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Volumn 2, Issue 4, 2008, Pages 845-854

Differential regulation of the transcriptional activity of the glucocorticoid receptor through site-specific phosphorylation

Author keywords

Coactivators; Gene regulation; Glucocorticoid receptor; Phosphorylation; Transactivation activity

Indexed keywords


EID: 77952664545     PISSN: 11775475     EISSN: 11775491     Source Type: Journal    
DOI: 10.2147/btt.s3820     Document Type: Review
Times cited : (28)

References (112)
  • 1
    • 0029093343 scopus 로고
    • Role of acidic and phosphorylated residues in gene activation by the glucocorticoid receptor
    • Almlof T, Wright AP, Gustafsson JA. 1995. Role of acidic and phosphorylated residues in gene activation by the glucocorticoid receptor, J Biol Chem, 270:17535-40.
    • (1995) J Biol Chem , vol.270 , pp. 17535-17540
    • Almlof, T.1    Wright, A.P.2    Gustafsson, J.A.3
  • 2
    • 0024333396 scopus 로고
    • Phosphorylation of steroid receptors
    • Auricchio F. 1989. Phosphorylation of steroid receptors. J Steroid Biochem, 32:613-22.
    • (1989) J Steroid Biochem , vol.32 , pp. 613-622
    • Auricchio, F.1
  • 3
    • 0029173863 scopus 로고
    • Phosphorylation and steroid hormone action
    • Bai W, Weigel NL. 1995. Phosphorylation and steroid hormone action. Vit Hormones, 51:289-313.
    • (1995) Vit Hormones , vol.51 , pp. 289-313
    • Bai, W.1    Weigel, N.L.2
  • 4
    • 0344527724 scopus 로고    scopus 로고
    • Trimethylamine N-Oxide-induced cooperative folding of an intrinsically unfolded transcription-activating fragment of human glucocorticoid receptor
    • Baskakov IV, Kumar R, Srinivasan G, et al. 1999. Trimethylamine N-Oxide-induced cooperative folding of an intrinsically unfolded transcription-activating fragment of human glucocorticoid receptor. J Biol Chem, 274:10693-6.
    • (1999) J Biol Chem , vol.274 , pp. 10693-10696
    • Baskakov, I.V.1    Kumar, R.2    Srinivasan, G.3
  • 5
    • 0024545638 scopus 로고
    • Gene regulation by steroid hormones
    • Beato M. 1989. Gene regulation by steroid hormones. Cell, 56:335-4.
    • (1989) Cell , vol.56 , pp. 335-344
    • Beato, M.1
  • 6
    • 18444405534 scopus 로고    scopus 로고
    • Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition
    • Bledsoe RK, Montana VG, Stanley TB, et al. 2002. Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition. Cell, 110:93-105.
    • (2002) Cell , vol.110 , pp. 93-105
    • Bledsoe, R.K.1    Montana, V.G.2    Stanley, T.B.3
  • 8
    • 40849102229 scopus 로고    scopus 로고
    • Differential recruitment of glucocorticoid receptor phospho-isoforms to glucocorticoid-induced genes
    • Blind RD, Garabedian MJ. 2008. Differential recruitment of glucocorticoid receptor phospho-isoforms to glucocorticoid-induced genes. J Steroid Biochem Mol Biol, 109:150-7.
    • (2008) J Steroid Biochem Mol Biol , vol.109 , pp. 150-157
    • Blind, R.D.1    Garabedian, M.J.2
  • 9
    • 0024524385 scopus 로고
    • The contribution of the N-and C-terminal regions of steroid receptors to activation of transcription is both receptor and cell-specific
    • Bocquel MT, Kumar V, Stricker C, et al. 1989. The contribution of the N-and C-terminal regions of steroid receptors to activation of transcription is both receptor and cell-specific. Nucleic Acids Res, 17:2581-95.
    • (1989) Nucleic Acids Res , vol.17 , pp. 2581-2595
    • Bocquel, M.T.1    Kumar, V.2    Stricker, C.3
  • 10
    • 0032053218 scopus 로고    scopus 로고
    • Glucocorticoid receptor phosphorylation: Overview, function and cell cycle-dependence
    • Bodwell JE, Webster JC, Jewell CM, et al. 1998. Glucocorticoid receptor phosphorylation: overview, function and cell cycle-dependence. J Steroid Biochem Mol Biol, 65:91-9.
    • (1998) J Steroid Biochem Mol Biol , vol.65 , pp. 91-99
    • Bodwell, J.E.1    Webster, J.C.2    Jewell, C.M.3
  • 11
    • 0025775736 scopus 로고
    • Identification of phosphorylated sites in the mouse glucocorticoid receptor
    • Bodwell JE, Orti E, Coull JM, et al. 1991. Identification of phosphorylated sites in the mouse glucocorticoid receptor. J Biol Chem, 266:7549-55.
    • (1991) J Biol Chem , vol.266 , pp. 7549-7555
    • Bodwell, J.E.1    Orti, E.2    Coull, J.M.3
  • 12
    • 0037020186 scopus 로고    scopus 로고
    • TIF2 mediates the synergy between RARb1 activation functions AF-1 and AF-2
    • Bommer M, Benecke A, Gronemeyer H. 2002. TIF2 mediates the synergy between RARb1 activation functions AF-1 and AF-2. J Biol Chem, 277:37961-6.
    • (2002) J Biol Chem , vol.277 , pp. 37961-37966
    • Bommer, M.1    Benecke, A.2    Gronemeyer, H.3
  • 13
    • 0026029808 scopus 로고
    • Activation of protein kinas C decreases phosphorylation of c-jun at sites that negatively regulate its DNA-binding activity
    • Boyle WJ, Smeal T, Defize LHK, et al. 1991. Activation of protein kinas C decreases phosphorylation of c-jun at sites that negatively regulate its DNA-binding activity. Cell, 64:573-84.
    • (1991) Cell , vol.64 , pp. 573-584
    • Boyle, W.J.1    Smeal, T.2    Defize, L.H.K.3
  • 14
    • 0037809267 scopus 로고    scopus 로고
    • Sumoylation of the progesterone receptor and of the steroid receptor coactivator SRC-1
    • Chauchereau A, Amazit L, Quesne M. 2003. Sumoylation of the progesterone receptor and of the steroid receptor coactivator SRC-1. J Biol Chem, 278:12335-43.
