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Volumn 275, Issue 1-2, 2007, Pages 13-29

Crosstalk between the glucocorticoid receptor and other transcription factors: Molecular aspects

Author keywords

AP 1; Crosstalk; Glucocorticoid receptor; NF B; Trans repression; Transcription

Indexed keywords

CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; GLUCOCORTICOID RECEPTOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; PROLACTIN; STAT5 PROTEIN; TOLL LIKE RECEPTOR; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR AP 1;

EID: 34547884315     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2007.07.003     Document Type: Review
Times cited : (238)

References (160)
  • 1
    • 0346849703 scopus 로고    scopus 로고
    • Homodimerization of the glucocorticoid receptor is not essential for response element binding: activation of the phenylethanolamine N-methyltransferase gene by dimerization-defective mutants
    • Adams M., Meijer O.C., Wang J., Bhargava A., and Pearce D. Homodimerization of the glucocorticoid receptor is not essential for response element binding: activation of the phenylethanolamine N-methyltransferase gene by dimerization-defective mutants. Mol. Endocrinol. 17 (2003) 2583-2592
    • (2003) Mol. Endocrinol. , vol.17 , pp. 2583-2592
    • Adams, M.1    Meijer, O.C.2    Wang, J.3    Bhargava, A.4    Pearce, D.5
  • 2
    • 0023686772 scopus 로고
    • Negative regulation by glucocorticoids through interference with a cAMP responsive enhancer
    • Akerblom I.E., Slater E.P., Beato M., Baxter J.D., and Mellon P.L. Negative regulation by glucocorticoids through interference with a cAMP responsive enhancer. Science 241 (1988) 350-353
    • (1988) Science , vol.241 , pp. 350-353
    • Akerblom, I.E.1    Slater, E.P.2    Beato, M.3    Baxter, J.D.4    Mellon, P.L.5
  • 3
    • 33845355511 scopus 로고    scopus 로고
    • Diversity of LEF/TCF action in development disease
    • Arce L., Yokoyama N.N., and Waterman M.L. Diversity of LEF/TCF action in development disease. Oncogene 25 (2006) 7492-7504
    • (2006) Oncogene , vol.25 , pp. 7492-7504
    • Arce, L.1    Yokoyama, N.N.2    Waterman, M.L.3
  • 5
    • 0034802887 scopus 로고    scopus 로고
    • The p65 (RelA) Subunit of NF-κB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression
    • Ashburner B.P., Westerheide S.D., and Baldwin Jr. A.S. The p65 (RelA) Subunit of NF-κB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression. Mol. Cell. Biol. 21 (2001) 7065-7077
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7065-7077
    • Ashburner, B.P.1    Westerheide, S.D.2    Baldwin Jr., A.S.3
  • 6
    • 0034004352 scopus 로고    scopus 로고
    • The LIM domain: regulation by association
    • Bach I. The LIM domain: regulation by association. Mech. Dev. 91 (2000) 5-17
    • (2000) Mech. Dev. , vol.91 , pp. 5-17
    • Bach, I.1
  • 7
    • 24144475284 scopus 로고    scopus 로고
    • Reversing histone methylation
    • Bannister A.J., and Kouzarides T. Reversing histone methylation. Nature 436 (2005) 1103-1106
    • (2005) Nature , vol.436 , pp. 1103-1106
    • Bannister, A.J.1    Kouzarides, T.2
  • 10
    • 0034731527 scopus 로고    scopus 로고
    • The glucocorticoid receptor and STAT6 physically and functionally interact in T-lymphocytes
    • Biola A., Andreau K., David M., Sturm M., Haake M., Bertoglio J., and Pallardy M. The glucocorticoid receptor and STAT6 physically and functionally interact in T-lymphocytes. FEBS Lett. 487 (2000) 229-233
    • (2000) FEBS Lett. , vol.487 , pp. 229-233
    • Biola, A.1    Andreau, K.2    David, M.3    Sturm, M.4    Haake, M.5    Bertoglio, J.6    Pallardy, M.7
  • 11
    • 0034972913 scopus 로고    scopus 로고
    • Interleukin-2 inhibits glucocorticoid receptor transcriptional activity through a mechanism involving STAT5 (signal transducer and activator of transcription 5) but not AP-1
    • Biola A., Lefebvre P., Perrin-Wolff M., Sturm M., Bertoglio J., and Pallardy M. Interleukin-2 inhibits glucocorticoid receptor transcriptional activity through a mechanism involving STAT5 (signal transducer and activator of transcription 5) but not AP-1. Mol. Endocrinol. 15 (2001) 1062-1076
    • (2001) Mol. Endocrinol. , vol.15 , pp. 1062-1076
    • Biola, A.1    Lefebvre, P.2    Perrin-Wolff, M.3    Sturm, M.4    Bertoglio, J.5    Pallardy, M.6
  • 13
    • 0026099260 scopus 로고
    • Ubiquitous transcription factor OTF-1 mediates induction of the MMTV promoter through synergistic interaction with hormone receptors
    • Bruggemeier U., Kalff M., Franke S., Scheidereit C., and Beato M. Ubiquitous transcription factor OTF-1 mediates induction of the MMTV promoter through synergistic interaction with hormone receptors. Cell 64 (1991) 565-572
    • (1991) Cell , vol.64 , pp. 565-572
    • Bruggemeier, U.1    Kalff, M.2    Franke, S.3    Scheidereit, C.4    Beato, M.5
  • 14
    • 0344874677 scopus 로고    scopus 로고
    • Glucocorticoid receptor-JNK interaction mediates inhibition of the JNK pathway by glucocorticoids
    • Bruna A., Nicolas M., Munoz A., Kyriakis J.M., and Caelles C. Glucocorticoid receptor-JNK interaction mediates inhibition of the JNK pathway by glucocorticoids. EMBO J. 22 (2003) 6035-6044
    • (2003) EMBO J. , vol.22 , pp. 6035-6044
    • Bruna, A.1    Nicolas, M.2    Munoz, A.3    Kyriakis, J.M.4    Caelles, C.5
  • 15
    • 14844299765 scopus 로고    scopus 로고
    • Chromatin-dependent E1A activity modulates NF-kappaB RelA-mediated repression of glucocorticoid receptor-dependent transcription
    • Burkhart B.A., Hebbar P.B., Trotter K.W., and Archer T.K. Chromatin-dependent E1A activity modulates NF-kappaB RelA-mediated repression of glucocorticoid receptor-dependent transcription. J. Biol. Chem. 280 (2005) 6349-6358
    • (2005) J. Biol. Chem. , vol.280 , pp. 6349-6358
    • Burkhart, B.A.1    Hebbar, P.B.2    Trotter, K.W.3    Archer, T.K.4
  • 16
    • 0031455626 scopus 로고    scopus 로고
    • Nuclear hormone receptor antagonism with AP-1 by inhibition of the JNK pathway
    • Caelles C., Gonzalez-Sancho J.M., and Munoz A. Nuclear hormone receptor antagonism with AP-1 by inhibition of the JNK pathway. Genes Dev. 11 (1997) 3351-3364
    • (1997) Genes Dev. , vol.11 , pp. 3351-3364
    • Caelles, C.1    Gonzalez-Sancho, J.M.2    Munoz, A.3
  • 18
    • 21244481640 scopus 로고    scopus 로고
    • Endotoxin tolerance disrupts chromatin remodeling and NF-κB transactivation at the IL-1β promoter
    • Chan C., Li L., McCall C.E., and Yoza B.K. Endotoxin tolerance disrupts chromatin remodeling and NF-κB transactivation at the IL-1β promoter. J. Immunol. 175 (2005) 461-468
    • (2005) J. Immunol. , vol.175 , pp. 461-468
    • Chan, C.1    Li, L.2    McCall, C.E.3    Yoza, B.K.4
  • 19
    • 1942536210 scopus 로고    scopus 로고
    • Natural glucocorticoid receptor mutants causing generalized glucocorticoid resistance: molecular genotype, genetic transmission, and clinical phenotype
    • Charmandari E., Kino T., Souvatzoglou E., Vottero A., Bhattacharyya N., and Chrousos G.P. Natural glucocorticoid receptor mutants causing generalized glucocorticoid resistance: molecular genotype, genetic transmission, and clinical phenotype. J. Clin. Endocr. Metab. 89 (2004) 1939-1949
    • (2004) J. Clin. Endocr. Metab. , vol.89 , pp. 1939-1949
    • Charmandari, E.1    Kino, T.2    Souvatzoglou, E.3    Vottero, A.4    Bhattacharyya, N.5    Chrousos, G.P.6
  • 20
    • 0025828945 scopus 로고
    • Repression of the human glycoprotein hormone alpha-subunit gene by glucocorticoids: evidence for receptor interactions with limiting transcriptional activators
    • Chatterjee V.K., Madison L.D., Mayo S., and Jameson J.L. Repression of the human glycoprotein hormone alpha-subunit gene by glucocorticoids: evidence for receptor interactions with limiting transcriptional activators. Mol. Endocrinol. 5 (1991) 100-110
    • (1991) Mol. Endocrinol. , vol.5 , pp. 100-110
    • Chatterjee, V.K.1    Madison, L.D.2    Mayo, S.3    Jameson, J.L.4
  • 23
    • 0025759019 scopus 로고
    • Interaction of the glucocorticoid receptor DNA-binding domain with DNA as a dimer is mediated by a short segment of five amino acids
    • Dahlman-Wright K., Wright A., Gustafsson J.A., and Carlstedt-Duke J. Interaction of the glucocorticoid receptor DNA-binding domain with DNA as a dimer is mediated by a short segment of five amino acids. J. Biol. Chem. 266 (1991) 3107-3112
    • (1991) J. Biol. Chem. , vol.266 , pp. 3107-3112
    • Dahlman-Wright, K.1    Wright, A.2    Gustafsson, J.A.3    Carlstedt-Duke, J.4
  • 24
    • 0028786336 scopus 로고
    • Transcriptional regulation by MAP kinases
