메뉴 건너뛰기




Volumn 33, Issue 2, 2012, Pages 271-299

Allosteric modulators of steroid hormone receptors: Structural dynamics and gene regulation

Author keywords

[No Author keywords available]

Indexed keywords

ANDROGEN RECEPTOR; CELL NUCLEUS RECEPTOR; CHOLESTEROL; COMPLEMENTARY DNA; ECDYSONE RECEPTOR; ESTROGEN RECEPTOR ALPHA; ESTROGEN RECEPTOR BETA; ESTROGEN RELATED RECEPTOR ALPHA; ESTROGEN RELATED RECEPTOR BETA; ESTROGEN RELATED RECEPTOR GAMMA; GLUCOCORTICOID RECEPTOR; LIGAND; MINERALOCORTICOID RECEPTOR; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PROGESTERONE RECEPTOR; RECEPTOR PROTEIN; RETINOID X RECEPTOR ALPHA; RETINOID X RECEPTOR BETA; RETINOID X RECEPTOR GAMMA; RNA POLYMERASE II; STEROID RECEPTOR; STEROID RECEPTOR COACTIVATOR 1; TATA BINDING PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR ETS 1; TRANSCRIPTION FACTOR FOXO; TRANSCRIPTION FACTOR FOXO A1; TRANSCRIPTION FACTOR GATA 2; UNCLASSIFIED DRUG; UNINDEXED DRUG; VITAMIN D RECEPTOR;

EID: 84862635896     PISSN: 0163769X     EISSN: None     Source Type: Journal    
DOI: 10.1210/er.2011-1033     Document Type: Review
Times cited : (103)

References (250)
  • 1
    • 8844262660 scopus 로고    scopus 로고
    • Principles for modulation of the nuclear receptor superfamily
    • Gronemeyer H, Gustafsson JA, Laudet V 2004 Principles for modulation of the nuclear receptor superfamily. Nat Rev Drug Discov 3:950-964
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 950-964
    • Gronemeyer, H.1    Gustafsson, J.A.2    Laudet, V.3
  • 3
    • 73249115366 scopus 로고    scopus 로고
    • Crosstalk in inflammation: the interplay of glucocorticoid receptor-based mechanisms and kinases and phosphatases
    • Beck IM, Vanden BergheW, Vermeulen L, Yamamoto KR, Haegeman G, De Bosscher K 2009 Crosstalk in inflammation: the interplay of glucocorticoid receptor-based mechanisms and kinases and phosphatases. Endocr Rev 30: 830-882
    • (2009) Endocr Rev , vol.30 , pp. 830-882
    • Beck, I.M.1    Vanden Berghe, W.2    Vermeulen, L.3    Yamamoto, K.R.4    Haegeman, G.5    De Bosscher, K.6
  • 4
    • 60549116406 scopus 로고    scopus 로고
    • Nuclear receptors: one big family
    • McEwan IJ 2009 Nuclear receptors: one big family. Methods Mol Biol 505:3-18
    • (2009) Methods Mol Biol , vol.505 , pp. 3-18
    • McEwan, I.J.1
  • 5
    • 77955500692 scopus 로고    scopus 로고
    • Modulation of steroid hormone receptor activity. Prog
    • Stanisiæ V, Lonard DM, O'Malley BW 2010 Modulation of steroid hormone receptor activity. Prog Brain Res 181: 153-176
    • (2010) Brain Res , vol.181 , pp. 153-176
    • Stanisiæ, V.1    Lonard, D.M.2    O'Malley, B.W.3
  • 6
    • 77951879058 scopus 로고    scopus 로고
    • Aldosterone: effects on the kidney and cardiovascular system
    • Briet M, Schiffrin EL 2010 Aldosterone: effects on the kidney and cardiovascular system. Nat Rev Nephrol 6:261-273
    • (2010) Nat Rev Nephrol , vol.6 , pp. 261-273
    • Briet, M.1    Schiffrin, E.L.2
  • 8
    • 78049329473 scopus 로고    scopus 로고
    • Minireview: role of kinases and chromatin remodeling in progesterone signaling to chromatin
    • Vicent GP, Nacht AS, Zaurín R, Ballaré C, Clausell J, Beato M 2010 Minireview: role of kinases and chromatin remodeling in progesterone signaling to chromatin. Mol Endocrinol 24:2088-2098
    • (2010) Mol Endocrinol , vol.24 , pp. 2088-2098
    • Vicent, G.P.1    Nacht, A.S.2    Zaurín, R.3    Ballaré, C.4    Clausell, J.5    Beato, M.6
  • 10
    • 79952799756 scopus 로고    scopus 로고
    • Cellular processing of the glucocorticoid receptor gene and protein: new mechanisms for generating tissue-specific actions of glucocorticoids
    • Oakley RH, Cidlowski JA 2011 Cellular processing of the glucocorticoid receptor gene and protein: new mechanisms for generating tissue-specific actions of glucocorticoids. J Biol Chem 286:3177-3184
    • (2011) J Biol Chem , vol.286 , pp. 3177-3184
    • Oakley, R.H.1    Cidlowski, J.A.2
  • 11
    • 79953871100 scopus 로고    scopus 로고
    • Widespread negative response elements mediate direct repression by agonist-liganded glucocorticoid receptor
    • Surjit M, Ganti KP, Mukherji A, Ye T, Hua G, Metzger D, Li M, Chambon P 2011 Widespread negative response elements mediate direct repression by agonist-liganded glucocorticoid receptor. Cell 145:224-241
    • (2011) Cell , vol.145 , pp. 224-241
    • Surjit, M.1    Ganti, K.P.2    Mukherji, A.3    Ye, T.4    Hua, G.5    Metzger, D.6    Li, M.7    Chambon, P.8
  • 13
    • 42049107310 scopus 로고    scopus 로고
    • A lifetime of aldosterone excess: long-term consequences of altered regulation of aldosterone production for cardiovascular function
    • Connell JM, MacKenzie SM, Freel EM, Fraser R, Davies E 2008 A lifetime of aldosterone excess: long-term consequences of altered regulation of aldosterone production for cardiovascular function. Endocr Rev 29:133-154
    • (2008) Endocr Rev , vol.29 , pp. 133-154
    • Connell, J.M.1    MacKenzie, S.M.2    Freel, E.M.3    Fraser, R.4    Davies, E.5
  • 14
    • 65549087111 scopus 로고    scopus 로고
    • Selective androgen receptor modulators as function promoting therapies
    • Bhasin S, Jasuja R 2009 Selective androgen receptor modulators as function promoting therapies. Curr Opin Clin Nutr Metab Care 12:232-240
    • (2009) Curr Opin Clin Nutr Metab Care , vol.12 , pp. 232-240
    • Bhasin, S.1    Jasuja, R.2
  • 18
    • 82655180375 scopus 로고    scopus 로고
    • Intrinsic disorder in the androgen receptor: identification, characterisation and drugability
    • McEwan IJ 2012 Intrinsic disorder in the androgen receptor: identification, characterisation and drugability. Mol BioSyst 8:82-90
    • (2012) Mol BioSyst , vol.8 , pp. 82-90
    • McEwan, I.J.1
  • 20
    • 3142511046 scopus 로고    scopus 로고
    • Receptor mechanisms of rapid extranuclear signalling initiated by steroid hormones
    • Boonyaratanakornkit V, Edwards DP 2004 Receptor mechanisms of rapid extranuclear signalling initiated by steroid hormones. Essays Biochem 40:105-120
    • (2004) Essays Biochem , vol.40 , pp. 105-120
    • Boonyaratanakornkit, V.1    Edwards, D.P.2
  • 22
    • 77957577240 scopus 로고    scopus 로고
    • Stress, sex, and neural adaptation to a changing environment: mechanisms of neuronal remodeling
    • McEwen BS 2010 Stress, sex, and neural adaptation to a changing environment: mechanisms of neuronal remodeling. Ann NY Acad Sci 1204 Suppl:E38-E59
    • (2010) Ann NY Acad Sci 1204 Suppl
    • McEwen, B.S.1
  • 23
    • 79955527505 scopus 로고    scopus 로고
    • Rapid non-genomic effects of corticosteroids and their role in the central stress response
    • Groeneweg FL, Karst H, de Kloet ER, Joëls M 2011 Rapid non-genomic effects of corticosteroids and their role in the central stress response. J Endocrinol 209:153-167
    • (2011) J Endocrinol , vol.209 , pp. 153-167
    • Groeneweg, F.L.1    Karst, H.2    de Kloet, E.R.3    Joëls, M.4
  • 24
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans RM 1988 The steroid and thyroid hormone receptor superfamily. Science 240:889-895
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 25
    • 3142624840 scopus 로고    scopus 로고
    • The evolution of the nuclear receptor superfamily
    • Escriva H, Bertrand S, Laudet V 2004 The evolution of the nuclear receptor superfamily. Essays Biochem 40:11-26
    • (2004) Essays Biochem , vol.40 , pp. 11-26
    • Escriva, H.1    Bertrand, S.2    Laudet, V.3
  • 27
    • 0022473069 scopus 로고
    • Sequence and expression of human estrogen receptor complementary DNA
    • Greene GL, Gilna P, Waterfield M, Baker A, Hort Y, Shine J 1986 Sequence and expression of human estrogen receptor complementary DNA. Science 231:1150-1154
    • (1986) Science , vol.231 , pp. 1150-1154
    • Greene, G.L.1    Gilna, P.2    Waterfield, M.3    Baker, A.4    Hort, Y.5    Shine, J.6
  • 31
    • 0023929785 scopus 로고
    • Molecular cloning of human and rat complementary DNA encoding androgen receptors
    • Chang CS, Kokontis J, Liao ST 1988 Molecular cloning of human and rat complementary DNA encoding androgen receptors. Science 240:324-326
    • (1988) Science , vol.240 , pp. 324-326
    • Chang, C.S.1    Kokontis, J.2    Liao, S.T.3
  • 32
    • 0024205612 scopus 로고
    • The human androgen receptor: complementary deoxyribonucleic acid cloning, sequence analysis and gene expression in prostate
    • Lubahn DB, Joseph DR, Sar M, Tan J, Higgs HN, Larson RE, French FS, Wilson EM 1988 The human androgen receptor: complementary deoxyribonucleic acid cloning, sequence analysis and gene expression in prostate. Mol Endocrinol 2:1265-1275
    • (1988) Mol Endocrinol , vol.2 , pp. 1265-1275
    • Lubahn, D.B.1    Joseph, D.R.2    Sar, M.3    Tan, J.4    Higgs, H.N.5    Larson, R.E.6    French, F.S.7    Wilson, E.M.8
  • 34
    • 36248969303 scopus 로고    scopus 로고
    • The molecular basis of eucaryotic transcription
    • Kornberg RD 2007 The molecular basis of eucaryotic transcription. Cell Death Differ 14:1989-1997
    • (2007) Cell Death Differ , vol.14 , pp. 1989-1997
    • Kornberg, R.D.1
  • 35
    • 77958111633 scopus 로고    scopus 로고
    • The metazoan mediator co-activator complex as an integrative hub for transcriptional regulation
    • Malik S, Roeder RG 2010 The metazoan mediator co-activator complex as an integrative hub for transcriptional regulation. Nat Rev Genet 11:761-772
    • (2010) Nat Rev Genet , vol.11 , pp. 761-772
    • Malik, S.1    Roeder, R.G.2
  • 36
    • 14544280757 scopus 로고    scopus 로고
    • Transcriptional regulation and the role of diverse coactivators in animal cells
    • Roeder RG 2005 Transcriptional regulation and the role of diverse coactivators in animal cells. FEBS Lett 579:909-915
