메뉴 건너뛰기




Volumn 18, Issue 6, 1998, Pages 3483-3494

Transactivation by retinoid X receptor-peroxisome proliferator-activated receptor γ (PPARγ) heterodimers: Intermolecular synergy requires only the PPRAγ hormone-dependent activation function

Author keywords

[No Author keywords available]

Indexed keywords

PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR; RETINOID X RECEPTOR;

EID: 0031813879     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.18.6.3483     Document Type: Article
Times cited : (161)

References (77)
  • 1
    • 0026726806 scopus 로고
    • Hormone and antihormone induce distinct conformational changes which are central to steroid receptor activation
    • Allan, G. F., X. Leng, S. Y. Tasi, N. L. Weigel, D. P. Edwards, M.-J. Tsai, and B. W. O'Malley. 1992. Hormone and antihormone induce distinct conformational changes which are central to steroid receptor activation. J. Biol. Chem. 267:19513-19520.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19513-19520
    • Allan, G.F.1    Leng, X.2    Tasi, S.Y.3    Weigel, N.L.4    Edwards, D.P.5    Tsai, M.-J.6    O'Malley, B.W.7
  • 2
    • 0027081043 scopus 로고
    • Ligand-dependent conformational changes in the progesterone receptor are necessary events that follow DNA binding
    • Allan, G. F., X. Leng, S. Y. Tsai, N. L. Weigel, D. P. Edwards, M.-J. Tsai, and B. W. O'Malley. 1992. Ligand-dependent conformational changes in the progesterone receptor are necessary events that follow DNA binding. Proc. Natl. Acad Sci. USA 89:11750-11754.
    • (1992) Proc. Natl. Acad Sci. USA , vol.89 , pp. 11750-11754
    • Allan, G.F.1    Leng, X.2    Tsai, S.Y.3    Weigel, N.L.4    Edwards, D.P.5    Tsai, M.-J.6    O'Malley, B.W.7
  • 3
    • 0028988482 scopus 로고
    • The τc activation domain of the thyroid hormone receptor is required for the 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 τc activation domain of the thyroid hormone receptor is required for the 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
  • 4
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister, A. J., and T. Kouzarides. 1997. The CBP co-activator is a histone acetyltransferase. Nature 284:641-643.
    • (1997) Nature , vol.284 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 5
    • 0027521287 scopus 로고
    • Transcriptional activation hy the estrogen receptor requires a conformational change in the ligand binding domain
    • Beekman, J. M., G. F. Allan, S. Y. Tsai, M.-J. Tsai, and B. W. O'Malley. 1993. Transcriptional activation hy the estrogen receptor requires a conformational change in the ligand binding domain. Mol. Endocrinol. 7:1266-1274.
    • (1993) Mol. Endocrinol. , vol.7 , pp. 1266-1274
    • Beekman, J.M.1    Allan, G.F.2    Tsai, S.Y.3    Tsai, M.-J.4    O'Malley, B.W.5
  • 7
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha
    • Bourguet, W., M. Ruff, P. Chambon, H. Gronemeyer, and D. Moras. 1995. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha. Nature 375:377-382.
    • (1995) Nature , vol.375 , pp. 377-382
    • Bourguet, W.1    Ruff, M.2    Chambon, P.3    Gronemeyer, H.4    Moras, D.5
  • 8
    • 0032498230 scopus 로고    scopus 로고
    • The enhanceosome and transcriptional synergy
    • Carey, M. 1998. The enhanceosome and transcriptional synergy. Cell 92:5-8.
    • (1998) Cell , vol.92 , pp. 5-8
    • Carey, M.1
  • 10
    • 0028202490 scopus 로고
    • Peroxisome proliferator and retinoid signaling pathways co-regulate preadipocyte phenotype and survival
    • Chawla, A., and M. A. Lazar. 1994. Peroxisome proliferator and retinoid signaling pathways co-regulate preadipocyte phenotype and survival. Proc. Natl. Acad. Sci. USA 91:1786-1790.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1786-1790
    • Chawla, A.1    Lazar, M.A.2
  • 11
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
    • Chen, H., R. J. Lin, R. L. Schiltz, D. Chakravarti, A. Nash, L. Nagy, M. L. Privalsky, Y. Nakatani, and R. M. Evans. 1997. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 90:569-580.
