메뉴 건너뛰기




Volumn 8, Issue 4, 2007, Pages 321-330

Glucocorticoid receptor physiology

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS RECEPTOR; GLUCOCORTICOID RECEPTOR; SILENCING MEDIATOR OF RETINOID AND THYROID HORMONE RECEPTOR; STEROID RECEPTOR;

EID: 38549122929     PISSN: 13899155     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11154-007-9059-8     Document Type: Review
Times cited : (186)

References (93)
  • 1
    • 3042589804 scopus 로고
    • On the mechanism of estrogen action
    • Jensen EV. On the mechanism of estrogen action. Perspect Biol Med 1962;6:47-59.
    • (1962) Perspect Biol Med , vol.6 , pp. 47-59
    • Jensen, E.V.1
  • 2
    • 38549155788 scopus 로고
    • Clinical effects of cortisone administered orally to 100 patients with rheumatoid arthritis
    • Ward E, Slocumb CH, Polley HF, Kendall EC, Hench PS. Clinical effects of cortisone administered orally to 100 patients with rheumatoid arthritis. Ann Rheum Dis 1951;10:477-84.
    • (1951) Ann Rheum Dis , vol.10 , pp. 477-484
    • Ward, E.1    Slocumb, C.H.2    Polley, H.F.3    Kendall, E.C.4    Hench, P.S.5
  • 3
    • 0014410108 scopus 로고
    • Specific and nonspecific physicochemical interactions of glucocorticoids and related steroids with rat thymus cells in vitro
    • Munck A, Brinck-Johnsen T. Specific and nonspecific physicochemical interactions of glucocorticoids and related steroids with rat thymus cells in vitro. J Biol Chem 1968;243:5556-65.
    • (1968) J Biol Chem , vol.243 , pp. 5556-5565
    • Munck, A.1    Brinck-Johnsen, T.2
  • 5
    • 0027529830 scopus 로고
    • Direct interaction of the tau 1 transactivation domain of the human glucocorticoid receptor with the basal transcriptional machinery
    • McEwan IJ, Wright AP, Dahlman-Wright K, Carlstedt-Duke J, Gustafsson JA. Direct interaction of the tau 1 transactivation domain of the human glucocorticoid receptor with the basal transcriptional machinery. Mol Cell Biol 1993;13:399-407.
    • (1993) Mol Cell Biol , vol.13 , pp. 399-407
    • McEwan, I.J.1    Wright, A.P.2    Dahlman-Wright, K.3    Carlstedt-Duke, J.4    Gustafsson, J.A.5
  • 7
    • 0027498883 scopus 로고
    • On the mechanism of DNA binding by nuclear hormone receptors: A structural and functional perspective
    • Freedman LP, Luisi BF. On the mechanism of DNA binding by nuclear hormone receptors: a structural and functional perspective. J Cell Biochem 1993;51:140-150.
    • (1993) J Cell Biochem , vol.51 , pp. 140-150
    • Freedman, L.P.1    Luisi, B.F.2
  • 8
    • 0028283503 scopus 로고
    • Molecular mechanisms of action of steroid/thyroid receptor superfamily members
    • Tsai MJ, O'Malley B. Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu Rev Biochem 1994;63:451-86.
    • (1994) Annu Rev Biochem , vol.63 , pp. 451-486
    • Tsai, M.J.1    O'Malley, B.2
  • 10
    • 0031778177 scopus 로고    scopus 로고
    • Basic guide to the mechanisms of antiestrogen action
    • MacGregor J, Jordan V. Basic guide to the mechanisms of antiestrogen action. Pharmacol Rev 1998;50:151-96.
    • (1998) Pharmacol Rev , vol.50 , pp. 151-196
    • MacGregor, J.1    Jordan, V.2
  • 11
    • 0034129679 scopus 로고    scopus 로고
    • Steroid hormone receptors: An update.
    • Beato M, Klug J. Steroid hormone receptors: an update. Hum Reprod Update 2000;6:225-36.
    • (2000) Hum Reprod Update , vol.6 , pp. 225-236
    • Beato, M.1    Klug, J.2
  • 12
    • 0031757167 scopus 로고    scopus 로고
    • Heat shock protein 90-dependent (geldanamycin-inhibited) movement of the glucocorticoid receptor through the cytoplasm to the nucleus requires intact cytoskeleton
    • Galigniana MD, Scruggs JL, Herrington J, Welsh MJ, Carter-Su C, Housley PR, Pratt WB. Heat shock protein 90-dependent (geldanamycin-inhibited) movement of the glucocorticoid receptor through the cytoplasm to the nucleus requires intact cytoskeleton. Mol Endocrinol 1998;12:1903-13.