    • (2005) FEBS Lett , vol.579 , pp. 909-915
    • Roeder, R.G.1
  • 37
    • 0343415609 scopus 로고    scopus 로고
    • The glucocorticoid receptor: rapid exchange with regulatory sites in living cells
    • McNally JG, MüllerWG, Walker D, Wolford R, HagerGL 2000 The glucocorticoid receptor: rapid exchange with regulatory sites in living cells. Science 287:1262-1265
    • (2000) Science , vol.287 , pp. 1262-1265
    • McNally, J.G.1    Müller, W.G.2    Walker, D.3    Wolford, R.4    Hager, G.L.5
  • 39
    • 1942502820 scopus 로고    scopus 로고
    • Rapid periodic binding and displacement of the glucocorticoid receptor during chromatin remodeling
    • Nagaich AK, Walker DA, Wolford R, Hager GL 2004 Rapid periodic binding and displacement of the glucocorticoid receptor during chromatin remodeling. Mol Cell 14: 163-174
    • (2004) Mol Cell , vol.14 , pp. 163-174
    • Nagaich, A.K.1    Walker, D.A.2    Wolford, R.3    Hager, G.L.4
  • 41
    • 14844348177 scopus 로고    scopus 로고
    • Ligand-specific dynamics of the progesterone receptor in living cells and during chromatin remodeling in vitro
    • Rayasam GV, Elbi C, Walker DA, Wolford R, Fletcher TM, Edwards DP, HagerGL 2005 Ligand-specific dynamics of the progesterone receptor in living cells and during chromatin remodeling in vitro. Mol Cell Biol 25:2406-2418
    • (2005) Mol Cell Biol , vol.25 , pp. 2406-2418
    • Rayasam, G.V.1    Elbi, C.2    Walker, D.A.3    Wolford, R.4    Fletcher, T.M.5    Edwards, D.P.6    Hager, G.L.7
  • 42
    • 0025062215 scopus 로고
    • Role of the two activating domains of the oestrogen receptor in the celltype and promoter-context dependent agonistic activity of the anti-oestrogen 4-hydroxytamoxifen
    • Berry M, Metzger D, Chambon P 1990 Role of the two activating domains of the oestrogen receptor in the celltype and promoter-context dependent agonistic activity of the anti-oestrogen 4-hydroxytamoxifen.EMBOJ 9:2811-2818
    • (1990) EMBOJ , vol.9 , pp. 2811-2818
    • Berry, M.1    Metzger, D.2    Chambon, P.3
  • 44
    • 69249110003 scopus 로고    scopus 로고
    • Normal and cancerrelated functions of the p160 steroid receptor co-activator (SRC) family
    • Xu J, Wu RC, O'Malley BW 2009 Normal and cancerrelated functions of the p160 steroid receptor co-activator (SRC) family. Nat Rev Cancer 9:615-630
    • (2009) Nat Rev Cancer , vol.9 , pp. 615-630
    • Xu, J.1    Wu, R.C.2    O'Malley, B.W.3
  • 45
    • 78751513652 scopus 로고    scopus 로고
    • Nuclear receptor coactivators: structural and functional biochemistry
    • Bulynko YA, O'Malley BW 2011 Nuclear receptor coactivators: structural and functional biochemistry. Biochemistry 50:313-328
    • (2011) Biochemistry , vol.50 , pp. 313-328
    • Bulynko, Y.A.1    O'Malley, B.W.2
  • 46
    • 1442351143 scopus 로고    scopus 로고
    • Coregulator function: a key to understanding tissue specificity of selective receptor modulators
    • Smith CL, O'Malley BW 2004 Coregulator function: a key to understanding tissue specificity of selective receptor modulators. Endocr Rev 25:45-71
    • (2004) Endocr Rev , vol.25 , pp. 45-71
    • Smith, C.L.1    O'Malley, B.W.2
  • 49
    • 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
  • 50
    • 27744511919 scopus 로고    scopus 로고
    • Structure and function of steroid receptorAF1transactivation domains: induction of active conformations
    • Lavery DN, McEwan IJ 2005 Structure and function of steroid receptorAF1transactivation domains: induction of active conformations. Biochem J 391:449-464
    • (2005) Biochem J , vol.391 , pp. 449-464
    • Lavery, D.N.1    McEwan, I.J.2
  • 51
    • 34249667205 scopus 로고    scopus 로고
    • Natural disordered sequences in the amino terminal domain of nuclear receptors: lessons from the androgen and glucocorticoid receptors
    • McEwan IJ, Lavery D, Fischer K, Watt K 2007 Natural disordered sequences in the amino terminal domain of nuclear receptors: lessons from the androgen and glucocorticoid receptors. Nucl Recept Signal 5:e001
    • (2007) Nucl Recept Signal , vol.5
    • McEwan, I.J.1    Lavery, D.2    Fischer, K.3    Watt, K.4
  • 52
    • 0017849608 scopus 로고
    • Separation of the hormone-and DNA-binding sites of the hepatic glucocorticoid receptor by means of proteolysis
    • Wrange O, Gustafsson JA 1978 Separation of the hormone-and DNA-binding sites of the hepatic glucocorticoid receptor by means of proteolysis. J Biol Chem 253:856-865
    • (1978) J Biol Chem , vol.253 , pp. 856-865
    • Wrange, O.1    Gustafsson, J.A.2
  • 53
    • 0020328733 scopus 로고
    • Immunochemical analysis of the glucocorticoid receptor: identification of a third domain separate from the steroidbinding and DNA-binding domains
    • Carlstedt-Duke J, Okret S, Wrange O, Gustafsson JA 1982 Immunochemical analysis of the glucocorticoid receptor: identification of a third domain separate from the steroidbinding and DNA-binding domains. Proc Natl Acad Sci USA 79:4260-4264
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 4260-4264
    • Carlstedt-Duke, J.1    Okret, S.2    Wrange, O.3    Gustafsson, J.A.4
  • 55
    • 0027484097 scopus 로고
    • Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes
    • Smith DF 1993 Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes. Mol Endocrinol 7:1418-1429
    • (1993) Mol Endocrinol , vol.7 , pp. 1418-1429
    • Smith, D.F.1
  • 56
    • 53149118242 scopus 로고    scopus 로고
    • The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts
    • Pratt WB, Morishima Y, Osawa Y 2008 The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts. J Biol Chem 283:22885-22889
    • (2008) J Biol Chem , vol.283 , pp. 22885-22889
    • Pratt, W.B.1    Morishima, Y.2    Osawa, Y.3
  • 57
    • 0037184112 scopus 로고    scopus 로고
    • Mutations at positions 547-553 of rat glucocorticoid receptors reveal that hsp90 binding requires the presence, but not defined composition, of a seven-amino acid sequence at the amino terminus of the ligand binding domain
    • Kaul S, Murphy PJ, Chen J, Brown L, Pratt WB, Simons SS. Jr 2002 Mutations at positions 547-553 of rat glucocorticoid receptors reveal that hsp90 binding requires the presence, but not defined composition, of a seven-amino acid sequence at the amino terminus of the ligand binding domain. J Biol Chem 277:36223-36232
    • (2002) J Biol Chem , vol.277 , pp. 36223-36232
    • Kaul, S.1    Murphy, P.J.2    Chen, J.3    Brown, L.4    Pratt, W.B.5    Simons Jr., S.S.6
  • 59
    • 0037150683 scopus 로고    scopus 로고
    • Disassembly of transcriptional regulatory complexes by molecular chaperones
    • Freeman BC, Yamamoto KR 2002 Disassembly of transcriptional regulatory complexes by molecular chaperones. Science 296:2232-2235
    • (2002) Science , vol.296 , pp. 2232-2235
    • Freeman, B.C.1    Yamamoto, K.R.2
  • 60
    • 77951901129 scopus 로고    scopus 로고
    • Structural overview of the nuclear receptor superfamily: insights into physiology and therapeutics
    • Huang P, Chandra V, Rastinejad F 2010 Structural overview of the nuclear receptor superfamily: insights into physiology and therapeutics. Annu Rev Physiol 72:247-272
    • (2010) Annu Rev Physiol , vol.72 , pp. 247-272
    • Huang, P.1    Chandra, V.2    Rastinejad, F.3
  • 61
    • 79951672289 scopus 로고    scopus 로고
    • Evolution of steroid receptors from an estrogen-sensitive ancestral receptor
    • Eick GN, Thornton JW 2011 Evolution of steroid receptors from an estrogen-sensitive ancestral receptor.MolCell Endocrinol 334:31-38
    • (2011) MolCell Endocrinol , vol.334 , pp. 31-38
    • Eick, G.N.1    Thornton, J.W.2
  • 62
    • 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 1997 A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387:733-736
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 64
    • 3242784885 scopus 로고    scopus 로고
    • Mechanism of the nuclear receptor molecular switch
    • Nagy L, Schwabe JW 2004 Mechanism of the nuclear receptor molecular switch. Trends Biochem Sci 29:317-324
    • (2004) Trends Biochem Sci , vol.29 , pp. 317-324
    • Nagy, L.1    Schwabe, J.W.2
  • 66
    • 8344226282 scopus 로고    scopus 로고
    • Structural basis for androgen receptor interdomain and coactivator interactions suggests a transition in nuclear receptor activation function dominance
    • He B, Gampe Jr RT, Kole AJ, Hnat AT, Stanley TB, An G, Stewart EL, Kalman RI, Minges JT, Wilson EM 2004 Structural basis for androgen receptor interdomain and coactivator interactions suggests a transition in nuclear receptor activation function dominance. Mol Cell 16:425-438
    • (2004) Mol Cell , vol.16 , pp. 425-438
    • He, B.1    Gampe Jr., R.T.2    Kole, A.J.3    Hnat, A.T.4    Stanley, T.B.5    An, G.6    Stewart, E.L.7    Kalman, R.I.8    Minges, J.T.9    Wilson, E.M.10
  • 68
    • 34047167881 scopus 로고    scopus 로고
    • A conformational switch in the ligandbinding domain regulates the dependence of the glucocorticoid receptor on Hsp90
    • Ricketson D, Hostick U, Fang L, Yamamoto KR, Darimont BD 2007 A conformational switch in the ligandbinding domain regulates the dependence of the glucocorticoid receptor on Hsp90. J Mol Biol 368:729-741
    • (2007) J Mol Biol , vol.368 , pp. 729-741
    • Ricketson, D.1    Hostick, U.2    Fang, L.3    Yamamoto, K.R.4    Darimont, B.D.5
  • 69
    • 0034733912 scopus 로고    scopus 로고
    • Ligand-protein interactions in nuclear receptors of hormones
    • Egea PF, Klaholz BP, Moras D 2000 Ligand-protein interactions in nuclear receptors of hormones. FEBS Lett 476: 62-67
    • (2000) FEBS Lett , vol.476 , pp. 62-67
    • Egea, P.F.1    Klaholz, B.P.2    Moras, D.3
