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Volumn 46, Issue 5, 2007, Pages 1273-1283

Low-resolution structures of thyroid hormone receptor dimers and tetramers in solution

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; DNA; HORMONES; MOLECULAR STRUCTURE; OLIGOMERS; X RAY ANALYSIS;

EID: 33846794812     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061698h     Document Type: Article
Times cited : (11)

References (69)
  • 1
    • 0034964207 scopus 로고    scopus 로고
    • Physiological and molecular basis of thyroid hormone action
    • Yen, P. M. (2001) Physiological and molecular basis of thyroid hormone action, Physiol. Rev. 81, 1097-1142.
    • (2001) Physiol. Rev , vol.81 , pp. 1097-1142
    • Yen, P.M.1
  • 2
    • 0027416347 scopus 로고
    • Thyroid hormone receptors: Multiple forms, multiple possibilities
    • Lazar, M. A. (1993) Thyroid hormone receptors: Multiple forms, multiple possibilities, Endocr. Rev. 14, 184-193.
    • (1993) Endocr. Rev , vol.14 , pp. 184-193
    • Lazar, M.A.1
  • 3
    • 0034957480 scopus 로고    scopus 로고
    • Nuclear hormone receptors and gene expression
    • Aranda, A., and Pascual, A. (2001) Nuclear hormone receptors and gene expression, Physiol. Rev. 81, 1269-1304.
    • (2001) Physiol. Rev , vol.81 , pp. 1269-1304
    • Aranda, A.1    Pascual, A.2
  • 4
    • 0028911237 scopus 로고
    • New insights into the structure and function of the thyroid hormone receptor
    • Cheng, S.-Y. (1995) New insights into the structure and function of the thyroid hormone receptor, J. Biomed. Sci. 2, 77-89.
    • (1995) J. Biomed. Sci , vol.2 , pp. 77-89
    • Cheng, S.-Y.1
  • 6
    • 1942453725 scopus 로고    scopus 로고
    • Selective activation of thyroid hormone signaling pathways by GC-1: A new approach to controlling cholesterol and body weight
    • Baxter, J. D., Webb, P., Grover, G., and Scanlan, T. S. (2004) Selective activation of thyroid hormone signaling pathways by GC-1: A new approach to controlling cholesterol and body weight, Trends Endocrin. Metab. 15, 154-157.
    • (2004) Trends Endocrin. Metab , vol.15 , pp. 154-157
    • Baxter, J.D.1    Webb, P.2    Grover, G.3    Scanlan, T.S.4
  • 7
    • 0028331874 scopus 로고
    • How do thyroid hormone receptors bind to structurally diverse response elements
    • Desvergne, B. (1994) How do thyroid hormone receptors bind to structurally diverse response elements, Mol. Cell. Endocrinol. 100, 125-131.
    • (1994) Mol. Cell. Endocrinol , vol.100 , pp. 125-131
    • Desvergne, B.1
  • 8
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator excahange in transcription function of nuclear receptors
    • Glass, C. K., and Rosenfeld, M. G. (2000) The coregulator excahange in transcription function of nuclear receptors, Genes Dev. 14, 121-141.
    • (2000) Genes Dev , vol.14 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 11
    • 0035805580 scopus 로고    scopus 로고
    • Definition of the surface in the thyroid hormone receptor ligand binding domain for association as homodimers and heterodimers with retinoid X receptor
    • Ribeiro, R. C. J., Feng, W., Wagner, R. L., Costa, C. H. R. M., Pereira, A. C., Apriletti, J. W., Fletterick, R. J., and Baxter, J. D. (2001) Definition of the surface in the thyroid hormone receptor ligand binding domain for association as homodimers and heterodimers with retinoid X receptor, J. Biol. Chem. 276, 14987-14995.
