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Volumn 1812, Issue 8, 2011, Pages 824-835

Molecular basis for gene-specific transactivation by nuclear receptors

Author keywords

Chromatin; Co factor interaction; DNA binding; DNA looping; Nuclear receptor specificity; Nuclear receptor structure

Indexed keywords

CELL NUCLEUS RECEPTOR; DNA; ESTROGEN RECEPTOR ALPHA; ESTROGEN RECEPTOR BETA; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR ALPHA; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; RETINOID X RECEPTOR ALPHA; ZINC FINGER PROTEIN;

EID: 79958286397     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2010.12.018     Document Type: Review
Times cited : (69)

References (163)
  • 4
    • 22244480341 scopus 로고    scopus 로고
    • Epiderma growth factor-induced signaling in breast cancer cells resufts in selective target gene activation by orphan nuclear receptor estrogen-related receptor alpha
    • Barry J.B., Giguere V. Epiderma growth factor-induced signaling in breast cancer cells resufts in selective target gene activation by orphan nuclear receptor estrogen-related receptor alpha. Cancer Res. 2005, 65:6120-6129.
    • (2005) Cancer Res. , vol.65 , pp. 6120-6129
    • Barry, J.B.1    Giguere, V.2
  • 5
    • 31444444774 scopus 로고    scopus 로고
    • A single nucleotide in an estrogen-related receptor alpha site can dictate mode of binding and peroxisome proliferator-activated receptor gamma coactivator 1 alpha activation of target promoters
    • Barry J.B., Laganiere J., Giguere V. A single nucleotide in an estrogen-related receptor alpha site can dictate mode of binding and peroxisome proliferator-activated receptor gamma coactivator 1 alpha activation of target promoters. Mol. Endocrinol. 2006, 20:302-310.
    • (2006) Mol. Endocrinol. , vol.20 , pp. 302-310
    • Barry, J.B.1    Laganiere, J.2    Giguere, V.3
  • 6
    • 0032606387 scopus 로고    scopus 로고
    • Intracellular localization and trafficking of steroid receptors
    • Baumann C.T., Lim C.S., Hager G.L. Intracellular localization and trafficking of steroid receptors. Cell Biochem. Biophys. 1999, 31:119-127.
    • (1999) Cell Biochem. Biophys. , vol.31 , pp. 119-127
    • Baumann, C.T.1    Lim, C.S.2    Hager, G.L.3
  • 7
    • 0035815621 scopus 로고    scopus 로고
    • Nuclear cytoplasmic shuttling by thyroid hormone receptors - multiple protein interactions are required for nuclear retention
    • Baumann C.T., Maruvada P., Hager G.L., Yen P.M. Nuclear cytoplasmic shuttling by thyroid hormone receptors - multiple protein interactions are required for nuclear retention. J. Biol. Chem. 2001, 276:11237-11245.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11237-11245
    • Baumann, C.T.1    Maruvada, P.2    Hager, G.L.3    Yen, P.M.4
  • 8
    • 70350450946 scopus 로고    scopus 로고
    • FoxA1 binding directs chromatin structure and the functional response of a glucocorticoid receptor-regulated promoter
    • Belikov S., Astrand C., Wrange O. FoxA1 binding directs chromatin structure and the functional response of a glucocorticoid receptor-regulated promoter. Mol. Cell. Biol. 2009, 29:5413-5425.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5413-5425
    • Belikov, S.1    Astrand, C.2    Wrange, O.3
  • 9
    • 0032230283 scopus 로고    scopus 로고
    • Functional interactions of the AF-2 activation domain core region of the human androgen receptor with the amino-terminal domain and with the transcriptional coactivator TIF2 (transcriptional intermediary factor 2)
    • Berrevoets C.A., Doesburg P., Steketee K., Trapman J., Brinkmann A.O. Functional interactions of the AF-2 activation domain core region of the human androgen receptor with the amino-terminal domain and with the transcriptional coactivator TIF2 (transcriptional intermediary factor 2). Mol. Endocrinol. 1998, 12:1172-1183.
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1172-1183
    • Berrevoets, C.A.1    Doesburg, P.2    Steketee, K.3    Trapman, J.4    Brinkmann, A.O.5
  • 10
    • 67949091258 scopus 로고    scopus 로고
    • Glucocorticoid receptor dynamics and gene regulation
    • Biddie S.C., Hager G.L. Glucocorticoid receptor dynamics and gene regulation. Stress Int. J. Biol. Stress 2009, 12:193-205.
    • (2009) Stress Int. J. Biol. Stress , vol.12 , pp. 193-205
    • Biddie, S.C.1    Hager, G.L.2
  • 11
    • 40849102229 scopus 로고    scopus 로고
    • Differential recruitment of glucocorticoid receptor phospho-isoforms to glucocorticoid-induced genes
    • Blind R.D., Garabedian M.J. Differential recruitment of glucocorticoid receptor phospho-isoforms to glucocorticoid-induced genes. J. Steroid Biochem. Mol. Biol. 2008, 109:150-157.
    • (2008) J. Steroid Biochem. Mol. Biol. , vol.109 , pp. 150-157
    • Blind, R.D.1    Garabedian, M.J.2
  • 12
    • 33644530060 scopus 로고    scopus 로고
    • A hyper-dynamic equilibrium between promoter-bound and nucleoplasmic dimers controls NF-kappa B-dependent gene activity
    • Bosisio D., Marazzi I., Agresti A., Shimizu N., Bianchi M.E., Natoli G. A hyper-dynamic equilibrium between promoter-bound and nucleoplasmic dimers controls NF-kappa B-dependent gene activity. EMBO J. 2006, 25:798-810.
    • (2006) EMBO J. , vol.25 , pp. 798-810
    • Bosisio, D.1    Marazzi, I.2    Agresti, A.3    Shimizu, N.4    Bianchi, M.E.5    Natoli, G.6
  • 13
    • 0029012163 scopus 로고
    • Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-[alpha]
    • Bourguet W., Ruff M., Chambon P., Gronemeyer H., Moras D. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-[alpha]. Nature 1995, 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
  • 15
    • 66449119706 scopus 로고    scopus 로고
    • The PPAR gamma 2 A/B-domain plays a gene-specific role in transactivation and cofactor recruitment
    • Bugge A., Grontved L., Aagaard M.M., Borup R., Mandrup S. The PPAR gamma 2 A/B-domain plays a gene-specific role in transactivation and cofactor recruitment. Mol. Endocrinol. 2009, 23:794-808.
    • (2009) Mol. Endocrinol. , vol.23 , pp. 794-808
    • Bugge, A.1    Grontved, L.2    Aagaard, M.M.3    Borup, R.4    Mandrup, S.5
  • 16
    • 77952921211 scopus 로고    scopus 로고
    • A novel intronic peroxisome proliferator activated receptor (PPAR) gamma enhancer in the uncoupling protein (UCP) 3 gene as a regulator of both UCP2 and -3 expression in adipocytes
    • Bugge A., Siersbaek M., Madsen M.S., Göndör A., Rougier C., Mandrup S. A novel intronic peroxisome proliferator activated receptor (PPAR) gamma enhancer in the uncoupling protein (UCP) 3 gene as a regulator of both UCP2 and -3 expression in adipocytes. Journal of Biological Chemistry 2010, 285(23):17310-17317.
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.23 , pp. 17310-17317
    • Bugge, A.1    Siersbaek, M.2    Madsen, M.S.3    Göndör, A.4    Rougier, C.5    Mandrup, S.6
  • 20
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • Chen J.D., Evans R.M. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 1995, 377:454-457.