    • (1998) Mol Endocrinol , vol.12 , pp. 1903-1913
    • Galigniana, M.D.1    Scruggs, J.L.2    Herrington, J.3    Welsh, M.J.4    Carter-Su, C.5    Housley, P.R.6    Pratt, W.B.7
  • 13
    • 0030026713 scopus 로고    scopus 로고
    • Molecular determinants of glucocorticoid receptor function and tissue sensitivity to glucocorticoids
    • Bamberger C, Schulte H, Chrousos G. Molecular determinants of glucocorticoid receptor function and tissue sensitivity to glucocorticoids. Endocr Rev 1996;17:245-61.
    • (1996) Endocr Rev , vol.17 , pp. 245-261
    • Bamberger, C.1    Schulte, H.2    Chrousos, G.3
  • 14
    • 0034130914 scopus 로고    scopus 로고
    • Molecular mechanisms of glucocorticoid action: What is important
    • Newton R. Molecular mechanisms of glucocorticoid action: what is important. Thorax 2000;55:603-13.
    • (2000) Thorax , vol.55 , pp. 603-613
    • Newton, R.1
  • 15
    • 0028913259 scopus 로고
    • Molecular genetic analysis of glucocorticoid signaling during mouse development
    • Cole T, Blendy J, Monaghan A, Schmid W, Aguzzi A, Schutz G. Molecular genetic analysis of glucocorticoid signaling during mouse development. Steroids 1995;60:93-6.
    • (1995) Steroids , vol.60 , pp. 93-96
    • Cole, T.1    Blendy, J.2    Monaghan, A.3    Schmid, W.4    Aguzzi, A.5    Schutz, G.6
  • 16
    • 0024545638 scopus 로고
    • Gene regulation by steroid hormones
    • Beato M. Gene regulation by steroid hormones. Cell 1989;56:335-44.
    • (1989) Cell , vol.56 , pp. 335-344
    • Beato, M.1
  • 18
    • 26944472106 scopus 로고    scopus 로고
    • Glucocorticoids: Effects on gene transcription
    • Adcock I, Ito K, Barnes P. Glucocorticoids: effects on gene transcription. Proc Am Thorac Soc 2004;1:247-54.
    • (2004) Proc Am Thorac Soc , vol.1 , pp. 247-254
    • Adcock, I.1    Ito, K.2    Barnes, P.3
  • 19
    • 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 TJ, 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;62:1205-15.
    • (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
  • 20
    • 4644263340 scopus 로고    scopus 로고
    • Effects of glucocorticoids on gene transcription
    • Hayashi R, Wada H, Ito K, Adcock I. Effects of glucocorticoids on gene transcription. Eur J Pharmacol 2004;500:51-62.
    • (2004) Eur J Pharmacol , vol.500 , pp. 51-62
    • Hayashi, R.1    Wada, H.2    Ito, K.3    Adcock, I.4
  • 21
    • 3142676411 scopus 로고    scopus 로고
    • Genetic dissection of corticosteroid receptor function in mice
    • Wintermantel T, Berger S, Greiner E, Schutz G. Genetic dissection of corticosteroid receptor function in mice. Horm Metab Res 2004;36:387-91.
    • (2004) Horm Metab Res , vol.36 , pp. 387-391
    • Wintermantel, T.1    Berger, S.2    Greiner, E.3    Schutz, G.4
  • 24
    • 0024384860 scopus 로고
    • Steroid binding activity is retained in a 16-kDa fragment of the steroid binding domain of rat glucocorticoid receptors
    • Simons SJ, Sistare F, Chakraborti P. Steroid binding activity is retained in a 16-kDa fragment of the steroid binding domain of rat glucocorticoid receptors. J Biol Chem 1989;264:14493-7.
    • (1989) J Biol Chem , vol.264 , pp. 14493-14497
    • Simons, S.J.1    Sistare, F.2    Chakraborti, P.3
  • 25
    • 0024567048 scopus 로고
    • Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor
    • Bresnick EH, Dalman FC, Sanchez ER, Pratt WB. Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor. J Biol Chem 1989;264:4992-7.
