메뉴 건너뛰기




Volumn 1773, Issue 3, 2007, Pages 427-439

TGFβ1 regulation of vimentin gene expression during differentiation of the C2C12 skeletal myogenic cell line requires Smads, AP-1 and Sp1 family members

Author keywords

AP 1 family; c Fos; c Jun; Myogenesis; Smad3; Sp1; TGF 1; Vimentin

Indexed keywords

PROTEIN C FOS; PROTEIN C JUN; SMAD PROTEIN; SMAD2 PROTEIN; SMAD3 PROTEIN; SMAD4 PROTEIN; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR SP1; TRANSCRIPTION FACTOR SP3; TRANSFORMING GROWTH FACTOR BETA1; VIMENTIN; HISTONE ACETYLTRANSFERASE PCAF; STRESS ACTIVATED PROTEIN KINASE;

EID: 33847039608     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2006.11.017     Document Type: Article
Times cited : (80)

References (56)
  • 1
    • 15244340251 scopus 로고    scopus 로고
    • TGFβ1, back to the future
    • Glick A.B. TGFβ1, back to the future. Cancer Biol. Ther. 3 (2004) 276-283
    • (2004) Cancer Biol. Ther. , vol.3 , pp. 276-283
    • Glick, A.B.1
  • 2
    • 23044466047 scopus 로고    scopus 로고
    • Specificity and versatility in TGF-β signaling through Smads
    • Feng X.-H., and Derynck R. Specificity and versatility in TGF-β signaling through Smads. Annu. Rev. Cell Dev. Biol. 21 (2005) 659-693
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 659-693
    • Feng, X.-H.1    Derynck, R.2
  • 4
    • 0022977185 scopus 로고
    • Regulation of myogenic differentiation by type beta transforming growth factor
    • Olson E.N., Sternberg E., Hu J.S., Spizz G., and Wilcox C. Regulation of myogenic differentiation by type beta transforming growth factor. J. Cell Biol. 103 (1986) 1799-1805
    • (1986) J. Cell Biol. , vol.103 , pp. 1799-1805
    • Olson, E.N.1    Sternberg, E.2    Hu, J.S.3    Spizz, G.4    Wilcox, C.5
  • 5
    • 0025909860 scopus 로고
    • Transforming growth factor beta represses the actions of myogenin through a mechanism independent of DNA binding
    • Brennan T.J., Edmondson D.G., Li L., and Olson E.N. Transforming growth factor beta represses the actions of myogenin through a mechanism independent of DNA binding. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 3822-3826
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 3822-3826
    • Brennan, T.J.1    Edmondson, D.G.2    Li, L.3    Olson, E.N.4
  • 6
    • 0024315692 scopus 로고
    • Fibroblast growth factor and transforming growth factor beta repress transcription of the myogenic regulatory gene MyoD1
    • Vaidya T.B., Rhodes S.J., Taparowsky E.J., and Konieczny S.F. Fibroblast growth factor and transforming growth factor beta repress transcription of the myogenic regulatory gene MyoD1. Mol. Cell. Biol. 9 (1989) 3576-3579
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3576-3579
    • Vaidya, T.B.1    Rhodes, S.J.2    Taparowsky, E.J.3    Konieczny, S.F.4
  • 7
    • 0035890328 scopus 로고    scopus 로고
    • TGF-β inhibits muscle differentiation through functional repression of myogenic transcription factors by Smad3
    • Liu D., Black B.L., and Derynck R. TGF-β inhibits muscle differentiation through functional repression of myogenic transcription factors by Smad3. Genes Dev. 15 (2001) 2950-2966
    • (2001) Genes Dev. , vol.15 , pp. 2950-2966
    • Liu, D.1    Black, B.L.2    Derynck, R.3
  • 8
    • 2342514242 scopus 로고    scopus 로고
    • TGF-β activated Smad3 represses MEF2-dependent transcription in myogenic differentiation
    • Liu D., Kang J.S., and Derynck R. TGF-β activated Smad3 represses MEF2-dependent transcription in myogenic differentiation. EMBO J. 23 (2004) 1557-1566
    • (2004) EMBO J. , vol.23 , pp. 1557-1566
    • Liu, D.1    Kang, J.S.2    Derynck, R.3
  • 9
    • 0025037964 scopus 로고
    • Intermediate filament dynamics