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 23
    • 0036184236 scopus 로고    scopus 로고
    • Opening of compacted chromatin by early developmental transcription factors HNF3 (FoxA) and GATA-4
    • Cirillo L.A., Lin F.R., Cuesta I., Friedman D., Jarnik M., Zaret K.S. Opening of compacted chromatin by early developmental transcription factors HNF3 (FoxA) and GATA-4. Mol. Cell 2002, 9:279-289.
    • (2002) Mol. Cell , vol.9 , pp. 279-289
    • Cirillo, L.A.1    Lin, F.R.2    Cuesta, I.3    Friedman, D.4    Jarnik, M.5    Zaret, K.S.6
  • 24
    • 0034465602 scopus 로고    scopus 로고
    • The nuclear corepressors recognize distinct nuclear receptor complexes
    • Cohen R.N., Putney A., Wondisford F.E., Hollenberg A.N. The nuclear corepressors recognize distinct nuclear receptor complexes. Mol. Endocrinol. 2000, 14:900-914.
    • (2000) Mol. Endocrinol. , vol.14 , pp. 900-914
    • Cohen, R.N.1    Putney, A.2    Wondisford, F.E.3    Hollenberg, A.N.4
  • 25
    • 0028901040 scopus 로고
    • Characterization of the amino-terminal transcriptional activation function of the human estrogen receptor in animal and yeast cells
    • Metzger Daniel, Bornert Jean-Marc, Chambon Pierre Characterization of the amino-terminal transcriptional activation function of the human estrogen receptor in animal and yeast cells. J. Biol. Chem. 1995, 270:9535-9542.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9535-9542
    • Metzger, D.1    Bornert, J.-M.2    Chambon, P.3
  • 27
    • 0033856986 scopus 로고    scopus 로고
    • Functional differences between the amino-terminal domains of estrogen receptors alpha and beta
    • Delaunay F., Pettersson K., Tujague M., Gustafsson J.A. Functional differences between the amino-terminal domains of estrogen receptors alpha and beta. Mol. Pharmacol. 2000, 58:584-590.
    • (2000) Mol. Pharmacol. , vol.58 , pp. 584-590
    • Delaunay, F.1    Pettersson, K.2    Tujague, M.3    Gustafsson, J.A.4
  • 28
    • 33644638521 scopus 로고    scopus 로고
    • Estrogen receptors and human disease
    • Deroo B.J., Korach K.S. Estrogen receptors and human disease. J. Clin. Invest. 2006, 116:561-570.
    • (2006) J. Clin. Invest. , vol.116 , pp. 561-570
    • Deroo, B.J.1    Korach, K.S.2
  • 29
    • 69949137692 scopus 로고    scopus 로고
    • Steroid hormone pulsing drives cyclic gene expression
    • Desvergne B., Heligon C. Steroid hormone pulsing drives cyclic gene expression. Nat. Cell Biol. 2009, 11:1051-1053.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1051-1053
    • Desvergne, B.1    Heligon, C.2
  • 30
    • 3042814763 scopus 로고    scopus 로고
    • Intramolecular interactions between the AF3 domain and the C-terminus of the human progesterone receptor are mediated through two LXXLL motifs
    • Dong X., Challis J.R.G., Lye S.J. Intramolecular interactions between the AF3 domain and the C-terminus of the human progesterone receptor are mediated through two LXXLL motifs. J. Mol. Endocrinol. 2004, 32:843-857.
    • (2004) J. Mol. Endocrinol. , vol.32 , pp. 843-857
    • Dong, X.1    Challis, J.R.G.2    Lye, S.J.3
  • 32
    • 1942518840 scopus 로고    scopus 로고
    • PPARs and the complex journey to obesity
    • Evans R.M., Barish G.D., Wang Y.X. PPARs and the complex journey to obesity. Nat. Med. 2004, 10:355-361.
    • (2004) Nat. Med. , vol.10 , pp. 355-361
    • Evans, R.M.1    Barish, G.D.2    Wang, Y.X.3
  • 33
    • 0032539721 scopus 로고    scopus 로고
    • Subcellular localization of mineralocorticoid receptors in living cells: effects of receptor agonists and antagonists
    • Fejes-Toth G., Pearce D., Naray-Fejes-Toth A. Subcellular localization of mineralocorticoid receptors in living cells: effects of receptor agonists and antagonists. Proc. Natl Acad. Sci. USA 1998, 95:2973-2978.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 2973-2978
    • Fejes-Toth, G.1    Pearce, D.2    Naray-Fejes-Toth, A.3
  • 35
    • 0023769378 scopus 로고
    • The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain
    • Freedman L.P., Luisi B.F., Korszun Z.R., Basavappa R., Sigler P.B., Yamamoto K.R. The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain. Nature 1988, 334:543-546.
    • (1988) Nature , vol.334 , pp. 543-546
    • Freedman, L.P.1    Luisi, B.F.2    Korszun, Z.R.3    Basavappa, R.4    Sigler, P.B.5    Yamamoto, K.R.6
  • 37
    • 73549096417 scopus 로고    scopus 로고
    • Site-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor
    • Garza A.M.S., Khan S.H., Kumar R. Site-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor. Mol. Cell. Biol. 2010, 30:220-230.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 220-230
    • Garza, A.M.S.1    Khan, S.H.2    Kumar, R.3
  • 38
    • 0037418634 scopus 로고    scopus 로고
    • Monomeric complex of human orphan estrogen related receptor-2 with DNA: a pseudo-dimer interface mediates extended half-site recognition
    • Gearhart M.D., Holmbeck S.M.A., Evans R.M., Dyson H.J., Wright P.E. Monomeric complex of human orphan estrogen related receptor-2 with DNA: a pseudo-dimer interface mediates extended half-site recognition. J. Mol. Biol. 2003, 327:819-832.
    • (2003) J. Mol. Biol. , vol.327 , pp. 819-832
    • Gearhart, M.D.1    Holmbeck, S.M.A.2    Evans, R.M.3    Dyson, H.J.4    Wright, P.E.5
  • 39
    • 0030948745 scopus 로고    scopus 로고
    • Trafficking of the androgen receptor in living cells with fused green fluorescent protein-androgen receptor
    • Georget V., Lobaccaro J.M., Terouanne B., Mangeat P., Nicolas J.C., Sultan C. Trafficking of the androgen receptor in living cells with fused green fluorescent protein-androgen receptor. Mol. Cell. Endocrinol. 1997, 129:17-26.
    • (1997) Mol. Cell. Endocrinol. , vol.129 , pp. 17-26
    • Georget, V.1    Lobaccaro, J.M.2    Terouanne, B.3    Mangeat, P.4    Nicolas, J.C.5    Sultan, C.6
  • 41
    • 0034000089 scopus 로고    scopus 로고
    • The opposing transcriptional activities of the two isoforms of the human progesterone receptor are due to differential cofactor binding
    • Giangrande P.H., Kimbrel E.A., Edwards D.P., McDonnell D.P. The opposing transcriptional activities of the two isoforms of the human progesterone receptor are due to differential cofactor binding. Mol. Cell. Biol. 2000, 20:3102-3115.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3102-3115
    • Giangrande, P.H.1    Kimbrel, E.A.2    Edwards, D.P.3    McDonnell, D.P.4
  • 42
    • 0033305499 scopus 로고    scopus 로고
    • Orphan nuclear receptors: from gene to function
    • Giguere V. Orphan nuclear receptors: from gene to function. Endocr. Rev. 1999, 20:689-725.
    • (1999) Endocr. Rev. , vol.20 , pp. 689-725
    • Giguere, V.1
  • 43
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • Glass C.K., Rosenfeld M.G. The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev. 2000, 14:121-141.
