메뉴 건너뛰기




Volumn 17, Issue 12, 1997, Pages 7195-7207

Constitutive activation of gene expression by thyroid hormone receptor results from reversal of p53-mediated repression

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; PROTEIN P53; THYROID HORMONE RECEPTOR;

EID: 0030667318     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.17.12.7195     Document Type: Article
Times cited : (27)

References (104)
  • 1
    • 0027219428 scopus 로고
    • The conserved ninth C-terminal heptad in thyroid hormone and retinoic acid receptors mediates diverse responses by affecting heterodimer but not homodimer formation
    • Au-Fliegner, M., E. Helmer, J. Casanova, B. M. Raaka, and H. H. Samuels. 1993. The conserved ninth C-terminal heptad in thyroid hormone and retinoic acid receptors mediates diverse responses by affecting heterodimer but not homodimer formation. Mol. Cell. Biol. 13:5725-5737.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5725-5737
    • Au-Fliegner, M.1    Helmer, E.2    Casanova, J.3    Raaka, B.M.4    Samuels, H.H.5
  • 2
    • 0025040233 scopus 로고
    • Suppression of human colorectal carcinoma cell growth by wild-type p53
    • Baker, S. J., S. Markowitz, E. R. Fearon, J. K. U. Willson, and B. Vogelstein. 1990. Suppression of human colorectal carcinoma cell growth by wild-type p53. Science 249:912-915.
    • (1990) Science , vol.249 , pp. 912-915
    • Baker, S.J.1    Markowitz, S.2    Fearon, E.R.3    Willson, J.K.U.4    Vogelstein, B.5
  • 3
    • 0026557594 scopus 로고
    • A transferable silencing domain is present in the thyroid hormone receptor, in the v-erbA oncogene product and in the retinoic acid receptor
    • Baniahmad, A., C. A. Kohne, and R. Renkawitz. 1992. A transferable silencing domain is present in the thyroid hormone receptor, in the v-erbA oncogene product and in the retinoic acid receptor. EMBO J. 11:1015-1023.
    • (1992) EMBO J. , vol.11 , pp. 1015-1023
    • Baniahmad, A.1    Kohne, C.A.2    Renkawitz, R.3
  • 4
    • 0028988482 scopus 로고
    • The τ4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencing
    • Baniahmad, A., X. Leng, T. P. Burris, S. Y. Tsai, M.-J. Tsai, and B. W. O'Malley. 1995. The τ4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencing. Mol. Cell. Biol. 15:76-86.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 76-86
    • Baniahmad, A.1    Leng, X.2    Burris, T.P.3    Tsai, S.Y.4    Tsai, M.-J.5    O'Malley, B.W.6
  • 5
    • 0027459198 scopus 로고
    • Mdm2 expression is induced by wild type p53 activity
    • Barak, Y. T., T. Juven, R. Haffner, and M. Oren. 1993. mdm2 expression is induced by wild type p53 activity. EMBO J. 12:461-468.
    • (1993) EMBO J. , vol.12 , pp. 461-468
    • Barak, Y.T.1    Juven, T.2    Haffner, R.3    Oren, M.4
  • 7
    • 0024869336 scopus 로고
    • Thyroid hormone aporeceptor represses T3-inducible promoters and blocks activity of the retinoic acid receptor
    • Brent, G. A., M. K. Dunn, J. W. Harney, T. Gulick, P. R. Larsen, and D. D. Moore. 1989. Thyroid hormone aporeceptor represses T3-inducible promoters and blocks activity of the retinoic acid receptor. New Biol. 1:329-336.
    • (1989) New Biol. , vol.1 , pp. 329-336
    • Brent, G.A.1    Dunn, M.K.2    Harney, J.W.3    Gulick, T.4    Larsen, P.R.5    Moore, D.D.6
  • 9
    • 0024357987 scopus 로고
    • Negative regulation of the thyroid stimulating hormone alpha gene by thyroid hormone: Receptor interaction adjacent to the TATA box
    • Chatterjee, V. K. K., J.-K. Lee, A. Rentoumis, and J. L. Jameson. 1989. Negative regulation of the thyroid stimulating hormone alpha gene by thyroid hormone: receptor interaction adjacent to the TATA box. Proc. Natl. Acad. Sci. USA 86:9114-9118.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9114-9118
    • Chatterjee, V.K.K.1    Lee, J.-K.2    Rentoumis, A.3    Jameson, J.L.4
  • 10
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • Chen, J. D., and R. M. Evans. 1995. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 377:454-457.
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 11
    • 0028949844 scopus 로고
    • Cloning of an intrinsic human TFIID subunit that interacts with multiple transcriptional activators
    • Chiang, C. M., and R. G. Roeder. 1995. Cloning of an intrinsic human TFIID subunit that interacts with multiple transcriptional activators. Science 267:531-536.
    • (1995) Science , vol.267 , pp. 531-536
    • Chiang, C.M.1    Roeder, R.G.2
  • 12
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Cho, Y., S. Gorina, P. D. Jeffrey, and N. P. Pavletich. 1994. Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science 265:346-355.
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 13
    • 0024336324 scopus 로고
    • Protein encoded by v-erbA functions as a thyroid hormone receptor antagonist
    • Damm, K., C. C. Thompson, and R. M. Evans. 1989. Protein encoded by v-erbA functions as a thyroid hormone receptor antagonist. Nature 339: 593-597.
    • (1989) Nature , vol.339 , pp. 593-597
    • Damm, K.1    Thompson, C.C.2    Evans, R.M.3
  • 14
    • 0022500166 scopus 로고
    • The trans-activator gene of the human T-cell lymphotrophic virus type III is required for replication
    • Dayton, A. I., J. G. Sodroski, C. A, Rosen, W. C. Goh, and W. A. Haseltine. 1986. The trans-activator gene of the human T-cell lymphotrophic virus type III is required for replication. Cell 44:941-947.