    • (1989) J Biol Chem , vol.264 , pp. 4992-4997
    • Bresnick, E.H.1    Dalman, F.C.2    Sanchez, E.R.3    Pratt, W.B.4
  • 26
    • 0030808079 scopus 로고    scopus 로고
    • Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus
    • Czar MJ, Galigniana MD, Silverstein AM, Pratt WB. Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus. Biochemistry 1997;36:7776-85.
    • (1997) Biochemistry , vol.36 , pp. 7776-7785
    • Czar, M.J.1    Galigniana, M.D.2    Silverstein, A.M.3    Pratt, W.B.4
  • 27
    • 0034463399 scopus 로고    scopus 로고
    • Molecular chaperone interactions with steroid receptors: An update
    • Cheung J, Smith D. Molecular chaperone interactions with steroid receptors: an update. Mol Endocrinol 2000;14:939-46.
    • (2000) Mol Endocrinol , vol.14 , pp. 939-946
    • Cheung, J.1    Smith, D.2
  • 28
    • 0029075280 scopus 로고
    • Binding of p23 and hsp90 during assembly with the progesterone receptor
    • Johnson JL, Toft DO. Binding of p23 and hsp90 during assembly with the progesterone receptor. Mol Endocrinol 1995;9:670-768.
    • (1995) Mol Endocrinol , vol.9 , pp. 670-768
    • Johnson, J.L.1    Toft, D.O.2
  • 29
    • 0037085381 scopus 로고    scopus 로고
    • A new first step in activation of steroid receptors: Hormone-induced switching of FKBP51 and FKBP52 immunophilins
    • Davies T, Ning Y, Sanchez E. A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins. J Biol Chem 2002;277:4597-600.
    • (2002) J Biol Chem , vol.277 , pp. 4597-4600
    • Davies, T.1    Ning, Y.2    Sanchez, E.3
  • 30
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt W, Toft D. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev 1997;18:306-60.
    • (1997) Endocr Rev , vol.18 , pp. 306-360
    • Pratt, W.1    Toft, D.2
  • 31
    • 3543037605 scopus 로고    scopus 로고
    • Tetratricopeptide repeat cochaperones in steroid receptor complexes
    • Smith D. Tetratricopeptide repeat cochaperones in steroid receptor complexes. Cell Stress Chaperones 2004;9:109-21.
    • (2004) Cell Stress Chaperones , vol.9 , pp. 109-121
    • Smith, D.1
  • 32
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • Glass CK, Rosenfeld MG. The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev 2000;14:121-41.
    • (2000) Genes Dev , vol.14 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 34
    • 2342447986 scopus 로고    scopus 로고
    • Importin 7 and importin alpha/importin beta are nuclear import receptors for the glucocorticoid receptor
    • Freedman ND, Yamamoto KR. Importin 7 and importin alpha/importin beta are nuclear import receptors for the glucocorticoid receptor. Mol Biol Cell 2004;15:2276-86.
    • (2004) Mol Biol Cell , vol.15 , pp. 2276-2286
    • Freedman, N.D.1    Yamamoto, K.R.2
  • 35
    • 0037643416 scopus 로고    scopus 로고
    • Molecular mechanisms of glucocorticoid action and resistance
    • Schaaf MJ, Cidlowski JA. Molecular mechanisms of glucocorticoid action and resistance. J Steroid Biochem Mol Biol 2002;83:37-48.
    • (2002) J Steroid Biochem Mol Biol , vol.83 , pp. 37-48
    • Schaaf, M.J.1    Cidlowski, J.A.2
  • 36
    • 0036231010 scopus 로고    scopus 로고
    • P38 Mitogen-activated protein kinase-induced glucocorticoid receptor phosphorylation reduces its activity: Role in steroid-insensitive asthma
    • Irusen E, Matthews JG, Takahashi A, Barnes PJ, Chung KF, Adcock IM. p38 Mitogen-activated protein kinase-induced glucocorticoid receptor phosphorylation reduces its activity: role in steroid-insensitive asthma. J Allergy Clin Immunol 2002;109:649-57.