    • Davis R.J. Transcriptional regulation by MAP kinases. Mol. Reprod. Dev. 42 (1995) 459-467
    • (1995) Mol. Reprod. Dev. , vol.42 , pp. 459-467
    • Davis, R.J.1
  • 25
    • 0031459881 scopus 로고    scopus 로고
    • Glucocorticoid-mediated repression of nuclear factor-kappaB-dependent transcription involves direct interference with transactivation
    • De Bosscher K., Schmitz M.L., Vanden Berghe W., Plaisance S., Fiers W., and Haegeman G. Glucocorticoid-mediated repression of nuclear factor-kappaB-dependent transcription involves direct interference with transactivation. Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 13504-13509
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 13504-13509
    • De Bosscher, K.1    Schmitz, M.L.2    Vanden Berghe, W.3    Plaisance, S.4    Fiers, W.5    Haegeman, G.6
  • 26
    • 0035147033 scopus 로고    scopus 로고
    • Glucocorticoid repression of AP-1 is not mediated by competition for nuclear coactivators
    • De Bosscher K., Vanden Berghe W., and Haegeman G. Glucocorticoid repression of AP-1 is not mediated by competition for nuclear coactivators. Mol. Endocrinol. 15 (2001) 219-227
    • (2001) Mol. Endocrinol. , vol.15 , pp. 219-227
    • De Bosscher, K.1    Vanden Berghe, W.2    Haegeman, G.3
  • 27
    • 0034636021 scopus 로고    scopus 로고
    • Glucocorticoids repress NF-kappaB-driven genes by disturbing the interaction of p65 with the basal transcription machinery, irrespective of coactivator levels in the cell
    • De Bosscher K., Vanden Berghe W., Vermeulen L., Plaisance S., Boone E., and Haegeman G. Glucocorticoids repress NF-kappaB-driven genes by disturbing the interaction of p65 with the basal transcription machinery, irrespective of coactivator levels in the cell. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 3919-3924
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 3919-3924
    • De Bosscher, K.1    Vanden Berghe, W.2    Vermeulen, L.3    Plaisance, S.4    Boone, E.5    Haegeman, G.6
  • 28
    • 0030962905 scopus 로고    scopus 로고
    • Differential hormone-dependent transcriptional activation and -repression by naturally occurring human glucocorticoid receptor variants
    • de Lange P., Koper J.W., Huizenga N.A., Brinkmann A.O., de Jong F.H., Karl M., Chrousos G.P., and Lamberts S.W. Differential hormone-dependent transcriptional activation and -repression by naturally occurring human glucocorticoid receptor variants. Mol. Endocrinol. 11 (1997) 1156-1164
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1156-1164
    • de Lange, P.1    Koper, J.W.2    Huizenga, N.A.3    Brinkmann, A.O.4    de Jong, F.H.5    Karl, M.6    Chrousos, G.P.7    Lamberts, S.W.8
  • 29
    • 1842531011 scopus 로고    scopus 로고
    • The glucocorticoid receptor and the orphan nuclear receptor chicken ovalbumin upstream promoter-transcription factor II interact with and mutually affect each other's transcriptional activities: implications for intermediary metabolism
    • de Martino M.U., Bhattachryya N., Alesci S., Ichijo T., Chrousos G.P., and Kino T. The glucocorticoid receptor and the orphan nuclear receptor chicken ovalbumin upstream promoter-transcription factor II interact with and mutually affect each other's transcriptional activities: implications for intermediary metabolism. Mol. Endocrinol. 18 (2004) 820-833
    • (2004) Mol. Endocrinol. , vol.18 , pp. 820-833
    • de Martino, M.U.1    Bhattachryya, N.2    Alesci, S.3    Ichijo, T.4    Chrousos, G.P.5    Kino, T.6
  • 30
    • 0025081214 scopus 로고
    • Transcription factor interactions: selectors of positive or negative regulation from a single DNA element
    • Diamond M.I., Miner J.N., Yoshinaga S.K., and Yamamoto K.R. Transcription factor interactions: selectors of positive or negative regulation from a single DNA element. Science 249 (1990) 1266-1272
    • (1990) Science , vol.249 , pp. 1266-1272
    • Diamond, M.I.1    Miner, J.N.2    Yoshinaga, S.K.3    Yamamoto, K.R.4
  • 33
    • 0028335121 scopus 로고
    • Participation of Ets transcription factors in the glucocorticoid response of the rat tyrosine aminotransferase gene
    • Espinas M.L., Roux J., Ghysdael J., Pictet R., and Grange T. Participation of Ets transcription factors in the glucocorticoid response of the rat tyrosine aminotransferase gene. Mol. Cell. Biol. 14 (1994) 4116-4125
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4116-4125
    • Espinas, M.L.1    Roux, J.2    Ghysdael, J.3    Pictet, R.4    Grange, T.5
  • 34
    • 9644307891 scopus 로고    scopus 로고
    • Glucocorticoid ligands specify different interactions with NF-kappaB by allosteric effects on the glucocorticoid receptor DNA binding domain
    • Garside H., Stevens A., Farrow S., Normand C., Houle B., Berry A., Maschera B., and Ray D. Glucocorticoid ligands specify different interactions with NF-kappaB by allosteric effects on the glucocorticoid receptor DNA binding domain. J. Biol. Chem. 279 (2004) 50050-50059
    • (2004) J. Biol. Chem. , vol.279 , pp. 50050-50059
    • Garside, H.1    Stevens, A.2    Farrow, S.3    Normand, C.4    Houle, B.5    Berry, A.6    Maschera, B.7    Ray, D.8
  • 35
    • 0027451431 scopus 로고
    • Functional interference between the Spi-1/PU.1 oncoprotein and steroid hormone or vitamin receptors
    • Gauthier J.M., Bourachot B., Doucas V., Yaniv M., and Moreau-Gachelin F. Functional interference between the Spi-1/PU.1 oncoprotein and steroid hormone or vitamin receptors. EMBO J. 12 (1993) 5089-5096
    • (1993) EMBO J. , vol.12 , pp. 5089-5096
    • Gauthier, J.M.1    Bourachot, B.2    Doucas, V.3    Yaniv, M.4    Moreau-Gachelin, F.5
  • 36
    • 33845970925 scopus 로고    scopus 로고
    • Parallel SUMOylation-dependent pathways mediate gene- and signal-specific transrepression by LXRs and PPARgamma
    • Ghisletti S., Huang W., Ogawa S., Pascual G., Lin M.E., Willson T.M., Rosenfeld M.G., and Glass C.K. Parallel SUMOylation-dependent pathways mediate gene- and signal-specific transrepression by LXRs and PPARgamma. Mol. Cell 25 (2007) 57-70
    • (2007) Mol. Cell , vol.25 , pp. 57-70
    • Ghisletti, S.1    Huang, W.2    Ogawa, S.3    Pascual, G.4    Lin, M.E.5    Willson, T.M.6    Rosenfeld, M.G.7    Glass, C.K.8
  • 37
    • 33644980870 scopus 로고    scopus 로고
    • HIC-5 is a novel repressor of lymphoid enhancer factor/T-cell factor-driven transcription
    • Ghogomu S.M., van Venrooy S., Ritthaler M., Wedlich D., and Gradl D. HIC-5 is a novel repressor of lymphoid enhancer factor/T-cell factor-driven transcription. J. Biol. Chem. 281 (2006) 1755-1764
    • (2006) J. Biol. Chem. , vol.281 , pp. 1755-1764
    • Ghogomu, S.M.1    van Venrooy, S.2    Ritthaler, M.3    Wedlich, D.4    Gradl, D.5
  • 38
    • 0034605125 scopus 로고    scopus 로고
    • Glucocorticoids antagonize AP-1 by inhibiting the activation/phosphorylation of JNK without affecting its subcellular distribution
    • Gonzalez M.V., Jimenez B., Berciano M.T., Gonzalez-Sancho J.M., Caelles C., Lafarga M., and Munoz A. Glucocorticoids antagonize AP-1 by inhibiting the activation/phosphorylation of JNK without affecting its subcellular distribution. J. Cell Biol. 150 (2000) 1199-1208
    • (2000) J. Cell Biol. , vol.150 , pp. 1199-1208
    • Gonzalez, M.V.1    Jimenez, B.2    Berciano, M.T.3    Gonzalez-Sancho, J.M.4    Caelles, C.5    Lafarga, M.6    Munoz, A.7
  • 40
    • 8844262660 scopus 로고    scopus 로고
    • Principles for modulation of the nuclear receptor superfamily
    • Gronemeyer H., Gustafsson J.A., and Laudet V. Principles for modulation of the nuclear receptor superfamily. Nat. Rev. Drug Discov. 3 (2004) 950-964
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 950-964
    • Gronemeyer, H.1    Gustafsson, J.A.2    Laudet, V.3
  • 42
    • 33846912187 scopus 로고    scopus 로고
    • STAMP, a novel predicted factor assisting TIF2 actions in glucocorticoid receptor-mediated induction and repression
    • He Y., and Simons Jr. S.S. STAMP, a novel predicted factor assisting TIF2 actions in glucocorticoid receptor-mediated induction and repression. Mol. Cell. Biol. 27 (2007) 1467-1485
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 1467-1485
    • He, Y.1    Simons Jr., S.S.2
  • 43
    • 0030789420 scopus 로고    scopus 로고
    • I kappaB alpha-independent downregulation of NF-kappaB activity by glucocorticoid receptor
    • Heck S., Bender K., Kullmann M., Göttlicher M., Herrlich P., and Cato A.C. I kappaB alpha-independent downregulation of NF-kappaB activity by glucocorticoid receptor. EMBO J. 16 (1997) 4698-4707
    • (1997) EMBO J. , vol.16 , pp. 4698-4707
    • Heck, S.1    Bender, K.2    Kullmann, M.3    Göttlicher, M.4    Herrlich, P.5    Cato, A.C.6