    • (1986) Cell , vol.44 , pp. 941-947
    • Dayton, A.I.1    Sodroski, J.G.2    Rosen, C.A.3    Goh, W.C.4    Haseltine, W.A.5
  • 15
    • 0029072676 scopus 로고
    • Interactions of thyroid hormone receptor with the human immunodeficiency virus type 1 (HIV-1) long terminal repeat and the HIV-1 trans-activator, tat
    • Desai-Yajnik, V., E. Hadzic, P. Modlinger, S. Malhotra, and H. H. Samuels. 1995. Interactions of thyroid hormone receptor with the human immunodeficiency virus type 1 (HIV-1) long terminal repeat and the HIV-1 trans-activator, tat. J. Virol. 69:5103-5112.
    • (1995) J. Virol. , vol.69 , pp. 5103-5112
    • Desai-Yajnik, V.1    Hadzic, E.2    Modlinger, P.3    Malhotra, S.4    Samuels, H.H.5
  • 16
    • 0027202123 scopus 로고
    • The NF-κB and Sp1 DNA motifs of the human immunodeficiency virus type 1 long terminal repeat function as novel thyroid hormone response elements
    • Desai-Yajnik, V., and H. H. Samuels. 1993. The NF-κB and Sp1 DNA motifs of the human immunodeficiency virus type 1 long terminal repeat function as novel thyroid hormone response elements. Mol. Cell. Biol. 13:5057-5069.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5057-5069
    • Desai-Yajnik, V.1    Samuels, H.H.2
  • 17
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in soluble extract from isolated mammalian nuclei
    • Dignam, J. D., R. M. Lebovitz, and R. G. Roeder. 1983. Accurate transcription initiation by RNA polymerase II in soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11:1475-1489.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 20
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans, R. M. 1988. The steroid and thyroid hormone receptor superfamily. Science 240:889-895.
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 21
    • 0025024469 scopus 로고
    • The p53 proto-oncogene can act as a suppressor of transformation
    • Fields, S., and S. K. Jang. 1990. The p53 proto-oncogene can act as a suppressor of transformation. Science 249:1046-1049.
    • (1990) Science , vol.249 , pp. 1046-1049
    • Fields, S.1    Jang, S.K.2
  • 23
    • 0023267294 scopus 로고
    • Cis-acting elements of the rat growth hormone gene which mediate basal and regulated expression by thyroid hormone
    • Flug, F., R. P. Copp, J. Casanova, Z. D. Horowitz, L. Janocko, M. Plotnick, and H. Samuels. 1987. cis-acting elements of the rat growth hormone gene which mediate basal and regulated expression by thyroid hormone. J. Biol. Chem. 262:6373-6382.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6373-6382
    • Flug, F.1    Copp, R.P.2    Casanova, J.3    Horowitz, Z.D.4    Janocko, L.5    Plotnick, M.6    Samuels, H.7
  • 24
    • 0026557820 scopus 로고
    • Half-site spacing and orientation determines whether thyroid hormone and retinoic acid receptors and related factors bind to DNA response elements as monomers, homodimers, or heterodimers
    • Forman, B. M., J. Casanova, B. M. Raaka, J. Ghysdael, and H. H. Samuels. 1992. Half-site spacing and orientation determines whether thyroid hormone and retinoic acid receptors and related factors bind to DNA response elements as monomers, homodimers, or heterodimers. Mol. Endocrinol. 6:429-442.
    • (1992) Mol. Endocrinol. , vol.6 , pp. 429-442
    • Forman, B.M.1    Casanova, J.2    Raaka, B.M.3    Ghysdael, J.4    Samuels, H.H.5
  • 25
    • 0025186267 scopus 로고
    • Interactions among a subfamily of nuclear hormone receptors: The regulatory zipper model
    • Forman, B. M., and H. H. Samuels. 1990. Interactions among a subfamily of nuclear hormone receptors: the regulatory zipper model. Mol. Endocrinol. 4:1293-1301.
    • (1990) Mol. Endocrinol. , vol.4 , pp. 1293-1301
    • Forman, B.M.1    Samuels, H.H.2
  • 26
    • 0026050565 scopus 로고
    • PEXPRESS: A family of expression vectors containing a single transcription unit active in prokaryotes, eukaryotes and in vitro
    • Forman, B. M., and H. H. Samuels. 1991. pEXPRESS: a family of expression vectors containing a single transcription unit active in prokaryotes, eukaryotes and in vitro. Gene 105:9-15.
    • (1991) Gene , vol.105 , pp. 9-15
    • Forman, B.M.1    Samuels, H.H.2
  • 27
    • 0029002298 scopus 로고
    • Unique response pathways are established by allosteric interactions among nuclear hormone receptors
    • Forman, B. M., K. Umesono, J. Chen, and R. M. Evans. 1995. Unique response pathways are established by allosteric interactions among nuclear hormone receptors. Cell 81:541-550.
    • (1995) Cell , vol.81 , pp. 541-550
    • Forman, B.M.1    Umesono, K.2    Chen, J.3    Evans, R.M.4
  • 28
    • 0024457916 scopus 로고
    • A domain containing leucine zipper like motifs mediates novel in vivo interactions between the thyroid hormone and retinoic acid receptors
    • Forman, B. M., C.-R. Yang, M. Au, J. Casanova, J. Ghysdael, and H. H. Samuels. 1989. A domain containing leucine zipper like motifs mediates novel in vivo interactions between the thyroid hormone and retinoic acid receptors. Mol. Endocrinol. 3:1610-1626.