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1    Lin, R.J.2    Schiltz, R.L.3    Chakravarti, D.4    Nash, A.5    Nagy, L.6    Privalsky, M.L.7    Nakatani, Y.8    Evans, R.M.9
  • 12
    • 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
  • 13
    • 0029794881 scopus 로고    scopus 로고
    • SMRT isoforms mediate repression and anti-repression of nuclear receptor heterodimers
    • Chen, J. D., K. Umesono, and R. M. Evans. 1996. SMRT isoforms mediate repression and anti-repression of nuclear receptor heterodimers. Proc. Natl. Acad. Sci. USA 93:7567-7571.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7567-7571
    • Chen, J.D.1    Umesono, K.2    Evans, R.M.3
  • 14
    • 0029930872 scopus 로고    scopus 로고
    • Modulation of nuclear receptor interactions by ligands: Kinetic analysis using surface plasmon resonance
    • Cheskis, B., and L. P. Freedman. 1996. Modulation of nuclear receptor interactions by ligands: kinetic analysis using surface plasmon resonance. Biochemistry 35:3309-3318.
    • (1996) Biochemistry , vol.35 , pp. 3309-3318
    • Cheskis, B.1    Freedman, L.P.2
  • 15
    • 0027526297 scopus 로고
    • Functional inhibition of retinoic acid response by dominant negative retinoic receptor mutants
    • Damm, K., R. A. Heyman, K. Umesono, and R. A. Evans. 1993. Functional inhibition of retinoic acid response by dominant negative retinoic receptor mutants. Proc. Natl. Acad. Sci. USA 90:2989-2993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2989-2993
    • Damm, K.1    Heyman, R.A.2    Umesono, K.3    Evans, R.A.4
  • 16
    • 1842295133 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptors and retinoid acid receptors differentially control the interactions of retinoid X receptor heterodimers with ligands, coactivators, and corepressors
    • DiRenzo, J., M. Soderstrom, R. Kurokawa, M.-H. Ogliastro, M. Ricote, S. Ingrey, A. Horlein, M. G. Rosenfeld, and C. K. Glass. 1997. Peroxisome proliferator-activated receptors and retinoid acid receptors differentially control the interactions of retinoid X receptor heterodimers with ligands, coactivators, and corepressors. Mol. Cell. Biol. 17:2166-2176.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2166-2176
    • DiRenzo, J.1    Soderstrom, M.2    Kurokawa, R.3    Ogliastro, M.-H.4    Ricote, M.5    Ingrey, S.6    Horlein, A.7    Rosenfeld, M.G.8    Glass, C.K.9
  • 17
    • 0031439111 scopus 로고    scopus 로고
    • P300 functions as a coactivator for the peroxisome proliferator-activated receptor α
    • Dowell, P., J. E. Ishmael, D. Avram, V. J. Peterson, D. J. Nevrivy, and M. Leid. 1997. p300 functions as a coactivator for the peroxisome proliferator-activated receptor α. J. Biol. Chem. 272:33435-33443.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33435-33443
    • Dowell, P.1    Ishmael, J.E.2    Avram, D.3    Peterson, V.J.4    Nevrivy, D.J.5    Leid, M.6
  • 19
    • 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
  • 20
    • 0026703387 scopus 로고
    • A ligand-induced conformational change in the estrogen receptor is localized in the steroid binding domain
    • Fritsch, M. C., C. M. Leary, J. D. Furlow, H. Ahrens, T. J. Schuh, G. C. Mueller, and J. Gorski. 1992. A ligand-induced conformational change in the estrogen receptor is localized in the steroid binding domain. Biochemistry 31:5303-5311.
    • (1992) Biochemistry , vol.31 , pp. 5303-5311
    • Fritsch, M.C.1    Leary, C.M.2    Furlow, J.D.3    Ahrens, H.4    Schuh, T.J.5    Mueller, G.C.6    Gorski, J.7
  • 22
    • 0028840419 scopus 로고
    • Transcriptional coactivators in yeast and beyond
    • Guarente, L. 1995. Transcriptional coactivators in yeast and beyond. Trends Biochem. Sci. 20:517-521.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 517-521
    • Guarente, L.1
  • 24
    • 0027411327 scopus 로고
    • Synergism in transcriptional activation: A kinetic view
    • Herschlag, D., and F. B. Johnson. 1993. Synergism in transcriptional activation: a kinetic view. Genes Dev. 7:173-179.