    • (2000) Genes Dev. , vol.14 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 44
    • 0035089827 scopus 로고    scopus 로고
    • The androgen receptor (AR) amino-terminus imposes androgen-specific regulation of AR gene expression via an exonic enhancer
    • Grad J.M., Lyons L.S., Robins D.M., Burnstein K.L. The androgen receptor (AR) amino-terminus imposes androgen-specific regulation of AR gene expression via an exonic enhancer. Endocrinology 2001, 142:1107-1116.
    • (2001) Endocrinology , vol.142 , pp. 1107-1116
    • Grad, J.M.1    Lyons, L.S.2    Robins, D.M.3    Burnstein, K.L.4
  • 45
    • 0028904382 scopus 로고
    • Hetty A.G.M.van der Korput, Jan Trapman, Albert O. Brinkmann, Identification of Two Transcription Activation Units in the N-terminal of the Human Androgen Receptor
    • Jenster Guido Hetty A.G.M.van der Korput, Jan Trapman, Albert O. Brinkmann, Identification of Two Transcription Activation Units in the N-terminal of the Human Androgen Receptor. J. Biol. Chem. 1995, 270:7341-7346.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7341-7346
    • Jenster, G.1
  • 46
    • 0037263134 scopus 로고    scopus 로고
    • DNA recognition by the androgen receptor: evidence for an alternative DNA-dependent dimerization, and an active role of sequences flanking the response element on transactivation
    • Haelens A., Verrijdt G., Callewaert L., Christiaens V., Schauwaers K., Peeters B., Rombauts W., Claessens F. DNA recognition by the androgen receptor: evidence for an alternative DNA-dependent dimerization, and an active role of sequences flanking the response element on transactivation. Biochem. J. 2003, 369:141-151.
    • (2003) Biochem. J. , vol.369 , pp. 141-151
    • Haelens, A.1    Verrijdt, G.2    Callewaert, L.3    Christiaens, V.4    Schauwaers, K.5    Peeters, B.6    Rombauts, W.7    Claessens, F.8
  • 47
    • 0035253089 scopus 로고    scopus 로고
    • Androgen-receptor-specific DNA binding to an element in the first exon of the human secretory component gene
    • Haelens A., Verrijdt G., Callewaert L., Peeters B., Rombauts W., Claessens F. Androgen-receptor-specific DNA binding to an element in the first exon of the human secretory component gene. Biochem. J. 2001, 353:611-620.
    • (2001) Biochem. J. , vol.353 , pp. 611-620
    • Haelens, A.1    Verrijdt, G.2    Callewaert, L.3    Peeters, B.4    Rombauts, W.5    Claessens, F.6
  • 49
    • 65249150266 scopus 로고    scopus 로고
    • Glucocorticoid receptor activation of the Ciz1-Lcn2 locus by long range interactions
    • Hakim O., John S., Ling J.Q., Biddie S.C., Hoffman A.R., Hager G.L. Glucocorticoid receptor activation of the Ciz1-Lcn2 locus by long range interactions. J. Biol. Chem. 2009, 284:6048-6052.
    • (2009) J. Biol. Chem. , vol.284 , pp. 6048-6052
    • Hakim, O.1    John, S.2    Ling, J.Q.3    Biddie, S.C.4    Hoffman, A.R.5    Hager, G.L.6
  • 51
    • 46349084348 scopus 로고    scopus 로고
    • Estrogen receptor beta isoform-specific induction of transforming growth factor beta-inducible early gene-1 in human osteoblast cells: An essential role for the activation function 1 domain
    • Hawse J.R., Subramaniam M., Monroe D.G., Hemmingsen A.H., Ingle J.N., Khosla S., Oursler M.J., Spelsberg T.C. Estrogen receptor beta isoform-specific induction of transforming growth factor beta-inducible early gene-1 in human osteoblast cells: An essential role for the activation function 1 domain. Mol. Endocrinol. 2008, 22:1579-1595.
    • (2008) Mol. Endocrinol. , vol.22 , pp. 1579-1595
    • Hawse, J.R.1    Subramaniam, M.2    Monroe, D.G.3    Hemmingsen, A.H.4    Ingle, J.N.5    Khosla, S.6    Oursler, M.J.7    Spelsberg, T.C.8
  • 52
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptor
    • Heery D.M., Kalkhoven E., Hoare S., Parker M.G. A signature motif in transcriptional co-activators mediates binding to nuclear receptor. Nature 1997, 387:733-736.
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 53
    • 77952567987 scopus 로고    scopus 로고
    • Simple combinations of lineage-determining transcription factors prime cis-regulatory elements required for macrophage and B cell identities
    • Heinz S., Benner C., Spann N., Bertolino E., Lin Y.C., Laslo P., Cheng J.X., Murre C., Singh H., Glass C.K. Simple combinations of lineage-determining transcription factors prime cis-regulatory elements required for macrophage and B cell identities. Mol. Cell 2010, 38:576-589.
    • (2010) Mol. Cell , vol.38 , pp. 576-589
    • Heinz, S.1    Benner, C.2    Spann, N.3    Bertolino, E.4    Lin, Y.C.5    Laslo, P.6    Cheng, J.X.7    Murre, C.8    Singh, H.9    Glass, C.K.10
  • 55
    • 69949146216 scopus 로고    scopus 로고
    • A progesterone receptor co-activator (JDP2) mediates activity through interaction with residues in the carboxyl-terminal extension of the DNA binding domain
    • Hill K.K., Roemer S.C., Jones D.N.M., Churchill M.E.A., Edwards D.P. A progesterone receptor co-activator (JDP2) mediates activity through interaction with residues in the carboxyl-terminal extension of the DNA binding domain. J. Biol. Chem. 2009, 284:24415-24424.
    • (2009) J. Biol. Chem. , vol.284 , pp. 24415-24424
    • Hill, K.K.1    Roemer, S.C.2    Jones, D.N.M.3    Churchill, M.E.A.4    Edwards, D.P.5
  • 56
    • 0023794190 scopus 로고
    • Multiple and cooperative trans-activation domains of the human glucocorticoid receptor
    • Hollenberg S.M., Evans R.M. Multiple and cooperative trans-activation domains of the human glucocorticoid receptor. Cell 1988, 55:899-906.
    • (1988) Cell , vol.55 , pp. 899-906
    • Hollenberg, S.M.1    Evans, R.M.2
  • 57
    • 67849116564 scopus 로고    scopus 로고
    • Bag-1M inhibits the transactivation of the glucocorticoid receptor via recruitment of corepressors
    • Hong W., Baniahmad A., Li J., Chang C.L., Gao W.Z., Liu Y.D. Bag-1M inhibits the transactivation of the glucocorticoid receptor via recruitment of corepressors. FEBS Lett. 2009, 583:2451-2456.
    • (2009) FEBS Lett. , vol.583 , pp. 2451-2456
    • Hong, W.1    Baniahmad, A.2    Li, J.3    Chang, C.L.4    Gao, W.Z.5    Liu, Y.D.6
  • 58
    • 54249091505 scopus 로고    scopus 로고
    • Bag-1M is a component of the in vivo DNA-glucocorticoid receptor complex at hormone-regulated promoter
    • Hong W., Baniahmad A., Liu Y.D., Li H.Q. Bag-1M is a component of the in vivo DNA-glucocorticoid receptor complex at hormone-regulated promoter. J. Mol. Biol. 2008, 384:22-30.