    • (1989) Mol. Endocrinol. , vol.3 , pp. 1610-1626
    • Forman, B.M.1    Yang, C.-R.2    Au, M.3    Casanova, J.4    Ghysdael, J.5    Samuels, H.H.6
  • 29
    • 0023735225 scopus 로고
    • C-erbA protooncogenes mediate thyroid hormone-dependent and independent regulation of the rat growth hormone and prolactin genes
    • Forman, B. M., C.-R. Yang, F. Stanley, J. Casanova, and H. H. Samuels. 1988. c-erbA protooncogenes mediate thyroid hormone-dependent and independent regulation of the rat growth hormone and prolactin genes. Mol. Endocrinol. 2:902-911.
    • (1988) Mol. Endocrinol. , vol.2 , pp. 902-911
    • Forman, B.M.1    Yang, C.-R.2    Stanley, F.3    Casanova, J.4    Samuels, H.H.5
  • 30
    • 0026685062 scopus 로고
    • Anatomy of the steroid receptor zinc finger region
    • Freedman, L. P. 1992. Anatomy of the steroid receptor zinc finger region. Endocrinol. Rev. 13:129-145.
    • (1992) Endocrinol. Rev. , vol.13 , pp. 129-145
    • Freedman, L.P.1
  • 31
    • 0025887476 scopus 로고
    • Wild-type p53 can down-modulate the activity of various promoters
    • Ginsberg, D., F. Mechta, M. Yaniv, and M. Oren. 1991. Wild-type p53 can down-modulate the activity of various promoters. Proc. Natl. Acad. Sci. USA 88:9979-9983.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9979-9983
    • Ginsberg, D.1    Mechta, F.2    Yaniv, M.3    Oren, M.4
  • 32
    • 0029044001 scopus 로고
    • A 10-amino-acid sequence in the N-terminal A/B domain of thyroid hormone receptor α is essential for transcriptional activation and interaction with the general transcription factor TFIIB
    • Hadzic, E., V. Desai-Yajnik, E. Helmer, S. Guo, J. Casanova, B. M. Raaka, and H. H. Samuels. 1995. A 10-amino-acid sequence in the N-terminal A/B domain of thyroid hormone receptor α is essential for transcriptional activation and interaction with the general transcription factor TFIIB. Mol. Cell. Biol. 15:4507-4517.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4507-4517
    • Hadzic, E.1    Desai-Yajnik, V.2    Helmer, E.3    Guo, S.4    Casanova, J.5    Raaka, B.M.6    Samuels, H.H.7
  • 33
    • 0028147405 scopus 로고
    • Physical and functional interaction between wild-type p53 and mdm2 proteins
    • Haines, D. S., J. E. Landers, L. J. Engle, and D. L. George. 1994. Physical and functional interaction between wild-type p53 and mdm2 proteins. Mol. Cell. Biol. 14:1171-1178.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1171-1178
    • Haines, D.S.1    Landers, J.E.2    Engle, L.J.3    George, D.L.4
  • 34
    • 0028842340 scopus 로고
    • A mutant p53 transgene accelerates tumor development in heterozygous but not nullizygous p53-deficient mice
    • Harvey, M., H. Vogel, D. Morris, A. Bradley, A. Bernstein, and L. A. Donehower. 1995. A mutant p53 transgene accelerates tumor development in heterozygous but not nullizygous p53-deficient mice. Nat. Genet. 9:305-311.
    • (1995) Nat. Genet. , vol.9 , pp. 305-311
    • Harvey, M.1    Vogel, H.2    Morris, D.3    Bradley, A.4    Bernstein, A.5    Donehower, L.A.6
  • 35
    • 0029985647 scopus 로고    scopus 로고
    • Cell type-specific inhibition of p53-mediated apoptosis by mdm2
    • Haupt, Y., Y. Barak, and M. Oren. 1996. Cell type-specific inhibition of p53-mediated apoptosis by mdm2. EMBO J. 15:1596-1606.
    • (1996) EMBO J. , vol.15 , pp. 1596-1606
    • Haupt, Y.1    Barak, Y.2    Oren, M.3
  • 36
    • 0030024894 scopus 로고    scopus 로고
    • Hormone-dependent and -independent transcriptional activation by thyroid hormone receptors are mediated by different mechanisms
    • Helmer, E. B., B. M. Raaka, and H. H. Samuels. 1996. Hormone-dependent and -independent transcriptional activation by thyroid hormone receptors are mediated by different mechanisms. Endocrinology 137:390-399.
    • (1996) Endocrinology , vol.137 , pp. 390-399
    • Helmer, E.B.1    Raaka, B.M.2    Samuels, H.H.3
  • 37
    • 0027438621 scopus 로고
    • Specific interactions of the human immunodeficiency virus tat proteins with a cellular protein kinase
    • Herrmann, C. H., and A. P. Rice. 1993. Specific interactions of the human immunodeficiency virus tat proteins with a cellular protein kinase. Virology 197:601-608.
    • (1993) Virology , vol.197 , pp. 601-608
    • Herrmann, C.H.1    Rice, A.P.2
  • 40
    • 0024585727 scopus 로고
    • Characterization of the domain structure of chick c-erbA by deletion mutation: In vitro translation and cell transfection studies
    • Horowitz, Z. D., C.-R. Yang, B. M. Forman, J. Casanova, and H. H. Samuels. 1989. Characterization of the domain structure of chick c-erbA by deletion mutation: in vitro translation and cell transfection studies. Mol. Endocrinol. 3:148-156.
    • (1989) Mol. Endocrinol. , vol.3 , pp. 148-156
    • Horowitz, Z.D.1    Yang, C.-R.2    Forman, B.M.3    Casanova, J.4    Samuels, H.H.5
  • 41
    • 0027501841 scopus 로고
    • Wild-type p53 can mediate sequence-specific transactivation of an internal promoter within the mdm2 gene
    • Juven, T., Y. Barak, A. Zauberman, D. L. George, and M. Oren. 1993. Wild-type p53 can mediate sequence-specific transactivation of an internal promoter within the mdm2 gene. Oncogene 8:3411-3416.