    • (2002) J Allergy Clin Immunol , vol.109 , pp. 649-657
    • Irusen, E.1    Matthews, J.G.2    Takahashi, A.3    Barnes, P.J.4    Chung, K.F.5    Adcock, I.M.6
  • 37
    • 0016266063 scopus 로고
    • Receptors from glucocorticoid-sensitive lymphoma cells and two classes of insensitive clones: Physical and DNA-binding properties
    • Yamamoto KR, Stampfer MR, Tomkins GM. Receptors from glucocorticoid- sensitive lymphoma cells and two classes of insensitive clones: physical and DNA-binding properties. Proc Natl Acad Sci U S A 1974;71:3901-5.
    • (1974) Proc Natl Acad Sci U S a , vol.71 , pp. 3901-3905
    • Yamamoto, K.R.1    Stampfer, M.R.2    Tomkins, G.M.3
  • 38
    • 0036794281 scopus 로고    scopus 로고
    • Nuclear export of glucocorticoid receptor is enhanced by c-Jun N-terminal kinase-mediated phosphorylation
    • Itoh M, Adachi M, Yasui H, Takekawa M, Tanaka H, Imai K. Nuclear export of glucocorticoid receptor is enhanced by c-Jun N-terminal kinase-mediated phosphorylation. Mol Endocrinol 2002;16:2382-92.
    • (2002) Mol Endocrinol , vol.16 , pp. 2382-2392
    • Itoh, M.1    Adachi, M.2    Yasui, H.3    Takekawa, M.4    Tanaka, H.5    Imai, K.6
  • 39
    • 0036318571 scopus 로고    scopus 로고
    • Regulation of estrogen receptor nuclear export by ligand-induced and p38-mediated receptor phosphorylation
    • Lee H, Bai W. Regulation of estrogen receptor nuclear export by ligand-induced and p38-mediated receptor phosphorylation. Mol Cell Biol 2002;22:5835-45.
    • (2002) Mol Cell Biol , vol.22 , pp. 5835-5845
    • Lee, H.1    Bai, W.2
  • 41
    • 0034463835 scopus 로고    scopus 로고
    • Protracted nuclear export of glucocorticoid receptor limits its turnover and does not require the exportin 1/CRM1-directed nuclear export pathway
    • Liu J, DeFranco DB. Protracted nuclear export of glucocorticoid receptor limits its turnover and does not require the exportin 1/CRM1-directed nuclear export pathway. Mol Endocrinol 2000;14:40-51.
    • (2000) Mol Endocrinol , vol.14 , pp. 40-51
    • Liu, J.1    Defranco, D.B.2
  • 42
    • 0025159176 scopus 로고
    • A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis
    • Sikorski RS, Boguski MS, Goebl M, Hieter P. A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis. Cell 1990;60:307-17.
    • (1990) Cell , vol.60 , pp. 307-317
    • Sikorski, R.S.1    Boguski, M.S.2    Goebl, M.3    Hieter, P.4
  • 43
    • 0344496513 scopus 로고    scopus 로고
    • The tetratricopeptide repeat: A structural motif mediating protein-protein interactions
    • Blatch G, Lassle M. The tetratricopeptide repeat: a structural motif mediating protein-protein interactions. Bioessays 1999;21:932-9.
    • (1999) Bioessays , vol.21 , pp. 932-939
    • Blatch, G.1    Lassle, M.2
  • 44
    • 0021988845 scopus 로고
    • Development of a monoclonal antibody to the rabbit 8.5S uterin progestin receptor
    • Nakao K, Myers JE, Faber LE. Development of a monoclonal antibody to the rabbit 8.5S uterin progestin receptor. Can J Biochem Cell Biol 1984;63:33-40.
    • (1984) Can J Biochem Cell Biol , vol.63 , pp. 33-40
    • Nakao, K.1    Myers, J.E.2    Faber, L.E.3
  • 45
    • 0017086114 scopus 로고
    • Comparative study of in vitro and in vivo drug effects on cell-mediated cytotoxicity
    • Borel J. Comparative study of in vitro and in vivo drug effects on cell-mediated cytotoxicity. Immunology 1976;31:631-41.
    • (1976) Immunology , vol.31 , pp. 631-641
    • Borel, J.1
  • 50
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moarefi I. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 2000;101:199-210.
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 51
    • 3543037605 scopus 로고    scopus 로고
    • Tetratricopeptide repeat cochaperones in steroid receptor complexes
    • Smith DF. Tetratricopeptide repeat cochaperones in steroid receptor complexes. Cell Stress Chaperones 2004;9:109-21.