    • (2001) J. Biol. Chem , vol.276 , pp. 14987-14995
    • Ribeiro, R.C.J.1    Feng, W.2    Wagner, R.L.3    Costa, C.H.R.M.4    Pereira, A.C.5    Apriletti, J.W.6    Fletterick, R.J.7    Baxter, J.D.8
  • 12
    • 21844450222 scopus 로고    scopus 로고
    • Rearrangements in thyroid hormone receptor charge clusters that stabilize bound 3,5′,5-triiodo-L-thyronine and inhibit homodimer formation
    • Togashi, M., Nguyen, P., Fletterick, R., Baxter, J. D., and Webb, P. (2005) Rearrangements in thyroid hormone receptor charge clusters that stabilize bound 3,5′,5-triiodo-L-thyronine and inhibit homodimer formation, J. Biol. Chem. 280, 25665-25673.
    • (2005) J. Biol. Chem , vol.280 , pp. 25665-25673
    • Togashi, M.1    Nguyen, P.2    Fletterick, R.3    Baxter, J.D.4    Webb, P.5
  • 13
    • 0035369335 scopus 로고    scopus 로고
    • Nuclear receptor interactions on DNA-response elements
    • Khorasanizadeh, S., and Rastinejad, F. (2001) Nuclear receptor interactions on DNA-response elements, Trends Biochem. Sci. 26, 384-390.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 384-390
    • Khorasanizadeh, S.1    Rastinejad, F.2
  • 15
    • 0031833450 scopus 로고    scopus 로고
    • The nuclear receptor ligand-binding domain: Structure and function
    • Moras, D., and Gronemeyer, H. (1998) The nuclear receptor ligand-binding domain: Structure and function, Curr. Opin. Cell Biol. 10, 384-391.
    • (1998) Curr. Opin. Cell Biol , vol.10 , pp. 384-391
    • Moras, D.1    Gronemeyer, H.2
  • 16
    • 0029044997 scopus 로고
    • Structural determinants of nuclear receptor assembly on DNA direct repeats
    • Rastinejad, F., Perlmann, T., Evans, R. M., and Sigler, P. B. (1995) Structural determinants of nuclear receptor assembly on DNA direct repeats, Nature 375, 203-211.
    • (1995) Nature , vol.375 , pp. 203-211
    • Rastinejad, F.1    Perlmann, T.2    Evans, R.M.3    Sigler, P.B.4
  • 19
    • 11244280002 scopus 로고    scopus 로고
    • Novel mode of deoxyribonucleic acid recognition by thyroid hormone receptors: Thyroid hormone receptor β-isoforms can bind as trimers to natural response elements comprised of reiterated half-sites
    • Mengeling, B. J., Pan, F., and Privalsky, M. L. (2005) Novel mode of deoxyribonucleic acid recognition by thyroid hormone receptors: Thyroid hormone receptor β-isoforms can bind as trimers to natural response elements comprised of reiterated half-sites, Mol. Endocrinol. 19, 35-51.
    • (2005) Mol. Endocrinol , vol.19 , pp. 35-51
    • Mengeling, B.J.1    Pan, F.2    Privalsky, M.L.3
  • 22
    • 0028887017 scopus 로고
    • Role of ligand in retinoid signaling. 9-cis-Retinoic acid modulates the oligomeric state of the retinoid X receptor
    • Kersten, S., Pan, L., Chambon, P., Gronemeyer, H., and Noy, N. (1995) Role of ligand in retinoid signaling. 9-cis-Retinoic acid modulates the oligomeric state of the retinoid X receptor, Biochemistry 34, 13717-13721.
    • (1995) Biochemistry , vol.34 , pp. 13717-13721
    • Kersten, S.1    Pan, L.2    Chambon, P.3    Gronemeyer, H.4    Noy, N.5
  • 23
    • 0028786255 scopus 로고
    • On the role of ligand in retinoid signaling:Positive cooperativity in the interactions of 9-cis retinoic acid with tetramers of the retinoid X receptor
    • Kersten, S., Pan, L., and Noy, N. (1995) On the role of ligand in retinoid signaling:Positive cooperativity in the interactions of 9-cis retinoic acid with tetramers of the retinoid X receptor, Biochemistry 34, 14263-14269.