    • (1993) Oncogene , vol.8 , pp. 3411-3416
    • Juven, T.1    Barak, Y.2    Zauberman, A.3    George, D.L.4    Oren, M.5
  • 42
    • 0026496885 scopus 로고
    • A mammalian cell cycle checkpoint pathway utilizing p53 and GADD45 is defective in ataxia Telangiectasia
    • Kastan, M. B., Q. Zhan, W. S. El-Deiry, F. Carrier, T. Jacks, W. V. Walsh, and A. J. Fornace. 1992. A mammalian cell cycle checkpoint pathway utilizing p53 and GADD45 is defective in ataxia Telangiectasia. Cell 71: 587-597.
    • (1992) Cell , vol.71 , pp. 587-597
    • Kastan, M.B.1    Zhan, Q.2    El-Deiry, W.S.3    Carrier, F.4    Jacks, T.5    Walsh, W.V.6    Fornace, A.J.7
  • 45
    • 0029972806 scopus 로고    scopus 로고
    • P53: Puzzle and paradigm
    • Ko, L. J., and C. Prives. 1996. p53: puzzle and paradigm. Genes Dev. 10:1054-1072.
    • (1996) Genes Dev. , vol.10 , pp. 1054-1072
    • Ko, L.J.1    Prives, C.2
  • 46
    • 0027956208 scopus 로고
    • Enhanced translation: A novel mechanism of mdm2 oncogene overexpression identified in human tumor cells
    • Landers, J. E., D. S. Haines, J. F. Strauss III, and D. L. George. 1994. Enhanced translation: a novel mechanism of mdm2 oncogene overexpression identified in human tumor cells. Oncogene 9:2745-2750.
    • (1994) Oncogene , vol.9 , pp. 2745-2750
    • Landers, J.E.1    Haines, D.S.2    Strauss III, J.F.3    George, D.L.4
  • 47
    • 0018348655 scopus 로고
    • T antigen is bound to host protein in SV40 transformed cells
    • Lane, D. P., and L. V. Crawford. 1979. T antigen is bound to host protein in SV40 transformed cells. Nature 278:261-263.
    • (1979) Nature , vol.278 , pp. 261-263
    • Lane, D.P.1    Crawford, L.V.2
  • 48
    • 0027416347 scopus 로고
    • Thyroid hormone receptors: Multiple forms, multiple possibilities
    • Lazar, M. A. 1993. Thyroid hormone receptors: multiple forms, multiple possibilities. Endocrinol. Rev. 14:184-193.
    • (1993) Endocrinol. Rev. , vol.14 , pp. 184-193
    • Lazar, M.A.1
  • 49
    • 0028890361 scopus 로고
    • Interaction of thyroid-hormone receptor with a conserved transcriptional mediator
    • Lee, J. W., F. Ryan, J. C. Swaffield, S. A. Johnston, and D. D. Moore. 1995. Interaction of thyroid-hormone receptor with a conserved transcriptional mediator. Nature 374:91-94.
    • (1995) Nature , vol.374 , pp. 91-94
    • Lee, J.W.1    Ryan, F.2    Swaffield, J.C.3    Johnston, S.A.4    Moore, D.D.5
  • 50
    • 0026471556 scopus 로고
    • Assignment of the β-thyroid hormone receptor to 3,5,3′-triiodothyronine-dependent inhibition of transcription from the thyrotropin-releasing hormone promoter in chick hypothalamic neurons
    • Lezoualch, F., A. H. S. Hassan, P. Giraud, J.-P. Loeffler, S. L. Lee, and B. A. Demeneix. 1992. Assignment of the β-thyroid hormone receptor to 3,5,3′-triiodothyronine-dependent inhibition of transcription from the thyrotropin-releasing hormone promoter in chick hypothalamic neurons. Mol. Endocrinol. 6:1797-1804.
    • (1992) Mol. Endocrinol. , vol.6 , pp. 1797-1804
    • Lezoualch, F.1    Hassan, A.H.S.2    Giraud, P.3    Loeffler, J.-P.4    Lee, S.L.5    Demeneix, B.A.6
  • 51
    • 0024571802 scopus 로고
    • Transcription activation by the adenovirus E1a protein
    • Lillie, J. W., and M. R. Green. 1989. Transcription activation by the adenovirus E1a protein. Nature 338:39-44.
    • (1989) Nature , vol.338 , pp. 39-44
    • Lillie, J.W.1    Green, M.R.2
  • 52
    • 0028303752 scopus 로고
    • Several Hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein
    • Lin, J., J. Chen, B. Elenbaas, and A. J. Levine. 1994. Several Hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein. Genes Dev. 8:1235-1246.
    • (1994) Genes Dev. , vol.8 , pp. 1235-1246
    • Lin, J.1    Chen, J.2    Elenbaas, B.3    Levine, A.J.4
  • 53
    • 0018760324 scopus 로고
    • Characterization of a 54K dalton cellular SV40 tumor antigen present in SV40-transformed cells and uninfected embryonal carcinoma cells
    • Linzer, D. I., and A. J. Levine. 1979. Characterization of a 54K dalton cellular SV40 tumor antigen present in SV40-transformed cells and uninfected embryonal carcinoma cells. Cell 17:43-52.
    • (1979) Cell , vol.17 , pp. 43-52
    • Linzer, D.I.1    Levine, A.J.2
  • 54
    • 0027316149 scopus 로고
    • The p53 activation domain binds the TATA box-binding polypeptide in holo-TFIID, and a neighboring p53 domain inhibits transcription
    • Liu, X., C. W. Miller, P. H. Koeffler, and A. J. Berk. 1993. The p53 activation domain binds the TATA box-binding polypeptide in holo-TFIID, and a neighboring p53 domain inhibits transcription. Mol. Cell. Biol. 13: 3291-3300.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3291-3300
    • Liu, X.1    Miller, C.W.2    Koeffler, P.H.3    Berk, A.J.4
  • 55
    • 0027318117 scopus 로고
    • Specific repression of TATA-mediated but not initiator mediated transcription by wild-type p53
    • Mack, D. H., J. Vartikar, J. M. Pipas, and L. Laimins. 1993. Specific repression of TATA-mediated but not initiator mediated transcription by wild-type p53. Nature 363:281-283.