    • (1993) Genes Dev. , vol.7 , pp. 173-179
    • Herschlag, D.1    Johnson, F.B.2
  • 25
    • 0030949836 scopus 로고    scopus 로고
    • GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors
    • Hong, H., K. Kohli, M. J. Garabedian, and M. R. Stallcup. 1997. GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors. Mol. Cell. Biol. 17:2735-2744.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2735-2744
    • Hong, H.1    Kohli, K.2    Garabedian, M.J.3    Stallcup, M.R.4
  • 26
    • 0028212908 scopus 로고
    • The role of activators in RNA polymerase II transcription complexes
    • Hori, R., and M. Carey. 1994. The role of activators in RNA polymerase II transcription complexes. Curr. Opin. Genet. Dev. 4:236-244.
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 236-244
    • Hori, R.1    Carey, M.2
  • 29
    • 0030029419 scopus 로고    scopus 로고
    • Adapter-mediated recruitment of RNA polymerase II to a signal-dependent activator
    • Kee, B. L., J. Arias, and M. R. Montminy. 1996. Adapter-mediated recruitment of RNA polymerase II to a signal-dependent activator. J. Biol. Chem. 271:2373-2375.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2373-2375
    • Kee, B.L.1    Arias, J.2    Montminy, M.R.3
  • 30
    • 0028012039 scopus 로고
    • Different agonist- and antagonist-induced conformational changes in retinoic acid receptors analyzed by protease mapping
    • Keidel, S., P. LeMotte, and C. Apfel. 1994. Different agonist-and antagonist-induced conformational changes in retinoic acid receptors analyzed by protease mapping. Mol. Cell. Biol. 14:287-298.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 287-298
    • Keidel, S.1    Lemotte, P.2    Apfel, C.3
  • 31
    • 0028972026 scopus 로고
    • A prostaglandin J2 metabolite binds peroxisome proliferator-activated receptor gamma and promotes adipocyte differentiation
    • Kliewer, S. A., J. M. Lenhard, T. M. Willson, I. Patel, D. C. Morris, and J. Lehmann. 1995. A prostaglandin J2 metabolite binds peroxisome proliferator-activated receptor gamma and promotes adipocyte differentiation. Cell 83:813-819.
    • (1995) Cell , vol.83 , pp. 813-819
    • Kliewer, S.A.1    Lenhard, J.M.2    Willson, T.M.3    Patel, I.4    Morris, D.C.5    Lehmann, J.6
  • 32
    • 0026705751 scopus 로고
    • Convergence of 9-cis retinoic acid and peroxisome proliferator signaling pathways through heterodimer formation of their receptors
    • Kliewer, S. A., K. Umesono, D. J. Noonan, R. A. Heyman, and R. A. Evans. 1992. Convergence of 9-cis retinoic acid and peroxisome proliferator signaling pathways through heterodimer formation of their receptors. Nature 358:771-774.
    • (1992) Nature , vol.358 , pp. 771-774
    • Kliewer, S.A.1    Umesono, K.2    Noonan, D.J.3    Heyman, R.A.4    Evans, R.A.5
  • 37
    • 0029115655 scopus 로고
    • 9-cis retinoic acid signaling: Changing partners causes some excitement
    • Leblanc, B. P., and H. G. Stunnenberg. 1995. 9-cis retinoic acid signaling: changing partners causes some excitement. Genes Dev. 9:1811-1816.
    • (1995) Genes Dev. , vol.9 , pp. 1811-1816
    • Leblanc, B.P.1    Stunnenberg, H.G.2
  • 38
    • 0027222793 scopus 로고
    • Structure of the retinoid X receptorα DNA binding domain: A helix required for homodimeric DNA binding
    • Lee, M. S., S. A. Kliewer, J. Provencal, P. E. Wright, and R. M. Evans. 1993. Structure of the retinoid X receptorα DNA binding domain: a helix required for homodimeric DNA binding. Science 260:1117-1121.