  • 71
    • 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, Danielian P, Parker MG, Stein RB, Pike JW, McDonnell DP 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    Danielian, P.4    Parker, M.G.5    Stein, R.B.6    Pike, J.W.7    McDonnell, D.P.8
  • 72
    • 0029796605 scopus 로고    scopus 로고
    • Different regions in activation function-1 of the human estrogen receptor required for antiestrogen- and estradiol-dependent transcription activation
    • McInerney EM, Katzenellenbogen BS 1996 Different regions in activation function-1 of the human estrogen receptor required for antiestrogen- and estradiol-dependent transcription activation. J Biol Chem 271:24172-24178
    • (1996) J Biol Chem , vol.271 , pp. 24172-24178
    • McInerney, E.M.1    Katzenellenbogen, B.S.2
  • 73
    • 2942750192 scopus 로고    scopus 로고
    • The relative contribution exerted by AF-1 and AF-2 transactivation functions in estrogen receptor α transcriptional activity depends upon the differentiation stage of the cell
    • Mérot Y, Métivier R, Penot G, Manu D, Saligaut C, Gannon F, Pakdel F, Kah O, Flouriot G 2004 The relative contribution exerted by AF-1 and AF-2 transactivation functions in estrogen receptor α transcriptional activity depends upon the differentiation stage of the cell. J Biol Chem 279:26184-26191
    • (2004) J Biol Chem , vol.279 , pp. 26184-26191
    • Mérot, Y.1    Métivier, R.2    Penot, G.3    Manu, D.4    Saligaut, C.5    Gannon, F.6    Pakdel, F.7    Kah, O.8    Flouriot, G.9
  • 75
    • 0025329841 scopus 로고
    • Characterization and colocalization of steroid binding and dimerization activities in the mouse estrogen receptor
    • Fawell SE, Lees JA, White R, Parker MG 1990 Characterization and colocalization of steroid binding and dimerization activities in the mouse estrogen receptor. Cell 60:953-962
    • (1990) Cell , vol.60 , pp. 953-962
    • Fawell, S.E.1    Lees, J.A.2    White, R.3    Parker, M.G.4
  • 76
    • 0035135217 scopus 로고    scopus 로고
    • Glucocorticoid receptor homodimers and glucocorticoid-mineralocorticoid receptor heterodimers form in the cytoplasm through alternative dimerization interfaces
    • Savory JG, Préfontaine GG, Lamprecht C, Liao M, Walther RF, Lefebvre YA, Haché RJ 2001 Glucocorticoid receptor homodimers and glucocorticoid-mineralocorticoid receptor heterodimers form in the cytoplasm through alternative dimerization interfaces. Mol Cell Biol 21:781-793
    • (2001) Mol Cell Biol , vol.21 , pp. 781-793
    • Savory, J.G.1    Préfontaine, G.G.2    Lamprecht, C.3    Liao, M.4    Walther, R.F.5    Lefebvre, Y.A.6    Haché, R.J.7
  • 78
    • 55049086227 scopus 로고    scopus 로고
    • The contribution of different androgen receptor domains to receptor dimerization and signaling
    • Centenera MM, Harris JM, Tilley WD, Butler LM 2008 The contribution of different androgen receptor domains to receptor dimerization and signaling. Mol Endocrinol 22:2373-2382
    • (2008) Mol Endocrinol , vol.22 , pp. 2373-2382
    • Centenera, M.M.1    Harris, J.M.2    Tilley, W.D.3    Butler, L.M.4
  • 79
    • 0029560494 scopus 로고
    • Evidence for an anti-parallel orientation of the ligand-activated human androgen receptor dimer
    • Langley E, Zhou ZX, Wilson EM 1995 Evidence for an anti-parallel orientation of the ligand-activated human androgen receptor dimer. J Biol Chem 270:29983-29990
    • (1995) J Biol Chem , vol.270 , pp. 29983-29990
    • Langley, E.1    Zhou, Z.X.2    Wilson, E.M.3
  • 80
    • 0031594713 scopus 로고    scopus 로고
    • Intermolecular NH2-/carboxyl-terminal interactions in androgen receptor dimerization revealed by mutations that cause androgen insensitivity
    • Langley E, Kemppainen JA, Wilson EM 1998 Intermolecular NH2-/carboxyl-terminal interactions in androgen receptor dimerization revealed by mutations that cause androgen insensitivity. J Biol Chem 273:92-101
    • (1998) J Biol Chem , vol.273 , pp. 92-101
    • Langley, E.1    Kemppainen, J.A.2    Wilson, E.M.3
  • 81
    • 0031039480 scopus 로고    scopus 로고
    • Functional in vivo interaction between the amino-terminal, transactivation domain and the ligand binding domain of the androgen receptor
    • Doesburg P, Kuil CW, Berrevoets CA, Steketee K, Faber PW, Mulder E, Brinkmann AO, Trapman J 1997 Functional in vivo interaction between the amino-terminal, transactivation domain and the ligand binding domain of the androgen receptor. Biochemistry 36:1052-1064
    • (1997) Biochemistry , vol.36 , pp. 1052-1064
    • Doesburg, P.1    Kuil, C.W.2    Berrevoets, C.A.3    Steketee, K.4    Faber, P.W.5    Mulder, E.6    Brinkmann, A.O.7    Trapman, J.8
  • 82
    • 0034725648 scopus 로고    scopus 로고
    • FXXLF and WXXLF sequences mediate the NH2-terminal interaction with the ligand binding domain of the androgen receptor
    • He B, Kemppainen JA, Wilson EM 2000 FXXLF and WXXLF sequences mediate the NH2-terminal interaction with the ligand binding domain of the androgen receptor. J Biol Chem 275:22986-22994
    • (2000) J Biol Chem , vol.275 , pp. 22986-22994
    • He, B.1    Kemppainen, J.A.2    Wilson, E.M.3
  • 83
    • 0037067766 scopus 로고    scopus 로고
    • Dependence of selective gene activation on the androgen receptor NH2-and COOH-terminal interaction
    • He B, Lee LW, Minges JT, Wilson EM 2002 Dependence of selective gene activation on the androgen receptor NH2-and COOH-terminal interaction. J Biol Chem 277:25631-25639
    • (2002) J Biol Chem , vol.277 , pp. 25631-25639
    • He, B.1    Lee, L.W.2    Minges, J.T.3    Wilson, E.M.4
  • 84
    • 0037424344 scopus 로고    scopus 로고
    • Dual function of an amino-terminal amphipatic helix in androgen receptor-mediated transactivation through specific and nonspecific response elements
    • Callewaert L, Verrijdt G, Christiaens V, Haelens A, Claessens F 2003 Dual function of an amino-terminal amphipatic helix in androgen receptor-mediated transactivation through specific and nonspecific response elements. J Biol Chem 278:8212-8218
    • (2003) J Biol Chem , vol.278 , pp. 8212-8218
    • Callewaert, L.1    Verrijdt, G.2    Christiaens, V.3    Haelens, A.4    Claessens, F.5
  • 85
    • 0034740164 scopus 로고    scopus 로고
    • Synergism between ERα transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: requirement for the AF-1 α-helical core and for a direct interaction between the N- and C-terminal domains
    • Métivier R, Penot G, Flouriot G, Pakdel F 2001 Synergism between ERα transactivation function 1 (AF-1) and AF-2 mediated by steroid receptor coactivator protein-1: requirement for the AF-1 α-helical core and for a direct interaction between the N- and C-terminal domains. Mol Endocrinol 15:1953-1970
    • (2001) Mol Endocrinol , vol.15 , pp. 1953-1970
    • Métivier, R.1    Penot, G.2    Flouriot, G.3    Pakdel, F.4
  • 86
    • 0029616211 scopus 로고
    • Ligand-dependent, transcriptionally productive association of the amino- and carboxyl-terminal regions of a steroid hormone nuclear receptor
    • Kraus WL, McInerney EM, Katzenellenbogen BS 1995 Ligand-dependent, transcriptionally productive association of the amino- and carboxyl-terminal regions of a steroid hormone nuclear receptor. Proc Natl Acad Sci USA 92: 12314-12318
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 12314-12318
    • Kraus, W.L.1    McInerney, E.M.2    Katzenellenbogen, B.S.3
  • 87
    • 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, McDonnell DP, Edwards DP 1999 Hormone-dependent interaction between the amino- and carboxyl-terminal domains of progesterone receptor in vitro and in vivo. Mol Endocrinol 13:910-924
    • (1999) Mol Endocrinol , vol.13 , pp. 910-924
    • Tetel, M.J.1    Giangrande, P.H.2    Leonhardt, S.A.3    McDonnell, D.P.4    Edwards, D.P.5
  • 88
    • 3042814763 scopus 로고    scopus 로고
    • Intramolecular interactions between the AF3 domain and the C-terminus of the human progesterone receptor are mediated through two LXXLL motifs
    • Dong X, Challis JR, Lye SJ 2004 Intramolecular interactions between the AF3 domain and the C-terminus of the human progesterone receptor are mediated through two LXXLL motifs. J Mol Endocrinol 32:843-857
    • (2004) J Mol Endocrinol , vol.32 , pp. 843-857
    • Dong, X.1    Challis, J.R.2    Lye, S.J.3
  • 89
    • 69449087342 scopus 로고    scopus 로고
    • Structural and functional characterisation of the interdomain interaction in the mineralocorticoid receptor
    • Pippal JB, Yao Y, Rogerson FM, Fuller PJ 2009 Structural and functional characterisation of the interdomain interaction in the mineralocorticoid receptor. Mol Endocrinol 23:1360-1370
    • (2009) Mol Endocrinol , vol.23 , pp. 1360-1370
    • Pippal, J.B.1    Yao, Y.2    Rogerson, F.M.3    Fuller, P.J.4
  • 90
    • 3142760881 scopus 로고    scopus 로고
    • DNA recognition by nuclear receptors
    • Claessens F, Gewirth DT 2004 DNA recognition by nuclear receptors. Essays Biochem 40:59-72
    • (2004) Essays Biochem , vol.40 , pp. 59-72
    • Claessens, F.1    Gewirth, D.T.2
  • 92
    • 0025223160 scopus 로고
    • Solution structure of the DNA-binding domain of the oestrogen receptor
    • Schwabe JW, Neuhaus D, Rhodes D 1990 Solution structure of the DNA-binding domain of the oestrogen receptor. Nature 348:458-461
    • (1990) Nature , vol.348 , pp. 458-461
    • Schwabe, J.W.1    Neuhaus, D.2    Rhodes, D.3
  • 93
    • 0027365669 scopus 로고
    • The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements
    • Schwabe JW, Chapman L, Finch JT, Rhodes D 1993 The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements. Cell 75:567-578
    • (1993) Cell , vol.75 , pp. 567-578