    • (2008) J. Mol. Biol. , vol.384 , pp. 22-30
    • Hong, W.1    Baniahmad, A.2    Liu, Y.D.3    Li, H.Q.4
  • 60
    • 0029943273 scopus 로고    scopus 로고
    • Visualization of glucocorticoid receptor translocation and intranuclear organization in living cells with a green fluorescent protein chimera
    • Htun H., Barsony J., Renyi I., Gould D.L., Hager G.L. Visualization of glucocorticoid receptor translocation and intranuclear organization in living cells with a green fluorescent protein chimera. Proc. Natl Acad. Sci. USA 1996, 93:4845-4850.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4845-4850
    • Htun, H.1    Barsony, J.2    Renyi, I.3    Gould, D.L.4    Hager, G.L.5
  • 61
    • 0033523917 scopus 로고    scopus 로고
    • The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors
    • Hu X., Lazar M.A. The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors. Nature 1999, 402:93-96.
    • (1999) Nature , vol.402 , pp. 93-96
    • Hu, X.1    Lazar, M.A.2
  • 62
    • 33744497272 scopus 로고    scopus 로고
    • The peroxisome proliferator-activated receptor N-terminal domain controls isotype-selective gene expression and adipogenesis
    • Hummasti S., Tontonoz P. The peroxisome proliferator-activated receptor N-terminal domain controls isotype-selective gene expression and adipogenesis. Mol. Endocrinol. 2006, 20:1261-1275.
    • (2006) Mol. Endocrinol. , vol.20 , pp. 1261-1275
    • Hummasti, S.1    Tontonoz, P.2
  • 63
    • 54049147721 scopus 로고    scopus 로고
    • Sumoylation of peroxisome proliferator-activated receptor gamma by apoptotic cells prevents lipopolysaccharide-induced NCoR removal from kappa B binding sites proinflammatory cytokines
    • Jennewein C., Kuhn A.M., Schmidt M.V., Meilladec-Jullig V., von Knethen A., Gonzalez F.J., Brune B. Sumoylation of peroxisome proliferator-activated receptor gamma by apoptotic cells prevents lipopolysaccharide-induced NCoR removal from kappa B binding sites proinflammatory cytokines. J. Immunol. 2008, 181:5646-5652.
    • (2008) J. Immunol. , vol.181 , pp. 5646-5652
    • Jennewein, C.1    Kuhn, A.M.2    Schmidt, M.V.3    Meilladec-Jullig, V.4    von Knethen, A.5    Gonzalez, F.J.6    Brune, B.7
  • 64
    • 0346656463 scopus 로고    scopus 로고
    • Androgen receptor corepressor-19kDa (ARR19), a leucine-rich protein that represses the transcriptional activity of androgen receptor through recruitment of histone deacetylase
    • Jeong B.C., Hong C.Y., Chattopadhyay S., Park J.H., Gong E.Y., Kim H.J., Chun S.Y., Lee K. Androgen receptor corepressor-19kDa (ARR19), a leucine-rich protein that represses the transcriptional activity of androgen receptor through recruitment of histone deacetylase. Mol. Endocrinol. 2004, 18:13-25.
    • (2004) Mol. Endocrinol. , vol.18 , pp. 13-25
    • Jeong, B.C.1    Hong, C.Y.2    Chattopadhyay, S.3    Park, J.H.4    Gong, E.Y.5    Kim, H.J.6    Chun, S.Y.7    Lee, K.8
  • 66
    • 54249089082 scopus 로고    scopus 로고
    • Chromatin remodeling complexes interact dynamically with a glucocorticoid receptor-regulated promoter
    • Johnson T.A., Elbi C., Parekh B.S., Hager G.L., John S. Chromatin remodeling complexes interact dynamically with a glucocorticoid receptor-regulated promoter. Mol. Biol. Cell 2008, 19:3308-3322.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3308-3322
    • Johnson, T.A.1    Elbi, C.2    Parekh, B.S.3    Hager, G.L.4    John, S.5
  • 67
    • 0025015647 scopus 로고
    • Antitumor promotion and antiinflammation - down-modulation of Ap-1 (Fos Jun) activity by glucocorticoid hormone
    • Jonat C., Rahmsdorf H.J., Park K.K., Cato A.C.B., Gebel S., Ponta H., Herrlich P. Antitumor promotion and antiinflammation - down-modulation of Ap-1 (Fos Jun) activity by glucocorticoid hormone. Cell 1990, 62:1189-1204.
    • (1990) Cell , vol.62 , pp. 1189-1204
    • Jonat, C.1    Rahmsdorf, H.J.2    Park, K.K.3    Cato, A.C.B.4    Gebel, S.5    Ponta, H.6    Herrlich, P.7
  • 68
    • 61449247171 scopus 로고    scopus 로고
    • SUMO-specific protease 1 (SENP1) reverses the hormone-augmented SUMOylation of androgen receptor and modulates gene responses in prostate cancer cells
    • Kaikkonen S., Jaaskelainen T., Karvonen U., Rytinki M.M., Makkonen H., Gioeli D., Paschal B.M., Palvimo J.J. SUMO-specific protease 1 (SENP1) reverses the hormone-augmented SUMOylation of androgen receptor and modulates gene responses in prostate cancer cells. Mol. Endocrinol. 2009, 23:292-307.
    • (2009) Mol. Endocrinol. , vol.23 , pp. 292-307
    • Kaikkonen, S.1    Jaaskelainen, T.2    Karvonen, U.3    Rytinki, M.M.4    Makkonen, H.5    Gioeli, D.6    Paschal, B.M.7    Palvimo, J.J.8
  • 69
    • 0037073728 scopus 로고    scopus 로고
    • Involvement of proteasome in the dynamic assembly of the androgen receptor transcription complex
    • Kang Z.G., Pirskanen A., Janne O.A., Palvimo J.J. Involvement of proteasome in the dynamic assembly of the androgen receptor transcription complex. J. Biol. Chem. 2002, 277:48366-48371.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48366-48371
    • Kang, Z.G.1    Pirskanen, A.2    Janne, O.A.3    Palvimo, J.J.4
  • 72
    • 0023640459 scopus 로고
    • Oestrogen and glucocorticoid responsive elements are closely related but distinct
    • Klock G., Strahle U., Schutz G. Oestrogen and glucocorticoid responsive elements are closely related but distinct. Nature 1987, 329:734-736.
    • (1987) Nature , vol.329 , pp. 734-736
    • Klock, G.1    Strahle, U.2    Schutz, G.3
  • 74
    • 77952554163 scopus 로고    scopus 로고
    • Partners in crime: deregulation of AR activity and androgen synthesis in prostate cancer
    • Knudsen K.E., Penning T.M. Partners in crime: deregulation of AR activity and androgen synthesis in prostate cancer. Trends Endocrinol. Metab. 2010, 21:315-324.
    • (2010) Trends Endocrinol. Metab. , vol.21 , pp. 315-324
    • Knudsen, K.E.1    Penning, T.M.2
  • 75
    • 1542743970 scopus 로고    scopus 로고
    • Induced alpha-helix structure in AF1 of the androgen receptor upon binding transcription factor TFIIF
    • Kumar R., Betney R., Li J.Q., Thompson E.B., Mcewan I.J. Induced alpha-helix structure in AF1 of the androgen receptor upon binding transcription factor TFIIF. Biochemistry 2004, 43:3008-3013.