    • (1993) Science , vol.260 , pp. 1117-1121
    • Lee, M.S.1    Kliewer, S.A.2    Provencal, J.3    Wright, P.E.4    Evans, R.M.5
  • 39
    • 0029016829 scopus 로고
    • An antidiabetic thiazolidinedione is a high affinity ligand for peroxisome proliferator-activated receptor gamma (PPARγ)
    • Lehmann, J. M., L. B. Moore, T. A. Smith-Oliver, W. O. Wilkison, T. M. Willson, and S. A. Kliewer. 1995. An antidiabetic thiazolidinedione is a high affinity ligand for peroxisome proliferator-activated receptor gamma (PPARγ). J. Biol. Chem. 270:12953-12956.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12953-12956
    • Lehmann, J.M.1    Moore, L.B.2    Smith-Oliver, T.A.3    Wilkison, W.O.4    Willson, T.M.5    Kliewer, S.A.6
  • 40
    • 0028336807 scopus 로고
    • Ligand-induced alteration of the protease sensitivity of retinoid X receptorα
    • Leid, M. 1994. Ligand-induced alteration of the protease sensitivity of retinoid X receptorα. J. Biol. Chem. 269:14175-14181.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14175-14181
    • Leid, M.1
  • 41
    • 0027754125 scopus 로고
    • Ligand-dependent conformational changes in thyroid hormone and retinoic acid receptors are potentially enhanced by heterodimerization with retinoic X receptor
    • Leng, X., S. Y. Tsai, B. W. O'Malley, and M.-J. Tsai. 1993. Ligand-dependent conformational changes in thyroid hormone and retinoic acid receptors are potentially enhanced by heterodimerization with retinoic X receptor. J. Steroid Biochem. Mol. Biol. 46:643-661.
    • (1993) J. Steroid Biochem. Mol. Biol. , vol.46 , pp. 643-661
    • Leng, X.1    Tsai, S.Y.2    O'Malley, B.W.3    Tsai, M.-J.4
  • 42
    • 0031041075 scopus 로고    scopus 로고
    • Regulating adipogenesis
    • Mandrup, S., and M. D. Lane. 1997. Regulating adipogenesis. J. Biol. Chem. 272:5367-5370.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5367-5370
    • Mandrup, S.1    Lane, M.D.2
  • 43
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptors
    • Mangelsdorf, D. J., and R. M. Evans. 1995. The RXR heterodimers and orphan receptors. Cell 83:841-850.
    • (1995) Cell , vol.83 , pp. 841-850
    • Mangelsdorf, D.J.1    Evans, R.M.2
  • 48
    • 0030902507 scopus 로고    scopus 로고
    • Analysis of a cAMP-responsive activator reveals a two-component mechanism for transcriptional induction via signal-dependent factors
    • Nakajima, T., C. Uchida, S. F. Anderson, J. D. Parvin, and M. Montminy. 1997. Analysis of a cAMP-responsive activator reveals a two-component mechanism for transcriptional induction via signal-dependent factors. Genes Dev. 11:738-747.
    • (1997) Genes Dev. , vol.11 , pp. 738-747
    • Nakajima, T.1    Uchida, C.2    Anderson, S.F.3    Parvin, J.D.4    Montminy, M.5
  • 49
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivator p300 and CBP are histone acetyltransferases
    • Ogryzko, V. V., R. L. Schitz, V. Russanova, B. H. Howard, and Y. Nakatani. 1996. The transcriptional coactivator p300 and CBP are histone acetyltransferases. Cell 87:953-959.
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Schitz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 50
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for 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 for 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
  • 51
    • 0031929308 scopus 로고    scopus 로고
    • Engineering novel specificities for ligand-activated transcription in the nuclear hormone receptor RXR
    • Peet, D. J., D. F. Doyle, D. R. Corey, and D. J. Mangelsdorf. 1998. Engineering novel specificities for ligand-activated transcription in the nuclear hormone receptor RXR. Chem. Biol. 5:13-21.
    • (1998) Chem. Biol. , vol.5 , pp. 13-21
    • Peet, D.J.1    Doyle, D.F.2    Corey, D.R.3    Mangelsdorf, D.J.4
  • 52
    • 0030960672 scopus 로고    scopus 로고
    • Transcriptional activation by recruitment
    • Ptashne, M., and A. Gann. 1997. Transcriptional activation by recruitment. Nature 386:569-577.
    • (1997) Nature , vol.386 , pp. 569-577
    • Ptashne, M.1    Gann, A.2
  • 53
    • 0029643780 scopus 로고
    • Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid
    • Renaud, J.-P., N. Rochel, M. Ruff, V. Vivat, P. Chambon, H. Gronemeyer, and D. Moras. 1995. Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid. Nature 378:681-689.