    • (2003) J Biol Chem , vol.278 , pp. 12335-12343
    • Chauchereau, A.1    Amazit, L.2    Quesne, M.3
  • 15
    • 0033520325 scopus 로고    scopus 로고
    • Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase
    • Chen H, Lin RJ, Xie W, et al. 1999. Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. Cell, 98:675-86.
    • (1999) Cell , vol.98 , pp. 675-686
    • Chen, H.1    Lin, R.J.2    Xie, W.3
  • 16
    • 48249157970 scopus 로고    scopus 로고
    • Glucocorticoid receptor phosphorylation differentially affects target gene expression
    • 2008 May 15. [Epub ahead of print]
    • Chen W, Dang T, Blind RD, et al. 2008. Glucocorticoid receptor phosphorylation differentially affects target gene expression. Mol Endocrinol, 2008 May 15. [Epub ahead of print].
    • (2008) Mol Endocrinol
    • Chen, W.1    Dang, T.2    Blind, R.D.3
  • 17
    • 0037107417 scopus 로고    scopus 로고
    • Control of CBP co-activating activity by arginine methylation
    • Chevillard-Briet M, Trouche D, Vandel L. 2002. Control of CBP co-activating activity by arginine methylation. EMBO J, 21:5457-66.
    • (2002) EMBO J , vol.21 , pp. 5457-5466
    • Chevillard-Briet, M.1    Trouche, D.2    Vandel, L.3
  • 18
    • 0029149085 scopus 로고
    • Molecular and structural basis of target recognition by calmodulin
    • Crivici A, Ikura M. 1995. Molecular and structural basis of target recognition by calmodulin. Annu Rev Biophys Biomol Struct, 24:85-116.
    • (1995) Annu Rev Biophys Biomol Struct , vol.24 , pp. 85-116
    • Crivici, A.1    Ikura, M.2
  • 19
    • 0028925759 scopus 로고
    • Structural characterization of a minimal functional transactivation domain from the human glucocorticoid receptor
    • Dahlman-Wright K, Baumann H, McEwan IJ, et al. 1995. Structural characterization of a minimal functional transactivation domain from the human glucocorticoid receptor. Proc Natl Acad Sci U S A, 92:1699-703.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 1699-1703
    • Dahlman-Wright, K.1    Baumann, H.2    McEwan, I.J.3
  • 20
    • 0037085381 scopus 로고    scopus 로고
    • A new first step in activation of steroid receptors: Hormone-induced switching of FKBP51 and FKBP52 immunophilins
    • Davies TH, Ning YM, Sánchez ER. 2002. A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins. J Biol Chem, 277:4597-600.
    • (2002) J Biol Chem , vol.277 , pp. 4597-4600
    • Davies, T.H.1    Ning, Y.M.2    Sánchez, E.R.3
  • 21
    • 44649085082 scopus 로고    scopus 로고
    • Crosstalk of signaling pathways in the regulation of the glucocorticoid receptor function
    • Davies L, Karthikeyan N, Lynch JT, et al. 2008. Crosstalk of signaling pathways in the regulation of the glucocorticoid receptor function. Mol Endocrinol, 22:1331-44.
    • (2008) Mol Endocrinol , vol.22 , pp. 1331-1344
    • Davies, L.1    Karthikeyan, N.2    Lynch, J.T.3
  • 22
    • 0029994198 scopus 로고    scopus 로고
    • Ten years after: Reclassification of steroidresponsive genes
    • Dean DM, Sanders MM. 1996. Ten years after: reclassification of steroidresponsive genes. Mol Endocrinol, 10:1489-95.
    • (1996) Mol Endocrinol , vol.10 , pp. 1489-1495
    • Dean, D.M.1    Sanders, M.M.2
  • 23
    • 0026406078 scopus 로고
    • Protein phosphatase types 1 and/or 2A regulate nucleocytoplasmic shuttling of glucocorticoid receptors
    • DeFranco DB, Qi M, Borror KC, et al. 1991. Protein phosphatase types 1 and/or 2A regulate nucleocytoplasmic shuttling of glucocorticoid receptors. Mol Endocrinol, 5:1215-28.
    • (1991) Mol Endocrinol , vol.5 , pp. 1215-1228
    • DeFranco, D.B.1    Qi, M.2    Borror, K.C.3
  • 24
    • 33751000477 scopus 로고    scopus 로고
    • Multiple glucocorticoid receptor isoforms and mechanisms of post-translational modification
    • Duma D, Jewell CM, Cidlowski JA. 2006. Multiple glucocorticoid receptor isoforms and mechanisms of post-translational modification. J Steroid Biochem Mol Biol, 102:11-21.
    • (2006) J Steroid Biochem Mol Biol , vol.102 , pp. 11-21
    • Duma, D.1    Jewell, C.M.2    Cidlowski, J.A.3
  • 25
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson HJ, Wright PE. 2002. Coupling of folding and binding for unstructured proteins. Curr Opin Struct Biol, 12:54-60.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 26
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans RM. 1988. The steroid and thyroid hormone receptor superfamily. Science, 240:889-5.
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 27
    • 33750316364 scopus 로고    scopus 로고
    • Post-translational modifications of steroid receptors
    • Faus H, Haendler B. 2006. Post-translational modifications of steroid receptors. Biomed Pharmacother, 60:520-8.
    • (2006) Biomed Pharmacother , vol.60 , pp. 520-528
    • Faus, H.1    Haendler, B.2
  • 28
    • 0001392322 scopus 로고    scopus 로고
    • AIB1 is a conduit for kinase-mediated growth factor signaling to the estrogen receptor
    • Font de Mora J, Brown M. 2000. AIB1 is a conduit for kinase-mediated growth factor signaling to the estrogen receptor. Mol Cell Biol, 20:5041-7.
    • (2000) Mol Cell Biol , vol.20 , pp. 5041-5047
    • Font de Mora, J.1    Brown, M.2
  • 29
    • 0037698091 scopus 로고    scopus 로고
    • Full activation of estrogen receptor alpha activation function-1 induces proliferation of breast cancer cells
    • Fujita T, Kobayashi Y, Wada O, et al. 2003. Full activation of estrogen receptor alpha activation function-1 induces proliferation of breast cancer cells. J Biol Chem, 278:26704-14.
    • (2003) J Biol Chem , vol.278 , pp. 26704-26714
    • Fujita, T.1    Kobayashi, Y.2    Wada, O.3
  • 30
    • 0022453518 scopus 로고
    • Functional domains of the human glucocorticoid receptor
    • Giguere V, Hollenberg SM, Rosenfeld MG. 1986. Functional domains of the human glucocorticoid receptor. Cell, 46:545-52.