    • Steinert P.M., and Liem R.K. Intermediate filament dynamics. Cell 60 (1990) 521-523
    • (1990) Cell , vol.60 , pp. 521-523
    • Steinert, P.M.1    Liem, R.K.2
  • 11
    • 0029117348 scopus 로고
    • What can be learned from intermediate filament gene regulation in the mouse embryo
    • Duprey P., and Paulin D. What can be learned from intermediate filament gene regulation in the mouse embryo. Int. J. Dev. Biol. 39 (1995) 443-457
    • (1995) Int. J. Dev. Biol. , vol.39 , pp. 443-457
    • Duprey, P.1    Paulin, D.2
  • 12
    • 0024349765 scopus 로고
    • Down-regulation of vimentin gene expression during myogenesis is controlled by a 5′-flanking sequence
    • Sax C.M., Farrell F.X., and Zehner Z.E. Down-regulation of vimentin gene expression during myogenesis is controlled by a 5′-flanking sequence. Gene 78 (1989) 235-242
    • (1989) Gene , vol.78 , pp. 235-242
    • Sax, C.M.1    Farrell, F.X.2    Zehner, Z.E.3
  • 13
    • 0030062159 scopus 로고    scopus 로고
    • A 28-bp negative element with multiple factor-binding activity controls expression of the vimentin-encoding gene
    • Moura-Neto V., Kryszke M.H., Li Z., Vicart P., Lilienbaum A., and Paulin D. A 28-bp negative element with multiple factor-binding activity controls expression of the vimentin-encoding gene. Gene 168 (1996) 261-266
    • (1996) Gene , vol.168 , pp. 261-266
    • Moura-Neto, V.1    Kryszke, M.H.2    Li, Z.3    Vicart, P.4    Lilienbaum, A.5    Paulin, D.6
  • 14
    • 0034724879 scopus 로고    scopus 로고
    • The zinc finger repressor, ZBP-89, binds to the silencer element of the human vimentin gene and complexes with the transcriptional activator, Sp1
    • Wieczorek E., Lin Z., Perkins E.B., Law D.J., Merchant J.L., and Zehner Z.E. The zinc finger repressor, ZBP-89, binds to the silencer element of the human vimentin gene and complexes with the transcriptional activator, Sp1. J. Biol. Chem. 275 (2000) 12879-12888
    • (2000) J. Biol. Chem. , vol.275 , pp. 12879-12888
    • Wieczorek, E.1    Lin, Z.2    Perkins, E.B.3    Law, D.J.4    Merchant, J.L.5    Zehner, Z.E.6
  • 15
    • 0031983125 scopus 로고    scopus 로고
    • Negative regulation of β-enolase gene transcription in embryonic muscle is dependent upon a zinc finger factor that binds to the G-rich box within the muscle-specific enhancer
    • Passantino R., Antona V., Barbieri G., Rubino P., Melchionna R., Cossu G., Feo S., and Giallongo A. Negative regulation of β-enolase gene transcription in embryonic muscle is dependent upon a zinc finger factor that binds to the G-rich box within the muscle-specific enhancer. J. Biol. Chem. 273 (1998) 484-494
    • (1998) J. Biol. Chem. , vol.273 , pp. 484-494
    • Passantino, R.1    Antona, V.2    Barbieri, G.3    Rubino, P.4    Melchionna, R.5    Cossu, G.6    Feo, S.7    Giallongo, A.8
  • 18
    • 0029062950 scopus 로고
    • Regulation of chicken vimentin gene expression by serum, phorbol ester, and growth factors: identification of a novel fibroblast growth factor-inducible element
    • Carey I., and Zehner Z.E. Regulation of chicken vimentin gene expression by serum, phorbol ester, and growth factors: identification of a novel fibroblast growth factor-inducible element. Cell Growth Differ. 6 (1995) 899-908
    • (1995) Cell Growth Differ. , vol.6 , pp. 899-908
    • Carey, I.1    Zehner, Z.E.2
  • 19
    • 0033627677 scopus 로고    scopus 로고
    • A Stat1a factor regulated the expression of the human vimentin gene by IFN-γ
    • Izmailova E.S., Snyder S.R., and Zehner Z.E. A Stat1a factor regulated the expression of the human vimentin gene by IFN-γ. J. Inter. Cytokine Res. 20 (2000) 13-20
    • (2000) J. Inter. Cytokine Res. , vol.20 , pp. 13-20
    • Izmailova, E.S.1    Snyder, S.R.2    Zehner, Z.E.3