    • Schwabe, J.W.1    Chapman, L.2    Finch, J.T.3    Rhodes, D.4
  • 95
    • 65249167505 scopus 로고    scopus 로고
    • DNA binding site sequence directs glucocorticoid receptor structure and activity
    • Meijsing SH, Pufall MA, So AY, Bates DL, Chen L, Yamamoto KR 2009 DNA binding site sequence directs glucocorticoid receptor structure and activity. Science 324: 407-410
    • (2009) Science , vol.324 , pp. 407-410
    • Meijsing, S.H.1    Pufall, M.A.2    So, A.Y.3    Bates, D.L.4    Chen, L.5    Yamamoto, K.R.6
  • 96
    • 33751551165 scopus 로고    scopus 로고
    • Structure of the progesterone receptor-deoxyribonucleic acid complex: novel interactions required for binding to half-site response elements
    • Roemer SC, Donham DC, Sherman L, Pon VH, Edwards DP, Churchill ME 2006 Structure of the progesterone receptor-deoxyribonucleic acid complex: novel interactions required for binding to half-site response elements. Mol Endocrinol 20:3042-3052
    • (2006) Mol Endocrinol , vol.20 , pp. 3042-3052
    • Roemer, S.C.1    Donham, D.C.2    Sherman, L.3    Pon, V.H.4    Edwards, D.P.5    Churchill, M.E.6
  • 97
    • 26444526919 scopus 로고    scopus 로고
    • Regulation of the amino-terminal transcription activation domain of progesterone receptor by a cofactorinduced protein folding mechanism
    • Wardell SE, Kwok SC, Sherman L, Hodges RS, Edwards DP 2005 Regulation of the amino-terminal transcription activation domain of progesterone receptor by a cofactorinduced protein folding mechanism. Mol Cell Biol 25: 8792-8808
    • (2005) Mol Cell Biol , vol.25 , pp. 8792-8808
    • Wardell, S.E.1    Kwok, S.C.2    Sherman, L.3    Hodges, R.S.4    Edwards, D.P.5
  • 98
    • 78049332125 scopus 로고    scopus 로고
    • The progesterone receptor hinge region regulates the kinetics of transcriptional responses through acetylation, phosphorylation, and nuclear retention
    • Daniel AR, Gaviglio AL, Czaplicki LM, Hillard CJ, Housa D, Lange CA 2010 The progesterone receptor hinge region regulates the kinetics of transcriptional responses through acetylation, phosphorylation, and nuclear retention. Mol Endocrinol 24:2126-2138
    • (2010) Mol Endocrinol , vol.24 , pp. 2126-2138
    • Daniel, A.R.1    Gaviglio, A.L.2    Czaplicki, L.M.3    Hillard, C.J.4    Housa, D.5    Lange, C.A.6
  • 101
    • 0034617058 scopus 로고    scopus 로고
    • P300 and p300/cAMP-response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation
    • Fu M, Wang C, Reutens AT, Wang J, Angeletti RH, Siconolfi-Baez L, Ogryzko V, Avantaggiati ML, Pestell RG 2000 P300 and p300/cAMP-response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation. J Biol Chem 275:20853-20860
    • (2000) J Biol Chem , vol.275 , pp. 20853-20860
    • Fu, M.1    Wang, C.2    Reutens, A.T.3    Wang, J.4    Angeletti, R.H.5    Siconolfi-Baez, L.6    Ogryzko, V.7    Avantaggiati, M.L.8    Pestell, R.G.9
  • 103
    • 43449108865 scopus 로고    scopus 로고
    • Androgen receptor acetylation sites differentially regulate gene control
    • Faus H, Haendler B 2008 Androgen receptor acetylation sites differentially regulate gene control. J Cell Biochem 104:511-524
    • (2008) J Cell Biochem , vol.104 , pp. 511-524
    • Faus, H.1    Haendler, B.2
  • 106
    • 69949146216 scopus 로고    scopus 로고
    • A progesterone receptor co-activator (JDP2) mediates activity through interaction with residues in the carboxyl-terminal extension of the DNA binding domain
    • Hill KK, Roemer SC, Jones DN, Churchill ME, Edwards DP 2009 A progesterone receptor co-activator (JDP2) mediates activity through interaction with residues in the carboxyl-terminal extension of the DNA binding domain. J Biol Chem 284:24415-24424
    • (2009) J Biol Chem , vol.284 , pp. 24415-24424
    • Hill, K.K.1    Roemer, S.C.2    Jones, D.N.3    Churchill, M.E.4    Edwards, D.P.5
  • 108
    • 0024095250 scopus 로고
    • The N-terminal DNA-binding 'zinc finger' of the oestrogen and glucocorticoid receptors determines target gene specificity
    • Green S, Kumar V, Theulaz I, Wahli W, Chambon P 1988 The N-terminal DNA-binding 'zinc finger' of the oestrogen and glucocorticoid receptors determines target gene specificity. EMBO J 7:3037-3044
    • (1988) EMBO J , vol.7 , pp. 3037-3044
    • Green, S.1    Kumar, V.2    Theulaz, I.3    Wahli, W.4    Chambon, P.5
  • 109
    • 0024500728 scopus 로고
    • Chimeric receptors used to probe the DNA-binding domain of the estrogen and glucocorticoid receptors
    • Green S, Chambon P 1989 Chimeric receptors used to probe the DNA-binding domain of the estrogen and glucocorticoid receptors. Cancer Res 49:2282s-2285s
    • (1989) Cancer Res , vol.49
    • Green, S.1    Chambon, P.2
  • 110
    • 0034697122 scopus 로고    scopus 로고
    • Differences in DNA binding characteristics of the androgen and glucocorticoid receptors can determine hormone-specific responses
    • Schoenmakers E, Verrijdt G, Peeters B, Verhoeven G, Rombauts W, Claessens F 2000 Differences in DNA binding characteristics of the androgen and glucocorticoid receptors can determine hormone-specific responses. J Biol Chem 275:12290-12297
    • (2000) J Biol Chem , vol.275 , pp. 12290-12297
    • Schoenmakers, E.1    Verrijdt, G.2    Peeters, B.3    Verhoeven, G.4    Rombauts, W.5    Claessens, F.6
  • 113
    • 34547931715 scopus 로고    scopus 로고
    • Cell- and gene-specific regulation of primary target genes by the androgen receptor
    • Bolton EC, So AY, Chaivorapol C, Haqq CM, Li H, Yamamoto KR 2007 Cell- and gene-specific regulation of primary target genes by the androgen receptor. Genes Dev 21:2005-2017
    • (2007) Genes Dev , vol.21 , pp. 2005-2017
    • Bolton, E.C.1    So, A.Y.2    Chaivorapol, C.3    Haqq, C.M.4    Li, H.5    Yamamoto, K.R.6
  • 114
    • 34447519218 scopus 로고    scopus 로고
    • Genomic analyses of transcription factor binding, histone acetylation, and gene expression reveal mechanistically distinct classes of estrogenregulated promoters
    • Kininis M, Chen BS, Diehl AG, Isaacs GD, Zhang T, Siepel AC, Clark AG, Kraus WL 2007 Genomic analyses of transcription factor binding, histone acetylation, and gene expression reveal mechanistically distinct classes of estrogenregulated promoters. Mol Cell Biol 27:5090-5104
    • (2007) Mol Cell Biol , vol.27 , pp. 5090-5104
    • Kininis, M.1    Chen, B.S.2    Diehl, A.G.3    Isaacs, G.D.4    Zhang, T.5    Siepel, A.C.6    Clark, A.G.7    Kraus, W.L.8
  • 116
    • 34347324118 scopus 로고    scopus 로고
    • Determinants of cell- and gene-specific transcriptional regulation by the glucocorticoid receptor
    • So AY, Chaivorapol C, Bolton EC, Li H, Yamamoto KR 2007 Determinants of cell- and gene-specific transcriptional regulation by the glucocorticoid receptor. PLoS Genet 3:e94
    • (2007) PLoS Genet , vol.3
    • So, A.Y.1    Chaivorapol, C.2    Bolton, E.C.3    Li, H.4    Yamamoto, K.R.5
  • 118
    • 44449126207 scopus 로고    scopus 로고
    • Conservation analysis predicts in vivo occupancy of glucocorticoid receptor-binding sequences at glucocorticoid-induced genes
    • So AY, Cooper SB, Feldman BJ, Manuchehri M, Yamamoto KR 2008 Conservation analysis predicts in vivo occupancy of glucocorticoid receptor-binding sequences at glucocorticoid-induced genes. Proc Natl Acad Sci USA 105:5745-5749
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 5745-5749
    • So, A.Y.1    Cooper, S.B.2    Feldman, B.J.3    Manuchehri, M.4    Yamamoto, K.R.5
  • 119
    • 3142596494 scopus 로고    scopus 로고
    • Transcriptional activation by nuclear receptors
    • Acevedo ML, Kraus WL 2004 Transcriptional activation by nuclear receptors. Essays Biochem 40:73-88
    • (2004) Essays Biochem , vol.40 , pp. 73-88
    • Acevedo, M.L.1    Kraus, W.L.2
  • 120
    • 33744792310 scopus 로고    scopus 로고
    • Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response
    • Rosenfeld MG, Lunyak VV, Glass CK 2006 Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response. Genes Dev 20:1405-1428
    • (2006) Genes Dev , vol.20 , pp. 1405-1428
    • Rosenfeld, M.G.1    Lunyak, V.V.2    Glass, C.K.3
  • 121
    • 0028901040 scopus 로고
    • Characterization of the amino-terminal transcriptional activation function of the human estrogen receptor in animal and yeast cells
    • Metzger D, Ali S, Bornert JM, Chambon P 1995 Characterization of the amino-terminal transcriptional activation function of the human estrogen receptor in animal and yeast cells. J Biol Chem 270:9535-9542
    • (1995) J Biol Chem , vol.270 , pp. 9535-9542
    • Metzger, D.1    Ali, S.2    Bornert, J.M.3    Chambon, P.4
  • 122
    • 0023794190 scopus 로고
    • Multiple and cooperative trans-activation domains of the human glucocorticoid receptor
    • Hollenberg SM, Evans RM 1988 Multiple and cooperative trans-activation domains of the human glucocorticoid receptor. Cell 55:899-906
    • (1988) Cell , vol.55 , pp. 899-906
    • Hollenberg, S.M.1    Evans, R.M.2
  • 123
    • 0028292958 scopus 로고
    • Delineation of a small region within the major transactivation domain of thehumanglucocorticoid receptor that mediates transactivation of gene expression
    • Dahlman-Wright K, Almlöf T, McEwan IJ, Gustafsson JA, Wright AP 1994 Delineation of a small region within the major transactivation domain of thehumanglucocorticoid receptor that mediates transactivation of gene expression. Proc Natl Acad Sci USA 91:1619-1623
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1619-1623
    • Dahlman-Wright, K.1    Almlöf, T.2    McEwan, I.J.3    Gustafsson, J.A.4    Wright, A.P.5
  • 124
    • 0040386484 scopus 로고    scopus 로고
    • Role of hydrophobic amino acid clusters in the transactivation activity of the human glucocorticoid receptor