    • (1995) Biochemistry , vol.34 , pp. 14263-14269
    • Kersten, S.1    Pan, L.2    Noy, N.3
  • 24
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α
    • Bourguet, W., Ruff, M., Chambon, P., Gronemeyer, H., and Moras, D. (1995) Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α, 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
  • 26
    • 10344247702 scopus 로고    scopus 로고
    • Evidence for ligand-independent transcriptional activation of the human estrogen-related receptor α (ERRα): Crystal structure of ERRα ligand binding domain in complex with peroxisome proliferator-activated receptor coactivator-1α
    • Kallen, J., Schlaeppi, J. M., Bitsch, F., Filipuzzi, I., Schilb, A., Riou, V., Graham, A., Strauss, A., Geiser, M., and Fournier, B. (2004) Evidence for ligand-independent transcriptional activation of the human estrogen-related receptor α (ERRα): Crystal structure of ERRα ligand binding domain in complex with peroxisome proliferator-activated receptor coactivator-1α J. Biol. Chem. 279, 49330-49337.
    • (2004) J. Biol. Chem , vol.279 , pp. 49330-49337
    • Kallen, J.1    Schlaeppi, J.M.2    Bitsch, F.3    Filipuzzi, I.4    Schilb, A.5    Riou, V.6    Graham, A.7    Strauss, A.8    Geiser, M.9    Fournier, B.10
  • 27
    • 0038503976 scopus 로고    scopus 로고
    • Structural basis for ligand-independent activation of the orphan nuclear receptor LRH-1
    • Sablin, E. P., Krylova, I. N., Fletterick, R. J., and Ingraham, H. A. (2003) Structural basis for ligand-independent activation of the orphan nuclear receptor LRH-1, Mol. Cell 11, 1575-1585.
    • (2003) Mol. Cell , vol.11 , pp. 1575-1585
    • Sablin, E.P.1    Krylova, I.N.2    Fletterick, R.J.3    Ingraham, H.A.4
  • 28
    • 0038526314 scopus 로고    scopus 로고
    • Structure and function of Nurr1 identifies a class of ligand-independent nuclear receptors
    • Wang, Z., Benoit, G., Liu, J., Prasad, S., Arnisalo, P., Liu, X., Xu, H., Walker, N., and Perlmann, T. (2003) Structure and function of Nurr1 identifies a class of ligand-independent nuclear receptors, Nature 423, 555-560.
    • (2003) Nature , vol.423 , pp. 555-560
    • Wang, Z.1    Benoit, G.2    Liu, J.3    Prasad, S.4    Arnisalo, P.5    Liu, X.6    Xu, H.7    Walker, N.8    Perlmann, T.9
  • 29
    • 0036187372 scopus 로고    scopus 로고
    • Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3
    • Greschik, H., Wurtz, J.-M., Sanglier, S., Bourguet, W., van Dorsselaer, A., Moras, D., and Renaud, J. P. (2002) Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3, Mol. Cell 9, 303-313.
    • (2002) Mol. Cell , vol.9 , pp. 303-313
    • Greschik, H.1    Wurtz, J.-M.2    Sanglier, S.3    Bourguet, W.4    van Dorsselaer, A.5    Moras, D.6    Renaud, J.P.7
  • 32
    • 0027993838 scopus 로고
    • HYDRO: A computer program for the prediction of hydrodynamic properties of macromolecules
    • de la Torre, J. G., Navarro, S., Lopez Martinez, M. C., Diaz, F. G., and Cascales, J. L. (1994) HYDRO: A computer program for the prediction of hydrodynamic properties of macromolecules, Biophys. J. 67, 530-531.
    • (1994) Biophys. J , vol.67 , pp. 530-531
    • de la Torre, J.G.1    Navarro, S.2    Lopez Martinez, M.C.3    Diaz, F.G.4    Cascales, J.L.5
  • 34
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D. I. (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria, J. Appl. Crystallogr. 25, 495-503.
    • (1992) J. Appl. Crystallogr , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 36
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun, D. I. (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing, Biophys. J. 76, 2879-2886.
    • (1999) Biophys. J , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 38
    • 0001252801 scopus 로고    scopus 로고
    • New developments in direct shape determination from small-angle scattering. 2, Uniqueness
    • Svergun, D. I., Volkov, V. V., Kozin, M. B., and Stuhrmann, H. B. (1996) New developments in direct shape determination from small-angle scattering. 2, Uniqueness, Acta Crystallogr. A52, 419-426.