    • (1986) Cell , vol.46 , pp. 545-552
    • Giguere, V.1    Hollenberg, S.M.2    Rosenfeld, M.G.3
  • 31
    • 19044380048 scopus 로고    scopus 로고
    • Androgen receptor phosphorylation
    • Gioeli D, Ficarro SB, Kwiek JJ, et al. 2002. Androgen receptor phosphorylation. J Biol Chem, 32:29304-14.
    • (2002) J Biol Chem , vol.32 , pp. 29304-29314
    • Gioeli, D.1    Ficarro, S.B.2    Kwiek, J.J.3
  • 33
    • 0023150589 scopus 로고
    • Glucocorticoid receptor mutants that are constitutive activators of transcriptional enhancement
    • Godowski PJ, Rusconi S, Miesfeld R, et al. 1987. Glucocorticoid receptor mutants that are constitutive activators of transcriptional enhancement. Nature, 325:365-8.
    • (1987) Nature , vol.325 , pp. 365-368
    • Godowski, P.J.1    Rusconi, S.2    Miesfeld, R.3
  • 34
    • 0025335811 scopus 로고
    • Solution structure of the DNA binding domain of the glucocorticoid receptor
    • Hard T, Kellenbach E, Boelens R, et al. 1990. Solution structure of the DNA binding domain of the glucocorticoid receptor. Science, 249:157-60.
    • (1990) Science , vol.249 , pp. 157-160
    • Hard, T.1    Kellenbach, E.2    Boelens, R.3
  • 35
    • 0030980221 scopus 로고    scopus 로고
    • Role of Ada adapter complex in gene activation by the glucocorticoid receptor
    • Henriksson A, Almlof T, Ford J, et al. 1997. Role of Ada adapter complex in gene activation by the glucocorticoid receptor. Mol Cell Biol, 17:3065-73.
    • (1997) Mol Cell Biol , vol.17 , pp. 3065-3073
    • Henriksson, A.1    Almlof, T.2    Ford, J.3
  • 36
    • 0033214780 scopus 로고    scopus 로고
    • Differential regulation of glucocorticoid receptor transcriptional activation via AF-1-associated proteins
    • Hittelman AB, Burakov D, Iniguez-Lluhi JA. 1999. Differential regulation of glucocorticoid receptor transcriptional activation via AF-1-associated proteins. EMBO J, 18:5380-8.
    • (1999) EMBO J , vol.18 , pp. 5380-5388
    • Hittelman, A.B.1    Burakov, D.2    Iniguez-Lluhi, J.A.3
  • 37
    • 0023649571 scopus 로고
    • Colocalization of DNAbinding and transcriptional activation functions in the human glucocorticoid receptor
    • Hollenberg SM, Giguere V, Segui P, et al. 1987. Colocalization of DNAbinding and transcriptional activation functions in the human glucocorticoid receptor. Cell, 49:39-46.
    • (1987) Cell , vol.49 , pp. 39-46
    • Hollenberg, S.M.1    Giguere, V.2    Segui, P.3
  • 38
    • 0029740105 scopus 로고    scopus 로고
    • Nuclear receptor coactivators and corepressors
    • Horwitz KB, Jackson TA, Bain DL, et al. 1996. Nuclear receptor coactivators and corepressors. Mol Endocrinol, 10:1167-77.
    • (1996) Mol Endocrinol , vol.10 , pp. 1167-1177
    • Horwitz, K.B.1    Jackson, T.A.2    Bain, D.L.3
  • 39
    • 0022407992 scopus 로고
    • The molybdatestabilized L-cell glucocorticoid receptor isolated by affinity chromatography or with a monoclonal antibody is associated with a 90-92-kDa nonsteroid-binding phosphoprotein
    • Housley PR, Sanchez ER, Westphal HM, et al. 1985. The molybdatestabilized L-cell glucocorticoid receptor isolated by affinity chromatography or with a monoclonal antibody is associated with a 90-92-kDa nonsteroid-binding phosphoprotein. J Biol Chem, 260:13810-17.
    • (1985) J Biol Chem , vol.260 , pp. 13810-13817
    • Housley, P.R.1    Sanchez, E.R.2    Westphal, H.M.3
  • 40
    • 0036408751 scopus 로고    scopus 로고
    • Intrinsic disorder in cell-signaling and cancer-associated proteins
    • Iakoucheva LM, Brown CJ, Lawson JD, et al. 2002. Intrinsic disorder in cell-signaling and cancer-associated proteins. J Mol Biol, 323:573-84.
    • (2002) J Mol Biol , vol.323 , pp. 573-584
    • Iakoucheva, L.M.1    Brown, C.J.2    Lawson, J.D.3
  • 41
    • 0030669765 scopus 로고    scopus 로고
    • Interaction between the amino-and carboxy-terminal regions of the rat androgen receptor modulates transcriptional activity and is influenced by nuclear receptor coactivators
    • Ikonen T, Palvimo JJ, Janne OA. 1997. Interaction between the amino-and carboxy-terminal regions of the rat androgen receptor modulates transcriptional activity and is influenced by nuclear receptor coactivators. J Biol Chem, 272:29821-8.
    • (1997) J Biol Chem , vol.272 , pp. 29821-29828
    • Ikonen, T.1    Palvimo, J.J.2    Janne, O.A.3
  • 42
    • 3042788350 scopus 로고    scopus 로고
    • Modulation of glucocorticoid receptor function via phosphorylation
    • Ismaili N, Garabedian MJ. 2004. Modulation of glucocorticoid receptor function via phosphorylation. Ann NY Acad Sci, 1024:86-101.
    • (2004) Ann NY Acad Sci , vol.1024 , pp. 86-101
    • Ismaili, N.1    Garabedian, M.J.2
  • 43
    • 15744388262 scopus 로고    scopus 로고
    • Stabilization of the unliganded glucocorticoid receptor by TSG101
    • Ismaili N, Blind R, Garabedian MJ. 2005. Stabilization of the unliganded glucocorticoid receptor by TSG101. J Biol Chem, 280:11120-6.
    • (2005) J Biol Chem , vol.280 , pp. 11120-11126
    • Ismaili, N.1    Blind, R.2    Garabedian, M.J.3
  • 44
    • 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, et al. 2006. Histone deacetylase 2-mediated deacetylation of the glucocorticoid receptor enables NF-kappaB suppression. J Exp Med, 203:7-13.