    • (2004) Cell Stress Chaperones , vol.9 , pp. 109-121
    • Smith, D.F.1
  • 52
    • 13544267438 scopus 로고    scopus 로고
    • Differential control of glucocorticoid receptor hormone-binding function by tetratricopeptide repeat (TPR) proteins and the immunosuppressive ligand FK506
    • Davies TH, Ning YM, Sanchez ER. Differential control of glucocorticoid receptor hormone-binding function by tetratricopeptide repeat (TPR) proteins and the immunosuppressive ligand FK506. Biochemistry 2005;44:2030-8.
    • (2005) Biochemistry , vol.44 , pp. 2030-2038
    • Davies, T.H.1    Ning, Y.M.2    Sanchez, E.R.3
  • 54
    • 0033601331 scopus 로고    scopus 로고
    • Different regions of the immunophilin FKBP52 determine its association with the glucocorticoid receptor, hsp90, and cytoplasmic dynein
    • Silverstein AM, Galigniana MD, Kanelakis KC, Radanyi C, Renoir JM, Pratt WB. Different regions of the immunophilin FKBP52 determine its association with the glucocorticoid receptor, hsp90, and cytoplasmic dynein. J Biol Chem 1999;274:36980-6.
    • (1999) J Biol Chem , vol.274 , pp. 36980-36986
    • Silverstein, A.M.1    Galigniana, M.D.2    Kanelakis, K.C.3    Radanyi, C.4    Renoir, J.M.5    Pratt, W.B.6
  • 55
    • 0035805599 scopus 로고    scopus 로고
    • Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus
    • Galigniana M, Radanyi C, Renoir J, Housley P, Pratt W. Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus. J Biol Chem 2001;276:14884-9.
    • (2001) J Biol Chem , vol.276 , pp. 14884-14889
    • Galigniana, M.1    Radanyi, C.2    Renoir, J.3    Housley, P.4    Pratt, W.5
  • 57
    • 18044366012 scopus 로고    scopus 로고
    • Mutations in squirrel monkey glucocorticoid receptor impair nuclear translocation
    • Her S, Patel P, Schatzberg A, Lyons D. Mutations in squirrel monkey glucocorticoid receptor impair nuclear translocation. J Steroid Biochem Mol Biol 2005;94:319-26.
    • (2005) J Steroid Biochem Mol Biol , vol.94 , pp. 319-326
    • Her, S.1    Patel, P.2    Schatzberg, A.3    Lyons, D.4
  • 58
    • 33746214633 scopus 로고    scopus 로고
    • Glucocorticoid resistance in squirrel monkeys results from a combination of a transcriptionally incompetent glucocorticoid receptor and overexpression of the glucocorticoid receptor co-chaperone FKBP51
    • Westberry J, Sadosky P, Hubler T, Gross K, Scammell J. Glucocorticoid resistance in squirrel monkeys results from a combination of a transcriptionally incompetent glucocorticoid receptor and overexpression of the glucocorticoid receptor co-chaperone FKBP51. J Steroid Biochem Mol Biol 2006;100:34-41.
    • (2006) J Steroid Biochem Mol Biol , vol.100 , pp. 34-41
    • Westberry, J.1    Sadosky, P.2    Hubler, T.3    Gross, K.4    Scammell, J.5
  • 59
    • 0033018628 scopus 로고    scopus 로고
    • Glucocorticoid resistance in the squirrel monkey is associated with overexpression of the immunophilin FKBP51
    • Reynolds PD, Ruan Y, Smith DF, Scammell JG. Glucocorticoid resistance in the squirrel monkey is associated with overexpression of the immunophilin FKBP51. J Clin Endocrinol Metab 1999;84:663-9.
    • (1999) J Clin Endocrinol Metab , vol.84 , pp. 663-669
    • Reynolds, P.D.1    Ruan, Y.2    Smith, D.F.3    Scammell, J.G.4
  • 60
    • 0028846193 scopus 로고
    • Sequence and characterization of a coactivator for the steroid hormone receptor superfamily
    • Onate SA, Tsai SY, Tsai MJ, O'Malley BW. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 1995;270:1354-7.
    • (1995) Science , vol.270 , pp. 1354-1357
    • Onate, S.A.1    Tsai, S.Y.2    Tsai, M.J.3    O'Malley, B.W.4
  • 61
    • 0033305547 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: Cellular and molecular biology
    • McKenna NJ, Lanz RB, O'Malley BW. Nuclear receptor coregulators: cellular and molecular biology. Endocr Rev 1999;20:321-44.