    • (2004) Biochemistry , vol.43 , pp. 3008-3013
    • Kumar, R.1    Betney, R.2    Li, J.Q.3    Thompson, E.B.4    Mcewan, I.J.5
  • 76
    • 9344227341 scopus 로고    scopus 로고
    • TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain
    • Kumar R., Volk D.E., Li J.Q., Lee J.C., Gorenstein D.G., Thompson E.B. TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain. Proc. Natl Acad. Sci. USA 2004, 101:16425-16430.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 16425-16430
    • Kumar, R.1    Volk, D.E.2    Li, J.Q.3    Lee, J.C.4    Gorenstein, D.G.5    Thompson, E.B.6
  • 78
    • 0031594713 scopus 로고    scopus 로고
    • Intermolecular NH2-/carboxyl-terminal interactions in androgen receptor dimerization revealed by mutations that cause androgen insensitivity
    • Langley E., Kemppainen J.A., Wilson E.M. Intermolecular NH2-/carboxyl-terminal interactions in androgen receptor dimerization revealed by mutations that cause androgen insensitivity. J. Biol. Chem. 1998, 273:92-101.
    • (1998) J. Biol. Chem. , vol.273 , pp. 92-101
    • Langley, E.1    Kemppainen, J.A.2    Wilson, E.M.3
  • 82
    • 77954821918 scopus 로고    scopus 로고
    • Farnesoid X receptor activation mediates head-to-tail chromatin looping in the Nr0b2 gene encoding small heterodimer partner
    • Li G.D., Thomas A.M., Hart S.N., Zhong X.B., Wu D.Q., Guo G.L. Farnesoid X receptor activation mediates head-to-tail chromatin looping in the Nr0b2 gene encoding small heterodimer partner. Mol. Endocrinol. 2010, 24:1404-1412.
    • (2010) Mol. Endocrinol. , vol.24 , pp. 1404-1412
    • Li, G.D.1    Thomas, A.M.2    Hart, S.N.3    Zhong, X.B.4    Wu, D.Q.5    Guo, G.L.6
  • 84
    • 0032941272 scopus 로고    scopus 로고
    • Differential localization and activity of the A- and B-forms of the human progesterone receptor using green fluorescent protein chimeras
    • Lim C.S., Baumann C.T., Htun H., Xian W.J., Irie M., Smith C.L., Hager G.L. Differential localization and activity of the A- and B-forms of the human progesterone receptor using green fluorescent protein chimeras. Mol. Endocrinol. 1999, 13:366-375.
    • (1999) Mol. Endocrinol. , vol.13 , pp. 366-375
    • Lim, C.S.1    Baumann, C.T.2    Htun, H.3    Xian, W.J.4    Irie, M.5    Smith, C.L.6    Hager, G.L.7
  • 85
    • 33645398779 scopus 로고    scopus 로고
    • Sequence-specific deoxyribonucleic acid (DNA) recognition by steroidogenic factor 1: A helix at the carboxy terminus of the DNA binding domain is necessary for complex stability
    • Little T.H., Zhang Y.B., Matulis C.K., Weck J., Zhang Z.P., Ramachandran A., Mayo K.E., Radhakrishnan I. Sequence-specific deoxyribonucleic acid (DNA) recognition by steroidogenic factor 1: A helix at the carboxy terminus of the DNA binding domain is necessary for complex stability. Mol. Endocrinol. 2006, 20:831-843.
    • (2006) Mol. Endocrinol. , vol.20 , pp. 831-843
    • Little, T.H.1    Zhang, Y.B.2    Matulis, C.K.3    Weck, J.4    Zhang, Z.P.5    Ramachandran, A.6    Mayo, K.E.7    Radhakrishnan, I.8
  • 87
    • 32544439893 scopus 로고    scopus 로고
    • Thyroid hormone-regulated target genes have distinct patterns of coactivator recruitment and histone acetylation
    • Liu Y., Xia X., Fondell J.D., Yen P.M. Thyroid hormone-regulated target genes have distinct patterns of coactivator recruitment and histone acetylation. Mol. Endocrinol. 2006, 20:483-490.
    • (2006) Mol. Endocrinol. , vol.20 , pp. 483-490
    • Liu, Y.1    Xia, X.2    Fondell, J.D.3    Yen, P.M.4
  • 88
    • 34548252291 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: Judges, juries, and executioners of cellular regulation
    • Lonard D.M., O'Malley B.W. Nuclear receptor coregulators: Judges, juries, and executioners of cellular regulation. Mol. Cell 2007, 27:691-700.
    • (2007) Mol. Cell , vol.27 , pp. 691-700
    • Lonard, D.M.1    O'Malley, B.W.2
  • 90
    • 0035824675 scopus 로고    scopus 로고
    • A glucocorticoid/retinoic acid receptor chimera that displays cytoplasmic/nuclear translocation in response to retinoic acid - A real time sensing assay for nuclear receptor ligands
    • Mackem S., Baumann C.T., Hager G.L. A glucocorticoid/retinoic acid receptor chimera that displays cytoplasmic/nuclear translocation in response to retinoic acid - A real time sensing assay for nuclear receptor ligands. J. Biol. Chem. 2001, 276:45501-45504.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45501-45504
    • Mackem, S.1    Baumann, C.T.2    Hager, G.L.3
  • 91
    • 0012473279 scopus 로고
    • G. Sch3tz, K. Umesono, B. Blumberg, P. Kastner, M. Mark, P. Chambon, R.M. Evans, The nuclear receptor superfamily: The second decade
    • Mangelsdorf D.J., Thummel C., Beato M., Herrlich P. G. Sch3tz, K. Umesono, B. Blumberg, P. Kastner, M. Mark, P. Chambon, R.M. Evans, The nuclear receptor superfamily: The second decade. Cell 1995, 83:835-839.
    • (1995) Cell , vol.83 , pp. 835-839
    • Mangelsdorf, D.J.1    Thummel, C.2    Beato, M.3    Herrlich, P.4
  • 92
    • 0031789876 scopus 로고    scopus 로고
    • Transcription activation by the human estrogen receptor subtype beta (ER beta) studied with ER beta and ER alpha receptor chimeras
    • McInerney E.M., Weis K.E., Sun J., Mosselman S., Katzenellenbogen B.S. Transcription activation by the human estrogen receptor subtype beta (ER beta) studied with ER beta and ER alpha receptor chimeras. Endocrinology 1998, 139:4513-4522.
    • (1998) Endocrinology , vol.139 , pp. 4513-4522
    • McInerney, E.M.1    Weis, K.E.2    Sun, J.3    Mosselman, S.4    Katzenellenbogen, B.S.5
  • 93
    • 0343415609 scopus 로고    scopus 로고
    • The glucocorticoid receptor: rapid exchange with regulatory sites in living cells
    • McNally J.G., Muller W.G., Walker D., Wolford R., Hager G.L. The glucocorticoid receptor: rapid exchange with regulatory sites in living cells. Science 2000, 287:1262-1265.
    • (2000) Science , vol.287 , pp. 1262-1265
    • McNally, J.G.1    Muller, W.G.2    Walker, D.3    Wolford, R.4    Hager, G.L.5
  • 94
    • 2442530463 scopus 로고    scopus 로고
    • The role of the C-terminal extension (CTE) of the estrogen receptor alpha and beta DNA binding domain in DNA binding and interaction with HMGB
    • Melvin V.S., Harrell C., Adelman J.S., Kraus W.L., Churchill M., Edwards D.P. The role of the C-terminal extension (CTE) of the estrogen receptor alpha and beta DNA binding domain in DNA binding and interaction with HMGB. J. Biol. Chem. 2004, 279:14763-14771.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14763-14771
    • Melvin, V.S.1    Harrell, C.2    Adelman, J.S.3    Kraus, W.L.4    Churchill, M.5    Edwards, D.P.6
  • 96
    • 0034740164 scopus 로고    scopus 로고
    • Synergism between ER alpha transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: Requirement for the AF-1 alpha-helical core and for a direct interaction between the N- and C-terminal domains
    • Metivier R., Penot G., Flouriot G., Pakdel F. Synergism between ER alpha transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: Requirement for the AF-1 alpha-helical core and for a direct interaction between the N- and C-terminal domains. Mol. Endocrinol. 2001, 15:1953-1970.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 1953-1970
    • Metivier, R.1    Penot, G.2    Flouriot, G.3    Pakdel, F.4
  • 97
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • Metivier R., Penot G., Hubner M.R., Reid G., Brand H., Kos M., Gannon F. Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell 2003, 115:751-763.