    • (2006) J Exp Med , vol.203 , pp. 7-13
    • Ito, K.1    Yamamura, S.2    Essilfie-Quaye, S.3
  • 45
    • 0031945458 scopus 로고    scopus 로고
    • Cell cycle regulation and apoptosis
    • King KL, Cidlowski JA. 1998. Cell cycle regulation and apoptosis. Annu Rev Physiol, 60:601-17.
    • (1998) Annu Rev Physiol , vol.60 , pp. 601-617
    • King, K.L.1    Cidlowski, J.A.2
  • 46
    • 34347255773 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 differentially regulates the transcriptional activity of the glucocorticoid receptor through phosphorylation: Clinical implications for the nervous system response to glucocorticoids and stress
    • Kino T, Ichijo T, Amin ND, et al. 2007. Cyclin-dependent kinase 5 differentially regulates the transcriptional activity of the glucocorticoid receptor through phosphorylation: Clinical implications for the nervous system response to glucocorticoids and stress. Mol Endocrinol, 21:1552-68.
    • (2007) Mol Endocrinol , vol.21 , pp. 1552-1568
    • Kino, T.1    Ichijo, T.2    Amin, N.D.3
  • 47
    • 17844365062 scopus 로고    scopus 로고
    • Linking the ubiquitin-proteasome pathway to chromatin remodeling/modification by nuclear receptors
    • Kinyamu HK, Chen J, Archer TK. 2005. Linking the ubiquitin-proteasome pathway to chromatin remodeling/modification by nuclear receptors, J Mol Endocrinol, 34:281-97.
    • (2005) J Mol Endocrinol , vol.34 , pp. 281-297
    • Kinyamu, H.K.1    Chen, J.2    Archer, T.K.3
  • 48
    • 0037119457 scopus 로고    scopus 로고
    • The nuclear receptor interaction domain of GRIP1 is modulated by covalent attachment of SUMO-1
    • Kotaja N, Karvonen U, Janne OA, et al. 2002. The nuclear receptor interaction domain of GRIP1 is modulated by covalent attachment of SUMO-1. J Biol Chem, 277:30283-8.
    • (2002) J Biol Chem , vol.277 , pp. 30283-30288
    • Kotaja, N.1    Karvonen, U.2    Janne, O.A.3
  • 49
    • 0030998260 scopus 로고    scopus 로고
    • Mitogen-activated and cyclin-dependent protein kinases selectively and differentially modulate transcriptional enhancement by the glucocorticoid receptor
    • Krstic MD, Rogatsky I, Yamamoto KR, et al. 1997. Mitogen-activated and cyclin-dependent protein kinases selectively and differentially modulate transcriptional enhancement by the glucocorticoid receptor, Mol Cell Biol, 17:3947-54.
    • (1997) Mol Cell Biol , vol.17 , pp. 3947-3954
    • Krstic, M.D.1    Rogatsky, I.2    Yamamoto, K.R.3
  • 50
    • 0028331871 scopus 로고
    • Steroid hormone receptor phosphorylation: Is there a physiological role?
    • Kuiper G, Brinkmann AO. 1994. Steroid hormone receptor phosphorylation: is there a physiological role? Mol Cell Endocrinol, 100:103-7.
    • (1994) Mol Cell Endocrinol , vol.100 , pp. 103-107
    • Kuiper, G.1    Brinkmann, A.O.2
  • 51
    • 0033054115 scopus 로고    scopus 로고
    • Structure and functions of the nuclear hormone receptors
    • Kumar R, Thompson EB. 1999a. Structure and functions of the nuclear hormone receptors. Steroids, 64:310-19.
    • (1999) Steroids , vol.64 , pp. 310-319
    • Kumar, R.1    Thompson, E.B.2
  • 52
    • 0033609855 scopus 로고    scopus 로고
    • Interdomain signaling in a two-domain fragment of human glucocorticoid receptor
    • Kumar R, Baskakov IV, Srinivasan G, et al. 1999b. Interdomain signaling in a two-domain fragment of human glucocorticoid receptor. J Biol Chem, 274:24737-41.
    • (1999) J Biol Chem , vol.274 , pp. 24737-24741
    • Kumar, R.1    Baskakov, I.V.2    Srinivasan, G.3
  • 53
    • 0037245786 scopus 로고    scopus 로고
    • Transactivation functions of the N-terminal domains of nuclear hormone receptors: Protein folding and coactivator interactions
    • Kumar R, Thompson EB. 2003. Transactivation functions of the N-terminal domains of nuclear hormone receptors: Protein folding and coactivator interactions. Mol Endocrinol, 17:1-10.
    • (2003) Mol Endocrinol , vol.17 , pp. 1-10
    • Kumar, R.1    Thompson, E.B.2
  • 54
    • 3142716735 scopus 로고    scopus 로고
    • Overview of the structural basis for transcription regulation by nuclear hormone receptors
    • Kumar R, Johnson BH, Thompson EB. 2004a. Overview of the structural basis for transcription regulation by nuclear hormone receptors. Essay Biochem, 40:27-39.
    • (2004) Essay Biochem , vol.40 , pp. 27-39
    • Kumar, R.1    Johnson, B.H.2    Thompson, E.B.3
  • 55
    • 9344227341 scopus 로고    scopus 로고
    • TBP binding induces structure in the recombinant glucocorticoid receptor AF1 domain
    • Kumar R, Volk DE, Li J, et al. 2004b. TBP binding induces structure in the recombinant glucocorticoid receptor AF1 domain. Proc Natl Acad Sci U S A, 101:16425-30.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 16425-16430
    • Kumar, R.1    Volk, D.E.2    Li, J.3
  • 56
    • 0036721526 scopus 로고    scopus 로고
    • Potentiation of glucocorticoid receptor transcriptional activity by sumoylation
    • Le Drean Y, Mincheneau N, Le Goff P, et al. 2002. Potentiation of glucocorticoid receptor transcriptional activity by sumoylation. Endocrinology, 143:3482-9.
    • (2002) Endocrinology , vol.143 , pp. 3482-3489
    • le Drean, Y.1    Mincheneau, N.2    le Goff, P.3
  • 57
    • 0032580207 scopus 로고    scopus 로고
    • Allosteric effects of DNA on transcriptional regulators
    • Lefstin JA, Yamamoto KR. 1998. Allosteric effects of DNA on transcriptional regulators. Nature, 392:885-8.
    • (1998) Nature , vol.392 , pp. 885-888
    • Lefstin, J.A.1    Yamamoto, K.R.2
  • 58
    • 33744961763 scopus 로고    scopus 로고
    • Intrinsic disorder in transcription factors
    • Liu J, Perumal NB, Oldfield CJ, et al. 2006. Intrinsic disorder in transcription factors. Biochem, 45:6873-88.