    • (1999) Endocr Rev , vol.20 , pp. 321-344
    • McKenna, N.J.1    Lanz, R.B.2    O'Malley, B.W.3
  • 62
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister AJ, Kouzarides T. The CBP co-activator is a histone acetyltransferase. Nature 1996;384:641-3.
    • (1996) Nature , vol.384 , pp. 641-543
    • Bannister, A.J.1    Kouzarides, T.2
  • 63
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 1996;87:953-9.
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 65
    • 0029904571 scopus 로고    scopus 로고
    • CREB-binding protein activates transcription through multiple domains
    • Swope DL, Mueller CL, Chrivia JC. CREB-binding protein activates transcription through multiple domains. J Biol Chem 1996;271:28138-45.
    • (1996) J Biol Chem , vol.271 , pp. 28138-28145
    • Swope, D.L.1    Mueller, C.L.2    Chrivia, J.C.3
  • 67
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery DM, Kalkhoven E, Hoare S, Parker MG. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 1997;387:733-6.
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 68
    • 0034612264 scopus 로고    scopus 로고
    • The steroid receptor coactivator SRC-3 (p/CIP/RAC3/AIB1/ACTR/TRAM-1) is required for normal growth, puberty, female reproductive function, and mammary gland development
    • Xu J, Liao L, Ning G, Yoshida-Komiya H, Deng C, O'Malley BW. The steroid receptor coactivator SRC-3 (p/CIP/RAC3/AIB1/ACTR/TRAM-1) is required for normal growth, puberty, female reproductive function, and mammary gland development. Proc Natl Acad Sci U S A 2000;97:6379-84.
    • (2000) Proc Natl Acad Sci U S a , vol.97 , pp. 6379-6384
    • Xu, J.1    Liao, L.2    Ning, G.3    Yoshida-Komiya, H.4    Deng, C.5    O'Malley, B.W.6
  • 69
    • 0036311892 scopus 로고    scopus 로고
    • The function of TIF2/GRIP1 in mouse reproduction is distinct from those of SRC-1 and p/CIP
    • Gehin M, Mark M, Dennefeld C, Dierich A, Gronemeyer H, Chambon P. The function of TIF2/GRIP1 in mouse reproduction is distinct from those of SRC-1 and p/CIP. Mol Cell Biol 2002;22:5923-37.
    • (2002) Mol Cell Biol , vol.22 , pp. 5923-5937
    • Gehin, M.1    Mark, M.2    Dennefeld, C.3    Dierich, A.4    Gronemeyer, H.5    Chambon, P.6
  • 70
    • 0032549744 scopus 로고    scopus 로고
    • Partial hormone resistance in mice with disruption of the steroid receptor coactivator-1 (SRC-1) gene
    • Xu J, Qiu Y, DeMayo FJ, Tsai SY, Tsai MJ, O'Malley BW. Partial hormone resistance in mice with disruption of the steroid receptor coactivator-1 (SRC-1) gene. Science 1998;279:1922-5.
    • (1998) Science , vol.279 , pp. 1922-1925
    • Xu, J.1    Qiu, Y.2    Demayo, F.J.3    Tsai, S.Y.4    Tsai, M.J.5    O'Malley, B.W.6
  • 71
    • 0032560555 scopus 로고    scopus 로고
    • Promotion of agonist activity of antiandrogens by the androgen receptor coactivator, ARA70, in human prostate cancer DU145 cells
    • Miyamoto H, Yeh S, Wilding G, Chang C. Promotion of agonist activity of antiandrogens by the androgen receptor coactivator, ARA70, in human prostate cancer DU145 cells. Proc Natl Acad Sci U S A 1998;95:7379-84.
    • (1998) Proc Natl Acad Sci U S a , vol.95 , pp. 7379-7384
    • Miyamoto, H.1    Yeh, S.2    Wilding, G.3    Chang, C.4
  • 72
    • 0033583033 scopus 로고    scopus 로고
    • Cloning and characterization of androgen receptor coactivator, ARA55, in human prostate
    • Fujimoto N, Yeh S, Kang HY, Inui S, Chang HC, Mizokami A, Chang C. Cloning and characterization of androgen receptor coactivator, ARA55, in human prostate. J Biol Chem 1999;274:8316-21.