    • Almlöf T, Gustafsson JA, Wright AP 1997 Role of hydrophobic amino acid clusters in the transactivation activity of the human glucocorticoid receptor. Mol Cell Biol 17:934-945
    • (1997) Mol Cell Biol , vol.17 , pp. 934-945
    • Almlöf, T.1    Gustafsson, J.A.2    Wright, A.P.3
  • 125
    • 0032581008 scopus 로고    scopus 로고
    • Role of important hydrophobic amino acids in the interaction between the glucocorticoid receptor τ 1-core activation domain and target factors
    • Almlöf T, Wallberg AE, Gustafsson JA, Wright AP 1998 Role of important hydrophobic amino acids in the interaction between the glucocorticoid receptor τ 1-core activation domain and target factors. Biochemistry 37:9586-9594
    • (1998) Biochemistry , vol.37 , pp. 9586-9594
    • Almlöf, T.1    Wallberg, A.E.2    Gustafsson, J.A.3    Wright, A.P.4
  • 126
    • 0029093343 scopus 로고
    • Role of acidic and phosphorylated residues in gene activation by the glucocorticoid receptor
    • Almlöf T, Wright AP, Gustafsson JA 1995 Role of acidic and phosphorylated residues in gene activation by the glucocorticoid receptor. J Biol Chem 270:17535-17540
    • (1995) J Biol Chem , vol.270 , pp. 17535-17540
    • Almlöf, T.1    Wright, A.P.2    Gustafsson, J.A.3
  • 127
    • 0031054799 scopus 로고    scopus 로고
    • Three amino acid substitutions selectively disrupt the activation but not the repression function of the glucocorticoid receptor N terminus
    • Iñiguez-Lluhí JA, Lou DY, Yamamoto KR 1997 Three amino acid substitutions selectively disrupt the activation but not the repression function of the glucocorticoid receptor N terminus. J Biol Chem 272:4149-4156
    • (1997) J Biol Chem , vol.272 , pp. 4149-4156
    • Iñiguez-Lluhí, J.A.1    Lou, D.Y.2    Yamamoto, K.R.3
  • 128
    • 0025957233 scopus 로고
    • Transcriptional activation and nuclear targeting signals of the human androgen receptor
    • Simental JA, SarM, LaneMV, French FS, WilsonEM1991 Transcriptional activation and nuclear targeting signals of the human androgen receptor. J Biol Chem 266:510-518
    • (1991) J Biol Chem , vol.266 , pp. 510-518
    • Simental, J.A.1    Sar, M.2    Lane, M.V.3    French, F.S.4    Wilson, E.M.5
  • 129
    • 0028904382 scopus 로고
    • Identification of two transcription activation units in the N-terminal domain of the human androgen receptor
    • Jenster G, van der Korput HA, Trapman J, BrinkmannAO 1995 Identification of two transcription activation units in the N-terminal domain of the human androgen receptor. J Biol Chem 270:7341-7346
    • (1995) J Biol Chem , vol.270 , pp. 7341-7346
    • Jenster, G.1    van der Korput, H.A.2    Trapman, J.3    Brinkmann, A.O.4
  • 130
    • 0029914188 scopus 로고    scopus 로고
    • Delineation of two distinct type 1 activation functions in the androgen receptor amino-terminal domain
    • Chamberlain NL, Whitacre DC, Miesfeld RL 1996 Delineation of two distinct type 1 activation functions in the androgen receptor amino-terminal domain. J Biol Chem 271:26772-26778
    • (1996) J Biol Chem , vol.271 , pp. 26772-26778
    • Chamberlain, N.L.1    Whitacre, D.C.2    Miesfeld, R.L.3
  • 131
    • 0346724760 scopus 로고    scopus 로고
    • Role of conserved hydrophobic amino acids in androgen receptor AF-1 function
    • Betney R, McEwan IJ 2003 Role of conserved hydrophobic amino acids in androgen receptor AF-1 function. J Mol Endocrinol 31:427-439
    • (2003) J Mol Endocrinol , vol.31 , pp. 427-439
    • Betney, R.1    McEwan, I.J.2
  • 133
    • 0032544740 scopus 로고    scopus 로고
    • Reconstitution of the Nterminal transcription activation function of human mineralocorticoid receptor in a defective human glucocorticoid receptor
    • Govindan MV, Warriar N 1998 Reconstitution of the Nterminal transcription activation function of human mineralocorticoid receptor in a defective human glucocorticoid receptor. J Biol Chem 273:24439-24447
    • (1998) J Biol Chem , vol.273 , pp. 24439-24447
    • Govindan, M.V.1    Warriar, N.2
  • 134
    • 0034464797 scopus 로고    scopus 로고
    • Characterization of transactivational property and coactivator mediation of rat mineralocorticoid receptor activation function-1 (AF-1)
    • Fuse H, Kitagawa H, Kato S 2000 Characterization of transactivational property and coactivator mediation of rat mineralocorticoid receptor activation function-1 (AF-1). Mol Endocrinol 14:889 -899
    • (2000) Mol Endocrinol , vol.14 , pp. 889-899
    • Fuse, H.1    Kitagawa, H.2    Kato, S.3
  • 135
    • 77957334372 scopus 로고    scopus 로고
    • Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure
    • Fischer K, Kelly SM, Watt K, Price NC, McEwan IJ 2010 Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure. Mol Endocrinol 24:1935-1948
    • (2010) Mol Endocrinol , vol.24 , pp. 1935-1948
    • Fischer, K.1    Kelly, S.M.2    Watt, K.3    Price, N.C.4    McEwan, I.J.5
  • 137
    • 69249090970 scopus 로고    scopus 로고
    • Direct interdomain interactions can mediate allosterism in the thyroid receptor
    • Putcha BD, Fernandez EJ 2009 Direct interdomain interactions can mediate allosterism in the thyroid receptor. J Biol Chem 284:22517-22524
    • (2009) J Biol Chem , vol.284 , pp. 22517-22524
    • Putcha, B.D.1    Fernandez, E.J.2
  • 139
    • 0024317270 scopus 로고
    • The human estrogen receptor has two independent nonacidic transcriptional activation functions
    • Tora L, White J, Brou C, Tasset D, Webster N, Scheer E, Chambon P 1989 The human estrogen receptor has two independent nonacidic transcriptional activation functions. Cell 59:477-487
    • (1989) Cell , vol.59 , pp. 477-487
    • Tora, L.1    White, J.2    Brou, C.3    Tasset, D.4    Webster, N.5    Scheer, E.6    Chambon, P.7
  • 140
    • 0037168648 scopus 로고    scopus 로고
    • Alternate surfaces of transcriptional coregulator GRIP1 function in different glucocorticoid receptor activation and repression contexts
    • Rogatsky I, Luecke HF, Leitman DC, Yamamoto KR 2002 Alternate surfaces of transcriptional coregulator GRIP1 function in different glucocorticoid receptor activation and repression contexts. Proc Natl Acad Sci USA 99:16701-16706
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16701-16706
    • Rogatsky, I.1    Luecke, H.F.2    Leitman, D.C.3    Yamamoto, K.R.4
  • 142
    • 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 277:26573-26580
    • (2002) J Biol Chem , vol.277 , pp. 26573-26580
    • Wang, Z.1    Frederick, J.2    Garabedian, M.J.3
  • 143
    • 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: 150-157
    • (2008) J Steroid Biochem Mol Biol , vol.109 , pp. 150-157
    • Blind, R.D.1    Garabedian, M.J.2
  • 145
    • 78149497463 scopus 로고    scopus 로고
    • Drugs for 'protein clouds': targeting intrinsically disordered transcription factors
    • Dunker AK, Uversky VN 2010 Drugs for 'protein clouds': targeting intrinsically disordered transcription factors. Curr Opin Pharmacol 10:782-788
    • (2010) Curr Opin Pharmacol , vol.10 , pp. 782-788
    • Dunker, A.K.1    Uversky, V.N.2
  • 147
    • 79960555958 scopus 로고    scopus 로고
    • Proteome-wide evidence for enhanced positive Darwinian selection within intrinsically disordered regions in proteins
    • Nilsson J, Grahn M, Wright AP 2011 Proteome-wide evidence for enhanced positive Darwinian selection within intrinsically disordered regions in proteins. Genome Biol 12:R65
    • (2011) Genome Biol , vol.12
    • Nilsson, J.1    Grahn, M.2    Wright, A.P.3
  • 149
    • 79958044914 scopus 로고    scopus 로고
    • Unstructural biology coming of age
    • Tompa P 2011 Unstructural biology coming of age. Curr Opin Struct Biol 21:419-425
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 419-425
    • Tompa, P.1
  • 150
    • 79958741408 scopus 로고    scopus 로고
    • Intrinsically disordered proteins fromA to Z
    • Uversky VN 2011 Intrinsically disordered proteins fromA to Z. Int J Biochem Cell Biol 43:1090-1103
    • (2011) Int J Biochem Cell Biol , vol.43 , pp. 1090-1103
    • Uversky, V.N.1
  • 153
    • 40949105259 scopus 로고    scopus 로고
    • Signal transduction via unstructured protein conduits
    • Dunker AK, Uversky VN 2008 Signal transduction via unstructured protein conduits. Nat Chem Biol 4:229-230
    • (2008) Nat Chem Biol , vol.4 , pp. 229-230
    • Dunker, A.K.1    Uversky, V.N.2
  • 155
    • 0037627721 scopus 로고    scopus 로고
    • Simulating disorder-order transitions in molecular recognition of unstructured proteins: where folding meets binding
    • Verkhivker GM, Bouzida D, Gehlhaar DK, Rejto PA, Freer ST, Rose PW 2003 Simulating disorder-order transitions in molecular recognition of unstructured proteins: where folding meets binding. Proc Natl Acad Sci USA 100:5148-5153
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5148-5153
    • Verkhivker, G.M.1    Bouzida, D.2    Gehlhaar, D.K.3    Rejto, P.A.4    Freer, S.T.5    Rose, P.W.6
  • 157
    • 77952335311 scopus 로고    scopus 로고
    • Net charge per residue modulates conformational ensembles of intrinsically disordered proteins
    • Mao AH, Crick SL, Vitalis A, Chicoine CL, Pappu RV 2010 Net charge per residue modulates conformational ensembles of intrinsically disordered proteins. Proc Natl Acad Sci USA 107:8183-8188
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 8183-8188
    • Mao, A.H.1    Crick, S.L.2    Vitalis, A.3    Chicoine, C.L.4    Pappu, R.V.5
  • 158
    • 77951174390 scopus 로고    scopus 로고
    • A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR
    • Wang X, Zhang S, Zhang J, Huang X, Xu C, Wang W, Liu Z, Wu J, Shi Y 2010 A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. J Biol Chem 285:4951-4963