    • (1993) Nature , vol.363 , pp. 281-283
    • Mack, D.H.1    Vartikar, J.2    Pipas, J.M.3    Laimins, L.4
  • 56
    • 0029164446 scopus 로고
    • The WT1 gene product stabilizes p53 and inhibits p53-mediated apoptosis
    • Maheswaran, S., C. Englert, P. Bennett, G. Heinrich, and D. A. Haber. 1995. The WT1 gene product stabilizes p53 and inhibits p53-mediated apoptosis. Genes Dev. 9:2143-2156.
    • (1995) Genes Dev. , vol.9 , pp. 2143-2156
    • Maheswaran, S.1    Englert, C.2    Bennett, P.3    Heinrich, G.4    Haber, D.A.5
  • 59
    • 0025749704 scopus 로고
    • The adenovirus E1A transforming protein activates the proliferating cell nuclear antigen promoter via an activating transcription factor site
    • Morris, G. F., and M. B. Mathews. 1991. The adenovirus E1A transforming protein activates the proliferating cell nuclear antigen promoter via an activating transcription factor site. J. Virol. 65:6397-6406.
    • (1991) J. Virol. , vol.65 , pp. 6397-6406
    • Morris, G.F.1    Mathews, M.B.2
  • 60
    • 0023797883 scopus 로고
    • Characterization of the hormone-binding domain of the chicken c-erbA/ thyroid hormone receptor protein
    • Munoz, A., M. Zenke, U. Gehring, J. Sap, H. Beug, and B. Vennstrom. 1988. Characterization of the hormone-binding domain of the chicken c-erbA/ thyroid hormone receptor protein. EMBO J. 7:155-159.
    • (1988) EMBO J. , vol.7 , pp. 155-159
    • Munoz, A.1    Zenke, M.2    Gehring, U.3    Sap, J.4    Beug, H.5    Vennstrom, B.6
  • 61
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator of the steroid hormone receptor superfamily
    • Onate, S. A., S. Y. Tsai, M.-J. -. Tsai, and B. W. O'Malley. 1995. Sequence and characterization of a coactivator of the steroid hormone receptor superfamily. Science 270:1354-1357.
    • (1995) Science , vol.270 , pp. 1354-1357
    • Onate, S.A.1    Tsai, S.Y.2    Tsai, M.-J.3    O'Malley, B.W.4
  • 62
    • 0019830333 scopus 로고
    • Post-translational regulation of the 54K cellular tumor antigen in normal and transformed cells
    • Oren, M., W. Maltzman, and A. J. Levine. 1981. Post-translational regulation of the 54K cellular tumor antigen in normal and transformed cells. Mol. Cell. Biol. 1:101-110.
    • (1981) Mol. Cell. Biol. , vol.1 , pp. 101-110
    • Oren, M.1    Maltzman, W.2    Levine, A.J.3
  • 63
    • 0026515868 scopus 로고
    • Roles of TATA and initiator elements in determining the start site location and direction of RNA polymerase II transcription
    • O'Shea-Greenfield, A., and S. T. Smale. 1992. Roles of TATA and initiator elements in determining the start site location and direction of RNA polymerase II transcription. J. Biol. Chem. 267:1391-1402.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1391-1402
    • O'Shea-Greenfield, A.1    Smale, S.T.2
  • 64
    • 0022637380 scopus 로고
    • Specific interaction between the p53 cellular tumor antigen and the major heat shock protein
    • Pinhasi-Kimhi, O., D. Michalovitz, D. Ben-Zeev, and M. Oren. 1986. Specific interaction between the p53 cellular tumor antigen and the major heat shock protein. Nature 320:182-185.
    • (1986) Nature , vol.320 , pp. 182-185
    • Pinhasi-Kimhi, O.1    Michalovitz, D.2    Ben-Zeev, D.3    Oren, M.4
  • 65
    • 85036675650 scopus 로고    scopus 로고
    • TLS is a high-affinity interactor for steroid, thyroid hormone, and retinoid receptors
    • in press
    • Powers, C. A., M. Mathur, B. M. Raaka, D. Ron, and H. H. Samuels. TLS is a high-affinity interactor for steroid, thyroid hormone, and retinoid receptors. Mol. Endocrinol., in press.
    • Mol. Endocrinol.
    • Powers, C.A.1    Mathur, M.2    Raaka, B.M.3    Ron, D.4    Samuels, H.H.5
  • 66
    • 0028832067 scopus 로고
    • The ligand binding domains of the thyroid hormone/retinoid receptor gene subfamily function in vivo to mediate heterodimerization, gene silencing and transactivation
    • Qi, J.-S., V. Desai-Yajnik, M. E. Greene, B. M. Raaka, and H. H. Samuels. 1995. The ligand binding domains of the thyroid hormone/retinoid receptor gene subfamily function in vivo to mediate heterodimerization, gene silencing and transactivation. Mol. Cell. Biol. 15:1817-1825.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1817-1825
    • Qi, J.-S.1    Desai-Yajnik, V.2    Greene, M.E.3    Raaka, B.M.4    Samuels, H.H.5
  • 67
    • 24444446497 scopus 로고    scopus 로고
    • Molecular interactions of p53 with thyroid hormone nuclear receptors
    • Qi, J.-S., V. Desai-Yajnik, and H. H. Samuels. 1996. Molecular interactions of p53 with thyroid hormone nuclear receptors. J. Invest. Med. 44:234A.