    • (1999) J Biol Chem , vol.274 , pp. 8316-8321
    • Fujimoto, N.1    Yeh, S.2    Kang, H.Y.3    Inui, S.4    Chang, H.C.5    Mizokami, A.6    Chang, C.7
  • 73
    • 0033625751 scopus 로고    scopus 로고
    • Interaction of the tau2 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 DB, Stallcup MR. Interaction of the tau2 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 2000;11:2007-18.
    • (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
  • 74
    • 0018002388 scopus 로고
    • The possible influence of temporal factors in androgenic responsiveness of urogenital tissue recombinants from wild-type and androgen-insensitive (Tfm) mice
    • Cunha GR, Lung B. The possible influence of temporal factors in androgenic responsiveness of urogenital tissue recombinants from wild-type and androgen-insensitive (Tfm) mice. J Exp Zool 1978;205:181-93.
    • (1978) J Exp Zool , vol.205 , pp. 181-193
    • Cunha, G.R.1    Lung, B.2
  • 75
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • Chen JD, Evans RM. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 1995;377:454-7.
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 77
    • 85047682255 scopus 로고    scopus 로고
    • Direct interactions between corepressors and coactivators permit the integration of nuclear receptor-mediated repression and activation
    • Li X, Kimbrel EA, Kenan DJ, McDonnell DP. Direct interactions between corepressors and coactivators permit the integration of nuclear receptor-mediated repression and activation. Mol Endocrinol 2002;16:1482-91.
    • (2002) Mol Endocrinol , vol.16 , pp. 1482-1491
    • Li, X.1    Kimbrel, E.A.2    Kenan, D.J.3    McDonnell, D.P.4
  • 78
    • 2542486258 scopus 로고    scopus 로고
    • Equilibrium interactions of corepressors and coactivators with agonist and antagonist complexes of glucocorticoid receptors
    • Wang Q, Blackford JA Jr., Song LN, Huang Y, Cho S, Simons SS Jr. Equilibrium interactions of corepressors and coactivators with agonist and antagonist complexes of glucocorticoid receptors. Mol Endocrinol 2004;18:1376-95.
    • (2004) Mol Endocrinol , vol.18 , pp. 1376-1395
    • Wang, Q.1    Blackford Jr., J.A.2    Song, L.N.3    Huang, Y.4    Cho, S.5    Simons Jr., S.S.6
  • 79
    • 0033347396 scopus 로고    scopus 로고
    • Opposing effects of corepressor and coactivators in determining the dose-response curve of agonists, and residual agonist activity of antagonists, for glucocorticoid receptor-regulated gene expression
    • Szapary D, Huang Y, Simons SS Jr. Opposing effects of corepressor and coactivators in determining the dose-response curve of agonists, and residual agonist activity of antagonists, for glucocorticoid receptor-regulated gene expression. Mol Endocrinol 1999;13:2108-21.
    • (1999) Mol Endocrinol , vol.13 , pp. 2108-2121
    • Szapary, D.1    Huang, Y.2    Simons Jr., S.S.3
  • 80
    • 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 CK, Rose DW, Rosenfeld MG. A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors. Cell 2004;116:511-26.
    • (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
  • 81
    • 0034663815 scopus 로고    scopus 로고
    • Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3
    • Li J, Wang J, Nawaz Z, Liu JM, Qin J, Wong J. Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3. Embo J 2000;19:4342-50.
    • (2000) Embo J , vol.19 , pp. 4342-4350
    • Li, J.1    Wang, J.2    Nawaz, Z.3    Liu, J.M.4    Qin, J.5    Wong, J.6
  • 82
    • 0027067001 scopus 로고
    • Ligand-dependent down-regulation of stably transfected human glucocorticoid receptors is associated with the loss of functional glucocorticoid responsiveness
    • Bellingham DL, Sar M, Cidlowski JA. Ligand-dependent down-regulation of stably transfected human glucocorticoid receptors is associated with the loss of functional glucocorticoid responsiveness. Mol Endocrinol 1992;6:2090-102.
    • (1992) Mol Endocrinol , vol.6 , pp. 2090-2102
    • Bellingham, D.L.1    Sar, M.2    Cidlowski, J.A.3
  • 83
    • 0033559204 scopus 로고    scopus 로고
    • Glucocorticoid-induced cell death requires autoinduction of glucocorticoid receptor expression in human leukemic T cells
    • Ramdas J, Liu W, Harmon JM. Glucocorticoid-induced cell death requires autoinduction of glucocorticoid receptor expression in human leukemic T cells. Cancer Res 1999;59:1378-85.