    • (2010) J Biol Chem , vol.285 , pp. 4951-4963
    • Wang, X.1    Zhang, S.2    Zhang, J.3    Huang, X.4    Xu, C.5    Wang, W.6    Liu, Z.7    Wu, J.8    Shi, Y.9
  • 160
    • 33751079861 scopus 로고    scopus 로고
    • Intrinsically unstructured N-terminal domain of bZIP transcription factor HY5
    • Yoon MK, Shin J, Choi G, Choi BS 2006 Intrinsically unstructured N-terminal domain of bZIP transcription factor HY5. Proteins 65:856-866
    • (2006) Proteins , vol.65 , pp. 856-866
    • Yoon, M.K.1    Shin, J.2    Choi, G.3    Choi, B.S.4
  • 161
    • 77955442470 scopus 로고    scopus 로고
    • Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP
    • Kjaergaard M, Teilum K, Poulsen FM 2010 Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. Proc Natl Acad Sci USA 107:12535-12540
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 12535-12540
    • Kjaergaard, M.1    Teilum, K.2    Poulsen, F.M.3
  • 162
    • 73449123761 scopus 로고    scopus 로고
    • Unfoldomics of human genetic diseases: illustrative examples of ordered and intrinsically disordered members of the human diseasome
    • Midic U, Oldfield CJ, Dunker AK, Obradovic Z, Uversky VN 2009 Unfoldomics of human genetic diseases: illustrative examples of ordered and intrinsically disordered members of the human diseasome. Protein Pept Lett 16:1533-1547
    • (2009) Protein Pept Lett , vol.16 , pp. 1533-1547
    • Midic, U.1    Oldfield, C.J.2    Dunker, A.K.3    Obradovic, Z.4    Uversky, V.N.5
  • 163
    • 47649096991 scopus 로고    scopus 로고
    • Structural biology of the tumor suppressor p53
    • Joerger AC, Fersht AR 2008 Structural biology of the tumor suppressor p53. Annu Rev Biochem 77:557-582
    • (2008) Annu Rev Biochem , vol.77 , pp. 557-582
    • Joerger, A.C.1    Fersht, A.R.2
  • 164
    • 69949131670 scopus 로고    scopus 로고
    • Structural and functional relationships of the steroid hormone receptors' N-terminal transactivation domain
    • Kumar R, Litwack G 2009 Structural and functional relationships of the steroid hormone receptors' N-terminal transactivation domain. Steroids 74:877-883
    • (2009) Steroids , vol.74 , pp. 877-883
    • Kumar, R.1    Litwack, G.2
  • 165
    • 58249105355 scopus 로고    scopus 로고
    • Role of intrinsically disordered protein regions/domains in transcriptional regulation
    • Garza AS, Ahmad N, Kumar R 2009 Role of intrinsically disordered protein regions/domains in transcriptional regulation. Life Sci 84:189-193
    • (2009) Life Sci , vol.84 , pp. 189-193
    • Garza, A.S.1    Ahmad, N.2    Kumar, R.3
  • 166
    • 55949130323 scopus 로고    scopus 로고
    • Intrinsic disorder in nuclear hormone receptors
    • KrasowskiMD, Reschly EJ, Ekins S 2008 Intrinsic disorder in nuclear hormone receptors. J Proteome Res 7:4359-4372
    • (2008) J Proteome Res , vol.7 , pp. 4359-4372
    • Krasowski, M.D.1    Reschly, E.J.2    Ekins, S.3
  • 167
    • 48249097986 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in human diseases: introducing the D2 concept
    • Uversky VN, Oldfield CJ, Dunker AK 2008 Intrinsically disordered proteins in human diseases: introducing the D2 concept. Annu Rev Biophys 37:215-246
    • (2008) Annu Rev Biophys , vol.37 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 168
    • 34247571020 scopus 로고    scopus 로고
    • Posttranslational modifications and subcellular localization signals: indicators of sequence regions without inherent 3D structure?
    • Eisenhaber B, Eisenhaber F 2007 Posttranslational modifications and subcellular localization signals: indicators of sequence regions without inherent 3D structure? Curr Protein Pept Sci 8:197-203
    • (2007) Curr Protein Pept Sci , vol.8 , pp. 197-203
    • Eisenhaber, B.1    Eisenhaber, F.2
  • 169
    • 0033054115 scopus 로고    scopus 로고
    • The structure of the nuclear hormone receptors
    • Kumar R, Thompson EB 1999 The structure of the nuclear hormone receptors. Steroids 64:310-319
    • (1999) Steroids , vol.64 , pp. 310-319
    • Kumar, R.1    Thompson, E.B.2
  • 170
    • 3142716735 scopus 로고    scopus 로고
    • Overview of the structural basis for transcription regulation by nuclear hormone receptors
    • Kumar R, Johnson BH, Thompson EB 2004 Overview of the structural basis for transcription regulation by nuclear hormone receptors. Essays Biochem 40:27-39
    • (2004) Essays Biochem , vol.40 , pp. 27-39
    • Kumar, R.1    Johnson, B.H.2    Thompson, E.B.3
  • 171
    • 77949909289 scopus 로고    scopus 로고
    • Nuclear hormone receptor architecture-form and dynamics: the 2009 FASEB summer conference on dynamic structure of the nuclear hormone receptors
    • McEwan IJ, Nardulli AM 2009 Nuclear hormone receptor architecture-form and dynamics: the 2009 FASEB summer conference on dynamic structure of the nuclear hormone receptors. Nucl Recept Signal 7:e011
    • (2009) Nucl Recept Signal , vol.7
    • McEwan, I.J.1    Nardulli, A.M.2
  • 173
    • 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, Ji YS, Bolen DW, Thompson EB 1999 Trimethylamine N-oxide-induced cooperative folding of an intrinsically unfolded transcription-activating fragment of human glucocorticoid receptor. J Biol Chem 274:10693-10696
    • (1999) J Biol Chem , vol.274 , pp. 10693-10696
    • Baskakov, I.V.1    Kumar, R.2    Srinivasan, G.3    Ji, Y.S.4    Bolen, D.W.5    Thompson, E.B.6
  • 174
    • 0035968162 scopus 로고    scopus 로고
    • The N-terminal region of human progesterone B-receptors: biophysical and biochemical comparison to A-receptors
    • Bain DL, Franden MA, McManaman JL, Takimoto GS, Horwitz KB 2001 The N-terminal region of human progesterone B-receptors: biophysical and biochemical comparison to A-receptors. J Biol Chem 276:23825-23831
    • (2001) J Biol Chem , vol.276 , pp. 23825-23831
    • Bain, D.L.1    Franden, M.A.2    McManaman, J.L.3    Takimoto, G.S.4    Horwitz, K.B.5
  • 175
    • 0035824562 scopus 로고    scopus 로고
    • The N-terminal regions of estrogen receptor α and β are unstructured in vitro and show different TBP binding properties
    • Wärnmark A, Wikström A, Wright AP, Gustafsson JA, Härd T 2001 The N-terminal regions of estrogen receptor α and β are unstructured in vitro and show different TBP binding properties. J Biol Chem 276:45939-45944
    • (2001) J Biol Chem , vol.276 , pp. 45939-45944
    • Wärnmark, A.1    Wikström, A.2    Wright, A.P.3    Gustafsson, J.A.4    Härd, T.5
  • 176
    • 0037205522 scopus 로고    scopus 로고
    • Conformational analysis of the androgen receptor aminoterminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions
    • Reid J, Kelly SM, Watt K, Price NC, McEwan IJ 2002 Conformational analysis of the androgen receptor aminoterminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions. J Biol Chem 277:20079-20086
    • (2002) J Biol Chem , vol.277 , pp. 20079-20086
    • Reid, J.1    Kelly, S.M.2    Watt, K.3    Price, N.C.4    McEwan, I.J.5
  • 179
    • 40849102545 scopus 로고    scopus 로고
    • Functional characterization of the native NH2-terminal transactivation domain of the human androgen receptor: binding kinetics for interactions with TFIIF and SRC-1a
    • Lavery DN, McEwan IJ 2008 Functional characterization of the native NH2-terminal transactivation domain of the human androgen receptor: binding kinetics for interactions with TFIIF and SRC-1a. Biochemistry 47:3352-3359
    • (2008) Biochemistry , vol.47 , pp. 3352-3359
    • Lavery, D.N.1    McEwan, I.J.2
  • 180
    • 73549096417 scopus 로고    scopus 로고
    • Site-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor
    • Garza AM, Khan SH, Kumar R 2010 Site-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor. Mol Cell Biol 30:220-230
    • (2010) Mol Cell Biol , vol.30 , pp. 220-230
    • Garza, A.M.1    Khan, S.H.2    Kumar, R.3
  • 181
    • 75149130096 scopus 로고    scopus 로고
    • Partial agonist activity of the progesterone receptor antagonist RU486 mediated by an amino-terminal domain coactivator and phosphorylation of serine 400
    • Wardell SE, Narayanan R, Weigel NL, Edwards DP 2010 Partial agonist activity of the progesterone receptor antagonist RU486 mediated by an amino-terminal domain coactivator and phosphorylation of serine 400. Mol Endocrinol 24:335-345
    • (2010) Mol Endocrinol , vol.24 , pp. 335-345
    • Wardell, S.E.1    Narayanan, R.2    Weigel, N.L.3    Edwards, D.P.4
  • 182
    • 79960066455 scopus 로고    scopus 로고
    • TBP binding-induced folding of the glucocorticoid receptor AF1 domain facilitates its interaction with steroid receptor coactivator-1
    • Khan SH, Ling J, Kumar R 2011 TBP binding-induced folding of the glucocorticoid receptor AF1 domain facilitates its interaction with steroid receptor coactivator-1. PLoS One 6:e21939
    • (2011) PLoS One , vol.6
    • Khan, S.H.1    Ling, J.2    Kumar, R.3
  • 184
    • 21344441515 scopus 로고    scopus 로고
    • Intra-domain communication between the N-terminal and DNA-binding domains of the androgen receptor: modulation of androgen response element DNA binding
    • Brodie J, McEwan IJ 2005 Intra-domain communication between the N-terminal and DNA-binding domains of the androgen receptor: modulation of androgen response element DNA binding. J Mol Endocrinol 34:603-615
    • (2005) J Mol Endocrinol , vol.34 , pp. 603-615
    • Brodie, J.1    McEwan, I.J.2
  • 186
    • 0141640853 scopus 로고    scopus 로고
    • The cochaperone Bag-1L enhances androgen receptor action via interaction with the NH2-terminal region of the receptor
    • Shatkina L, Mink S, Rogatsch H, Klocker H, Langer G, Nestl A, Cato AC 2003 The cochaperone Bag-1L enhances androgen receptor action via interaction with the NH2-terminal region of the receptor. Mol Cell Biol 23:7189-7197