    • (1996) J. Invest. Med. , vol.44
    • Qi, J.-S.1    Desai-Yajnik, V.2    Samuels, H.H.3
  • 68
    • 0026648086 scopus 로고
    • Identification of a growth suppression domain within the retinoblastoma gene product
    • Qin, X., T. Chittenden, D. M. Livingston, and J. W G Kaelin. 1992. Identification of a growth suppression domain within the retinoblastoma gene product. Genes Dev. 6:953-964.
    • (1992) Genes Dev. , vol.6 , pp. 953-964
    • Qin, X.1    Chittenden, T.2    Livingston, D.M.3    Kaelin, J.W.G.4
  • 69
    • 0021004708 scopus 로고
    • Two distinct mechanisms regulate the levels of a cellular tumor antigen, p53
    • Reich, N. C., M. Oren, and A. J. Levine. 1983. Two distinct mechanisms regulate the levels of a cellular tumor antigen, p53. Mol. Cell. Biol. 3:2143-2150.
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 2143-2150
    • Reich, N.C.1    Oren, M.2    Levine, A.J.3
  • 70
    • 0028170786 scopus 로고
    • Wild-type and mutant HIV-1 and HIV-2 tat proteins expressed in Escherichia coli as fusions with glutathione S-transferase
    • Rhim, H., C. O. Echetebu, C. H. Herrman, and A. P. Rice. 1994. Wild-type and mutant HIV-1 and HIV-2 tat proteins expressed in Escherichia coli as fusions with glutathione S-transferase. J. Acquired Immune Defic. Syndr. 7:1116-1121.
    • (1994) J. Acquired Immune Defic. Syndr. , vol.7 , pp. 1116-1121
    • Rhim, H.1    Echetebu, C.O.2    Herrman, C.H.3    Rice, A.P.4
  • 71
    • 0027138211 scopus 로고
    • A novel cis element mediating ligand-independent activation by c-erbA: Implications for hormonal regulation
    • Saatcioglu, F., T. Deng, and M. Karin. 1993. A novel cis element mediating ligand-independent activation by c-erbA: implications for hormonal regulation. Cell 75:1095-1105.
    • (1993) Cell , vol.75 , pp. 1095-1105
    • Saatcioglu, F.1    Deng, T.2    Karin, M.3
  • 72
    • 0028847563 scopus 로고
    • Modulation of p53-mediated transcriptional repression and apoptosis by the adenovirus E1B 19K protein
    • Sabbatini, P., S. K. Chiou, L. Rao, and E. White. 1995. Modulation of p53-mediated transcriptional repression and apoptosis by the adenovirus E1B 19K protein. Mol. Cell. Biol. 15:1060-1070.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1060-1070
    • Sabbatini, P.1    Chiou, S.K.2    Rao, L.3    White, E.4
  • 73
    • 0025775929 scopus 로고
    • Repression of the interleukin 6 gene promoter by p53 and the retinoblastoma susceptibility product
    • Santhanam, U., A. Ray, and P. B. Sehgal. 1991. Repression of the interleukin 6 gene promoter by p53 and the retinoblastoma susceptibility product. Proc. Natl. Acad. Sci. USA 88:7605-7609.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7605-7609
    • Santhanam, U.1    Ray, A.2    Sehgal, P.B.3
  • 75
    • 0026639142 scopus 로고
    • Synergistic activation of the rat growth hormone promoter by Pit-1 and the thyroid hormone receptor
    • Schaufele, F., B. L. West, and J. Baxter. 1992. Synergistic activation of the rat growth hormone promoter by Pit-1 and the thyroid hormone receptor. Mol. Endocrinol. 6:656-665.
    • (1992) Mol. Endocrinol. , vol.6 , pp. 656-665
    • Schaufele, F.1    West, B.L.2    Baxter, J.3
  • 76
    • 0025639158 scopus 로고
    • The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53
    • Scheffner, M., B. A. Werness, J. M. Huibregtse, A. J. Levine, and P. M. Howley. 1990. The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53. Cell 61:1129-1136.
    • (1990) Cell , vol.61 , pp. 1129-1136
    • Scheffner, M.1    Werness, B.A.2    Huibregtse, J.M.3    Levine, A.J.4    Howley, P.M.5
  • 77
    • 0026047492 scopus 로고
    • Thyroid hormone receptor/c-erba and v-erbA: A single amino acid difference in the C-terminal region influences dominant negative activity and receptor dimer formation
    • Selmi, S., and H. H. Samuels. 1991. Thyroid hormone receptor/c-erbA and v-erbA: a single amino acid difference in the C-terminal region influences dominant negative activity and receptor dimer formation. J. Biol. Chem. 266:11589-11593.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11589-11593
    • Selmi, S.1    Samuels, H.H.2
  • 78
    • 0028238213 scopus 로고
    • Immediate early up-regulation of bax expression by p53 but not TGFβ1: A paradigm for distinct apoptotic pathways
    • Selvakumaran, M., H. K. Liu, T. Miyashita, H. G. Wang, S. Krajewski, J. C. Reed, B. Hoffman, and D. Liebermann. 1994. Immediate early up-regulation of bax expression by p53 but not TGFβ1: a paradigm for distinct apoptotic pathways. Oncogene 9:1791-1798.