    • (1999) Cancer Res , vol.59 , pp. 1378-1385
    • Ramdas, J.1    Liu, W.2    Harmon, J.M.3
  • 84
    • 0027266849 scopus 로고
    • Homologous down regulation of the glucocorticoid receptor: The molecular machinery
    • Oakley RH, Cidlowski JA. Homologous down regulation of the glucocorticoid receptor: the molecular machinery. Crit Rev Eukaryot Gene Expr 1993;3:63-88.
    • (1993) Crit Rev Eukaryot Gene Expr , vol.3 , pp. 63-88
    • Oakley, R.H.1    Cidlowski, J.A.2
  • 85
    • 0035900780 scopus 로고    scopus 로고
    • Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids
    • Wallace AD, Cidlowski JA. Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids. J Biol Chem 2001;276:42714-21.
    • (2001) J Biol Chem , vol.276 , pp. 42714-42721
    • Wallace, A.D.1    Cidlowski, J.A.2
  • 86
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges D, Zwickl P, Baumeister W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 1999;68:1015-68.
    • (1999) Annu Rev Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 87
    • 0034065822 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis: Biological regulation via destruction
    • Ciechanover A, Orian A, Schwartz AL. Ubiquitin-mediated proteolysis: biological regulation via destruction. Bioessays 2000;22:442-51.
    • (2000) Bioessays , vol.22 , pp. 442-451
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 88
    • 0035883863 scopus 로고    scopus 로고
    • Ligand-dependent interaction of the glucocorticoid receptor with p53 enhances their degradation by Hdm2
    • Sengupta S, Wasylyk B. Ligand-dependent interaction of the glucocorticoid receptor with p53 enhances their degradation by Hdm2. Genes Dev 2001;15:2367-80.
    • (2001) Genes Dev , vol.15 , pp. 2367-2380
    • Sengupta, S.1    Wasylyk, B.2
  • 89
    • 0041630956 scopus 로고    scopus 로고
    • Estrogen receptor-dependent proteasomal degradation of the glucocorticoid receptor is coupled to an increase in mdm2 protein expression
    • Kinyamu HK, Archer TK. Estrogen receptor-dependent proteasomal degradation of the glucocorticoid receptor is coupled to an increase in mdm2 protein expression. Mol Cell Biol 2003;23:5867-81.
    • (2003) Mol Cell Biol , vol.23 , pp. 5867-5881
    • Kinyamu, H.K.1    Archer, T.K.2
  • 91
    • 22344452512 scopus 로고    scopus 로고
    • Alternative effects of the ubiquitin-proteasome pathway on glucocorticoid receptor down-regulation and transactivation are mediated by CHIP, an E3 ligase
    • Wang X, DeFranco DB. Alternative effects of the ubiquitin-proteasome pathway on glucocorticoid receptor down-regulation and transactivation are mediated by CHIP, an E3 ligase. Mol Endocrinol 2005;19:1474-82.
    • (2005) Mol Endocrinol , vol.19 , pp. 1474-1482
    • Wang, X.1    Defranco, D.B.2
  • 92
    • 0036718782 scopus 로고    scopus 로고
    • Glucocorticoid receptors in hippocampal neurons that do not engage proteasomes escape from hormone-dependent down-regulation but maintain transactivation activity
    • Wang X, Pongrac JL, DeFranco DB. Glucocorticoid receptors in hippocampal neurons that do not engage proteasomes escape from hormone-dependent down-regulation but maintain transactivation activity. Mol Endocrinol 2002;16:1987-98.
    • (2002) Mol Endocrinol , vol.16 , pp. 1987-1998
    • Wang, X.1    Pongrac, J.L.2    Defranco, D.B.3
  • 93
    • 0034655758 scopus 로고    scopus 로고
    • Glucocorticoid receptor regulation in the rat embryo: A potential site for developmental toxicity
    • Ghosh B, Wood CR, Held GA, Abbott BD, Lau C. Glucocorticoid receptor regulation in the rat embryo: a potential site for developmental toxicity. Toxicol Appl Pharmacol 2000;164:221-9.
    • (2000) Toxicol Appl Pharmacol , vol.164 , pp. 221-229
    • Ghosh, B.1    Wood, C.R.2    Held, G.A.3    Abbott, B.D.4    Lau, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.