    • (2006) Biochem , vol.45 , pp. 6873-6888
    • Liu, J.1    Perumal, N.B.2    Oldfield, C.J.3
  • 59
    • 0025780755 scopus 로고
    • Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA
    • Luisi BF, Xu WX, Otwinowski Z, et al. 1991. Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA. Nature, 352:497-505.
    • (1991) Nature , vol.352 , pp. 497-505
    • Luisi, B.F.1    Xu, W.X.2    Otwinowski, Z.3
  • 60
    • 0035933737 scopus 로고    scopus 로고
    • Growth factors signal to steroid receptors through mitogen-activated protein kinase regulation of p160 coactivator activity
    • Lopez GN, Turck CW, Schaufele F, et al. 2001. Growth factors signal to steroid receptors through mitogen-activated protein kinase regulation of p160 coactivator activity. J Biol Chem, 276:22177-82.
    • (2001) J Biol Chem , vol.276 , pp. 22177-22182
    • Lopez, G.N.1    Turck, C.W.2    Schaufele, F.3
  • 61
    • 12244256087 scopus 로고    scopus 로고
    • A novel estrogen receptor alphaassociated protein, template-activating factor Ibeta, inhibits acetylation and transactivation
    • Loven AM, Muster N, Yates JR, et al. 2003. A novel estrogen receptor alphaassociated protein, template-activating factor Ibeta, inhibits acetylation and transactivation. Mol Endocrinol, 17:67-78.
    • (2003) Mol Endocrinol , vol.17 , pp. 67-78
    • Loven, A.M.1    Muster, N.2    Yates, J.R.3
  • 62
    • 0027377597 scopus 로고
    • Site-directed mutagenesis of the phosphorylation sites in the mouse glucocorticoid receptor
    • Mason SA, Housley PR. 1993. Site-directed mutagenesis of the phosphorylation sites in the mouse glucocorticoid receptor, J Biol Chem, 268:21501-4.
    • (1993) J Biol Chem , vol.268 , pp. 21501-21504
    • Mason, S.A.1    Housley, P.R.2
  • 63
    • 0033305547 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: Cellular and molecular biology
    • McKenna NJ, Lanz RB, O'Malley BW. 1999. Nuclear receptor coregulators: cellular and molecular biology. Endocrine Rev, 20:321-44.
    • (1999) Endocrine Rev , vol.20 , pp. 321-344
    • McKenna, N.J.1    Lanz, R.B.2    O'Malley, B.W.3
  • 64
    • 18144387385 scopus 로고    scopus 로고
    • Mechanism of hormone action
    • In: Griffin JE, Ojeda SR (Eds), (5th ed). New York: Oxford University Press
    • Mendelson CR. 2004. Mechanism of hormone action. In: Griffin JE, Ojeda SR (Eds). Text Book of Endocrine Physiology (5th ed). New York: Oxford University Press, pp. 49-88.
    • (2004) Text Book of Endocrine Physiology , pp. 49-88
    • Mendelson, C.R.1
  • 65
    • 0034740164 scopus 로고    scopus 로고
    • Synergism between ERMMtransactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: Requirement for the AF-1 1-helical core and for a direct interaction between the N-and C-terminal domains
    • Metivier R, Penot G, Flouriot G. 2001. Synergism between ERMMtransactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: requirement for the AF-1 1-helical core and for a direct interaction between the N-and C-terminal domains. Mol Endocrinol, 15:1953-70.
    • (2001) Mol Endocrinol , vol.15 , pp. 1953-1970
    • Metivier, R.1    Penot, G.2    Flouriot, G.3
  • 66
    • 0023235562 scopus 로고
    • Glucocorticoid receptor mutants that define a small region sufficient for enhancer activation
    • Miesfeld R, Godowski PJ, Maler BA, et al. 1987. Glucocorticoid receptor mutants that define a small region sufficient for enhancer activation. Science, 236:423-7.
    • (1987) Science , vol.236 , pp. 423-427
    • Miesfeld, R.1    Godowski, P.J.2    Maler, B.A.3
  • 67
    • 22344458207 scopus 로고    scopus 로고
    • p38 MAP kinase is a key mediator in glucocorticoid-induced apoptosis of lymphoid cells: Correlation between p38 MAPK activation and site-specific phosphorylation of the human glucocorticoid receptor at serine 211
    • Milller AL, Webb MS, Copik AJ, et al. 2005. p38 MAP kinase is a key mediator in glucocorticoid-induced apoptosis of lymphoid cells: Correlation between p38 MAPK activation and site-specific phosphorylation of the human glucocorticoid receptor at serine 211. Mol Endocrinol, 19:1569-83.
    • (2005) Mol Endocrinol , vol.19 , pp. 1569-1583
    • Milller, A.L.1    Webb, M.S.2    Copik, A.J.3
  • 68
    • 1342294313 scopus 로고    scopus 로고
    • The Hsp90 cochaperone p23 is the limiting component of the multiprotein Hsp90/ Hsp70-based chaperone system in vivo where it acts to stabilize the client protein Hsp90 complex
    • Morishima Y, Kanelakis KC, Murphy PJM, et al. 2003. The Hsp90 cochaperone p23 is the limiting component of the multiprotein Hsp90/ Hsp70-based chaperone system in vivo where it acts to stabilize the client protein Hsp90 complex, J Biol Chem, 278:48754-63.
    • (2003) J Biol Chem , vol.278 , pp. 48754-48763
    • Morishima, Y.1    Kanelakis, K.C.2    Murphy, P.J.M.3
  • 69
    • 0035131438 scopus 로고    scopus 로고
    • Roles of partly unfolded conformations in macromolecular self-assembly
    • Namba K. 2001. Roles of partly unfolded conformations in macromolecular self-assembly. Genes Cells, 6:1-12.
    • (2001) Genes Cells , vol.6 , pp. 1-12
    • Namba, K.1
  • 70
    • 0026714673 scopus 로고
    • Phosphorylation of CREB affects its binding to high and low affinity sites: Implications for cAMP induced gene transcription
    • Nichols M, Weih F, Schmid W, et al. 1992. Phosphorylation of CREB affects its binding to high and low affinity sites: implications for cAMP induced gene transcription. EMBO J, 11:3337-46.
    • (1992) EMBO J , vol.11 , pp. 3337-3346
    • Nichols, M.1    Weih, F.2    Schmid, W.3
  • 71
    • 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 RM, Yamamoto KR. 2000. The glucocorticoid receptor inhibits NFkappaB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain, Genes Dev, 14:2314-29.