    • (1996) Acta Crystallogr , vol.A52 , pp. 419-426
    • Svergun, D.I.1    Volkov, V.V.2    Kozin, M.B.3    Stuhrmann, H.B.4
  • 40
    • 0001012624 scopus 로고
    • New method for determination of surface form and internal structure of dissolved globular proteins from small angle X-ray measurements
    • Sturmann, H. B. (1970) New method for determination of surface form and internal structure of dissolved globular proteins from small angle X-ray measurements, J. Chem. Phys. 72, 177-182.
    • (1970) J. Chem. Phys , vol.72 , pp. 177-182
    • Sturmann, H.B.1
  • 42
    • 0030669764 scopus 로고    scopus 로고
    • The tetramerization region of the retinoid X receptor is important for transcriptional activation by the receptor
    • Kersten, S., Reczek, P., and Noy, N. (1997) The tetramerization region of the retinoid X receptor is important for transcriptional activation by the receptor, J. Biol. Chem. 272, 29759-29768.
    • (1997) J. Biol. Chem , vol.272 , pp. 29759-29768
    • Kersten, S.1    Reczek, P.2    Noy, N.3
  • 43
  • 44
    • 0028833051 scopus 로고
    • Cooperative formation of high-order oligomers by retinoid X receptors: An unexpected mode of DNA recognition
    • Chen, H., and Privalsky, M. L. (1995) Cooperative formation of high-order oligomers by retinoid X receptors: An unexpected mode of DNA recognition, Proc. Natl. Acad. Sci. U.S.A. 92, 422-426.
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 422-426
    • Chen, H.1    Privalsky, M.L.2
  • 45
    • 0030942259 scopus 로고    scopus 로고
    • Plasticity of tetramer formation by retinoid X receptors. An alternative paradigm for DNA recognition
    • Lin, B.C., Wong, C. W., Chen, H. W., and Privalsky, M. L. (1997) Plasticity of tetramer formation by retinoid X receptors. An alternative paradigm for DNA recognition, J. Biol. Chem. 272, 9860-9867.
    • (1997) J. Biol. Chem , vol.272 , pp. 9860-9867
    • Lin, B.C.1    Wong, C.W.2    Chen, H.W.3    Privalsky, M.L.4
  • 46
    • 0033868825 scopus 로고    scopus 로고
    • Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains
    • Bourguet, W., Vivat, V., Wurtz, J. M., Chambon, P., Gronemeyer, H., and Moras, D. (2000) Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains, Mol. Cell 5, 289-298.
    • (2000) Mol. Cell , vol.5 , pp. 289-298
    • Bourguet, W.1    Vivat, V.2    Wurtz, J.M.3    Chambon, P.4    Gronemeyer, H.5    Moras, D.6
  • 47
    • 0033855471 scopus 로고    scopus 로고
    • Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix
    • Gampe, R. T., Jr., Montana, V. G., Lambert, M. H., Wisely, G. B., Milburn, M. V., and Xu, H. E. (2000) Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix, Genes Dev. 14, 2229-2241.
    • (2000) Genes Dev , vol.14 , pp. 2229-2241
    • Gampe Jr., R.T.1    Montana, V.G.2    Lambert, M.H.3    Wisely, G.B.4    Milburn, M.V.5    Xu, H.E.6
  • 49
    • 0032568527 scopus 로고    scopus 로고
    • Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains
    • Tanenbaum, D. M., Wang, Y., Williams, S. P., and Sigler, P. B. (1998) Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains, Proc. Natl. Acad. Sci. U.S.A. 95, 5998-6003.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 5998-6003
    • Tanenbaum, D.M.1    Wang, Y.2    Williams, S.P.3    Sigler, P.B.4
  • 50
    • 0035937246 scopus 로고    scopus 로고
    • Effects of ligand binding on the association properties and conformation in solution of retinoic acid receptors RXR and RAR
    • Egea, P. F., Rochel, N., Birck, C., Vachette, P., Timmins, P. A., and Moras, D. (2001) Effects of ligand binding on the association properties and conformation in solution of retinoic acid receptors RXR and RAR, J. Mol. Biol. 307, 557-576.