  • 21
    • 0002045323 scopus 로고    scopus 로고
    • The epithelial to mesenchymal transition and metastatic progression in carcinoma
    • Gilles C., and Thompson E.W. The epithelial to mesenchymal transition and metastatic progression in carcinoma. Breast J. 2 (1996) 83-96
    • (1996) Breast J. , vol.2 , pp. 83-96
    • Gilles, C.1    Thompson, E.W.2
  • 22
    • 0023449347 scopus 로고
    • Functional analysis and growth factor regulation of the human vimentin promoter
    • Rittling S.R., and Baserga R. Functional analysis and growth factor regulation of the human vimentin promoter. Mol. Cell. Biol. 7 (1987) 3908-3915
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3908-3915
    • Rittling, S.R.1    Baserga, R.2
  • 23
    • 0027505566 scopus 로고
    • Activation of the human vimentin gene by the Tax human T-cell leukemia virus I: mechanisms of regulation by the NF-κB transcription factor
    • Lilienbaum A., and Paulin D. Activation of the human vimentin gene by the Tax human T-cell leukemia virus I: mechanisms of regulation by the NF-κB transcription factor. J. Biol. Chem. 268 (1993) 2180-2188
    • (1993) J. Biol. Chem. , vol.268 , pp. 2180-2188
    • Lilienbaum, A.1    Paulin, D.2
  • 24
    • 0029969178 scopus 로고    scopus 로고
    • PEA3 transactivates vimentin promoter in mammary epithelial and tumor cells
    • Chen J.H., Vercamer C., Li Z., Paulin D., Vandenbunder B., and Stehelin D. PEA3 transactivates vimentin promoter in mammary epithelial and tumor cells. Oncogene 13 (1996) 1667-1675
    • (1996) Oncogene , vol.13 , pp. 1667-1675
    • Chen, J.H.1    Vercamer, C.2    Li, Z.3    Paulin, D.4    Vandenbunder, B.5    Stehelin, D.6
  • 25
    • 0027498310 scopus 로고
    • Identification of a negative element in the human vimentin promoter: modulation by the human T-cell leukemia virus type I Tax protein
    • Salvetti A., Lilienbaum A., Li Z., Paulin D., and Gazzolo L. Identification of a negative element in the human vimentin promoter: modulation by the human T-cell leukemia virus type I Tax protein. Mol. Cell. Biol. 13 (1993) 89-97
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 89-97
    • Salvetti, A.1    Lilienbaum, A.2    Li, Z.3    Paulin, D.4    Gazzolo, L.5
  • 26
    • 0024571416 scopus 로고
    • AP-1/jun binding sites mediate serum inducibility of the human vimentin promoter
    • Rittling S.R., Coutinho L., Amram T., and Kolbe M. AP-1/jun binding sites mediate serum inducibility of the human vimentin promoter. Nucleic Acids Res. 17 (1989) 1619-1633
    • (1989) Nucleic Acids Res. , vol.17 , pp. 1619-1633
    • Rittling, S.R.1    Coutinho, L.2    Amram, T.3    Kolbe, M.4
  • 27
    • 0033119153 scopus 로고    scopus 로고
    • An antisilencer element is involved in the transcriptional regulation of the human vimentin gene
    • Izmailova E.S., and Zehner Z.E. An antisilencer element is involved in the transcriptional regulation of the human vimentin gene. Gene 230 (1999) 111-120
    • (1999) Gene , vol.230 , pp. 111-120
    • Izmailova, E.S.1    Zehner, Z.E.2
  • 28
    • 0346102826 scopus 로고    scopus 로고
    • c-Jun and the dominant-negative mutant, TAM67, induce vimentin gene expression by interacting with the activator Sp1
    • Wu Y., Zhang X., and Zehner Z.E. c-Jun and the dominant-negative mutant, TAM67, induce vimentin gene expression by interacting with the activator Sp1. Oncogene 22 (2003) 8891-8901
    • (2003) Oncogene , vol.22 , pp. 8891-8901
    • Wu, Y.1    Zhang, X.2    Zehner, Z.E.3
  • 30
    • 0027049533 scopus 로고
    • FGF inactivates myogenic helix-loop-helix proteins through phosphorylation of a conserved protein kinase C site in their DNA-binding domains