    • (2003) Cell , vol.115 , pp. 751-763
    • Metivier, R.1    Penot, G.2    Hubner, M.R.3    Reid, G.4    Brand, H.5    Kos, M.6    Gannon, F.7
  • 98
    • 0347753697 scopus 로고    scopus 로고
    • Peroxisome-proliferator-activated receptors and cancers: complex stories
    • Michalik L., Desvergne B., Wahli W. Peroxisome-proliferator-activated receptors and cancers: complex stories. Nat. Rev. Cancer 2004, 4:61-70.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 61-70
    • Michalik, L.1    Desvergne, B.2    Wahli, W.3
  • 100
    • 0035793376 scopus 로고    scopus 로고
    • Nuclear structure - protein dynamics: Implications for nuclear architecture and gene expression
    • Misteli T. Nuclear structure - protein dynamics: Implications for nuclear architecture and gene expression. Science 2001, 291:843-847.
    • (2001) Science , vol.291 , pp. 843-847
    • Misteli, T.1
  • 101
    • 67349271210 scopus 로고    scopus 로고
    • Circadian rhythm transcription factor CLOCK regulates the transcriptional activity of the glucocorticoid receptor by acetylating its hinge region lysine cluster: potential physiological implications
    • Nader N., Chrousos G.P., Kino T. Circadian rhythm transcription factor CLOCK regulates the transcriptional activity of the glucocorticoid receptor by acetylating its hinge region lysine cluster: potential physiological implications. FASEB J. 2009, 23:1572-1583.
    • (2009) FASEB J. , vol.23 , pp. 1572-1583
    • Nader, N.1    Chrousos, G.P.2    Kino, T.3
  • 102
    • 1942502820 scopus 로고    scopus 로고
    • Rapid periodic binding and displacement of the glucocorticoid receptor during chromatin remodeling
    • Nagaich A.K., Walker D.A., Wolford R., Hager G.L. Rapid periodic binding and displacement of the glucocorticoid receptor during chromatin remodeling. Mol. Cell 2004, 14:163-174.
    • (2004) Mol. Cell , vol.14 , pp. 163-174
    • Nagaich, A.K.1    Walker, D.A.2    Wolford, R.3    Hager, G.L.4
  • 103
    • 55749101777 scopus 로고    scopus 로고
    • Genome-wide profiling of PPARgamma:RXR and RNA polymerase II occupancy reveals temporal activation of distinct metabolic pathways and changes in RXR dimer composition during adipogenesis
    • Nielsen R., Pedersen T.Å., Hagenbeek D., Moulos P., Siersbæk R., Megens E., Denissov S., Børgesen M., Francoijs K.J., Mandrup S., Stunnenberg H.G. Genome-wide profiling of PPARgamma:RXR and RNA polymerase II occupancy reveals temporal activation of distinct metabolic pathways and changes in RXR dimer composition during adipogenesis. Genes Dev. 2008, 22:2953-2967.
    • (2008) Genes Dev. , vol.22 , pp. 2953-2967
    • Nielsen, R.1    Pedersen, T.Å.2    Hagenbeek, D.3    Moulos, P.4    Siersbæk, R.5    Megens, E.6    Denissov, S.7    Børgesen, M.8    Francoijs, K.J.9    Mandrup, S.10    Stunnenberg, H.G.11
  • 109
    • 0021087686 scopus 로고
    • J.+. Gustafsson, K.R. Yamamoto, Sequence-specific binding of glucocorticoid receptor to MTV DNA at sites within and upstream of the transcribed region
    • Payvar F., DeFranco D., Firestone G.L., Edgar B., Wrange Í., Okret S. J.+. Gustafsson, K.R. Yamamoto, Sequence-specific binding of glucocorticoid receptor to MTV DNA at sites within and upstream of the transcribed region. Cell 1983, 35:381-392.
    • (1983) Cell , vol.35 , pp. 381-392
    • Payvar, F.1    DeFranco, D.2    Firestone, G.L.3    Edgar, B.4    Wrange, Í.5    Okret, S.6
  • 110
    • 1342264315 scopus 로고    scopus 로고
    • A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors
    • Perissi V., Aggarwal A., Glass C.K., Rose D.W., Rosenfeld M.G. A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors. Cell 2004, 116:511-526.
    • (2004) Cell , vol.116 , pp. 511-526
    • Perissi, V.1    Aggarwal, A.2    Glass, C.K.3    Rose, D.W.4    Rosenfeld, M.G.5
  • 112
    • 0030747070 scopus 로고    scopus 로고
    • Mouse estrogen receptor beta forms estrogen response element-binding heterodimers with estrogen receptor {alpha}
    • Pettersson K., Grandien K., Kuiper G.G.J.M., Gustafsson J.A. Mouse estrogen receptor beta forms estrogen response element-binding heterodimers with estrogen receptor {alpha}. Mol. Endocrinol. 1997, 11:1486-1496.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1486-1496
    • Pettersson, K.1    Grandien, K.2    Kuiper, G.G.J.M.3    Gustafsson, J.A.4
  • 114
    • 0034687807 scopus 로고    scopus 로고
    • Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)
    • Poukka H., Karvonen U., Janne O.A., Palvimo J.J. Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc. Natl Acad. Sci. USA 2000, 97:14145-14150.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 14145-14150
    • Poukka, H.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 115
    • 77949878458 scopus 로고    scopus 로고
    • SUMOylation of human peroxisome proliferator-activated receptor alpha inhibits its trans-activity through the recruitment of the nuclear corepressor NCoR
    • Pourcet B., Pineda-Torra I., Derudas B., Staels B., Glineur C. SUMOylation of human peroxisome proliferator-activated receptor alpha inhibits its trans-activity through the recruitment of the nuclear corepressor NCoR. J. Biol. Chem. 2010, 285:5983-5992.
    • (2010) J. Biol. Chem. , vol.285 , pp. 5983-5992
    • Pourcet, B.1    Pineda-Torra, I.2    Derudas, B.3    Staels, B.4    Glineur, C.5
  • 116
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt W.B., Toft D.O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr. Rev. 1997, 18:306-360.
    • (1997) Endocr. Rev. , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 117
    • 33845658998 scopus 로고    scopus 로고
    • Nuclear localization of liver X receptor alpha and beta is differentially regulated
    • Prufer K., Boudreaux J. Nuclear localization of liver X receptor alpha and beta is differentially regulated. J. Cell. Biochem. 2007, 100:69-85.
    • (2007) J. Cell. Biochem. , vol.100 , pp. 69-85
    • Prufer, K.1    Boudreaux, J.2
  • 118
    • 0035253128 scopus 로고    scopus 로고
    • Retinoid X receptor and its partners in the nuclear receptor family
    • Rastinejad F. Retinoid X receptor and its partners in the nuclear receptor family. Curr. Opin. Struct. Biol. 2001, 11:33-38.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 33-38
    • Rastinejad, F.1
  • 119
    • 0029044997 scopus 로고
    • Structural determinants of nuclear receptor assembly on DNA direct repeats
    • Rastinejad F., Perlmann T., Evans R.M., Sigler P.B. Structural determinants of nuclear receptor assembly on DNA direct repeats. Nature 1995, 375:203-211.