    • (2000) Genes Dev , vol.14 , pp. 2314-2329
    • Nissen, R.M.1    Yamamoto, K.R.2
  • 72
    • 0026597699 scopus 로고
    • Phosphorylation of steroid hormone receptors
    • Orti E, Bodwell JE, Munck A. 1992. Phosphorylation of steroid hormone receptors. Endocri Rev, 13:105-28.
    • (1992) Endocri Rev , vol.13 , pp. 105-128
    • Orti, E.1    Bodwell, J.E.2    Munck, A.3
  • 73
    • 0024817032 scopus 로고
    • A dynamic model for glucocorticoid receptor phosphorylation and cycling in insect cells
    • Orti E, Mendel DB, Smith LI, et al. 1989. A dynamic model for glucocorticoid receptor phosphorylation and cycling in insect cells. J Steroid Biochem, 34:85-96.
    • (1989) J Steroid Biochem , vol.34 , pp. 85-96
    • Orti, E.1    Mendel, D.B.2    Smith, L.I.3
  • 74
    • 1542284574 scopus 로고    scopus 로고
    • Three cyclin-dependent kinases preferentially phosphorylate different parts of C-terminal domain of the large subunit of RNA polymerase II
    • Pinhero R, Liaw P, Bertens K. 2004. Three cyclin-dependent kinases preferentially phosphorylate different parts of C-terminal domain of the large subunit of RNA polymerase II. Euro J Biochem, 271:1004-14.
    • (2004) Euro J Biochem , vol.271 , pp. 1004-1014
    • Pinhero, R.1    Liaw, P.2    Bertens, K.3
  • 75
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt WB, Toft DO. 1997. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endo Rev, 18:306-60.
    • (1997) Endo Rev , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 76
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt WB, Toft DO. 2003. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery, Exp Biol Med, 228:111-33.
    • (2003) Exp Biol Med , vol.228 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 77
    • 18244399631 scopus 로고    scopus 로고
    • Cytokine stimulation of energy expenditure through p38 MAP kinase activation of PPAReecoactivator-1
    • Puigserver P, Rhee J, Lin J, et al. 2001. Cytokine stimulation of energy expenditure through p38 MAP kinase activation of PPAReecoactivator-1. Mol Cell, 8:971-82.
    • (2001) Mol Cell , vol.8 , pp. 971-982
    • Puigserver, P.1    Rhee, J.2    Lin, J.3
  • 78
    • 0345564849 scopus 로고    scopus 로고
    • Target-specific utilization of transcriptional regulatory surfaces by the glucocorticoid receptor
    • Rogatsky I, Wang JC, Derynck MK, et al. 2003. Target-specific utilization of transcriptional regulatory surfaces by the glucocorticoid receptor, Proc Natl Acad Sci U S A, 100:13845-50.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 13845-13850
    • Rogatsky, I.1    Wang, J.C.2    Derynck, M.K.3
  • 79
    • 0032486406 scopus 로고    scopus 로고
    • Phosphorylation and inhibition of rat glucocorticoid receptor transcriptional activation by glycogen synthase kinase-3 (GSK-3). Species-specific differences between human and rat glucocorticoid receptor signaling as revealed through GSK-3 phosphorylation
    • Rogatsky I, Waase CL, Garabedian MJ. 1998a. Phosphorylation and inhibition of rat glucocorticoid receptor transcriptional activation by glycogen synthase kinase-3 (GSK-3). Species-specific differences between human and rat glucocorticoid receptor signaling as revealed through GSK-3 phosphorylation. J Biol Chem, 273:14315-21.
    • (1998) J Biol Chem , vol.273 , pp. 14315-14321
    • Rogatsky, I.1    Waase, C.L.2    Garabedian, M.J.3
  • 80
    • 0032478254 scopus 로고    scopus 로고
    • Antagonism of glucocorticoid receptor transcriptional activation by the c-Jun N-terminal kinase
    • Rogatsky I, Logan SK, Garabedian MJ. 1998b. Antagonism of glucocorticoid receptor transcriptional activation by the c-Jun N-terminal kinase. Proc Natl Acad Sci U S A, 95:2050-5.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 2050-2055
    • Rogatsky, I.1    Logan, S.K.2    Garabedian, M.J.3
  • 81
    • 0030974158 scopus 로고    scopus 로고
    • Glucocorticoid receptor-mediated cell cycle arrest is achieved through distinct cell-specific transcriptional regulatory mechanisms
    • Rogatsky I, Trowbridge JM, Garabedian MJ. 1997. Glucocorticoid receptor-mediated cell cycle arrest is achieved through distinct cell-specific transcriptional regulatory mechanisms. Mol Cell Biol, 17:3181-93.
    • (1997) Mol Cell Biol , vol.17 , pp. 3181-3193
    • Rogatsky, I.1    Trowbridge, J.M.2    Garabedian, M.J.3
  • 82
    • 22744437069 scopus 로고    scopus 로고
    • Natively disordered proteins: Functions and predictions
    • Romero P, Obradovic Z, Dunker AK. 2004. Natively disordered proteins: functions and predictions. Appl Bioinformatics, 3:105-13.
    • (2004) Appl Bioinformatics , vol.3 , pp. 105-113
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 83
    • 0034635553 scopus 로고    scopus 로고
    • Phosphorylation of steroid receptor coactivator-1. Identification of phosphorylation sites and phosphorylation through the mitogen-activated protein kinase pathway
    • Rowan BG, Weigel NL, O'Malley BW. 2000a. Phosphorylation of steroid receptor coactivator-1. Identification of phosphorylation sites and phosphorylation through the mitogen-activated protein kinase pathway. J Biol Chem, 275:4475-83.
    • (2000) J Biol Chem , vol.275 , pp. 4475-4483
    • Rowan, B.G.1    Weigel, N.L.2    O'Malley, B.W.3
  • 84
    • 0034460313 scopus 로고    scopus 로고
    • 8-Bromo-cyclic AMP induces phosphorylation of two sites in SRC-1 that facilitate ligand-independent activation of the chicken progesterone receptor and are critical for functional cooperation between SRC-1 and CREB binding protein
    • Rowan BG, Garrison N, Weigel NL, et al. 2000b. 8-Bromo-cyclic AMP induces phosphorylation of two sites in SRC-1 that facilitate ligand-independent activation of the chicken progesterone receptor and are critical for functional cooperation between SRC-1 and CREB binding protein. Mol Cell Biol, 20:8720-30.
