0033578721 scopus 로고    scopus 로고
    • Involvement of the p38 mitogen-activated protein kinase pathway in transforming growth factor-beta-induced gene expression
    • Hanafusa H., Ninomiya-Tsuji J., Masuyama N., Nishita M., Fujisawa J., Shibuya H.et al. Involvement of the p38 mitogen-activated protein kinase pathway in transforming growth factor-beta-induced gene expression. J Biol Chem. 274:1999;27161-27167.
    • (1999) J Biol Chem , vol.274 , pp. 27161-27167
    • Hanafusa, H.1    Ninomiya-Tsuji, J.2    Masuyama, N.3    Nishita, M.4    Fujisawa, J.5    Shibuya, H.6
  • 148
    • 0033521529 scopus 로고    scopus 로고
    • XIAP, a cellular member of the inhibitor of apoptosis protein family, links the receptors to TAB1-TAK1 in the BMP signaling pathway
    • Yamaguchi K., Nagai S., Ninomiya-Tsuji J., Nishita M., Tamai K., Irie K.et al. XIAP, a cellular member of the inhibitor of apoptosis protein family, links the receptors to TAB1-TAK1 in the BMP signaling pathway. EMBO J. 18:1999;179-187.
    • (1999) EMBO J , vol.18 , pp. 179-187
    • Yamaguchi, K.1    Nagai, S.2    Ninomiya-Tsuji, J.3    Nishita, M.4    Tamai, K.5    Irie, K.6
  • 149
    • 0035854738 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis protein functions as a cofactor in transforming growth factor-beta signaling
    • Birkey Reffey S., Wurthner J.U., Parks W.T., Roberts A.B., Duckett C.S. X-linked inhibitor of apoptosis protein functions as a cofactor in transforming growth factor-beta signaling. J Biol Chem. 276:2001;26542-26549.
    • (2001) J Biol Chem , vol.276 , pp. 26542-26549
    • Birkey Reffey, S.1    Wurthner, J.U.2    Parks, W.T.3    Roberts, A.B.4    Duckett, C.S.5
  • 150
    • 0035185853 scopus 로고    scopus 로고
    • Transforming growth factor-beta1 mediates epithelial to mesenchymal transdifferentiation through a RhoA-dependent mechanism
    • Bhowmick N.A., Ghiassi M., Bakin A., Aakre M., Lundquist C.A., Engel M.E.et al. Transforming growth factor-beta1 mediates epithelial to mesenchymal transdifferentiation through a RhoA-dependent mechanism. Mol Biol Cell. 12:2001;27-36.
    • (2001) Mol Biol Cell , vol.12 , pp. 27-36
    • Bhowmick, N.A.1    Ghiassi, M.2    Bakin, A.3    Aakre, M.4    Lundquist, C.A.5    Engel, M.E.6
  • 151
    • 0041842627 scopus 로고    scopus 로고
    • Cytoskeletal rearrangement and signal transduction in TGF-beta1-stimulated mesangial cell collagen accumulation
    • Hubchak S.C., Runyan C.E., Kreisberg J.I., Schnaper H.W. Cytoskeletal rearrangement and signal transduction in TGF-beta1-stimulated mesangial cell collagen accumulation. J Am Soc Nephrol. 14:2003;1969-1980.
    • (2003) J Am Soc Nephrol , vol.14 , pp. 1969-1980
    • Hubchak, S.C.1    Runyan, C.E.2    Kreisberg, J.I.3    Schnaper, H.W.4
  • 152
    • 0033603816 scopus 로고    scopus 로고
    • Activin a and TGF-beta stimulate phosphorylation of focal adhesion proteins and cytoskeletal reorganization in rat aortic smooth muscle cells
    • Riedy M.C., Brown M.C., Molloy C.J., Turner C.E. Activin A and TGF-beta stimulate phosphorylation of focal adhesion proteins and cytoskeletal reorganization in rat aortic smooth muscle cells. Exp Cell Res. 251:1999;194-202.