  • 44
    • 0027934108 scopus 로고
    • A distinct modulating domain in glucocorticoid receptor monomers in the repression of activity of the transcription factor AP-1
    • Heck S., Kullmann M., Gast A., Ponta H., Rahmsdorf H.J., Herrlich P., and Cato A.C. A distinct modulating domain in glucocorticoid receptor monomers in the repression of activity of the transcription factor AP-1. EMBO J. 13 (1994) 4087-4095
    • (1994) EMBO J. , vol.13 , pp. 4087-4095
    • Heck, S.1    Kullmann, M.2    Gast, A.3    Ponta, H.4    Rahmsdorf, H.J.5    Herrlich, P.6    Cato, A.C.7
  • 45
    • 0032213365 scopus 로고    scopus 로고
    • Inhibition by dexamethasone of antigen-induced c-Jun N-terminal kinase activation in rat basophilic leukemia cells
    • Hirasawa N., Sato Y., Fujita Y., Mue S., and Ohuchi K. Inhibition by dexamethasone of antigen-induced c-Jun N-terminal kinase activation in rat basophilic leukemia cells. J. Immunol. 161 (1998) 4939-4943
    • (1998) J. Immunol. , vol.161 , pp. 4939-4943
    • Hirasawa, N.1    Sato, Y.2    Fujita, Y.3    Mue, S.4    Ohuchi, K.5
  • 46
    • 30744458869 scopus 로고    scopus 로고
    • IκB kinase α-mediated derepression of SMRT potentiates acetylation of RelA/p65 by p300
    • Hoberg J.E., Popko A.E., Ramsey C.S., and Mayo M.W. IκB kinase α-mediated derepression of SMRT potentiates acetylation of RelA/p65 by p300. Mol. Cell. Biol. 26 (2006) 457-471
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 457-471
    • Hoberg, J.E.1    Popko, A.E.2    Ramsey, C.S.3    Mayo, M.W.4
  • 47
    • 6344241039 scopus 로고    scopus 로고
    • SMRT derepression by the IκB kinase α: a prerequisite to NF-κB transcription and survival
    • Hoberg J.E., Yeung F., and Mayo M.W. SMRT derepression by the IκB kinase α: a prerequisite to NF-κB transcription and survival. Mol. Cell 16 (2004) 245-255
    • (2004) Mol. Cell , vol.16 , pp. 245-255
    • Hoberg, J.E.1    Yeung, F.2    Mayo, M.W.3
  • 48
    • 4344679818 scopus 로고    scopus 로고
    • Analysis of two CBP (cAMP-response-element-binding protein-binding protein) interacting sites in GRIP1 (glucocorticoid-receptor-interacting protein), and their importance for the function of GRIP1
    • Huang S.M., and Cheng Y.S. Analysis of two CBP (cAMP-response-element-binding protein-binding protein) interacting sites in GRIP1 (glucocorticoid-receptor-interacting protein), and their importance for the function of GRIP1. Biochem. J. 382 (2004) 111-119
    • (2004) Biochem. J. , vol.382 , pp. 111-119
    • Huang, S.M.1    Cheng, Y.S.2
  • 49
    • 0031765105 scopus 로고    scopus 로고
    • Inhibition of mitogen-activated protein kinase activity and proliferation of an early osteoblast cell line (MBA 15.4) by dexamethasone: role of protein phosphatases
    • Hulley P.A., Gordon F., and Hough F.S. Inhibition of mitogen-activated protein kinase activity and proliferation of an early osteoblast cell line (MBA 15.4) by dexamethasone: role of protein phosphatases. Endocrinology 139 (1998) 2423-2431
    • (1998) Endocrinology , vol.139 , pp. 2423-2431
    • Hulley, P.A.1    Gordon, F.2    Hough, F.S.3
  • 50
    • 0026026319 scopus 로고
    • Point mutation causing a single amino acid substitution in the hormone binding domain of the glucocorticoid receptor in familial glucocorticoid resistance
    • Hurley D.M., Accili D., Stratakis C.A., Karl M., Vamvakopoulos N., Rorer E., Constantine K., Taylor S.I., and Chrousos G.P. Point mutation causing a single amino acid substitution in the hormone binding domain of the glucocorticoid receptor in familial glucocorticoid resistance. J. Clin. Invest. 87 (1991) 680-686
    • (1991) J. Clin. Invest. , vol.87 , pp. 680-686
    • Hurley, D.M.1    Accili, D.2    Stratakis, C.A.3    Karl, M.4    Vamvakopoulos, N.5    Rorer, E.6    Constantine, K.7    Taylor, S.I.8    Chrousos, G.P.9
  • 51
    • 29644434851 scopus 로고    scopus 로고
    • The Smad6-histone deacetylase 3 complex silences the transcriptional activity of the glucocorticoid receptor: potential clinical implications
    • Ichijo T., Voutetakis A., Cotrim A.P., Bhattachryya N., Fujii M., Chrousos G.P., and Kino T. The Smad6-histone deacetylase 3 complex silences the transcriptional activity of the glucocorticoid receptor: potential clinical implications. J. Biol. Chem. 280 (2005) 42067-42077
    • (2005) J. Biol. Chem. , vol.280 , pp. 42067-42077
    • Ichijo, T.1    Voutetakis, A.2    Cotrim, A.P.3    Bhattachryya, N.4    Fujii, M.5    Chrousos, G.P.6    Kino, T.7
  • 52
    • 0027415164 scopus 로고
    • Glucocorticoid receptor-cAMP response element-binding protein interaction and the response of the phosphoenolpyruvate carboxykinase gene to glucocorticoids
    • Imai E., Miner J.N., Mitchell J.A., Yamamoto K.R., and Granner D.K. Glucocorticoid receptor-cAMP response element-binding protein interaction and the response of the phosphoenolpyruvate carboxykinase gene to glucocorticoids. J. Biol. Chem. 268 (1993) 5353-5356
    • (1993) J. Biol. Chem. , vol.268 , pp. 5353-5356
    • Imai, E.1    Miner, J.N.2    Mitchell, J.A.3    Yamamoto, K.R.4    Granner, D.K.5
  • 53
    • 0346259944 scopus 로고    scopus 로고
    • Inhibition of p38 MAPK by glucocorticoids via induction of MAPK phosphatase-1 enhances nontypeable Haemophilus influenzae-induced expression of toll-like receptor 2
    • Imasato A., Desbois-Mouthon C., Han J., Kai H., Cato A.C., Akira S., and Li J.D. Inhibition of p38 MAPK by glucocorticoids via induction of MAPK phosphatase-1 enhances nontypeable Haemophilus influenzae-induced expression of toll-like receptor 2. J. Biol. Chem. 277 (2002) 47444-47450
    • (2002) J. Biol. Chem. , vol.277 , pp. 47444-47450
    • Imasato, A.1    Desbois-Mouthon, C.2    Han, J.3    Kai, H.4    Cato, A.C.5    Akira, S.6    Li, J.D.7
  • 54
    • 0033821409 scopus 로고    scopus 로고
    • Glucocorticoid receptor recruitment of histone deacetylase 2 inhibits interleukin-1beta-induced histone H4 acetylation on lysines 8 and 12
    • Ito K., Barnes P.J., and Adcock I.M. Glucocorticoid receptor recruitment of histone deacetylase 2 inhibits interleukin-1beta-induced histone H4 acetylation on lysines 8 and 12. Mol. Cell. Biol. 20 (2000) 6891-6903
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6891-6903
    • Ito, K.1    Barnes, P.J.2    Adcock, I.M.3
  • 55
    • 0035839497 scopus 로고    scopus 로고
    • p65-activated histone acetyltransferase activity is repressed by glucocorticoids: mifepristone fails to recruit HDAC2 to the p65-HAT complex
    • Ito K., Jazrawi E., Cosio B., Barnes P.J., and Adcock I.M. p65-activated histone acetyltransferase activity is repressed by glucocorticoids: mifepristone fails to recruit HDAC2 to the p65-HAT complex. J. Biol. Chem. 276 (2001) 30208-30215
    • (2001) J. Biol. Chem. , vol.276 , pp. 30208-30215
    • Ito, K.1    Jazrawi, E.2    Cosio, B.3    Barnes, P.J.4    Adcock, I.M.5
  • 56
    • 31344446119 scopus 로고    scopus 로고
    • Histone deacetylase 2-mediated deacetylation of the glucocorticoid receptor enables NF-kappaB suppression
    • Ito K., Yamamura S., Essilfie-Quaye S., Cosio B., Ito M., Barnes P.J., and Adcock I.M. Histone deacetylase 2-mediated deacetylation of the glucocorticoid receptor enables NF-kappaB suppression. J. Exp. Med. 203 (2006) 7-13
    • (2006) J. Exp. Med. , vol.203 , pp. 7-13
    • Ito, K.1    Yamamura, S.2    Essilfie-Quaye, S.3    Cosio, B.4    Ito, M.5    Barnes, P.J.6    Adcock, I.M.7
  • 57
    • 20744443470 scopus 로고    scopus 로고
    • Repression of interleukin-5 transcription by the glucocorticoid receptor targets GATA3 signaling and involves histone deacetylase recruitment
    • Jee Y.K., Gilmour J., Kelly A., Bowen H., Richards D., Soh C., Smith P., Hawrylowicz C., Cousins D., Lee T., and Lavender P. Repression of interleukin-5 transcription by the glucocorticoid receptor targets GATA3 signaling and involves histone deacetylase recruitment. J. Biol. Chem. 280 (2005) 23243-23250
    • (2005) J. Biol. Chem. , vol.280 , pp. 23243-23250
    • Jee, Y.K.1    Gilmour, J.2    Kelly, A.3    Bowen, H.4    Richards, D.5    Soh, C.6    Smith, P.7    Hawrylowicz, C.8    Cousins, D.9    Lee, T.10    Lavender, P.11
  • 58
  • 59
    • 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., Gebel S., Ponta H., and Herrlich P. Antitumor promotion and antiinflammation: down-modulation of AP-1 (Fos/Jun) activity by glucocorticoid hormone. Cell 62 (1990) 1189-1204
    • (1990) Cell , vol.62 , pp. 1189-1204
    • Jonat, C.1    Rahmsdorf, H.J.2    Park, K.K.3    Cato, A.C.4    Gebel, S.5    Ponta, H.6    Herrlich, P.7
  • 60
    • 8444240109 scopus 로고    scopus 로고
    • The LIM domain: from the cytoskeleton to the nucleus