    • (1995) Nature , vol.378 , pp. 681-689
    • Renaud, J.-P.1    Rochel, N.2    Ruff, M.3    Vivat, V.4    Chambon, P.5    Gronemeyer, H.6    Moras, D.7
  • 54
    • 0029085038 scopus 로고
    • Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation
    • Schulman, I. G., D. Chakravarti, H. Juguilon, A. Romo, and R. M. Evans. 1995. Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation. Proc. Natl. Acad. Sci. USA 92:8288-8292.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8288-8292
    • Schulman, I.G.1    Chakravarti, D.2    Juguilon, H.3    Romo, A.4    Evans, R.M.5
  • 55
    • 0029938795 scopus 로고    scopus 로고
    • Activation and repression by nuclear hormone receptors: Hormone modulates an equilibrium between active and repressive states
    • Schulman, I. G., H. Juguilon, and R. M. Evans. 1996. Activation and repression by nuclear hormone receptors: hormone modulates an equilibrium between active and repressive states. Mol. Cell. Biol. 16:3807-3818.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3807-3818
    • Schulman, I.G.1    Juguilon, H.2    Evans, R.M.3
  • 56
    • 0031043055 scopus 로고    scopus 로고
    • The phantom ligand effect: Allosteric control of transcription by the retinoid X receptor
    • Schulman, I. G., C. Li, J. W. R. Schwabe, and R. M. Evans. 1997. The phantom ligand effect: allosteric control of transcription by the retinoid X receptor. Genes Dev. 11:299-308.
    • (1997) Genes Dev. , vol.11 , pp. 299-308
    • Schulman, I.G.1    Li, C.2    Schwabe, J.W.R.3    Evans, R.M.4
  • 57
    • 84920309813 scopus 로고    scopus 로고
    • Unpublished observations
    • Schulman, I. G. Unpublished observations.
    • Schulman, I.G.1
  • 58
    • 0030113441 scopus 로고    scopus 로고
    • Transcriptional control: How nuclear receptors get turned on
    • Schwabe, J. W. R. 1996. Transcriptional control: how nuclear receptors get turned on. Curr. Biol. 6:372-374.
    • (1996) Curr. Biol. , vol.6 , pp. 372-374
    • Schwabe, J.W.R.1
  • 59
    • 0024384860 scopus 로고
    • Steroid binding activity is retained in a 16-kDa fragment of the steroid binding domain of rat glucocorticoid receptor
    • Simons, S. S., F. D. Sistare, and P. K. Chakraboti. 1989. Steroid binding activity is retained in a 16-kDa fragment of the steroid binding domain of rat glucocorticoid receptor. J. Biol. Chem. 264:14493-14497.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14493-14497
    • Simons, S.S.1    Sistare, F.D.2    Chakraboti, P.K.3
  • 60
    • 0029786690 scopus 로고    scopus 로고
    • CREB binding protein acts synergistically with steroid receptor coactivator-1 to enhance steroid receptor-dependent transcription
    • Smith, C. L., S. A. Onate, M.-J. Tsai, and B. W. O'Malley. 1996. CREB binding protein acts synergistically with steroid receptor coactivator-1 to enhance steroid receptor-dependent transcription. Proc. Natl. Acad. Sci. USA 93:8884-8888.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8884-8888
    • Smith, C.L.1    Onate, S.A.2    Tsai, M.-J.3    O'Malley, B.W.4
  • 63
    • 0029050907 scopus 로고
    • Mutagenesis of the ligand binding domain of the human retinoic acid receptor α identifies critical residues for 9-cis-retinoic acid binding
    • Tate, B. F., and J. F. Grippo. 1995. Mutagenesis of the ligand binding domain of the human retinoic acid receptor α identifies critical residues for 9-cis-retinoic acid binding. J. Biol. Chem. 270:20258-20263.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20258-20263
    • Tate, B.F.1    Grippo, J.F.2
  • 64
    • 0028641559 scopus 로고
    • Stimulation of adipogenesis in fibroblasts by PPARγ2, a lipid-activated transcription factor
    • Tontonoz, P., E. Hu, and B. M. Spiegelman. 1994. Stimulation of adipogenesis in fibroblasts by PPARγ2, a lipid-activated transcription factor. Cell 79:1147-1156.