    • (1999) Exp Cell Res , vol.251 , pp. 194-202
    • Riedy, M.C.1    Brown, M.C.2    Molloy, C.J.3    Turner, C.E.4
  • 154
    • 0036197606 scopus 로고    scopus 로고
    • Transforming growth factor-beta-induced mobilization of actin cytoskeleton requires signaling by small GTPases Cdc42 and RhoA
    • Edlund S., Landstrom M., Heldin C.H., Aspenstrom P. Transforming growth factor-beta-induced mobilization of actin cytoskeleton requires signaling by small GTPases Cdc42 and RhoA. Mol Biol Cell. 13:2002;902-914.
    • (2002) Mol Biol Cell , vol.13 , pp. 902-914
    • Edlund, S.1    Landstrom, M.2    Heldin, C.H.3    Aspenstrom, P.4
  • 155
  • 156
    • 0041440180 scopus 로고    scopus 로고
    • Nuclear translocation of LIM kinase mediates Rho-Rho kinase regulation of cyclin D1 expression
    • Roovers K., Klein E.A., Castagnino P., Assoian R.K. Nuclear translocation of LIM kinase mediates Rho-Rho kinase regulation of cyclin D1 expression. Dev Cell. 5:2003;273-284.
    • (2003) Dev Cell , vol.5 , pp. 273-284
    • Roovers, K.1    Klein, E.A.2    Castagnino, P.3    Assoian, R.K.4
  • 157
    • 0036714017 scopus 로고    scopus 로고
    • Inhibition of transforming growth factor-beta signaling by low molecular weight compounds interfering with ATP- or substrate-binding sites of the TGF beta type I receptor kinase
    • Yakymovych I., Engstrom U., Grimsby S., Heldin C.H., Souchelnytskyi S. Inhibition of transforming growth factor-beta signaling by low molecular weight compounds interfering with ATP- or substrate-binding sites of the TGF beta type I receptor kinase. Biochemistry. 41:2002;11000-11007.
    • (2002) Biochemistry , vol.41 , pp. 11000-11007
    • Yakymovych, I.1    Engstrom, U.2    Grimsby, S.3    Heldin, C.H.4    Souchelnytskyi, S.5
  • 158
    • 0036085920 scopus 로고    scopus 로고
    • SB-431542 is a potent and specific inhibitor of transforming growth factor-beta superfamily type I activin receptor-like kinase (ALK) receptors ALK4, ALK5, and ALK7
    • Inman G.J., Nicolas F.J., Callahan J.F., Harling J.D., Gaster L.M., Reith A.D.et al. SB-431542 is a potent and specific inhibitor of transforming growth factor-beta superfamily type I activin receptor-like kinase (ALK) receptors ALK4, ALK5, and ALK7. Mol Pharmacol. 62:2002;65-74.
    • (2002) Mol Pharmacol , vol.62 , pp. 65-74
    • Inman, G.J.1    Nicolas, F.J.2    Callahan, J.F.3    Harling, J.D.4    Gaster, L.M.5    Reith, A.D.6
  • 159
    • 0037186459 scopus 로고    scopus 로고
    • Identification of novel inhibitors of the transforming growth factor beta1 (TGF-beta1) type 1 receptor (ALK5)
    • Callahan J.F., Burgess J.L., Fornwald J.A., Gaster L.M., Harling J.D., Harrington F.P.et al. Identification of novel inhibitors of the transforming growth factor beta1 (TGF-beta1) type 1 receptor (ALK5). J Med Chem. 45:2002;999-1001.
    • (2002) J Med Chem , vol.45 , pp. 999-1001
    • Callahan, J.F.1    Burgess, J.L.2    Fornwald, J.A.3    Gaster, L.M.4    Harling, J.D.5    Harrington, F.P.6
  • 160
    • 0141864365 scopus 로고    scopus 로고
    • Myostatin signals through a transforming growth factor beta-like signaling pathway to block adipogenesis
    • Rebbapragada A., Benchabane H., Wrana J.L., Celeste A.J., Attisano L. Myostatin signals through a transforming growth factor beta-like signaling pathway to block adipogenesis. Mol Cell Biol. 23:2003;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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.