    • (1994) Oncogene , vol.9 , pp. 1791-1798
    • Selvakumaran, M.1    Liu, H.K.2    Miyashita, T.3    Wang, H.G.4    Krajewski, S.5    Reed, J.C.6    Hoffman, B.7    Liebermann, D.8
  • 79
    • 0026446686 scopus 로고
    • Identification of a minimal transforming domain of p53: Negative dominance through abrogation of sequence-specific DNA binding
    • Shaulian, E., A. Zauberman, D. Ginsberg, and M. Oren. 1992. Identification of a minimal transforming domain of p53: negative dominance through abrogation of sequence-specific DNA binding. Mol. Cell. Biol. 12:5581-5592.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5581-5592
    • Shaulian, E.1    Zauberman, A.2    Ginsberg, D.3    Oren, M.4
  • 80
    • 0026752654 scopus 로고
    • Negative regulation of Rb expression by the p53 gene product
    • Shiio, Y., T. Yamamoto, and N. Yamaguchi. 1992. Negative regulation of Rb expression by the p53 gene product. Proc. Natl. Acad. Sci. USA 89: 5206-5210.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5206-5210
    • Shiio, Y.1    Yamamoto, T.2    Yamaguchi, N.3
  • 81
    • 0028290465 scopus 로고
    • DNA sequence specificity of the v-Erb A oncoprotein/thyroid hormone receptor: Role of the P-box and its interaction with more N-terminal determinants of DNA recognition
    • Smit-McBride, Z., and M. L. Privalsky. 1994. DNA sequence specificity of the v-Erb A oncoprotein/thyroid hormone receptor: role of the P-box and its interaction with more N-terminal determinants of DNA recognition. Mol. Endocrinol. 8:819-828.
    • (1994) Mol. Endocrinol. , vol.8 , pp. 819-828
    • Smit-McBride, Z.1    Privalsky, M.L.2
  • 82
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D. B., and K. S. Johnson. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67:31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 83
    • 0025375355 scopus 로고
    • Structural aspects of the p53 protein in relation to gene evolution
    • Soussi, T., C. C. deFromentel, and P. May. 1990. Structural aspects of the p53 protein in relation to gene evolution. Oncogene 5:945-952.
    • (1990) Oncogene , vol.5 , pp. 945-952
    • Soussi, T.1    Defromentel, C.C.2    May, P.3
  • 84
    • 0026637484 scopus 로고
    • A C-terminal α-helix plus basic region motif is the major structural determinant of p53 tetramerization
    • Sturzbecher, H. W., R. Brain, C. Addison, K. Rudge, M. Remm, M. Grimaldi, E. Keenan, and J. R. Jenkins. 1992. A C-terminal α-helix plus basic region motif is the major structural determinant of p53 tetramerization. Oncogene 7:1513-1523.
    • (1992) Oncogene , vol.7 , pp. 1513-1523
    • Sturzbecher, H.W.1    Brain, R.2    Addison, C.3    Rudge, K.4    Remm, M.5    Grimaldi, M.6    Keenan, E.7    Jenkins, J.R.8
  • 85
    • 0028345217 scopus 로고
    • Overlapping domains on the p53 protein regulate its transcriptional activation and repression functions
    • Subler, M. A., D. W. Martin, and S. Deb. 1994. Overlapping domains on the p53 protein regulate its transcriptional activation and repression functions. Oncogene 9:1351-1359.
    • (1994) Oncogene , vol.9 , pp. 1351-1359
    • Subler, M.A.1    Martin, D.W.2    Deb, S.3
  • 86
    • 0027222646 scopus 로고
    • EBNA-5, an Epstein-Barr virus-encoded nuclear antigen binds to the retinoblastoma and p53 proteins
    • Szekely. L., G. Selivanova, K. Magnusson, P. G. Klein, and K. G. Wilman. 1993. EBNA-5, an Epstein-Barr virus-encoded nuclear antigen binds to the retinoblastoma and p53 proteins. Proc. Natl. Acad. Sci. USA 90:5455-5459.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5455-5459
    • Szekely, L.1    Selivanova, G.2    Magnusson, K.3    Klein, P.G.4    Wilman, K.G.5
  • 87
    • 0028789982 scopus 로고
    • Differential inhibition of signaling pathways by dominant-negative SH2/SH3 adapter proteins
    • Tanaka, M., R. Gupta, and B. J. Mayer. 1995. Differential inhibition of signaling pathways by dominant-negative SH2/SH3 adapter proteins. Mol. Cell. Biol. 15:6829-6837.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6829-6837
    • Tanaka, M.1    Gupta, R.2    Mayer, B.J.3
  • 88
    • 0029788134 scopus 로고    scopus 로고
    • Induction of apoptosis by p53 is independent of its oligomeric state and can be abolished by HPV-18 E6 through ubiquitin mediated degradation
    • Thomas, M., G. Matlashewski, D. Pim, and L. Banks. 1996. Induction of apoptosis by p53 is independent of its oligomeric state and can be abolished by HPV-18 E6 through ubiquitin mediated degradation. Oncogene 13:265-273.
    • (1996) Oncogene , vol.13 , pp. 265-273
    • Thomas, M.1    Matlashewski, G.2    Pim, D.3    Banks, L.4
  • 89
    • 0025516375 scopus 로고
    • Nuclear receptors for retinoic acid and thyroid hormone regulate transcription of keratin genes
    • Tomic, M., C.-K. Jiang, H. S. Epstein, I. M. Freedberg, H. H. Samuels, and M. Blumenberg. 1990. Nuclear receptors for retinoic acid and thyroid hormone regulate transcription of keratin genes. Cell Reg. 1:965-973.
    • (1990) Cell Reg. , vol.1 , pp. 965-973
    • Tomic, M.1    Jiang, C.-K.2    Epstein, H.S.3    Freedberg, I.M.4    Samuels, H.H.5    Blumenberg, M.6
  • 90
    • 0030030298 scopus 로고    scopus 로고
    • Novel regulation of keratin gene expression by thyroid hormone and retinoid receptors
    • Tomic-Canic, M., D. Day, H. H. Samuels, I. M. Freedberg, and M. Blumenberg. 1996. Novel regulation of keratin gene expression by thyroid hormone and retinoid receptors. J. Biol. Chem. 271:1416-1423.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1416-1423
    • Tomic-Canic, M.1    Day, D.2    Samuels, H.H.3    Freedberg, I.M.4    Blumenberg, M.5
  • 91
    • 0023756692 scopus 로고
    • Retinoic acid and thyroid hormone induce gene expression through a common responsive element
    • Umesono, K., V. Giguere, C. K. Glass, M. G. Rosenfeld, and R. M. Evans. 1988. Retinoic acid and thyroid hormone induce gene expression through a common responsive element. Nature 336:262-265.