    • Li L., Zhou J., James G., Hellier-Harrison R., Czech M.P., and Olson E.N. FGF inactivates myogenic helix-loop-helix proteins through phosphorylation of a conserved protein kinase C site in their DNA-binding domains. Cell 71 (1992) 1182-1194
    • (1992) Cell , vol.71 , pp. 1182-1194
    • Li, L.1    Zhou, J.2    James, G.3    Hellier-Harrison, R.4    Czech, M.P.5    Olson, E.N.6
  • 32
    • 0347134486 scopus 로고    scopus 로고
    • Proteomic analysis of the tumorigenic human prostate cell line M12 after microcell-mediated transfer of chromosome 19 demonstrates reduction of vimentin
    • Liu X., Wu Y., Zehner Z.E., Jackson-Cook C.K., and Ware J.L. Proteomic analysis of the tumorigenic human prostate cell line M12 after microcell-mediated transfer of chromosome 19 demonstrates reduction of vimentin. Electrophoresis 24 (2004) 3445-3453
    • (2004) Electrophoresis , vol.24 , pp. 3445-3453
    • Liu, X.1    Wu, Y.2    Zehner, Z.E.3    Jackson-Cook, C.K.4    Ware, J.L.5
  • 33
    • 0038268057 scopus 로고    scopus 로고
    • ZBP-89 represses vimentin gene transcription by interacting with the transcriptional activator, Sp1
    • Zhang X., Diab I.H., and Zehner Z.E. ZBP-89 represses vimentin gene transcription by interacting with the transcriptional activator, Sp1. Nucleic Acids Res. 31 (2003) 2900-2914
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2900-2914
    • Zhang, X.1    Diab, I.H.2    Zehner, Z.E.3
  • 34
    • 0942268712 scopus 로고    scopus 로고
    • Stat3 enhances vimentin gene expression by binding to the antisilencer element and interacting with the repressor protein, ZBP-89
    • Wu Y., Diab I., Zhang X., Izmailova E.S., and Zehner Z.E. Stat3 enhances vimentin gene expression by binding to the antisilencer element and interacting with the repressor protein, ZBP-89. Oncogene 23 (2004) 168-178
    • (2004) Oncogene , vol.23 , pp. 168-178
    • Wu, Y.1    Diab, I.2    Zhang, X.3    Izmailova, E.S.4    Zehner, Z.E.5
  • 35
    • 0032528236 scopus 로고    scopus 로고
    • The tumor suppressor Smad4/DPC4 and transcriptional adaptor CBP/p300 are coactivators for Smad3 in TGF-β-induced transcriptional activation
    • Feng X.-H., Zhang Y., Wu R.-Y., and Derynck R. The tumor suppressor Smad4/DPC4 and transcriptional adaptor CBP/p300 are coactivators for Smad3 in TGF-β-induced transcriptional activation. Genes Dev. 12 (1998) 2153-2163
    • (1998) Genes Dev. , vol.12 , pp. 2153-2163
    • Feng, X.-H.1    Zhang, Y.2    Wu, R.-Y.3    Derynck, R.4
  • 36
    • 0034596993 scopus 로고    scopus 로고
    • Ink4B transcription in response to TGF-β
    • Ink4B transcription in response to TGF-β. EMBO J. 19 (2000) 5178-5193
    • (2000) EMBO J. , vol.19 , pp. 5178-5193
    • Feng, X.-H.1    Lin, X.2    Derynck, R.3
  • 37
    • 0028871755 scopus 로고
    • E1A promotes association between p300 and pRB in multimeric complexes required for normal biological activity
    • Wang H.-G.H., Moran E., and Yaciuk P. E1A promotes association between p300 and pRB in multimeric complexes required for normal biological activity. J. Virol. 69 (1995) 7917-7924
    • (1995) J. Virol. , vol.69 , pp. 7917-7924
    • Wang, H.-G.H.1    Moran, E.2    Yaciuk, P.3
  • 38
    • 0025371673 scopus 로고
    • A negative element involved in vimentin gene expression
    • Farrell F.X., Sax C.M., and Zehner Z.E. A negative element involved in vimentin gene expression. Mol. Cell. Biol. 10 (1990) 2349-2358
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2349-2358
    • Farrell, F.X.1    Sax, C.M.2    Zehner, Z.E.3
  • 39
    • 1242293760 scopus 로고    scopus 로고
    • Transforming growth factor-β1 induces the differentiation of myogenic cells into fibrotic cells in injured skeletal muscle