    • (2000) Mol Cell Biol , vol.20 , pp. 8720-8730
    • Rowan, B.G.1    Garrison, N.2    Weigel, N.L.3
  • 85
    • 0023664416 scopus 로고
    • Relationship of the 90 kDa murine heat shock protein with the untransformed and transformed states of the cell glucocorticoid receptor
    • Sanchez ER, Meshinchi S, Tienrungroz W, et al. 1987. Relationship of the 90 kDa murine heat shock protein with the untransformed and transformed states of the cell glucocorticoid receptor. J Biol Chem, 262:6986-91.
    • (1987) J Biol Chem , vol.262 , pp. 6986-6991
    • Sanchez, E.R.1    Meshinchi, S.2    Tienrungroz, W.3
  • 86
    • 0035844227 scopus 로고    scopus 로고
    • Stimulation of p300-mediated transcription by the kinase MEKK1
    • See RH, Calvo D, Shi Y, et al. 2001. Stimulation of p300-mediated transcription by the kinase MEKK1. J Biol Chem, 276:16310-7.
    • (2001) J Biol Chem , vol.276 , pp. 16310-16317
    • See, R.H.1    Calvo, D.2    Shi, Y.3
  • 87
    • 0034462693 scopus 로고    scopus 로고
    • Functional interaction between nucleosome assembly proteins and p300/CREBbinding protein family coactivators
    • Shikama N, Chan HM, Krstic-Demonacos M, et al. 2000. Functional interaction between nucleosome assembly proteins and p300/CREBbinding protein family coactivators, Mol Cell Biol, 20:8933-43.
    • (2000) Mol Cell Biol , vol.20 , pp. 8933-8943
    • Shikama, N.1    Chan, H.M.2    Krstic-Demonacos, M.3
  • 88
    • 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, et al. 1999. Different regions of the immunophilin FKBP52 determine its association with the glucocorticoid receptor, hsp90, and cytoplasmic dynein. J Biol Chem, 274:36980-6.
    • (1999) J Biol Chem , vol.274 , pp. 36980-36986
    • Silverstein, A.M.1    Galigniana, M.D.2    Kanelakis, K.C.3
  • 89
    • 0028713459 scopus 로고
    • Function/activity of specific amino acids in glucocorticoid receptors
    • In: Litwack G (ed), New York: Academic Press
    • Simons SS Jr. 1994. Function/activity of specific amino acids in glucocorticoid receptors. In: Litwack G (ed). Vitamins and Hormones Volume 49: Steroids. New York: Academic Press, pp. 49-130.
    • (1994) Vitamins and Hormones Volume 49: Steroids , pp. 49-130
    • Simons Jr., S.S.1
  • 90
    • 0026608983 scopus 로고
    • Effects of okadaic acid, a protein phosphatase inhibitor, on glucocorticoid receptor-mediated enhancement
    • Somers JP, DeFranco DB. 1992. Effects of okadaic acid, a protein phosphatase inhibitor, on glucocorticoid receptor-mediated enhancement. Mol Endocrinol, 6:26-34.
    • (1992) Mol Endocrinol , vol.6 , pp. 26-34
    • Somers, J.P.1    DeFranco, D.B.2
  • 91
    • 0029894563 scopus 로고    scopus 로고
    • Intracellular receptors use a common mechanism to interpret signaling information at response elements
    • Starr DB, Matsui W, Thomas JR, et al. 1996. Intracellular receptors use a common mechanism to interpret signaling information at response elements. Genes Devel, 10:1271-83.
    • (1996) Genes Devel , vol.10 , pp. 1271-1283
    • Starr, D.B.1    Matsui, W.2    Thomas, J.R.3
  • 92
    • 6344265739 scopus 로고    scopus 로고
    • Inhibition of glucocorticoid receptor-mediated transcriptional activation by p38 mitogen-activated protein (MAP) kinase
    • Szatmary Z, Garabedian MJ, Vilcek J. 2004. Inhibition of glucocorticoid receptor-mediated transcriptional activation by p38 mitogen-activated protein (MAP) kinase. J Biol Chem, 279:43708-15.
    • (2004) J Biol Chem , vol.279 , pp. 43708-43715
    • Szatmary, Z.1    Garabedian, M.J.2    Vilcek, J.3
  • 93
    • 0033305373 scopus 로고    scopus 로고
    • Hormone-dependent interaction between the amino-and carboxyl-terminal domains of progesterone receptor in vitro and in vivo
    • Tetel MJ, Giangrande PH, Leonhardt SA, et al. 1999. Hormone-dependent interaction between the amino-and carboxyl-terminal domains of progesterone receptor in vitro and in vivo. Mol Endocrinol, 13:910-24.
    • (1999) Mol Endocrinol , vol.13 , pp. 910-924
    • Tetel, M.J.1    Giangrande, P.H.2    Leonhardt, S.A.3
  • 94
    • 0038074345 scopus 로고    scopus 로고
    • DNA binding of nuclear hormone receptors influences their structure and function
    • Thompson EB, Kumar R. 2003. DNA binding of nuclear hormone receptors influences their structure and function. Biochem Biophys Res Commun, 306:1-4.
    • (2003) Biochem Biophys Res Commun , vol.306 , pp. 1-4
    • Thompson, E.B.1    Kumar, R.2
  • 95
    • 0036847208 scopus 로고    scopus 로고
    • Small ubiquitin-related modifier-1 (SUMO-1) modification of the glucocorticoid receptor
    • Tian S, Poukka H, Palvimo JJ, et al. 2002. Small ubiquitin-related modifier-1 (SUMO-1) modification of the glucocorticoid receptor. Biochem J, 367:907-11.
    • (2002) Biochem J , vol.367 , pp. 907-911
    • Tian, S.1    Poukka, H.2    Palvimo, J.J.3
  • 96
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P. 2002. Intrinsically unstructured proteins. Trends Biochem Sci, 27:527-33.
    • (2002) Trends Biochem Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 97
    • 84995870933 scopus 로고
    • Human estrogen receptor transactivational capacity is determined by both cellular and promoter context and mediated by two functionally distinct intramolecular regions
    • Tzukerman MT, Esty A, Santiso-Mere D. 1994. Human estrogen receptor transactivational capacity is determined by both cellular and promoter context and mediated by two functionally distinct intramolecular regions. Mol Endocrinol, 8:21-30.