    • (2001) J. Mol. Biol , vol.307 , pp. 557-576
    • Egea, P.F.1    Rochel, N.2    Birck, C.3    Vachette, P.4    Timmins, P.A.5    Moras, D.6
  • 51
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin, M. B., and Svergun, D. I. (2001) Automated matching of high- and low-resolution structural models, J. Appl. Crystallogr. 34, 33-41.
    • (2001) J. Appl. Crystallogr , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 54
    • 0028103275 scopus 로고
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4 (1994) Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr , vol.D50 , pp. 760-763
  • 55
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P., and Cowtan, K. (2004) Coot: Model-building tools for molecular graphics, Acta Crystallogr D60, 2126-2132.
    • (2004) Acta Crystallogr , vol.D60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 56
    • 0034849689 scopus 로고    scopus 로고
    • MASSHA: A graphics system for rigid-body modelling of macromolecular complexes against solution scattering data
    • Konarev, P. V., Petoukhov, M. V., and Svergun, D. I. (2001) MASSHA: A graphics system for rigid-body modelling of macromolecular complexes against solution scattering data, J. Appl. Crystallogr. 34, 527-532.
    • (2001) J. Appl. Crystallogr , vol.34 , pp. 527-532
    • Konarev, P.V.1    Petoukhov, M.V.2    Svergun, D.I.3
  • 57
    • 0029185933 scopus 로고
    • CRYSOL: A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun, D. I., Barberato, C., and Koch, M. H. (1995) CRYSOL: A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates, J. Appl. Crystallogr. 28, 768-773.
    • (1995) J. Appl. Crystallogr , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.3
  • 58
    • 0035907232 scopus 로고    scopus 로고
    • Transcriptional repression by thyroid hormone receptors: A role for receptor homodimers in the recruitment of SMRT corepressor
    • Yoh, S. M., and Privalsky, M. L. (2001) Transcriptional repression by thyroid hormone receptors: A role for receptor homodimers in the recruitment of SMRT corepressor, J. Biol. Chem. 276, 16857-16867.
    • (2001) J. Biol. Chem , vol.276 , pp. 16857-16867
    • Yoh, S.M.1    Privalsky, M.L.2
  • 59
    • 0035830908 scopus 로고    scopus 로고
    • Thyroid hormone response element sequence and the recruitment of retinoid X receptors for thyroid hormone responsiveness
    • Wu, Y., Xu, B., and Koenig, R. J. (2001) Thyroid hormone response element sequence and the recruitment of retinoid X receptors for thyroid hormone responsiveness, J. Biol. Chem. 276, 3929-3936.
    • (2001) J. Biol. Chem , vol.276 , pp. 3929-3936
    • Wu, Y.1    Xu, B.2    Koenig, R.J.3
  • 61
    • 0030953793 scopus 로고    scopus 로고
    • The DNA binding pattern of the retinoid X receptor is regulated by ligand-dependent modulation of its oligomeric state
    • Kersten, S., Gronemeyer, H., and Noy, N. (1997) The DNA binding pattern of the retinoid X receptor is regulated by ligand-dependent modulation of its oligomeric state, J. Biol. Chem. 272, 12771-12777.
    • (1997) J. Biol. Chem , vol.272 , pp. 12771-12777
    • Kersten, S.1    Gronemeyer, H.2    Noy, N.3
  • 62
    • 0031929308 scopus 로고    scopus 로고
    • Engineering novel specificities for ligand-activated transcription in the nuclear hormone receptor RXR
    • Peet, D. J., Doyle, D. F., Corey, D. R., and Mangelsdorf, D. J. (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
  • 63
    • 0030865548 scopus 로고    scopus 로고
    • A mutation mimicking ligand-induced conformational change yields a constitutive RXR that senses allosteric effects in heterodimers
    • Vivat, V., Zechel, C., Wurtz, J. M., Bourguet, W., Kagechika, H., Umemiya, H., Shudo, K., Moras, D., Gronemeyer, H., and Chambon, P. (1997) A mutation mimicking ligand-induced conformational change yields a constitutive RXR that senses allosteric effects in heterodimers, EMBO J. 16, 5697-5709.