    • (1994) Cell , vol.79 , pp. 1147-1156
    • Tontonoz, P.1    Hu, E.2    Spiegelman, B.M.3
  • 66
    • 0030912539 scopus 로고    scopus 로고
    • The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function
    • Torchia, J., D. W. Rose, J. Inostroza, Y. Kamei, S. Westin, C. K. Glass, and M. G. Rosenfeld. 1997. The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature 387:677-684.
    • (1997) Nature , vol.387 , pp. 677-684
    • Torchia, J.1    Rose, D.W.2    Inostroza, J.3    Kamei, Y.4    Westin, S.5    Glass, C.K.6    Rosenfeld, M.G.7
  • 68
    • 0026653659 scopus 로고
    • The mechanism of RU486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor
    • Vegeto, E., G. F. Allan, W. T. Schrader, M.-J. Tsai, D. P. McDonnell, and B. W. O'Malley. 1992. The mechanism of RU486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor. Cell 69:703-713.
    • (1992) Cell , vol.69 , pp. 703-713
    • Vegeto, E.1    Allan, G.F.2    Schrader, W.T.3    Tsai, M.-J.4    McDonnell, D.P.5    O'Malley, B.W.6
  • 69
    • 0029954339 scopus 로고    scopus 로고
    • TIF2, a 16-kDa transcriptional mediator for ligand-dependent activation function AF-2 of nuclear receptors
    • Voegel, J. J., M. J. S. Heine, C. Zechel, P. Chambon, and H. Gronemeyer. 1996. TIF2, a 16-kDa transcriptional mediator for ligand-dependent activation function AF-2 of nuclear receptors. EMBO J. 15:3667-3675.
    • (1996) EMBO J. , vol.15 , pp. 3667-3675
    • Voegel, J.J.1    Heine, M.J.S.2    Zechel, C.3    Chambon, P.4    Gronemeyer, H.5
  • 71
    • 0031011661 scopus 로고    scopus 로고
    • Heterodimeric interaction between retinoid X receptor a and orphan nuclear receptor OR1 reveals dimerization-induced activation as a novel mechanism of nuclear receptor activation
    • Wiebel, F. F., and J.-A. Gustafsson. 1997. Heterodimeric interaction between retinoid X receptor a and orphan nuclear receptor OR1 reveals dimerization-induced activation as a novel mechanism of nuclear receptor activation. Mol. Cell. Biol. 17:3977-3986.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3977-3986
    • Wiebel, F.F.1    Gustafsson, J.-A.2
  • 72
    • 0031042762 scopus 로고    scopus 로고
    • Unique requirements for retinoid-dependent transcriptional activation by the orphan receptor LXR
    • Willy, P. J., and D. J. Mangelsdorf. 1997. Unique requirements for retinoid-dependent transcriptional activation by the orphan receptor LXR. Genes Dev. 11:289-298.
    • (1997) Genes Dev. , vol.11 , pp. 289-298
    • Willy, P.J.1    Mangelsdorf, D.J.2
  • 74
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • Yang, X.-J., V. V. Ogryzko, J.-I. Nishikawa, B. E. Howard, and Y. Nakatani. 1996. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382:319-324.
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.-J.1    Ogryzko, V.V.2    Nishikawa, J.-I.3    Howard, B.E.4    Nakatani, Y.5
  • 75
    • 0029773871 scopus 로고    scopus 로고
    • The nuclear hormone receptor coactivator SRC-1 is a specific target of p300
    • Yao, T.-P., G. Ku, N. Zhou, and D. M. Livingston. 1996. The nuclear hormone receptor coactivator SRC-1 is a specific target of p300. Proc. Natl. Acad. Sci. USA 93:10626-10631.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10626-10631
    • Yao, T.-P.1    Ku, G.2    Zhou, N.3    Livingston, D.M.4
  • 77
    • 0030991152 scopus 로고    scopus 로고
    • Stoichiometric and steric principles governing repression by nuclear hormone receptors
    • Zamir, I., J. Zhang, and M. A. Lazar. 1997. Stoichiometric and steric principles governing repression by nuclear hormone receptors. Genes Dev. 11:835-846.
    • (1997) Genes Dev. , vol.11 , pp. 835-846
    • Zamir, I.1    Zhang, J.2    Lazar, M.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.