    • (1995) Nature , vol.375 , pp. 203-211
    • Rastinejad, F.1    Perlmann, T.2    Evans, R.M.3    Sigler, P.B.4
  • 121
    • 14844348177 scopus 로고    scopus 로고
    • Ligand-specific dynamics of the progesterone receptor in living cells and during chromatin remodeling in vitro
    • Rayasam G.V., Elbi C., Walker D.A., Wolford R., Fletcher T.M., Edwards D.P., Hager G.L. Ligand-specific dynamics of the progesterone receptor in living cells and during chromatin remodeling in vitro. Mol. Cell. Biol. 2005, 25:2406-2418.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 2406-2418
    • Rayasam, G.V.1    Elbi, C.2    Walker, D.A.3    Wolford, R.4    Fletcher, T.M.5    Edwards, D.P.6    Hager, G.L.7
  • 122
    • 0029643780 scopus 로고
    • Crystal structure of the RAR-[gamma] ligand-binding domain bound to all-trans retinoic acid
    • Renaud J.P., Rochel N., Ruff M., Vivat V., Chambon P., Gronemeyer H., Moras D. Crystal structure of the RAR-[gamma] ligand-binding domain bound to all-trans retinoic acid. Nature 1995, 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
  • 123
    • 0037085303 scopus 로고    scopus 로고
    • Differential gene regulation by the two progesterone receptor isoforms in human breast cancer cells
    • Richer J.K., Jacobsen B.M., Manning N.G., Abel M.G., Wolf D.M., Horwitz K.B. Differential gene regulation by the two progesterone receptor isoforms in human breast cancer cells. J. Biol. Chem. 2002, 277:5209-5218.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5209-5218
    • Richer, J.K.1    Jacobsen, B.M.2    Manning, N.G.3    Abel, M.G.4    Wolf, D.M.5    Horwitz, K.B.6
  • 124
    • 0033521025 scopus 로고    scopus 로고
    • Characterization of the amino-terminal activation domain of the peroxisome proliferator-activated receptor alpha
    • Hi Rika, Osada Shiho, Yumoto Noburu, Osumi Takashi Characterization of the amino-terminal activation domain of the peroxisome proliferator-activated receptor alpha. J. Biol. Chem. 1999, 274:35152-35158.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35152-35158
    • Hi, R.1    Osada, S.2    Yumoto, N.3    Osumi, T.4
  • 125
    • 33751551165 scopus 로고    scopus 로고
    • Structure of the progesterone receptor-deoxyribonucleic acid complex: novel interactions required for binding to half-site response elements
    • Roemer S.C., Donham D.C., Sherman L., Pon V.H., Edwards D.P., Churchill M.E.A. Structure of the progesterone receptor-deoxyribonucleic acid complex: novel interactions required for binding to half-site response elements. Mol. Endocrinol. 2006, 20:3042-3052.
    • (2006) Mol. Endocrinol. , vol.20 , pp. 3042-3052
    • Roemer, S.C.1    Donham, D.C.2    Sherman, L.3    Pon, V.H.4    Edwards, D.P.5    Churchill, M.E.A.6
  • 129
    • 73249124826 scopus 로고    scopus 로고
    • Molecular switch in the glucocorticoid receptor: active and passive antagonist conformations
    • Schoch G.A., D'Arcy B., Stihle M., Burger D., Bar D., Benz J., Thoma R., Ruf A. Molecular switch in the glucocorticoid receptor: active and passive antagonist conformations. J. Mol. Biol. 2010, 395:568-577.
    • (2010) J. Mol. Biol. , vol.395 , pp. 568-577
    • Schoch, G.A.1    D'Arcy, B.2    Stihle, M.3    Burger, D.4    Bar, D.5    Benz, J.6    Thoma, R.7    Ruf, A.8
  • 130
    • 0033178805 scopus 로고    scopus 로고
    • Differential DNA binding by the androgen and glucocorticoid receptors involves the second Zn-finger and a C-terminal extension of the DNA-binding domains
    • Schoenmakers E., Alen P., Verrijdt G., Peeters B., Verhoeven G., Rombauts W., Claessens F. Differential DNA binding by the androgen and glucocorticoid receptors involves the second Zn-finger and a C-terminal extension of the DNA-binding domains. Biochem. J. 1999, 341:515-521.
    • (1999) Biochem. J. , vol.341 , pp. 515-521
    • Schoenmakers, E.1    Alen, P.2    Verrijdt, G.3    Peeters, B.4    Verhoeven, G.5    Rombauts, W.6    Claessens, F.7
  • 131
    • 0027365669 scopus 로고
    • The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: How receptors discriminate between their response elements
    • Schwabe J.W.R., Chapman L., Finch J.T., Rhodes D. The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: How receptors discriminate between their response elements. Cell 1993, 75:567-578.
    • (1993) Cell , vol.75 , pp. 567-578
    • Schwabe, J.W.R.1    Chapman, L.2    Finch, J.T.3    Rhodes, D.4
  • 132
    • 0025223160 scopus 로고
    • Solution structure of the DMA-binding domain of the oestrogen receptor
    • Schwabe J.W.R., Neuhaus D., Rhodes D. Solution structure of the DMA-binding domain of the oestrogen receptor. Nature 1990, 348:458-461.
    • (1990) Nature , vol.348 , pp. 458-461
    • Schwabe, J.W.R.1    Neuhaus, D.2    Rhodes, D.3
  • 134
    • 0033637703 scopus 로고    scopus 로고
    • Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription
    • Shang Y.F., Hu X., DiRenzo J., Lazar M.A., Brown M. Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell 2000, 103:843-852.
    • (2000) Cell , vol.103 , pp. 843-852
    • Shang, Y.F.1    Hu, X.2    DiRenzo, J.3    Lazar, M.A.4    Brown, M.5
  • 137
    • 77953616459 scopus 로고    scopus 로고
    • The tri-nucleotide spacer sequence between estrogen response element half-sites is conserved and modulates ER alpha-mediated transcriptional responses
    • Shu F.J., Sidell N., Yang D.Z., Kallen C.B. The tri-nucleotide spacer sequence between estrogen response element half-sites is conserved and modulates ER alpha-mediated transcriptional responses. J. Steroid Biochem. Mol. Biol. 2010, 120:172-179.
    • (2010) J. Steroid Biochem. Mol. Biol. , vol.120 , pp. 172-179
    • Shu, F.J.1    Sidell, N.2    Yang, D.Z.3    Kallen, C.B.4
  • 138
    • 23444431623 scopus 로고    scopus 로고
    • Mechanisms of disease: Retinoid X receptor heterodimers in the metabolic syndrome
    • Shulman A.I., Mangelsdorf D.J. Mechanisms of disease: Retinoid X receptor heterodimers in the metabolic syndrome. N. Engl. J. Med. 2005, 353:604-615.
    • (2005) N. Engl. J. Med. , vol.353 , pp. 604-615
    • Shulman, A.I.1    Mangelsdorf, D.J.2
  • 139
    • 34347324118 scopus 로고    scopus 로고
    • Determinants of cell- and gene-specific transcriptional regulation by the glucocorticoid receptor
    • So A.Y.-L., Chaivorapol C., Bolton E.C., Li H., Yamamoto K.R. Determinants of cell- and gene-specific transcriptional regulation by the glucocorticoid receptor. PLoS Genet. 2007, 3:e94.