    • (1997) EMBO J , vol.16 , pp. 5697-5709
    • Vivat, V.1    Zechel, C.2    Wurtz, J.M.3    Bourguet, W.4    Kagechika, H.5    Umemiya, H.6    Shudo, K.7    Moras, D.8    Gronemeyer, H.9    Chambon, P.10
  • 64
    • 0024354839 scopus 로고
    • The rat growth hormone gene contains multiple thyroid response elements
    • Muscat, G. E., Griggs, R., Norman, M. F., Lavin, T. N., Baxter, J. D., and West, B. L. (1989) The rat growth hormone gene contains multiple thyroid response elements, J. Biol. Chem. 264, 12063-12073.
    • (1989) J. Biol. Chem , vol.264 , pp. 12063-12073
    • Muscat, G.E.1    Griggs, R.2    Norman, M.F.3    Lavin, T.N.4    Baxter, J.D.5    West, B.L.6
  • 65
    • 0027581632 scopus 로고
    • Characterization of the thyroid hormone response element in the skeletal α-actin gene: Regulation of T3 receptor binding by retinoid X receptor
    • Muscat, G. E., Griggs, R., Downes, M., and Emery, J. (1993) Characterization of the thyroid hormone response element in the skeletal α-actin gene: Regulation of T3 receptor binding by retinoid X receptor, Cell Growth Differ. 4, 269-279.
    • (1993) Cell Growth Differ , vol.4 , pp. 269-279
    • Muscat, G.E.1    Griggs, R.2    Downes, M.3    Emery, J.4
  • 66
    • 0028361264 scopus 로고
    • Activation of MyoD gene transcription by 3,5,3′-triiodo- L-thyronine: A direct role for thyroid hormone and retinoid X receptors
    • Muscat, G. E., Mynett-Johnson, L., Dowhan, D., Downes, M., and Griggs, R. (1994) Activation of MyoD gene transcription by 3,5,3′-triiodo- L-thyronine: A direct role for thyroid hormone and retinoid X receptors, Nucleic Acids Res. 22, 583-591.
    • (1994) Nucleic Acids Res , vol.22 , pp. 583-591
    • Muscat, G.E.1    Mynett-Johnson, L.2    Dowhan, D.3    Downes, M.4    Griggs, R.5
  • 67
    • 0032574702 scopus 로고    scopus 로고
    • Properties of overlapping EREs: Synergistic activation of transcription and cooperative binding of ER
    • Massaad, C., Coumoul, X., Sabbah, M., Garlatti, M., Redeuilh, G., and Barouki, R. (1998) Properties of overlapping EREs: Synergistic activation of transcription and cooperative binding of ER, Biochemistry 37, 6023-6032.
    • (1998) Biochemistry , vol.37 , pp. 6023-6032
    • Massaad, C.1    Coumoul, X.2    Sabbah, M.3    Garlatti, M.4    Redeuilh, G.5    Barouki, R.6
  • 68
    • 0025291548 scopus 로고
    • Synergistic activation of transcription by the human estrogen receptor bound to tandem responsive elements
    • Ponglikitmongkol, M., White, J. H., and Chambon, P. (1990) Synergistic activation of transcription by the human estrogen receptor bound to tandem responsive elements, EMBO J. 9, 2221-2231.
    • (1990) EMBO J , vol.9 , pp. 2221-2231
    • Ponglikitmongkol, M.1    White, J.H.2    Chambon, P.3
  • 69
    • 0027942079 scopus 로고
    • A functional glucocorticoid-responsive unit composed of two overlapping inactive receptor-binding sites: Evidence for formation of a receptor tetramer
    • Garlatti, M., Daheshia, M., Slater, E., Bouguet, J., Hanoune, J., Beato, M., and Barouki, R. (1994) A functional glucocorticoid-responsive unit composed of two overlapping inactive receptor-binding sites: Evidence for formation of a receptor tetramer, Mol. Cell. Biol. 14, 8007-8017.
    • (1994) Mol. Cell. Biol , vol.14 , pp. 8007-8017
    • Garlatti, M.1    Daheshia, M.2    Slater, E.3    Bouguet, J.4    Hanoune, J.5    Beato, M.6    Barouki, R.7


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