    • Li Y., Foster W., Deasy B.M., Chan Y., Prisk V., Tang Y., Cummins J., and Huard J. Transforming growth factor-β1 induces the differentiation of myogenic cells into fibrotic cells in injured skeletal muscle. Am. J. Pathol. 164 (2004) 1007-1019
    • (2004) Am. J. Pathol. , vol.164 , pp. 1007-1019
    • Li, Y.1    Foster, W.2    Deasy, B.M.3    Chan, Y.4    Prisk, V.5    Tang, Y.6    Cummins, J.7    Huard, J.8
  • 40
    • 0035936918 scopus 로고    scopus 로고
    • Involvement of histone H4 gene transcription factor 1 in downregulation of vimentin gene expression during skeletal muscle differentiation
    • Kryszke M.H., Moura-Neto V., Lilienbaum A., Paulin D., and Auclair C. Involvement of histone H4 gene transcription factor 1 in downregulation of vimentin gene expression during skeletal muscle differentiation. FEBS Lett. 491 (2001) 30-34
    • (2001) FEBS Lett. , vol.491 , pp. 30-34
    • Kryszke, M.H.1    Moura-Neto, V.2    Lilienbaum, A.3    Paulin, D.4    Auclair, C.5
  • 41
    • 0032809684 scopus 로고    scopus 로고
    • A GC-box is required for expression of the human vimentin gene
    • Izmailova E.S., Wieczorek E., Perkins E.B., and Zehner Z.E. A GC-box is required for expression of the human vimentin gene. Gene 235 (1999) 69-75
    • (1999) Gene , vol.235 , pp. 69-75
    • Izmailova, E.S.1    Wieczorek, E.2    Perkins, E.B.3    Zehner, Z.E.4
  • 44
    • 0035821745 scopus 로고    scopus 로고
    • Smad3/AP-1 interactions control transcriptional responses to TGF-β in a promoter-specific manner
    • Verrecchia F., Vindevoghel L., Lechleider R.J., Uitto J., Roberts A.B., and Mauviel A. Smad3/AP-1 interactions control transcriptional responses to TGF-β in a promoter-specific manner. Oncogene 20 (2001) 3332-3340
    • (2001) Oncogene , vol.20 , pp. 3332-3340
    • Verrecchia, F.1    Vindevoghel, L.2    Lechleider, R.J.3    Uitto, J.4    Roberts, A.B.5    Mauviel, A.6
  • 45
    • 0032572723 scopus 로고    scopus 로고
    • Smad3 and Smad4 cooperate with c-Jun/c-Fos to mediate TGF-β-induced transcription
    • Zhang Y., Feng X.-H., and Derynck R. Smad3 and Smad4 cooperate with c-Jun/c-Fos to mediate TGF-β-induced transcription. Nature 394 (1998) 909-913
    • (1998) Nature , vol.394 , pp. 909-913
    • Zhang, Y.1    Feng, X.-H.2    Derynck, R.3
  • 47
    • 0034666152 scopus 로고    scopus 로고
    • Efficient TGF-β induction of the Smad7 gene requires cooperation between AP-1, Sp1, and Smad proteins on the mouse Smad7promoter
    • Brodin G., Ahgren A., tenDijke P., Heldin C.-H., and Heuchel R. Efficient TGF-β induction of the Smad7 gene requires cooperation between AP-1, Sp1, and Smad proteins on the mouse Smad7promoter. J. Biol. Chem. 275 (2000) 29023-29030
    • (2000) J. Biol. Chem. , vol.275 , pp. 29023-29030
    • Brodin, G.1    Ahgren, A.2    tenDijke, P.3    Heldin, C.-H.4    Heuchel, R.5
  • 48
    • 0027477423 scopus 로고
    • Expression of c-jun/AP-1 during myogenic differentiation in mouse C2C12 Myoblasts
    • Thinakaran G., Ojala J., and Bag J. Expression of c-jun/AP-1 during myogenic differentiation in mouse C2C12 Myoblasts. FEBS Lett. 319 (1993) 271-276
    • (1993) FEBS Lett. , vol.319 , pp. 271-276
    • Thinakaran, G.1    Ojala, J.2    Bag, J.3
  • 49
    • 0030923133 scopus 로고    scopus 로고
    • Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions
    • Aronheim A., Zandi E., Hennemann H., Elledge S.J., and Karin M. Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions. Mol. Cell. Biol. 17 (1997) 3094-3102
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3094-3102
    • Aronheim, A.1    Zandi, E.2    Hennemann, H.3    Elledge, S.J.4    Karin, M.5
  • 50
    • 0037131310 scopus 로고    scopus 로고