    • (2003) Mol Cell Biol , vol.23 , pp. 7189-7197
    • Shatkina, L.1    Mink, S.2    Rogatsch, H.3    Klocker, H.4    Langer, G.5    Nestl, A.6    Cato, A.C.7
  • 187
    • 0035947672 scopus 로고    scopus 로고
    • The conformation of the glucocorticoid receptor af1/tau1 domain induced by osmolyte binds co-regulatory proteins
    • Kumar R, Lee JC, Bolen DW, Thompson EB 2001 The conformation of the glucocorticoid receptor af1/tau1 domain induced by osmolyte binds co-regulatory proteins. J Biol Chem 276:18146-18152
    • (2001) J Biol Chem , vol.276 , pp. 18146-18152
    • Kumar, R.1    Lee, J.C.2    Bolen, D.W.3    Thompson, E.B.4
  • 188
    • 1542743970 scopus 로고    scopus 로고
    • Induced α-helix structure in AF1 of the androgen receptor upon binding transcription factor TFIIF
    • Kumar R, Betney R, Li J, Thompson EB, McEwan IJ 2004 Induced α-helix structure in AF1 of the androgen receptor upon binding transcription factor TFIIF. Biochemistry 43: 3008-3013
    • (2004) Biochemistry , vol.43 , pp. 3008-3013
    • Kumar, R.1    Betney, R.2    Li, J.3    Thompson, E.B.4    McEwan, I.J.5
  • 189
    • 40849144778 scopus 로고    scopus 로고
    • Structural characterization of the native NH2-terminal transactivation domain of the human androgen receptor: a collapsed disordered conformation underlies structural plasticity and protein-induced folding
    • Lavery DN, McEwan IJ 2008 Structural characterization of the native NH2-terminal transactivation domain of the human androgen receptor: a collapsed disordered conformation underlies structural plasticity and protein-induced folding. Biochemistry 47:3360-3369
    • (2008) Biochemistry , vol.47 , pp. 3360-3369
    • Lavery, D.N.1    McEwan, I.J.2
  • 190
    • 79956121909 scopus 로고    scopus 로고
    • Naturally occurring osmolyte, trehalose induces functional conformation in an intrinsically disordered activation domain of glucocorticoid receptor
    • Khan SH, Arnott JA, Kumar R 2011 Naturally occurring osmolyte, trehalose induces functional conformation in an intrinsically disordered activation domain of glucocorticoid receptor. PLoS One 6:e19689
    • (2011) PLoS One , vol.6
    • Khan, S.H.1    Arnott, J.A.2    Kumar, R.3
  • 191
    • 0030070502 scopus 로고    scopus 로고
    • Structural studies of mutant glucocorticoid receptor transactivation domains establish a link between transactivation activity in vivo and α-helix-forming potential in vitro
    • Dahlman-Wright K, McEwan IJ 1996 Structural studies of mutant glucocorticoid receptor transactivation domains establish a link between transactivation activity in vivo and α-helix-forming potential in vitro. Biochemistry 35:1323-1327
    • (1996) Biochemistry , vol.35 , pp. 1323-1327
    • Dahlman-Wright, K.1    McEwan, I.J.2
  • 192
    • 0037162456 scopus 로고    scopus 로고
    • Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components
    • Timasheff SN 2002 Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components. Proc Natl Acad Sci USA 99:9721-9726
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9721-9726
    • Timasheff, S.N.1
  • 193
    • 33749365298 scopus 로고    scopus 로고
    • A molecular mechanism for osmolyte-induced protein stability
    • Street TO, Bolen DW, Rose GD 2006 A molecular mechanism for osmolyte-induced protein stability. Proc Natl Acad Sci USA 103:13997-14002
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13997-14002
    • Street, T.O.1    Bolen, D.W.2    Rose, G.D.3
  • 194
    • 70350337659 scopus 로고    scopus 로고
    • Role of naturally occurring osmolytes in protein folding and stability
    • Kumar R 2009 Role of naturally occurring osmolytes in protein folding and stability. Arch Biochem Biophys 491: 1-6
    • (2009) Arch Biochem Biophys , vol.491 , pp. 1-6
    • Kumar, R.1
  • 195
    • 76749109966 scopus 로고    scopus 로고
    • Hydrogen bonding progressively strengthens upon transfer of the protein urea-denatured state to water and protecting osmolytes
    • Holthauzen LM, Rösgen J, Bolen DW 2010 Hydrogen bonding progressively strengthens upon transfer of the protein urea-denatured state to water and protecting osmolytes. Biochemistry 49:1310-1318
    • (2010) Biochemistry , vol.49 , pp. 1310-1318
    • Holthauzen, L.M.1    Rösgen, J.2    Bolen, D.W.3
  • 196
    • 34548396816 scopus 로고    scopus 로고
    • Effects of different osmolytes on the induced folding of the N-terminal activation domain (AF1) of the glucocorticoid receptor
    • Kumar R, Serrette JM, Khan SH, Miller AL, ThompsonEB 2007 Effects of different osmolytes on the induced folding of the N-terminal activation domain (AF1) of the glucocorticoid receptor. Arch Biochem Biophys 465:452-460
    • (2007) Arch Biochem Biophys , vol.465 , pp. 452-460
    • Kumar, R.1    Serrette, J.M.2    Khan, S.H.3    Miller, A.L.4    Thompson, E.B.5
  • 197
    • 54349095652 scopus 로고    scopus 로고
    • Osmolyte-induced folding of an intrinsically disordered activation function subdomain of glucocorticoid receptor
    • Kumar R 2008 Osmolyte-induced folding of an intrinsically disordered activation function subdomain of glucocorticoid receptor. J Recept Signal Transduct Res 28:465-474
    • (2008) J Recept Signal Transduct Res , vol.28 , pp. 465-474
    • Kumar, R.1
  • 199
    • 0035976933 scopus 로고    scopus 로고
    • Estrogen response elements alter coactivator recruitment through allosteric modulation of estrogen receptor β conformation
    • Loven MA, Likhite VS, Choi I, Nardulli AM 2001 Estrogen response elements alter coactivator recruitment through allosteric modulation of estrogen receptor β conformation. J Biol Chem 276:45282-45288
    • (2001) J Biol Chem , vol.276 , pp. 45282-45288
    • Loven, M.A.1    Likhite, V.S.2    Choi, I.3    Nardulli, A.M.4
  • 200
    • 0031900850 scopus 로고    scopus 로고
    • Estrogen response elements function as allosteric modulators of estrogen receptor conformation
    • Wood JR, Greene GL, Nardulli AM 1998 Estrogen response elements function as allosteric modulators of estrogen receptor conformation. Mol Cell Biol 18:1927-1934
    • (1998) Mol Cell Biol , vol.18 , pp. 1927-1934
    • Wood, J.R.1    Greene, G.L.2    Nardulli, A.M.3
  • 201
    • 0034969440 scopus 로고    scopus 로고
    • Allosteric modulation of estrogen receptor conformation by different estrogen response elements
    • Wood JR, Likhite VS, Loven MA, Nardulli AM 2001 Allosteric modulation of estrogen receptor conformation by different estrogen response elements. Mol Endocrinol 15: 1114-1126
    • (2001) Mol Endocrinol , vol.15 , pp. 1114-1126
    • Wood, J.R.1    Likhite, V.S.2    Loven, M.A.3    Nardulli, A.M.4
  • 202
    • 0036262430 scopus 로고    scopus 로고
    • PS2 Gene expression in HepG2 cells: complex regulation through crosstalk between the estrogen receptor α, an estrogen-responsive element, and the activator protein 1 response element
    • Barkhem T, Haldosén LA, Gustafsson JA, Nilsson S 2002 PS2 Gene expression in HepG2 cells: complex regulation through crosstalk between the estrogen receptor α, an estrogen-responsive element, and the activator protein 1 response element. Mol Pharmacol 61:1273-1283
    • (2002) Mol Pharmacol , vol.61 , pp. 1273-1283
    • Barkhem, T.1    Haldosén, L.A.2    Gustafsson, J.A.3    Nilsson, S.4
  • 203
    • 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. Endocr Rev 20:321-344
    • (1999) Endocr Rev , vol.20 , pp. 321-344
    • McKenna, N.J.1    Lanz, R.B.2    O'Malley, B.W.3
  • 205
    • 0029740873 scopus 로고    scopus 로고
    • Functional interaction of the c-Myc transactivation domain with the TATA binding protein: evidence for an induced fit model of transactivation domain folding
    • McEwan IJ, Dahlman-Wright K, Ford J, Wright AP 1996 Functional interaction of the c-Myc transactivation domain with the TATA binding protein: evidence for an induced fit model of transactivation domain folding. Biochemistry 35:9584-9593
    • (1996) Biochemistry , vol.35 , pp. 9584-9593
    • McEwan, I.J.1    Dahlman-Wright, K.2    Ford, J.3    Wright, A.P.4
  • 206
    • 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
  • 210
    • 0033512783 scopus 로고    scopus 로고
    • The AF1 and AF2 domains of the androgen receptor interact with distinct regions of SRC1
    • Bevan CL, Hoare S, Claessens F, Heery DM, Parker MG 1999 The AF1 and AF2 domains of the androgen receptor interact with distinct regions of SRC1. Mol Cell Biol 19: 8383-8392
    • (1999) Mol Cell Biol , vol.19 , pp. 8383-8392
    • Bevan, C.L.1    Hoare, S.2    Claessens, F.3    Heery, D.M.4    Parker, M.G.5
  • 211
    • 0034252288 scopus 로고    scopus 로고
    • Synergy between estrogen receptor α activation functions AF1 and AF2 mediated by transcription intermediary factor TIF2
    • Benecke A, Chambon P, Gronemeyer H 2000 Synergy between estrogen receptor α activation functions AF1 and AF2 mediated by transcription intermediary factor TIF2. EMBO Rep 1:151-157
    • (2000) EMBO Rep , vol.1 , pp. 151-157
    • Benecke, A.1    Chambon, P.2    Gronemeyer, H.3
  • 212
    • 0032524634 scopus 로고    scopus 로고
    • The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors
    • Onate SA, Boonyaratanakornkit V, Spencer TE, Tsai SY, Tsai MJ, Edwards DP, O'Malley BW 1998 The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors. J Biol Chem 273:12101-12108
    • (1998) J Biol Chem , vol.273 , pp. 12101-12108
    • Onate, S.A.1    Boonyaratanakornkit, V.2    Spencer, T.E.3    Tsai, S.Y.4    Tsai, M.J.5    Edwards, D.P.6    O'Malley, B.W.7
  • 214
    • 34250821717 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding of an intrinsically disordered protein