    • Kadrmas J.L., and Beckerle M.C. The LIM domain: from the cytoskeleton to the nucleus. Nat. Rev. Mol. Cell. Biol. 5 (2004) 920-931
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , pp. 920-931
    • Kadrmas, J.L.1    Beckerle, M.C.2
  • 62
    • 0021242444 scopus 로고
    • Characterization of DNA sequences through which cadmium and glucocorticoid hormones induce human metallothionein-IIA gene
    • Karin M., Haslinger A., Holtgreve H., Richards R.I., Krauter P., Westphal H.M., and Beato M. Characterization of DNA sequences through which cadmium and glucocorticoid hormones induce human metallothionein-IIA gene. Nature 308 (1984) 513-519
    • (1984) Nature , vol.308 , pp. 513-519
    • Karin, M.1    Haslinger, A.2    Holtgreve, H.3    Richards, R.I.4    Krauter, P.5    Westphal, H.M.6    Beato, M.7
  • 63
    • 33646349207 scopus 로고    scopus 로고
    • Wound-induced p38MAPK-dependent histone H3 phosphorylation correlates with increased COX-2 expression in enterocytes
    • Karrasch T., Steinbrecher K.A., Allard B., Baldwin A.S., and Jobin C. Wound-induced p38MAPK-dependent histone H3 phosphorylation correlates with increased COX-2 expression in enterocytes. J. Cell. Physiol. 207 (2006) 809-815
    • (2006) J. Cell. Physiol. , vol.207 , pp. 809-815
    • Karrasch, T.1    Steinbrecher, K.A.2    Allard, B.3    Baldwin, A.S.4    Jobin, C.5
  • 64
    • 0033808255 scopus 로고    scopus 로고
    • Corticosteroid actions in hippocampus require DNA binding of glucocorticoid receptor homodimers
    • Karst H., Karten Y.J., Reichardt H.M., de Kloet E.R., Schutz G., and Joels M. Corticosteroid actions in hippocampus require DNA binding of glucocorticoid receptor homodimers. Nat. Neurosci. 3 (2000) 977-978
    • (2000) Nat. Neurosci. , vol.3 , pp. 977-978
    • Karst, H.1    Karten, Y.J.2    Reichardt, H.M.3    de Kloet, E.R.4    Schutz, G.5    Joels, M.6
  • 65
    • 0037126628 scopus 로고    scopus 로고
    • Glucocorticoids inhibit MAP kinase via increased expression and decreased degradation of MKP-1
    • Kassel O., Sancono A., Kratzschmar J., Kreft B., Stassen M., and Cato A.C. Glucocorticoids inhibit MAP kinase via increased expression and decreased degradation of MKP-1. EMBO J. 20 (2001) 7108-7116
    • (2001) EMBO J. , vol.20 , pp. 7108-7116
    • Kassel, O.1    Sancono, A.2    Kratzschmar, J.3    Kreft, B.4    Stassen, M.5    Cato, A.C.6
  • 66
    • 5444233785 scopus 로고    scopus 로고
    • A nuclear isoform of the focal adhesion LIM-domain protein Trip6 integrates activating and repressing signals at AP-1- and NF-κB-regulated promoters
    • Kassel O., Schneider S., Heilbock C., Litfin M., Göttlicher M., and Herrlich P. A nuclear isoform of the focal adhesion LIM-domain protein Trip6 integrates activating and repressing signals at AP-1- and NF-κB-regulated promoters. Genes Dev. 18 (2004) 2518-2528
    • (2004) Genes Dev. , vol.18 , pp. 2518-2528
    • Kassel, O.1    Schneider, S.2    Heilbock, C.3    Litfin, M.4    Göttlicher, M.5    Herrlich, P.6
  • 68
    • 0027269689 scopus 로고
    • Fos is a preferential target of glucocorticoid receptor inhibition of AP-1 activity in vitro
    • Kerppola T.K., Luk D., and Curran T. Fos is a preferential target of glucocorticoid receptor inhibition of AP-1 activity in vitro. Mol. Cell. Biol. 13 (1993) 3782-3791
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3782-3791
    • Kerppola, T.K.1    Luk, D.2    Curran, T.3
  • 69
    • 18144417838 scopus 로고    scopus 로고
    • Glucocorticoid receptor (GR)-associated SMRT binding to C/EBPβ TAD and Nrf2 Neh4/5: role of SMRT recruited to GR in GSTA2 gene repression
    • Ki S.H., Cho I.J., Choi D.W., and Kim S.G. Glucocorticoid receptor (GR)-associated SMRT binding to C/EBPβ TAD and Nrf2 Neh4/5: role of SMRT recruited to GR in GSTA2 gene repression. Mol. Cell. Biol. 25 (2005) 4150-4165
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 4150-4165
    • Ki, S.H.1    Cho, I.J.2    Choi, D.W.3    Kim, S.G.4
  • 70
    • 0026579203 scopus 로고
    • Interference between pathway-specific transcription factors: glucocorticoids antagonize phorbol ester-induced AP-1 activity without altering AP-1 site occupation in vivo
    • König H., Ponta H., Rahmsdorf H.J., and Herrlich P. Interference between pathway-specific transcription factors: glucocorticoids antagonize phorbol ester-induced AP-1 activity without altering AP-1 site occupation in vivo. EMBO J. 11 (1992) 2241-2246
    • (1992) EMBO J. , vol.11 , pp. 2241-2246
    • König, H.1    Ponta, H.2    Rahmsdorf, H.J.3    Herrlich, P.4
  • 71
    • 0037135628 scopus 로고    scopus 로고
    • A point mutation of the AF2 transactivation domain of the glucocorticoid receptor disrupts its interaction with steroid receptor coactivator 1
    • Kucera T., Waltner-Law M., Scott D.K., Prasad R., and Granner D.K. A point mutation of the AF2 transactivation domain of the glucocorticoid receptor disrupts its interaction with steroid receptor coactivator 1. J. Biol. Chem. 277 (2002) 26098-26102
    • (2002) J. Biol. Chem. , vol.277 , pp. 26098-26102
    • Kucera, T.1    Waltner-Law, M.2    Scott, D.K.3    Prasad, R.4    Granner, D.K.5
  • 72
    • 0347480262 scopus 로고    scopus 로고
    • Identification of a novel glucocorticoid receptor mutation in budesonide-resistant human bronchial epithelial cells
    • Kunz S., Sandoval R., Carlsson P., Carlstedt-Duke J., Bloom J.W., and Miesfeld R.L. Identification of a novel glucocorticoid receptor mutation in budesonide-resistant human bronchial epithelial cells. Mol. Endocrinol. 17 (2003) 2566-2582
    • (2003) Mol. Endocrinol. , vol.17 , pp. 2566-2582
    • Kunz, S.1    Sandoval, R.2    Carlsson, P.3    Carlstedt-Duke, J.4    Bloom, J.W.5    Miesfeld, R.L.6
  • 73
    • 0032142918 scopus 로고    scopus 로고
    • Roles of histone acetyltransferases and deacetylases in gene regulation
    • Kuo M.H., and Allis C.D. Roles of histone acetyltransferases and deacetylases in gene regulation. Bioessay 20 (1998) 615-626
    • (1998) Bioessay , vol.20 , pp. 615-626
    • Kuo, M.H.1    Allis, C.D.2
  • 74
    • 0026686619 scopus 로고
    • Functional interference between the ubiquitous and constitutive octamer transcription factor 1 (OTF-1) and the glucocorticoid receptor by direct protein-protein interaction involving the homeo subdomain of OTF-1
    • Kutoh E., Stromstedt P.E., and Poellinger L. Functional interference between the ubiquitous and constitutive octamer transcription factor 1 (OTF-1) and the glucocorticoid receptor by direct protein-protein interaction involving the homeo subdomain of OTF-1. Mol. Cell. Biol. 12 (1992) 4960-4969
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4960-4969
    • Kutoh, E.1    Stromstedt, P.E.2    Poellinger, L.3
  • 76
    • 0036841288 scopus 로고    scopus 로고
    • Dexamethasone causes sustained expression of mitogen-activated protein kinase (MAPK) phosphatase 1 and phosphatase-mediated inhibition of MAPK p38
    • Lasa M., Abraham S.M., Boucheron C., Saklatvala J., and Clark A.R. Dexamethasone causes sustained expression of mitogen-activated protein kinase (MAPK) phosphatase 1 and phosphatase-mediated inhibition of MAPK p38. Mol. Cell. Biol. 22 (2002) 7802-7811
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7802-7811
    • Lasa, M.1    Abraham, S.M.2    Boucheron, C.3    Saklatvala, J.4    Clark, A.R.5
  • 77
    • 0035138742 scopus 로고    scopus 로고
    • Dexamethasone destabilizes cyclooxygenase 2 mRNA by inhibiting mitogen-activated protein kinase p38
    • Lasa M., Brook M., Saklatvala J., and Clark A.R. Dexamethasone destabilizes cyclooxygenase 2 mRNA by inhibiting mitogen-activated protein kinase p38. Mol. Cell. Biol. 21 (2001) 771-780
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 771-780
    • Lasa, M.1    Brook, M.2    Saklatvala, J.3    Clark, A.R.4
  • 78
    • 0030846576 scopus 로고    scopus 로고
    • Promoter-dependent synergy between glucocorticoid receptor and Stat5 in the activation of beta-casein gene transcription
    • Lechner J., Welte T., Tomasi J.K., Bruno P., Cairns C., Gustafsson J., and Doppler W. Promoter-dependent synergy between glucocorticoid receptor and Stat5 in the activation of beta-casein gene transcription. J. Biol. Chem. 272 (1997) 20954-20960
    • (1997) J. Biol. Chem. , vol.272 , pp. 20954-20960
    • Lechner, J.1    Welte, T.2    Tomasi, J.K.3    Bruno, P.4    Cairns, C.5    Gustafsson, J.6    Doppler, W.7
  • 79
    • 0032479304 scopus 로고    scopus 로고
    • Steroid receptor coactivator-1 coactivates activating protein-1-mediated transactivations through interaction with the c-Jun and c-Fos subunits