    • (1994) Mol Endocrinol , vol.8 , pp. 21-30
    • Tzukerman, M.T.1    Esty, A.2    Santiso-Mere, D.3
  • 98
    • 0035900780 scopus 로고    scopus 로고
    • Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids
    • Wallace AD, Cidlowski JA. 2001. Proteasome-mediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids. J Biol Chem, 276:42714-21.
    • (2001) J Biol Chem , vol.276 , pp. 42714-42721
    • Wallace, A.D.1    Cidlowski, J.A.2
  • 99
    • 0033609295 scopus 로고    scopus 로고
    • Phosphorylation/dephosphorylation of androgen as a determinant of androgen agonistic or antagonistic activity
    • Wang LG, Liu MX, Kreis W, et al. 1999. Phosphorylation/dephosphorylation of androgen as a determinant of androgen agonistic or antagonistic activity. Biochem Biophys Res Commun, 259:21-8.
    • (1999) Biochem Biophys Res Commun , vol.259 , pp. 21-28
    • Wang, L.G.1    Liu, M.X.2    Kreis, W.3
  • 100
    • 33847198615 scopus 로고    scopus 로고
    • Modulation of glucocorticoid receptor phosphorylation and transcriptional activity by a C-terminal-associated protein phosphatase
    • Wang Z, Chen W, Kono E, et al. 2007. Modulation of glucocorticoid receptor phosphorylation and transcriptional activity by a C-terminal-associated protein phosphatase. Mol Endocrinol, 21:625-34.
    • (2007) Mol Endocrinol , vol.21 , pp. 625-634
    • Wang, Z.1    Chen, W.2    Kono, E.3
  • 101
    • 0037135596 scopus 로고    scopus 로고
    • Deciphering the phosphorylation "code" of the glucocorticoid receptor in vivo
    • Wang Z, Frederick J, Garabedian MJ. 2002. Deciphering the phosphorylation "code" of the glucocorticoid receptor in vivo. J Biol Chem, 277:26573-80.
    • (2002) J Biol Chem , vol.277 , pp. 26573-26580
    • Wang, Z.1    Frederick, J.2    Garabedian, M.J.3
  • 102
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, et al. 2004. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol, 337:635-45.
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3
  • 103
    • 0030900729 scopus 로고    scopus 로고
    • Mouse glucocorticoid receptor phosphorylation status influences multiple functions of the receptor protein
    • Webster JC, Jewell CM, Bodwell JE, et al. 1997. Mouse glucocorticoid receptor phosphorylation status influences multiple functions of the receptor protein. J Biol Chem, 272:9287-93.
    • (1997) J Biol Chem , vol.272 , pp. 9287-9293
    • Webster, J.C.1    Jewell, C.M.2    Bodwell, J.E.3
  • 104
    • 34250690433 scopus 로고    scopus 로고
    • Kinases and protein phosphorylation as regulators of steroid hormone action
    • Weigel NL, Moore NL. 2007a. Kinases and protein phosphorylation as regulators of steroid hormone action. Nucl Recept Signal, 5:e005.
    • (2007) Nucl Recept Signal , vol.5
    • Weigel, N.L.1    Moore, N.L.2
  • 105
    • 33847081689 scopus 로고    scopus 로고
    • Cyclins, cyclin dependent kinases, and regulation of steroid receptor action
    • Weigel NL, Moore NL. 2007b. Cyclins, cyclin dependent kinases, and regulation of steroid receptor action. Mol Cell Endocrinol, 265-66:157-61.
    • (2007) Mol Cell Endocrinol , vol.265-266 , pp. 157-161
    • Weigel, N.L.1    Moore, N.L.2
  • 106
    • 0040597130 scopus 로고    scopus 로고
    • Constitutive phosphorylation of the acidic tails of the high mobility group 1 proteins by casein kinase II alters their conformation, stability, and DNA binding specificity
    • Wisniewski JR, Szewczuk Z, Petry I, et al. 1999. Constitutive phosphorylation of the acidic tails of the high mobility group 1 proteins by casein kinase II alters their conformation, stability, and DNA binding specificity. J Biol Chem, 274:20116-22.
    • (1999) J Biol Chem , vol.274 , pp. 20116-20122
    • Wisniewski, J.R.1    Szewczuk, Z.2    Petry, I.3
  • 107
    • 18844373937 scopus 로고    scopus 로고
    • Transcriptional regulation by steroid receptor coactivator phosphorylation
    • Wu RC, Smith CL, O'Malley BW. 2005. Transcriptional regulation by steroid receptor coactivator phosphorylation. Endocr Rev, 26:393-9.
    • (2005) Endocr Rev , vol.26 , pp. 393-399
    • Wu, R.C.1    Smith, C.L.2    O'Malley, B.W.3
  • 108
    • 4644252581 scopus 로고    scopus 로고
    • Selective phosphorylations of the SRC-3/ AIB1 coactivator integrate genomic responses to multiple cellular signaling pathways
    • Wu RC, Qin J, Yi P, et al. 2004. Selective phosphorylations of the SRC-3/ AIB1 coactivator integrate genomic responses to multiple cellular signaling pathways. Mol Cell, 15:937-49.
    • (2004) Mol Cell , vol.15 , pp. 937-949
    • Wu, R.C.1    Qin, J.2    Yi, P.3
  • 109
    • 0022327612 scopus 로고
    • Steroid receptor regulated transcription of specific genes and gene network
    • Yamamoto KR. 1985. Steroid receptor regulated transcription of specific genes and gene network. Annu Rev Genet, 19:209-52.
    • (1985) Annu Rev Genet , vol.19 , pp. 209-252
    • Yamamoto, K.R.1
  • 111
    • 0035914324 scopus 로고    scopus 로고
    • Regulation of transcription by AMP-activated protein kinase: Phosphorylation of p300 blocks its interaction with nuclear receptors
    • Yang W, Hong YH, Shen XQ, et al. 2001. Regulation of transcription by AMP-activated protein kinase: phosphorylation of p300 blocks its interaction with nuclear receptors. J Biol Chem, 276:38341-4.
    • (2001) J Biol Chem , vol.276 , pp. 38341-38344
    • Yang, W.1    Hong, Y.H.2    Shen, X.Q.3
  • 112
    • 18144399332 scopus 로고    scopus 로고
    • The human glucocorticoid receptor: One gene, multiple proteins and diverse responses
    • Zhou J, Cidlowski JA. 2005. The human glucocorticoid receptor: one gene, multiple proteins and diverse responses. Steroids, 70:407-17.
    • (2005) Steroids , vol.70 , pp. 407-417
    • Zhou, J.1    Cidlowski, J.A.2


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