    • Sugase K, Dyson HJ, Wright PE 2007 Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature 447:1021-1025
    • (2007) Nature , vol.447 , pp. 1021-1025
    • Sugase, K.1    Dyson, H.J.2    Wright, P.E.3
  • 215
    • 0037174886 scopus 로고    scopus 로고
    • The androgen receptor interacts with multiple regions of the large subunit of general transcription factor TFIIF
    • Reid J, Murray I, Watt K, Betney R, McEwan IJ 2002 The androgen receptor interacts with multiple regions of the large subunit of general transcription factor TFIIF. J Biol Chem 277:41247-41253
    • (2002) J Biol Chem , vol.277 , pp. 41247-41253
    • Reid, J.1    Murray, I.2    Watt, K.3    Betney, R.4    McEwan, I.J.5
  • 216
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: the flycasting mechanism
    • Shoemaker BA, Portman JJ, Wolynes PG 2000 Speeding molecular recognition by using the folding funnel: the flycasting mechanism. Proc Natl Acad Sci USA 97:8868-8873
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 217
    • 0035955635 scopus 로고    scopus 로고
    • How transcriptional activators bind target proteins
    • Hermann S, Berndt KD, Wright AP 2001 How transcriptional activators bind target proteins. J Biol Chem 276: 40127-40132
    • (2001) J Biol Chem , vol.276 , pp. 40127-40132
    • Hermann, S.1    Berndt, K.D.2    Wright, A.P.3
  • 220
    • 0036829096 scopus 로고    scopus 로고
    • Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators
    • Zor T, Mayr BM, Dyson HJ, Montminy MR, Wright PE 2002 Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators. J Biol Chem 277:42241-42248
    • (2002) J Biol Chem , vol.277 , pp. 42241-42248
    • Zor, T.1    Mayr, B.M.2    Dyson, H.J.3    Montminy, M.R.4    Wright, P.E.5
  • 221
    • 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
  • 223
    • 79952155998 scopus 로고    scopus 로고
    • Lysine methylation and functional modulation of androgen receptor by Set9 methyltransferase
    • Ko S, Ahn J, Song CS, Kim S, Knapczyk-Stwora K, Chatterjee B 2011 Lysine methylation and functional modulation of androgen receptor by Set9 methyltransferase. Mol Endocrinol 25:433-444
    • (2011) Mol Endocrinol , vol.25 , pp. 433-444
    • Ko, S.1    Ahn, J.2    Song, C.S.3    Kim, S.4    Knapczyk-Stwora, K.5    Chatterjee, B.6
  • 224
    • 40849126935 scopus 로고    scopus 로고
    • Phosphorylation-dependent sumoylation regulates estrogen-related receptor-α and -γ transcriptional activity through a synergy control motif
    • TremblayAM, Wilson BJ, Yang XJ, Giguère V 2008 Phosphorylation-dependent sumoylation regulates estrogen-related receptor-α and -γ transcriptional activity through a synergy control motif. Mol Endocrinol 22:570-584
    • (2008) Mol Endocrinol , vol.22 , pp. 570-584
    • Tremblay, A.M.1    Wilson, B.J.2    Yang, X.J.3    Giguère, V.4
  • 225
    • 34948900221 scopus 로고    scopus 로고
    • Steroid receptor phosphorylation: a key modulator of multiple receptor functions
    • Weigel NL, Moore NL 2007 Steroid receptor phosphorylation: a key modulator of multiple receptor functions.Mol Endocrinol 21:2311-2319
    • (2007) Mol Endocrinol , vol.21 , pp. 2311-2319
    • Weigel, N.L.1    Moore, N.L.2
  • 226
    • 0033636597 scopus 로고    scopus 로고
    • Activation of estrogen receptor α by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7
    • Chen D, Riedl T, Washbrook E, Pace PE, Coombes RC, Egly JM, Ali S 2000 Activation of estrogen receptor α by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7. Mol Cell 6:127-137
    • (2000) Mol Cell , vol.6 , pp. 127-137
    • Chen, D.1    Riedl, T.2    Washbrook, E.3    Pace, P.E.4    Coombes, R.C.5    Egly, J.M.6    Ali, S.7
  • 227
    • 22344458207 scopus 로고    scopus 로고
    • P38 Mitogen-activated protein kinase(MAPK)is a key mediator in glucocorticoidinduced apoptosis of lymphoid cells: correlation between p38MAPKactivation and site-specific phosphorylation of the human glucocorticoid receptor at serine 211
    • Miller AL, Webb MS, Copik AJ, Wang Y, Johnson BH, Kumar R, Thompson EB 2005 P38 Mitogen-activated protein kinase(MAPK)is a key mediator in glucocorticoidinduced apoptosis of lymphoid cells: correlation between p38MAPKactivation and site-specific phosphorylation of the human glucocorticoid receptor at serine 211. Mol Endocrinol 19:1569-1583
    • (2005) Mol Endocrinol , vol.19 , pp. 1569-1583
    • Miller, A.L.1    Webb, M.S.2    Copik, A.J.3    Wang, Y.4    Johnson, B.H.5    Kumar, R.6    Thompson, E.B.7
  • 229
    • 33748579587 scopus 로고    scopus 로고
    • Alternative O-GlcN acylation/O-phosphorylation of Ser16 induce different conformational disturbances to theNterminus of murine estrogen receptorβ
    • Chen YX, Du JT, Zhou LX, Liu XH, Zhao YF, Nakanishi H, Li YM 2006 Alternative O-GlcN acylation/O-phosphorylation of Ser16 induce different conformational disturbances to theNterminus of murine estrogen receptorβ. Chem Biol 13:937-944
    • (2006) Chem Biol , vol.13 , pp. 937-944
    • Chen, Y.X.1    Du, J.T.2    Zhou, L.X.3    Liu, X.H.4    Zhao, Y.F.5    Nakanishi, H.6    Li, Y.M.7
  • 230
    • 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 392:885-888
    • (1998) Nature , vol.392 , pp. 885-888
    • Lefstin, J.A.1    Yamamoto, K.R.2
  • 232
    • 34347235156 scopus 로고    scopus 로고
    • Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins
    • Hilser VJ, Thompson EB 2007 Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins. Proc Natl Acad Sci USA 104:8311-8315
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8311-8315
    • Hilser, V.J.1    Thompson, E.B.2
  • 233
    • 77951024989 scopus 로고    scopus 로고
    • Influence of flanking sequences on signaling between the activation function AF1 and DNA-binding domain of the glucocorticoid receptor
    • Kumar R, Thompson EB 2010 Influence of flanking sequences on signaling between the activation function AF1 and DNA-binding domain of the glucocorticoid receptor. Arch Biochem Biophys 496:140-145
    • (2010) Arch Biochem Biophys , vol.496 , pp. 140-145
    • Kumar, R.1    Thompson, E.B.2
  • 234
    • 0002366905 scopus 로고    scopus 로고
    • Selective estrogen receptor modulators (SERMs): a first step in the development of perfect hormone replacement therapy regimen
    • McDonnell DP 2000 Selective estrogen receptor modulators (SERMs): a first step in the development of perfect hormone replacement therapy regimen. J Soc Gynecol Investig 7:S10-S15
    • (2000) J Soc Gynecol Investig , vol.7
    • McDonnell, D.P.1
  • 235
    • 0034735872 scopus 로고    scopus 로고
    • Development of peptide antagonists that target estrogen receptor-cofactor interactions
    • McDonnell DP, Chang CY, Norris JD 2000 Development of peptide antagonists that target estrogen receptor-cofactor interactions. J Steroid Biochem Mol Biol 74:327-335
    • (2000) J Steroid Biochem Mol Biol , vol.74 , pp. 327-335
    • McDonnell, D.P.1    Chang, C.Y.2    Norris, J.D.3
  • 242
    • 57749092687 scopus 로고    scopus 로고
    • Consequences of poly-glutamine repeat length for the conformation and folding of the androgen receptor amino-terminal domain
    • Davies P, Watt K, Kelly SM, Clark C, Price NC, McEwan IJ 2008 Consequences of poly-glutamine repeat length for the conformation and folding of the androgen receptor amino-terminal domain. J Mol Endocrinol 41:301-314
    • (2008) J Mol Endocrinol , vol.41 , pp. 301-314
    • Davies, P.1    Watt, K.2    Kelly, S.M.3    Clark, C.4    Price, N.C.5    McEwan, I.J.6
  • 243
    • 9344227341 scopus 로고    scopus 로고
    • TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain
    • Kumar R, Volk DE, Li J, Lee JC, Gorenstein DG, Thompson EB 2004 TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain. Proc Natl Acad Sci USA 101:16425-16430
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16425-16430
    • Kumar, R.1    Volk, D.E.2    Li, J.3    Lee, J.C.4    Gorenstein, D.G.5    Thompson, E.B.6
  • 244
    • 67650218286 scopus 로고    scopus 로고
    • Isoform-specific variation in the intrinsic disorder of the ecdysteroid receptor N-terminal domain
    • Nocula-£ugowska M, Rymarczyk G, Lisowski M, Ozyhar A 2009 Isoform-specific variation in the intrinsic disorder of the ecdysteroid receptor N-terminal domain. Proteins 76:291-308
    • (2009) Proteins , vol.76 , pp. 291-308
    • Nocula-ugowska, M.1    Rymarczyk, G.2    Lisowski, M.3    Ozyhar, A.4
  • 246
    • 3142672066 scopus 로고    scopus 로고
    • An androgen receptor NH2-terminal conserved motif interacts with the COOH terminus of the Hsp70-interacting protein (CHIP)
    • He B, Bai S, Hnat AT, Kalman RI, Minges JT, Patterson C, Wilson EM 2004 An androgen receptor NH2-terminal conserved motif interacts with the COOH terminus of the Hsp70-interacting protein (CHIP). J Biol Chem 279: 30643-30653
    • (2004) J Biol Chem , vol.279 , pp. 30643-30653
    • He, B.1    Bai, S.2    Hnat, A.T.3    Kalman, R.I.4    Minges, J.T.5    Patterson, C.6    Wilson, E.M.7
  • 248
    • 20744437001 scopus 로고    scopus 로고
    • RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins
    • Yang ZR, Thomson R, McNeil P, Esnouf RM 2005 RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins. Bioinformatics 21:3369-3376
    • (2005) Bioinformatics , vol.21 , pp. 3369-3376
    • Yang, Z.R.1    Thomson, R.2    McNeil, P.3    Esnouf, R.M.4
  • 249
    • 0042622240 scopus 로고    scopus 로고
    • Glob-Plot: exploring protein sequences for globularity and disorder
    • Linding R, Russell RB, Neduva V, Gibson TJ 2003 Glob-Plot: exploring protein sequences for globularity and disorder. Nucleic Acids Res 31:3701-3708
    • (2003) Nucleic Acids Res , vol.31 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.