    • Lee S.K., Kim H.J., Na S.Y., Kim T.S., Choi H.S., Im S.Y., and Lee J.W. Steroid receptor coactivator-1 coactivates activating protein-1-mediated transactivations through interaction with the c-Jun and c-Fos subunits. J. Biol. Chem. 273 (1998) 16651-16654
    • (1998) J. Biol. Chem. , vol.273 , pp. 16651-16654
    • Lee, S.K.1    Kim, H.J.2    Na, S.Y.3    Kim, T.S.4    Choi, H.S.5    Im, S.Y.6    Lee, J.W.7
  • 80
    • 0142091544 scopus 로고    scopus 로고
    • STAT3-dependent enhanceosome assembly and disassembly: synergy with GR for full transcriptional increase of the alpha 2-macroglobulin gene
    • Lerner L., Henriksen M.A., Zhang X., and Darnell Jr. J.E. STAT3-dependent enhanceosome assembly and disassembly: synergy with GR for full transcriptional increase of the alpha 2-macroglobulin gene. Genes Dev. 17 (2003) 2564-2577
    • (2003) Genes Dev. , vol.17 , pp. 2564-2577
    • Lerner, L.1    Henriksen, M.A.2    Zhang, X.3    Darnell Jr., J.E.4
  • 81
    • 33947655345 scopus 로고    scopus 로고
    • The activated glucocorticoid receptor inhibits the transcription factor T-bet by direct protein-protein interaction
    • Liberman A.C., Refojo D., Druker J., Toscano M., Rein T., Holsboer F., and Arzt E. The activated glucocorticoid receptor inhibits the transcription factor T-bet by direct protein-protein interaction. FASEB J. 21 (2007) 1177-1188
    • (2007) FASEB J. , vol.21 , pp. 1177-1188
    • Liberman, A.C.1    Refojo, D.2    Druker, J.3    Toscano, M.4    Rein, T.5    Holsboer, F.6    Arzt, E.7
  • 82
    • 0030824266 scopus 로고    scopus 로고
    • A new function for the C-terminal zinc finger of the glucocorticoid receptor. Repression of RelA transactivation
    • Liden J., Delaunay F., Rafter I., Gustafsson J., and Okret S. A new function for the C-terminal zinc finger of the glucocorticoid receptor. Repression of RelA transactivation. J. Biol. Chem. 272 (1997) 21467-21472
    • (1997) J. Biol. Chem. , vol.272 , pp. 21467-21472
    • Liden, J.1    Delaunay, F.2    Rafter, I.3    Gustafsson, J.4    Okret, S.5
  • 83
    • 0027939902 scopus 로고
    • Glucocorticoids activate somatostatin gene transcription through co-operative interaction with the cyclic AMP signalling pathway
    • Liu J.L., Papachristou D.N., and Patel Y.C. Glucocorticoids activate somatostatin gene transcription through co-operative interaction with the cyclic AMP signalling pathway. Biochem. J. 301 (1994) 863-869
    • (1994) Biochem. J. , vol.301 , pp. 863-869
    • Liu, J.L.1    Papachristou, D.N.2    Patel, Y.C.3
  • 84
    • 33646238485 scopus 로고    scopus 로고
    • Modulation of glucocorticoid receptor-interacting protein 1 (GRIP1) transactivation and co-activation activities through its C-terminal repression and self-association domains
    • Liu P.-Y., Hsieh T.-Y., Chou W.-Y., and Huang S.-M. Modulation of glucocorticoid receptor-interacting protein 1 (GRIP1) transactivation and co-activation activities through its C-terminal repression and self-association domains. FEBS J. 273 (2006) 2172-2183
    • (2006) FEBS J. , vol.273 , pp. 2172-2183
    • Liu, P.-Y.1    Hsieh, T.-Y.2    Chou, W.-Y.3    Huang, S.-M.4
  • 85
    • 0025150272 scopus 로고
    • Mutual transrepression of Fos and the glucocorticoid receptor: involvement of a functional domain in Fos which is absent in FosB
    • Lucibello F.C., Slater E.P., Jooss K.U., Beato M., and Muller R. Mutual transrepression of Fos and the glucocorticoid receptor: involvement of a functional domain in Fos which is absent in FosB. EMBO J. 9 (1990) 2827-2834
    • (1990) EMBO J. , vol.9 , pp. 2827-2834
    • Lucibello, F.C.1    Slater, E.P.2    Jooss, K.U.3    Beato, M.4    Muller, R.5
  • 86
    • 18244381020 scopus 로고    scopus 로고
    • The glucocorticoid receptor blocks P-TEFb recruitment by NFkappaB to effect promoter-specific transcriptional repression
    • Luecke H.F., and Yamamoto K.R. The glucocorticoid receptor blocks P-TEFb recruitment by NFkappaB to effect promoter-specific transcriptional repression. Genes Dev. 19 (2005) 1116-1127
    • (2005) Genes Dev. , vol.19 , pp. 1116-1127
    • Luecke, H.F.1    Yamamoto, K.R.2
  • 87
    • 2942617294 scopus 로고    scopus 로고
    • Coordination of cell signaling, chromatin remodeling, histone modifications, and regulator recruitment in human matrix metalloproteinase 9 gene transcription
    • Ma Z., Shah R.C., Chang M.J., and Benveniste E.N. Coordination of cell signaling, chromatin remodeling, histone modifications, and regulator recruitment in human matrix metalloproteinase 9 gene transcription. Mol. Cell. Biol. 24 (2004) 5496-5509
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5496-5509
    • Ma, Z.1    Shah, R.C.2    Chang, M.J.3    Benveniste, E.N.4
  • 88
    • 15444376898 scopus 로고    scopus 로고
    • Protein-protein interactions and transcriptional antagonism between the subfamily of NGFI-B/Nur77 orphan nuclear receptors and glucocorticoid receptor
    • Martens C., Bilodeau S., Maira M., Gauthier Y., and Drouin J. Protein-protein interactions and transcriptional antagonism between the subfamily of NGFI-B/Nur77 orphan nuclear receptors and glucocorticoid receptor. Mol. Endocrinol. 19 (2005) 885-897
    • (2005) Mol. Endocrinol. , vol.19 , pp. 885-897
    • Martens, C.1    Bilodeau, S.2    Maira, M.3    Gauthier, Y.4    Drouin, J.5
  • 89
    • 0037380161 scopus 로고    scopus 로고
    • Recent advances in understanding chromatin remodeling by Swi/Snf complexes
    • Martens J.A., and Winston F. Recent advances in understanding chromatin remodeling by Swi/Snf complexes. Cur. Opin. Genet. Dev. 13 (2003) 136-142
    • (2003) Cur. Opin. Genet. Dev. , vol.13 , pp. 136-142
    • Martens, J.A.1    Winston, F.2
  • 90
    • 0037370029 scopus 로고    scopus 로고
    • Cascade of distinct histone modifications during collagenase gene activation
    • Martens J.H., Verlaan M., Kalkhoven E., and Zantema A. Cascade of distinct histone modifications during collagenase gene activation. Mol. Cell. Biol. 23 (2003) 1808-1816
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1808-1816
    • Martens, J.H.1    Verlaan, M.2    Kalkhoven, E.3    Zantema, A.4
  • 91
    • 0031916865 scopus 로고    scopus 로고
    • Cross-talk between nuclear factor-kappa B and the steroid hormone receptors: mechanisms of mutual antagonism
    • McKay L.I., and Cidlowski J.A. Cross-talk between nuclear factor-kappa B and the steroid hormone receptors: mechanisms of mutual antagonism. Mol. Endocrinol. 12 (1998) 45-56
    • (1998) Mol. Endocrinol. , vol.12 , pp. 45-56
    • McKay, L.I.1    Cidlowski, J.A.2
  • 92
    • 0034464826 scopus 로고    scopus 로고
    • CBP (CREB binding protein) integrates NF-kappaB (nuclear factor-kappaB) and glucocorticoid receptor physical interactions and antagonism
    • McKay L.I., and Cidlowski J.A. CBP (CREB binding protein) integrates NF-kappaB (nuclear factor-kappaB) and glucocorticoid receptor physical interactions and antagonism. Mol. Endocrinol. 14 (2000) 1222-1234
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1222-1234
    • McKay, L.I.1    Cidlowski, J.A.2
  • 93
    • 33745673129 scopus 로고    scopus 로고
    • Coactivator-associated arginine methyltransferase-1 enhances Nuclear Factor-κB-mediated gene transcription through methylation of histone H3 at arginine 17
    • Miao F., Li S., Chavez V., Lanting L., and Natarajan R. Coactivator-associated arginine methyltransferase-1 enhances Nuclear Factor-κB-mediated gene transcription through methylation of histone H3 at arginine 17. Mol. Endocrinol. 20 (2006) 1562-1573
    • (2006) Mol. Endocrinol. , vol.20 , pp. 1562-1573
    • Miao, F.1    Li, S.2    Chavez, V.3    Lanting, L.4    Natarajan, R.5
  • 94
    • 0023333976 scopus 로고
    • Interaction of the TGGCA-binding protein with upstream sequences is required for efficient transcription of mouse mammary tumor virus
    • Miksicek R., Borgmeyer U., and Nowock J. Interaction of the TGGCA-binding protein with upstream sequences is required for efficient transcription of mouse mammary tumor virus. EMBO J. 6 (1987) 1355-1360
    • (1987) EMBO J. , vol.6 , pp. 1355-1360
    • Miksicek, R.1    Borgmeyer, U.2    Nowock, J.3
  • 95
    • 0036685418 scopus 로고    scopus 로고
    • Designer glucocorticoids
    • Miner J.N. Designer glucocorticoids. Biochem. Pharmacol. 64 (2002) 355-361
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 355-361
    • Miner, J.N.1
  • 96
    • 0028305712 scopus 로고
    • Novel mechanism of glucocorticoid-mediated gene repression. Nuclear factor-kappa B is target for glucocorticoid-mediated interleukin 8 gene repression