    • Induction of terminal differentiation by the c-Jun dimerization protein JPD2 in C2 myoblasts and rhabdomyosarcoma cells
    • Ostrovsky O., Bengal E., and Aronheim A. Induction of terminal differentiation by the c-Jun dimerization protein JPD2 in C2 myoblasts and rhabdomyosarcoma cells. J. Biol. Chem. 277 (2002) 40043-40054
    • (2002) J. Biol. Chem. , vol.277 , pp. 40043-40054
    • Ostrovsky, O.1    Bengal, E.2    Aronheim, A.3
  • 51
    • 0032527756 scopus 로고    scopus 로고
    • TGF-β-stimulated cooperation of Smad proteins with the coactivators CBP/p300
    • Janknecht R., Wells N.J., and Hunter T. TGF-β-stimulated cooperation of Smad proteins with the coactivators CBP/p300. Genes Dev. 12 (1998) 2114-2119
    • (1998) Genes Dev. , vol.12 , pp. 2114-2119
    • Janknecht, R.1    Wells, N.J.2    Hunter, T.3
  • 52
    • 0027533132 scopus 로고
    • Identification of specific adenovirus E1A N-terminal residues critical to the binding of cellular proteins and to the control of cell growth
    • Wang H.-G.H., Rikitake Y., Carter M.C., Yaciuk P., Abraham S.E., Zerler B., and Moran E. Identification of specific adenovirus E1A N-terminal residues critical to the binding of cellular proteins and to the control of cell growth. J. Virol. 67 (1993) 476-488
    • (1993) J. Virol. , vol.67 , pp. 476-488
    • Wang, H.-G.H.1    Rikitake, Y.2    Carter, M.C.3    Yaciuk, P.4    Abraham, S.E.5    Zerler, B.6    Moran, E.7
  • 53
    • 0036272787 scopus 로고    scopus 로고
    • JDP2, a repressor of AP-1, recruits a histone deacetylase 3 complex to inhibit the retinoic acid-induced differentiation of F9 cells
    • Jin C., Li H., Murata T., Sun K., Horikoshi M., Chiu R., and Yokoyama K.K. JDP2, a repressor of AP-1, recruits a histone deacetylase 3 complex to inhibit the retinoic acid-induced differentiation of F9 cells. Mol. Cell. Biol. 22 (2002) 4815-4826
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4815-4826
    • Jin, C.1    Li, H.2    Murata, T.3    Sun, K.4    Horikoshi, M.5    Chiu, R.6    Yokoyama, K.K.7
  • 54
    • 0032979988 scopus 로고    scopus 로고
    • Smad3-Smad4 and AP-1 complexes synergize in transcriptional activation of the c-Jun promoter by transforming growth factor β
    • Wong C., Rougier-Chapman E.M., Frederick J.P., Datto M.B., Liberati N.T., Li J.M., and Wang X.F. Smad3-Smad4 and AP-1 complexes synergize in transcriptional activation of the c-Jun promoter by transforming growth factor β. Mol. Cell. Biol. 19 (1999) 1821-1830
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1821-1830
    • Wong, C.1    Rougier-Chapman, E.M.2    Frederick, J.P.3    Datto, M.B.4    Liberati, N.T.5    Li, J.M.6    Wang, X.F.7
  • 55
    • 0034704076 scopus 로고    scopus 로고
    • Regulation of plasminogen activator inhibitor-1 expression by Transforming Growth Factor-β-induced physical and functional interactions between Smads and Sp1
    • Datta P.K., Blake M.C., and Moses H.L. Regulation of plasminogen activator inhibitor-1 expression by Transforming Growth Factor-β-induced physical and functional interactions between Smads and Sp1. J. Biol. Chem. 275 (2000) 40014-40019
    • (2000) J. Biol. Chem. , vol.275 , pp. 40014-40019
    • Datta, P.K.1    Blake, M.C.2    Moses, H.L.3
  • 56
    • 0034623987 scopus 로고    scopus 로고
    • Structural and functional characterization of the transforming growth factor-beta-induced Smad3/c-Jun transcriptional cooperativity
    • Qing J., Zhang Y., and Derynck R. Structural and functional characterization of the transforming growth factor-beta-induced Smad3/c-Jun transcriptional cooperativity. J. Biol. Chem. 275 (2000) 38802-38812
    • (2000) J. Biol. Chem. , vol.275 , pp. 38802-38812
    • Qing, J.1    Zhang, Y.2    Derynck, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.