    • (2007) PLoS Genet. , vol.3
    • So, A.Y.-L.1    Chaivorapol, C.2    Bolton, E.C.3    Li, H.4    Yamamoto, K.R.5
  • 140
    • 12144290835 scopus 로고    scopus 로고
    • Rapid glucocorticoid receptor exchange at a promoter is coupled to transcription and regulated by chaperones and proteasomes
    • Stavreva D.A., Muller W.G., Hager G.L., Smith C.L., McNally J.G. Rapid glucocorticoid receptor exchange at a promoter is coupled to transcription and regulated by chaperones and proteasomes. Mol. Cell. Biol. 2004, 24:2682-2697.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 2682-2697
    • Stavreva, D.A.1    Muller, W.G.2    Hager, G.L.3    Smith, C.L.4    McNally, J.G.5
  • 143
    • 77950934795 scopus 로고    scopus 로고
    • The shape of the DNA minor groove directs binding by the DNA-bending protein Fis
    • Stella S., Cascio D., Johnson R.C. The shape of the DNA minor groove directs binding by the DNA-bending protein Fis. Genes Dev. 2010, 24:814-826.
    • (2010) Genes Dev. , vol.24 , pp. 814-826
    • Stella, S.1    Cascio, D.2    Johnson, R.C.3
  • 144
    • 1842324170 scopus 로고
    • Article sample title placed here
    • Str Test U. article sample title placed here. Proc. Natl Acad. Sci. USA 1987, 84:7871-7875.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 7871-7875
    • Str Test, U.1
  • 148
    • 0343371427 scopus 로고    scopus 로고
    • Contribution of steroid receptor coactivator-1 and CREB binding protein in ligand-independent activity of estrogen receptor beta
    • Tremblay A., Vincent G. Contribution of steroid receptor coactivator-1 and CREB binding protein in ligand-independent activity of estrogen receptor beta. J. Steroid Biochem. Mol. Biol. 2001, 77:19-27.
    • (2001) J. Steroid Biochem. Mol. Biol. , vol.77 , pp. 19-27
    • Tremblay, A.1    Vincent, G.2
  • 149
    • 0024337858 scopus 로고
    • Determinants of Target Gene Specificity for Steroid Thyroid-Hormone Receptors
    • Umesono K., Evans R.M. Determinants of Target Gene Specificity for Steroid Thyroid-Hormone Receptors. Cell 1989, 57:1139-1146.
    • (1989) Cell , vol.57 , pp. 1139-1146
    • Umesono, K.1    Evans, R.M.2
  • 150
    • 0024337858 scopus 로고
    • Determinants of target gene specificity for steroid/thyroid hormone receptors
    • Umesono K., Evans R.M. Determinants of target gene specificity for steroid/thyroid hormone receptors. Cell 1989, 57:1139-1146.
    • (1989) Cell , vol.57 , pp. 1139-1146
    • Umesono, K.1    Evans, R.M.2
  • 151
    • 0023756692 scopus 로고
    • Retinoic acid and thyroid hormone induce gene expression through a common responsive element
    • Umesono K., Giguere V., Glass C.K., Rosenfeld M.G., Evans R.M. Retinoic acid and thyroid hormone induce gene expression through a common responsive element. Nature 1988, 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
  • 155
    • 26444526919 scopus 로고    scopus 로고
    • Regulation of the amino-terminal transcription activation domain of progesterone receptor by a cofactor-induced protein folding mechanism
    • Wardell S.E., Kwok S.C., Sherman L., Hodges R.S., Edwards D.P. Regulation of the amino-terminal transcription activation domain of progesterone receptor by a cofactor-induced protein folding mechanism. Mol. Cell. Biol. 2005, 25:8792-8808.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8792-8808
    • Wardell, S.E.1    Kwok, S.C.2    Sherman, L.3    Hodges, R.S.4    Edwards, D.P.5
  • 156
    • 0035824562 scopus 로고    scopus 로고
    • The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties
    • Warnmark A., Wikstrom A., Wright A.P.H., Gustafsson J.A., Hard T. The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties. J. Biol. Chem. 2001, 276:45939-45944.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45939-45944
    • Warnmark, A.1    Wikstrom, A.2    Wright, A.P.H.3    Gustafsson, J.A.4    Hard, T.5
  • 158
    • 0018359588 scopus 로고
    • Chromatin structure of specific genes: 2. Disruption of chromatin structure during gene activity
    • Wu C., Wong Y.C., Elgin S.C.R. Chromatin structure of specific genes: 2. Disruption of chromatin structure during gene activity. Cell 1979, 16:807-814.
    • (1979) Cell , vol.16 , pp. 807-814
    • Wu, C.1    Wong, Y.C.2    Elgin, S.C.R.3
  • 159
    • 0025188132 scopus 로고
    • Transcriptional interference between c-jun and the glucocorticoid receptor - mutual inhibition of dna-binding due to direct protein protein-interaction
    • Yangyen H.F., Chambard J.C., Sun Y.L., Smeal T., Schmidt T.J., Drouin J., Karin M. Transcriptional interference between c-jun and the glucocorticoid receptor - mutual inhibition of dna-binding due to direct protein protein-interaction. Cell 1990, 62:1205-1215.
    • (1990) Cell , vol.62 , pp. 1205-1215
    • Yangyen, H.F.1    Chambard, J.C.2    Sun, Y.L.3    Smeal, T.4    Schmidt, T.J.5    Drouin, J.6    Karin, M.7
  • 160
    • 0028294902 scopus 로고
    • Dimerization interfaces formed between the dna-binding domains determine the cooperative binding of Rxr Rar and Rxr Tr heterodimers to Dr5 and Dr4 elements
    • Zechel C., Shen X.Q., Chambon P., Gronemeyer H. Dimerization interfaces formed between the dna-binding domains determine the cooperative binding of Rxr Rar and Rxr Tr heterodimers to Dr5 and Dr4 elements. EMBO J. 1994, 13:1414-1424.
    • (1994) EMBO J. , vol.13 , pp. 1414-1424
    • Zechel, C.1    Shen, X.Q.2    Chambon, P.3    Gronemeyer, H.4
  • 161
    • 0028313996 scopus 로고
    • The dimerization interfaces formed between the DNA-binding domains of RXR. RAR and TR determine the binding-specificity and polarity of the full-length receptors to direct repeats
    • Zechel C., Shen X.Q., Chen J.Y., Chen Z.P., Chambon P., Gronemeyer H. The dimerization interfaces formed between the DNA-binding domains of RXR. RAR and TR determine the binding-specificity and polarity of the full-length receptors to direct repeats. EMBO J. 1994, 13:1425-1433.
    • (1994) EMBO J. , vol.13 , pp. 1425-1433
    • Zechel, C.1    Shen, X.Q.2    Chen, J.Y.3    Chen, Z.P.4    Chambon, P.5    Gronemeyer, H.6
  • 162
    • 0032538637 scopus 로고    scopus 로고
    • Hormone-induced translocation of thyroid hormone receptors in living cells visualized using a receptor green fluorescent protein chimera
    • Zhu X.G., Hanover J.A., Hager G.L., Cheng S.Y. Hormone-induced translocation of thyroid hormone receptors in living cells visualized using a receptor green fluorescent protein chimera. J. Biol. Chem. 1998, 273:27058-27063.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27058-27063
    • Zhu, X.G.1    Hanover, J.A.2    Hager, G.L.3    Cheng, S.Y.4
  • 163
    • 0028206987 scopus 로고
    • Evolution of distinct DNA-binding specificities within the nuclear receptor family of transcription factors
    • Zilliacus J., Carlstedt-Duke J., Gustafsson J.A., Wright A.P. Evolution of distinct DNA-binding specificities within the nuclear receptor family of transcription factors. Proc. Natl Acad. Sci. USA 1994, 91:4175-4179.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4175-4179
    • Zilliacus, J.1    Carlstedt-Duke, J.2    Gustafsson, J.A.3    Wright, A.P.4


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