    • Mukaida N., Morita M., Ishikawa Y., Rice N., Okamoto S., Kasahara T., and Matsushima K. Novel mechanism of glucocorticoid-mediated gene repression. Nuclear factor-kappa B is target for glucocorticoid-mediated interleukin 8 gene repression. J. Biol. Chem. 269 (1994) 13289-13295
    • (1994) J. Biol. Chem. , vol.269 , pp. 13289-13295
    • Mukaida, N.1    Morita, M.2    Ishikawa, Y.3    Rice, N.4    Okamoto, S.5    Kasahara, T.6    Matsushima, K.7
  • 98
    • 0032080237 scopus 로고    scopus 로고
    • Steroid receptor coactivator-1 interacts with the p50 subunit and coactivates nuclear factor kappa B-mediated transactivations
    • Na S.-Y., Lee S.-K., Han S.-J., Choi H.-S., Im S.-Y., and Lee J.W. Steroid receptor coactivator-1 interacts with the p50 subunit and coactivates nuclear factor kappa B-mediated transactivations. J. Biol. Chem. 273 (1998) 10831-10834
    • (1998) J. Biol. Chem. , vol.273 , pp. 10831-10834
    • Na, S.-Y.1    Lee, S.-K.2    Han, S.-J.3    Choi, H.-S.4    Im, S.-Y.5    Lee, J.W.6
  • 99
    • 21244495174 scopus 로고    scopus 로고
    • Beta2-adrenoceptor agonists, like glucocorticoids, repress eotaxin gene transcription by selective inhibition of histone H4 acetylation
    • Nie M., Knox A.J., and Pang L. Beta2-adrenoceptor agonists, like glucocorticoids, repress eotaxin gene transcription by selective inhibition of histone H4 acetylation. J. Immunol. 175 (2005) 478-486
    • (2005) J. Immunol. , vol.175 , pp. 478-486
    • Nie, M.1    Knox, A.J.2    Pang, L.3
  • 100
    • 0034665748 scopus 로고    scopus 로고
    • The glucocorticoid receptor inhibits NFkappaB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain
    • Nissen R.M., and Yamamoto K.R. The glucocorticoid receptor inhibits NFkappaB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain. Genes Dev. 14 (2000) 2314-2329
    • (2000) Genes Dev. , vol.14 , pp. 2314-2329
    • Nissen, R.M.1    Yamamoto, K.R.2
  • 101
    • 0032729458 scopus 로고    scopus 로고
    • Signaling through beta-catenin and Lef/Tcf
    • Novak A., and Dedhar S. Signaling through beta-catenin and Lef/Tcf. Cell. Mol. Life Sci. 56 (1999) 523-537
    • (1999) Cell. Mol. Life Sci. , vol.56 , pp. 523-537
    • Novak, A.1    Dedhar, S.2
  • 105
    • 1942424854 scopus 로고    scopus 로고
    • Glucocorticoid enhances the expression of dickkopf-1 in human osteoblasts: novel mechanism of glucocorticoid-induced osteoporosis
    • Ohnaka K., Taniguchi H., Kawate H., Nawata H., and Takayanagi R. Glucocorticoid enhances the expression of dickkopf-1 in human osteoblasts: novel mechanism of glucocorticoid-induced osteoporosis. Biochem. Biophys. Res. Commun. 318 (2004) 259-264
    • (2004) Biochem. Biophys. Res. Commun. , vol.318 , pp. 259-264
    • Ohnaka, K.1    Taniguchi, H.2    Kawate, H.3    Nawata, H.4    Takayanagi, R.5
  • 106
    • 0035940455 scopus 로고    scopus 로고
    • Point mutation in the mouse glucocorticoid receptor preventing DNA binding impairs spatial memory
    • Oitzl M.S., Reichardt H.M., Joels M., and de Kloet E.R. Point mutation in the mouse glucocorticoid receptor preventing DNA binding impairs spatial memory. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 12790-12795
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 12790-12795
    • Oitzl, M.S.1    Reichardt, H.M.2    Joels, M.3    de Kloet, E.R.4
  • 107
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
    • Onate S.A., Tsai S.Y., Tsai M.J., and O'Malley B.W. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270 (1995) 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
  • 109
    • 0030614504 scopus 로고    scopus 로고
    • Regulation of NF-kappaB by cyclin-dependent kinases associated with the p300 coactivator
    • Perkins N.D., Felzien L.K., Betts J.C., Leung K., Beach D.H., and Nabel G.J. Regulation of NF-kappaB by cyclin-dependent kinases associated with the p300 coactivator. Science 275 (1997) 523-527
    • (1997) Science , vol.275 , pp. 523-527
    • Perkins, N.D.1    Felzien, L.K.2    Betts, J.C.3    Leung, K.4    Beach, D.H.5    Nabel, G.J.6
  • 110
    • 0032230282 scopus 로고    scopus 로고
    • p300/CREB-binding protein enhances the prolactin-mediated transcriptional induction through direct interaction with the transactivation domain of Stat5, but does not participate in the Stat5-mediated suppression of the glucocorticoid response
    • Pfitzner E., Jahne R., Wissler M., Stoecklin E., and Groner B. p300/CREB-binding protein enhances the prolactin-mediated transcriptional induction through direct interaction with the transactivation domain of Stat5, but does not participate in the Stat5-mediated suppression of the glucocorticoid response. Mol. Endocrinol. 12 (1998) 1582-1593
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1582-1593
    • Pfitzner, E.1    Jahne, R.2    Wissler, M.3    Stoecklin, E.4    Groner, B.5
  • 113
    • 0141613756 scopus 로고    scopus 로고
    • Phosphorylation of serine 10 in histone H3, what for?
    • Prigent C., and Dimitrov S. Phosphorylation of serine 10 in histone H3, what for?. J. Cell Sci. 116 (2003) 3677-3685
    • (2003) J. Cell Sci. , vol.116 , pp. 3677-3685
    • Prigent, C.1    Dimitrov, S.2
  • 114
    • 0025770260 scopus 로고
    • Repressor to activator switch by mutations in the first Zn finger of the glucocorticoid receptor: is direct DNA binding necessary?
    • Ray A., LaForge K.S., and Sehgal P.B. Repressor to activator switch by mutations in the first Zn finger of the glucocorticoid receptor: is direct DNA binding necessary?. Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 7086-7090
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 7086-7090
    • Ray, A.1    LaForge, K.S.2    Sehgal, P.B.3
  • 115
    • 0028107237 scopus 로고
    • Physical association and functional antagonism between the p65 subunit of transcription factor NF-kappa B and the glucocorticoid receptor
    • Ray A., and Prefontaine K.E. Physical association and functional antagonism between the p65 subunit of transcription factor NF-kappa B and the glucocorticoid receptor. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 752-756
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 752-756
    • Ray, A.1    Prefontaine, K.E.2
  • 116
    • 0033304646 scopus 로고    scopus 로고
    • Structure/function of the human glucocorticoid receptor: tyrosine 735 is important for transactivation
    • Ray D.W., Suen C.S., Brass A., Soden J., and White A. Structure/function of the human glucocorticoid receptor: tyrosine 735 is important for transactivation. Mol. Endocrinol. 13 (1999) 1855-1863
    • (1999) Mol. Endocrinol. , vol.13 , pp. 1855-1863
    • Ray, D.W.1    Suen, C.S.2    Brass, A.3    Soden, J.4    White, A.5
  • 119
    • 30444456366 scopus 로고    scopus 로고
    • The GRIP1:IRF3 interaction as a target for glucocorticoid receptor-mediated immunosuppression
    • Reily M.M., Pantoja C., Hu X., Chinenov Y., and Rogatsky I. The GRIP1:IRF3 interaction as a target for glucocorticoid receptor-mediated immunosuppression. EMBO J. 25 (2006) 108-117
    • (2006) EMBO J. , vol.25 , pp. 108-117
    • Reily, M.M.1    Pantoja, C.2    Hu, X.3    Chinenov, Y.4    Rogatsky, I.5
  • 120
    • 0030587114 scopus 로고    scopus 로고
    • Activation of the mitogen-activated protein kinase cascade is suppressed by low concentrations of dexamethasone in mast cells
    • Rider L.G., Hirasawa N., Santini F., and Beaven M.A. Activation of the mitogen-activated protein kinase cascade is suppressed by low concentrations of dexamethasone in mast cells. J. Immunol. 157 (1996) 2374-2380
    • (1996) J. Immunol. , vol.157 , pp. 2374-2380
    • Rider, L.G.1    Hirasawa, N.2    Santini, F.3    Beaven, M.A.4
  • 121
    • 0037168648 scopus 로고    scopus 로고
    • Alternate surfaces of transcriptional coregulator GRIP1 function in different glucocorticoid receptor activation and repression contexts
    • Rogatsky I., Luecke H.F., Leitman D.C., and Yamamoto K.R. Alternate surfaces of transcriptional coregulator GRIP1 function in different glucocorticoid receptor activation and repression contexts. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 16701-16706
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16701-16706
    • Rogatsky, I.1    Luecke, H.F.2    Leitman, D.C.3    Yamamoto, K.R.4
  • 123
    • 0035502975 scopus 로고    scopus 로고
    • Factor recruitment and TIF2/GRIP1 corepressor activity at a collagenase-3 response element that mediates regulation by phorbol esters and hormones
    • Rogatsky I., Zarember K.A., and Yamamoto K.R. Factor recruitment and TIF2/GRIP1 corepressor activity at a collagenase-3 response element that mediates regulation by phorbol esters and hormones. EMBO J. 20 (2001) 6071-6083
    • (2001) EMBO J. , vol.20 , pp. 6071-6083
    • Rogatsky, I.1    Zarember, K.A.2    Yamamoto, K.R.3