    • (1988) Nature , vol.336 , pp. 262-265
    • Umesono, K.1    Giguere, V.2    Glass, C.K.3    Rosenfeld, M.G.4    Evans, R.M.5
  • 92
    • 0025812291 scopus 로고
    • Direct repeats as selective response elements for the thyroid hormone, retinoic acid, and vitamin D receptors
    • Umesono, K., K. K. Murakami, C. C. Thompson, and R. M. Evans. 1991. Direct repeats as selective response elements for the thyroid hormone, retinoic acid, and vitamin D receptors. Cell 65:1255-1266.
    • (1991) Cell , vol.65 , pp. 1255-1266
    • Umesono, K.1    Murakami, K.K.2    Thompson, C.C.3    Evans, R.M.4
  • 94
    • 0027361285 scopus 로고
    • Dominant and non-dominant negative c-erbAβ1 receptors associated with thyroid hormone resistance syndromes augment TPA-induction of the collagenase promoter and exhibit defective T3-mediated repression
    • Ways, D. K., W. Qin, P. Cook, P. J. Parker, J. B. Menke, E. Hao, A. M. Smith, C. Jones, J. M. Hershman, M. E. Geffner, F. Su, H. H. Samuels, and S. J. Usala. 1993. Dominant and non-dominant negative c-erbAβ1 receptors associated with thyroid hormone resistance syndromes augment TPA-induction of the collagenase promoter and exhibit defective T3-mediated repression. Mol. Endocrinol. 7:1112-1120.
    • (1993) Mol. Endocrinol. , vol.7 , pp. 1112-1120
    • Ways, D.K.1    Qin, W.2    Cook, P.3    Parker, P.J.4    Menke, J.B.5    Hao, E.6    Smith, A.M.7    Jones, C.8    Hershman, J.M.9    Geffner, M.E.10    Su, F.11    Samuels, H.H.12    Usala, S.J.13
  • 97
    • 0025271203 scopus 로고
    • Association of human papillomavirus types 16 and 18 E6 proteins with p53
    • Werness, B. A., A. J. Levine, and P. M. Howley. 1990. Association of human papillomavirus types 16 and 18 E6 proteins with p53. Science 248:76-79.
    • (1990) Science , vol.248 , pp. 76-79
    • Werness, B.A.1    Levine, A.J.2    Howley, P.M.3
  • 98
    • 0027244853 scopus 로고
    • The p53-mdm-2 autoregulatory feedback loop
    • Wu, X., J. H. Bayle, D. Olson, and A. J. Levine. 1993. The p53-mdm-2 autoregulatory feedback loop. Genes Dev. 7:1125-1132.
    • (1993) Genes Dev. , vol.7 , pp. 1125-1132
    • Wu, X.1    Bayle, J.H.2    Olson, D.3    Levine, A.J.4
  • 99
    • 0028243587 scopus 로고
    • Effect of tumor suppressors on cell cycle-regulatory genes: RB suppresses p34cdc2 expression and normal p53 suppresses cyclin A expression
    • Yamamoto, M., M. Yoshida, K. Ono, T. Fujita, N. Ohtani-Fujita, T. Sakai, and T. Nikaido. 1994. Effect of tumor suppressors on cell cycle-regulatory genes: RB suppresses p34cdc2 expression and normal p53 suppresses cyclin A expression. Exp. Cell Res. 210:94-101.
    • (1994) Exp. Cell Res. , vol.210 , pp. 94-101
    • Yamamoto, M.1    Yoshida, M.2    Ono, K.3    Fujita, T.4    Ohtani-Fujita, N.5    Sakai, T.6    Nikaido, T.7
  • 100
    • 0029978846 scopus 로고    scopus 로고
    • Modulation of the transcriptional activity of thyroid hormone receptors by the tumor suppressor p53
    • Yap, N., C.-L. Yu, and S.-Y. Cheng. 1996. Modulation of the transcriptional activity of thyroid hormone receptors by the tumor suppressor p53. Proc. Natl. Acad. Sci. USA 93:4273-4277.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4273-4277
    • Yap, N.1    Yu, C.-L.2    Cheng, S.-Y.3
  • 101
    • 0026560315 scopus 로고
    • Inhibition of p53 transactivation required for transformation by adenovirus early 1B protein
    • Yew, P. R., and A. J. Berk. 1992. Inhibition of p53 transactivation required for transformation by adenovirus early 1B protein. Nature 347:82-85.
    • (1992) Nature , vol.347 , pp. 82-85
    • Yew, P.R.1    Berk, A.J.2
  • 103
    • 0026702212 scopus 로고
    • Wild-type p53 mediates positive regulation of gene expression through a specific DNA sequence element
    • Zambetti, G. P., J. Bargonetti, K. Walker, C. Prives, and A. J. Levine. 1992. Wild-type p53 mediates positive regulation of gene expression through a specific DNA sequence element. Genes Dev. 6:1143-1152.
    • (1992) Genes Dev. , vol.6 , pp. 1143-1152
    • Zambetti, G.P.1    Bargonetti, J.2    Walker, K.3    Prives, C.4    Levine, A.J.5
  • 104
    • 0025339079 scopus 로고
    • V-erbA oncogene activation entails the loss of hormone-dependent regulator activity of c-erbA
    • Zenke, M., A. Munoz, J. Sap, B. Vennstrom, and H. Beug. 1990. v-erbA oncogene activation entails the loss of hormone-dependent regulator activity of c-erbA. Cell 61:1035-1049.
    • (1990) Cell , vol.61 , pp. 1035-1049
    • Zenke, M.1    Munoz, A.2    Sap, J.3    Vennstrom, B.4    Beug, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.