  • 124
    • 0024080921 scopus 로고
    • Hormone-mediated repression: a negative glucocorticoid response element from the bovine prolactin gene
    • Sakai D.D., Helms S., Carlstedt-Duke J., Gustafsson J.A., Rottman F.M., and Yamamoto K.R. Hormone-mediated repression: a negative glucocorticoid response element from the bovine prolactin gene. Genes Dev. 2 (1988) 1144-1154
    • (1988) Genes Dev. , vol.2 , pp. 1144-1154
    • Sakai, D.D.1    Helms, S.2    Carlstedt-Duke, J.3    Gustafsson, J.A.4    Rottman, F.M.5    Yamamoto, K.R.6
  • 125
    • 1942502336 scopus 로고    scopus 로고
    • The coactivator LXXLL nuclear receptor recognition motif
    • Savkur R.S., and Burris T.P. The coactivator LXXLL nuclear receptor recognition motif. J. Pept. Res. 63 (2004) 207-212
    • (2004) J. Pept. Res. , vol.63 , pp. 207-212
    • Savkur, R.S.1    Burris, T.P.2
  • 126
    • 0037643416 scopus 로고    scopus 로고
    • Molecular mechanisms of glucocorticoid action and resistance
    • Schaaf M.J., and Cidlowski J.A. Molecular mechanisms of glucocorticoid action and resistance. J. Steroid. Biochem. Mol. Biol. 83 (2002) 37-48
    • (2002) J. Steroid. Biochem. Mol. Biol. , vol.83 , pp. 37-48
    • Schaaf, M.J.1    Cidlowski, J.A.2
  • 127
    • 33745633332 scopus 로고    scopus 로고
    • Insight into the molecular mechanisms of glucocorticoid receptor action promotes identification of novel ligands with an improved therapeutic index
    • Schäcke H., Rehwinkel H., Asadullah K., and Cato A.C. Insight into the molecular mechanisms of glucocorticoid receptor action promotes identification of novel ligands with an improved therapeutic index. Exp. Dermatol. 15 (2006) 565-573
    • (2006) Exp. Dermatol. , vol.15 , pp. 565-573
    • Schäcke, H.1    Rehwinkel, H.2    Asadullah, K.3    Cato, A.C.4
  • 128
    • 0028831128 scopus 로고
    • Characterization of mechanisms involved in transrepression of NF-kappa B by activated glucocorticoid receptors
    • Scheinman R.I., Gualberto A., Jewell C.M., Cidlowski J.A., and Baldwin Jr. A.S. Characterization of mechanisms involved in transrepression of NF-kappa B by activated glucocorticoid receptors. Mol. Cell. Biol. 15 (1995) 943-953
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 943-953
    • Scheinman, R.I.1    Gualberto, A.2    Jewell, C.M.3    Cidlowski, J.A.4    Baldwin Jr., A.S.5
  • 129
    • 0024744568 scopus 로고
    • Mutations in the glucocorticoid receptor zinc finger region that distinguish interdigitated DNA binding and transcriptional enhancement activities
    • Schena M., Freedman L.P., and Yamamoto K.R. Mutations in the glucocorticoid receptor zinc finger region that distinguish interdigitated DNA binding and transcriptional enhancement activities. Genes Dev. 3 (1989) 1590-1601
    • (1989) Genes Dev. , vol.3 , pp. 1590-1601
    • Schena, M.1    Freedman, L.P.2    Yamamoto, K.R.3
  • 132
    • 0026001070 scopus 로고
    • Cell-specific inhibitory and stimulatory effects of Fos and Jun on transcription activation by nuclear receptors
    • Shemshedini L., Knauthe R., Sassone-Corsi P., Pornon A., and Gronemeyer H. Cell-specific inhibitory and stimulatory effects of Fos and Jun on transcription activation by nuclear receptors. EMBO J. 10 (1991) 3839-3849
    • (1991) EMBO J. , vol.10 , pp. 3839-3849
    • Shemshedini, L.1    Knauthe, R.2    Sassone-Corsi, P.3    Pornon, A.4    Gronemeyer, H.5
  • 133
    • 0032491483 scopus 로고    scopus 로고
    • Nuclear integration of glucocorticoid receptor and nuclear factor-kappaB signaling by CREB-binding protein and steroid receptor coactivator-1
    • Sheppard K.A., Phelps K.M., Williams A.J., Thanos D., Glass C.K., Rosenfeld M.G., Gerritsen M.E., and Collins T. Nuclear integration of glucocorticoid receptor and nuclear factor-kappaB signaling by CREB-binding protein and steroid receptor coactivator-1. J. Biol. Chem. 273 (1998) 29291-29294
    • (1998) J. Biol. Chem. , vol.273 , pp. 29291-29294
    • Sheppard, K.A.1    Phelps, K.M.2    Williams, A.J.3    Thanos, D.4    Glass, C.K.5    Rosenfeld, M.G.6    Gerritsen, M.E.7    Collins, T.8
  • 134
    • 0036803602 scopus 로고    scopus 로고
    • In the cellular garden of forking paths: how p38 MAPKs signal for downstream assistance
    • Shi Y., and Gaestel M. In the cellular garden of forking paths: how p38 MAPKs signal for downstream assistance. Biol. Chem. 383 (2002) 1519-1536
    • (2002) Biol. Chem. , vol.383 , pp. 1519-1536
    • Shi, Y.1    Gaestel, M.2
  • 135
    • 33645667110 scopus 로고    scopus 로고
    • SWI/SNF: the crossroads where extracellular signaling pathways meet chromatin
    • Simone C. SWI/SNF: the crossroads where extracellular signaling pathways meet chromatin. J. Cell. Physiol. 207 (2006) 309-314
    • (2006) J. Cell. Physiol. , vol.207 , pp. 309-314
    • Simone, C.1
  • 136
    • 5444225805 scopus 로고    scopus 로고
    • Elongation by RNA polymerase II: the short and long of it
    • Sims III R.J., Belotserkovskaya R., and Reinberg D. Elongation by RNA polymerase II: the short and long of it. Genes Dev. 18 (2004) 2437-2468
    • (2004) Genes Dev. , vol.18 , pp. 2437-2468
    • Sims III, R.J.1    Belotserkovskaya, R.2    Reinberg, D.3
  • 137
    • 12544250379 scopus 로고    scopus 로고
    • Glucocorticoids inhibit the transcriptional activity of LEF/TCF in differentiating osteoblasts in a glycogen synthase kinase-3beta-dependent and -independent manner
    • Smith E., and Frenkel B. Glucocorticoids inhibit the transcriptional activity of LEF/TCF in differentiating osteoblasts in a glycogen synthase kinase-3beta-dependent and -independent manner. J. Biol. Chem. 280 (2005) 2388-2394
    • (2005) J. Biol. Chem. , vol.280 , pp. 2388-2394
    • Smith, E.1    Frenkel, B.2
  • 138
    • 0032742092 scopus 로고    scopus 로고
    • Glucocorticoid receptor inhibits transforming growth factor-beta signaling by directly targeting the transcriptional activation function of Smad3
    • Song C.Z., Tian X., and Gelehrter T.D. Glucocorticoid receptor inhibits transforming growth factor-beta signaling by directly targeting the transcriptional activation function of Smad3. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 11776-11781
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 11776-11781
    • Song, C.Z.1    Tian, X.2    Gelehrter, T.D.3
  • 139
    • 0026857927 scopus 로고
    • Mutual cross-interference between glucocorticoid receptor and CREB inhibits transactivation in placental cells
    • Stauber C., Altschmied J., Akerblom I.E., Marron J.L., and Mellon P.L. Mutual cross-interference between glucocorticoid receptor and CREB inhibits transactivation in placental cells. New Biol. 4 (1992) 527-540
    • (1992) New Biol. , vol.4 , pp. 527-540
    • Stauber, C.1    Altschmied, J.2    Akerblom, I.E.3    Marron, J.L.4    Mellon, P.L.5
  • 140
    • 0037621919 scopus 로고    scopus 로고
    • Dissociation of steroid receptor coactivator 1 and nuclear receptor corepressor recruitment to the human glucocorticoid receptor by modification of the ligand-receptor interface: the role of tyrosine 735
    • Stevens A., Garside H., Berry A., Waters C., White A., and Ray D. Dissociation of steroid receptor coactivator 1 and nuclear receptor corepressor recruitment to the human glucocorticoid receptor by modification of the ligand-receptor interface: the role of tyrosine 735. Mol. Endocrinol. 17 (2003) 845-859
    • (2003) Mol. Endocrinol. , vol.17 , pp. 845-859
    • Stevens, A.1    Garside, H.2    Berry, A.3    Waters, C.4    White, A.5    Ray, D.6
  • 141
    • 0029851231 scopus 로고    scopus 로고
    • Functional interactions between Stat5 and the glucocorticoid receptor
    • Stöcklin E., Wissler M., Gouilleux F., and Groner B. Functional interactions between Stat5 and the glucocorticoid receptor. Nature 383 (1996) 726-728
    • (1996) Nature , vol.383 , pp. 726-728
    • Stöcklin, E.1    Wissler, M.2    Gouilleux, F.3    Groner, B.4
  • 142
    • 0030868701 scopus 로고    scopus 로고
    • Specific DNA binding of Stat5, but not of glucocorticoid receptor, is required for their functional cooperation in the regulation of gene transcription
    • Stoecklin E., Wissler M., Moriggl R., and Groner B. Specific DNA binding of Stat5, but not of glucocorticoid receptor, is required for their functional cooperation in the regulation of gene transcription. Mol. Cell. Biol. 17 (1997) 6708-6716
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6708-6716
    • Stoecklin, E.1    Wissler, M.2    Moriggl, R.3    Groner, B.4
  • 143
    • 0025804498 scopus 로고
    • The glucocorticoid receptor binds to a sequence overlapping the TATA box of the human osteocalcin promoter: a potential mechanism for negative regulation
    • Strömstedt P.E., Poellinger L., Gustafsson J.A., and Carlstedt-Duke J. The glucocorticoid receptor binds to a sequence overlapping the TATA box of the human osteocalcin promoter: a potential mechanism for negative regulation. Mol. Cell. Biol. 11 (1991) 3379-3383
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3379-3383
    • Strömstedt, P.E.1    Poellinger, L.2    Gustafsson, J.A.3    Carlstedt-Duke, J.4
  • 144
    • 0032483406 scopus 로고    scopus 로고
    • Glucocorticoids repress transcription from a negative glucocorticoid response element recognized by two homeodomain-containing proteins, Pbx and Oct-1
    • Subramaniam N., Cairns W., and Okret S. Glucocorticoids repress transcription from a negative glucocorticoid response element recognized by two homeodomain-containing proteins, Pbx and Oct-1. J. Biol. Chem. 273 (1998) 23567-23574
    • (1998) J. Biol. Chem. , vol.273 , pp. 23567-23574
    • Subramaniam, N.1    Cairns, W.2    Okret, S.3
  • 145
    • 0030881742 scopus 로고    scopus 로고
    • Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) is required for lipopolysaccharide stimulation of tumor necrosis factor alpha (TNF-alpha) translation: glucocorticoids inhibit TNF-alpha translation by blocking JNK/SAPK
    • Swantek J.L., Cobb M.H., and Geppert T.D. Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) is required for lipopolysaccharide stimulation of tumor necrosis factor alpha (TNF-alpha) translation: glucocorticoids inhibit TNF-alpha translation by blocking JNK/SAPK. Mol. Cell. Biol. 17 (1997) 6274-6282
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6274-6282
    • Swantek, J.L.1    Cobb, M.H.2    Geppert, T.D.3
  • 146
    • 0031743573 scopus 로고    scopus 로고
    • Crosstalk between the interleukin-6 (IL-6)-JAK-STAT and the glucocorticoid-nuclear receptor pathway: synergistic activation of IL-6 response element by IL-6 and glucocorticoid
    • Takeda T., Kurachi H., Yamamoto T., Nishio Y., Nakatsuji Y., Morishige K., Miyake A., and Murata Y. Crosstalk between the interleukin-6 (IL-6)-JAK-STAT and the glucocorticoid-nuclear receptor pathway: synergistic activation of IL-6 response element by IL-6 and glucocorticoid. J. Endocrinol. 159 (1998) 323-330
    • (1998) J. Endocrinol. , vol.159 , pp. 323-330
    • Takeda, T.1    Kurachi, H.2    Yamamoto, T.3    Nishio, Y.4    Nakatsuji, Y.5    Morishige, K.6    Miyake, A.7    Murata, Y.8
  • 147
    • 0025827416 scopus 로고
    • Characterisation of functional inhibition of the glucocorticoid receptor by Fos/Jun
    • Touray M., Ryan F., Jaggi R., and Martin F. Characterisation of functional inhibition of the glucocorticoid receptor by Fos/Jun. Oncogene 6 (1991) 1227-1234
    • (1991) Oncogene , vol.6 , pp. 1227-1234
    • Touray, M.1    Ryan, F.2    Jaggi, R.3    Martin, F.4
  • 148
    • 18244397482 scopus 로고    scopus 로고
    • Molecular mechanisms of glucocorticoids in the control of inflammation and lymphocyte apoptosis
    • Tuckermann J.P., Kleiman A., McPherson K.G., and Reichardt H.M. Molecular mechanisms of glucocorticoids in the control of inflammation and lymphocyte apoptosis. Crit. Rev. Clin. Lab. Sci. 42 (2005) 71-104
    • (2005) Crit. Rev. Clin. Lab. Sci. , vol.42 , pp. 71-104
    • Tuckermann, J.P.1    Kleiman, A.2    McPherson, K.G.3    Reichardt, H.M.4
  • 150
    • 0033611050 scopus 로고    scopus 로고
    • The DNA binding-independent function of the glucocorticoid receptor mediates repression of AP-1-dependent genes in skin
    • Tuckermann J.P., Reichardt H.M., Arribas R., Richter K.H., Schutz G., and Angel P. The DNA binding-independent function of the glucocorticoid receptor mediates repression of AP-1-dependent genes in skin. J. Cell Biol. 147 (1999) 1365-1370
    • (1999) J. Cell Biol. , vol.147 , pp. 1365-1370
    • Tuckermann, J.P.1    Reichardt, H.M.2    Arribas, R.3    Richter, K.H.4    Schutz, G.5    Angel, P.6
  • 151
    • 0024337858 scopus 로고
    • Determinants of target gene specificity for steroid/thyroid hormone receptors
    • Umesono K., and Evans R.M. Determinants of target gene specificity for steroid/thyroid hormone receptors. Cell 57 (1989) 1139-1146
    • (1989) Cell , vol.57 , pp. 1139-1146
    • Umesono, K.1    Evans, R.M.2
  • 153
    • 0041813250 scopus 로고    scopus 로고
    • JNK phosphorylation relieves HDAC3-dependent suppression of the transcriptional activity of c-Jun
    • Weiss C., Schneider S., Wagner E.F., Zhang X., Seto E., and Bohmann D. JNK phosphorylation relieves HDAC3-dependent suppression of the transcriptional activity of c-Jun. EMBO J. 22 (2003) 3686-3695
    • (2003) EMBO J. , vol.22 , pp. 3686-3695
    • Weiss, C.1    Schneider, S.2    Wagner, E.F.3    Zhang, X.4    Seto, E.5    Bohmann, D.6
  • 154
    • 0025771222 scopus 로고
    • Interference and synergism of glucocorticoid receptor and octamer factors
    • Wieland S., Dobbeling U., and Rusconi S. Interference and synergism of glucocorticoid receptor and octamer factors. EMBO J. 10 (1991) 2513-2521
    • (1991) EMBO J. , vol.10 , pp. 2513-2521
    • Wieland, S.1    Dobbeling, U.2    Rusconi, S.3
  • 155
    • 0347065364 scopus 로고    scopus 로고
    • Interferon regulatory factor-3-mediated activation of the interferon-sensitive response element by Toll-like receptor (TLR) 4 but not TLR3 requires the p65 subunit of NF-κB
    • Wietek C., Miggin S.M., Jefferies C.A., and O'Neill L.A.J. Interferon regulatory factor-3-mediated activation of the interferon-sensitive response element by Toll-like receptor (TLR) 4 but not TLR3 requires the p65 subunit of NF-κB. J. Biol. Chem. 278 (2003) 50923-50931
    • (2003) J. Biol. Chem. , vol.278 , pp. 50923-50931
    • Wietek, C.1    Miggin, S.M.2    Jefferies, C.A.3    O'Neill, L.A.J.4
  • 156
    • 13544257114 scopus 로고    scopus 로고
    • Nuclear hormone receptor coregulator GRIP1 suppresses, whereas SRC1A and p/CIP coactivate, by domain-specific binding of MyoD
    • Wu H.-Y., Hamamori Y., Xu J., Chang S.C., Saluna T., Chang M.-F., O'Malley B.W., and Kedes L. Nuclear hormone receptor coregulator GRIP1 suppresses, whereas SRC1A and p/CIP coactivate, by domain-specific binding of MyoD. J. Biol. Chem. 280 (2005) 3129-3137
    • (2005) J. Biol. Chem. , vol.280 , pp. 3129-3137
    • Wu, H.-Y.1    Hamamori, Y.2    Xu, J.3    Chang, S.C.4    Saluna, T.5    Chang, M.-F.6    O'Malley, B.W.7    Kedes, L.8
  • 157
    • 0346656466 scopus 로고    scopus 로고
    • Repression of p65 transcriptional activation by the glucocorticoid receptor in the absence of receptor-coactivator interactions
    • Wu J., Li Y., Dietz J., and Lala D.S. Repression of p65 transcriptional activation by the glucocorticoid receptor in the absence of receptor-coactivator interactions. Mol. Endocrinol. 18 (2004) 53-62
    • (2004) Mol. Endocrinol. , vol.18 , pp. 53-62
    • Wu, J.1    Li, Y.2    Dietz, J.3    Lala, D.S.4
  • 158
    • 0033119162 scopus 로고    scopus 로고
    • Coactivator and corepressor complexes in nuclear receptor function
    • Xu L., Glass C.K., and Rosenfeld M.G. Coactivator and corepressor complexes in nuclear receptor function. Curr. Opin. Genet. Dev. 9 (1999) 140-147
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 140-147
    • Xu, L.1    Glass, C.K.2    Rosenfeld, M.G.3
  • 159
    • 0033625751 scopus 로고    scopus 로고
    • Interaction of the tau 2 transcriptional activation domain of glucocorticoid receptor with a novel steroid receptor coactivator, Hic-5, which localizes to both focal adhesions and the nuclear matrix
    • Yang L., Guerrero J., Hong H., DeFranco D.B., and Stallcup M.R. Interaction of the tau 2 transcriptional activation domain of glucocorticoid receptor with a novel steroid receptor coactivator, Hic-5, which localizes to both focal adhesions and the nuclear matrix. Mol. Biol. Cell 11 (2000) 2007-2018
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2007-2018
    • Yang, L.1    Guerrero, J.2    Hong, H.3    DeFranco, D.B.4    Stallcup, M.R.5
  • 160
    • 0025188132 scopus 로고
    • Transcriptional interference between c-Jun and the glucocorticoid receptor: mutual inhibition of DNA binding due to direct protein-protein interaction
    • Yang-Yen H.F., Chambard J.C., Sun Y.L., Smeal T., Schmidt T.J., Drouin J., and Karin M. Transcriptional interference between c-Jun and the glucocorticoid receptor: mutual inhibition of DNA binding due to direct protein-protein interaction. Cell 62 (1990) 1205-1215
    • (1990) Cell , vol.62 , pp. 1205-1215
    • Yang-Yen, H.F.1    Chambard, J.C.2    Sun, Y.L.3    Smeal, T.4    Schmidt, T.J.5    Drouin, J.6    Karin, M.7


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