메뉴 건너뛰기




Volumn 28, Issue 2, 2014, Pages 173-182

Minireview: Dynamic structures of nuclear hormone receptors: New promises and challenges

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION FUNCTION 1 PROTEIN; CELL NUCLEUS RECEPTOR; INTRINSICALLY DISORDERED PROTEIN; PROTEIN; UNCLASSIFIED DRUG; CELL RECEPTOR;

EID: 84892495900     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2013-1334     Document Type: Review
Times cited : (67)

References (93)
  • 1
    • 84862635896 scopus 로고    scopus 로고
    • Allosteric modulators of steroid hormone receptors: Structural dynamics and gene regulation
    • Kumar R, McEwan IJ. Allosteric modulators of steroid hormone receptors: structural dynamics and gene regulation. Endocr Rev. 2012;33(2):271-299.
    • (2012) Endocr Rev. , vol.33 , Issue.2 , pp. 271-299
    • Kumar, R.1    McEwan, I.J.2
  • 2
    • 80053562371 scopus 로고    scopus 로고
    • Development of subtypeselective oestrogen receptor-based therapeutics
    • Nilsson S, Koehler KF, Gustafsson J Å. Development of subtypeselective oestrogen receptor-based therapeutics. Nat Rev Drug Discov. 2011;10(10):778-792.
    • (2011) Nat Rev Drug Discov. , vol.10 , Issue.10 , pp. 778-792
    • Nilsson, S.1    Koehler, K.F.2    Gustafsson, J.Å.3
  • 3
    • 78149501152 scopus 로고    scopus 로고
    • The molecular mechanisms underlying the pharmacological actions of ER modulators: Implications for new drug discovery in breast cancer
    • McDonnell DP, Wardell SE. The molecular mechanisms underlying the pharmacological actions of ER modulators: implications for new drug discovery in breast cancer. Curr Opin Pharmacol. 2010;10(6):620-628.
    • (2010) Curr Opin Pharmacol. , vol.10 , Issue.6 , pp. 620-628
    • McDonnell, D.P.1    Wardell, S.E.2
  • 4
    • 79953005347 scopus 로고    scopus 로고
    • Small molecule inhibitors as probes for estrogen and androgen receptor action
    • Shapiro DJ, Mao C, Cherian MT. Small molecule inhibitors as probes for estrogen and androgen receptor action. J Biol Chem. 2011;286(6):4043-4048.
    • (2011) J Biol Chem. , vol.286 , Issue.6 , pp. 4043-4048
    • Shapiro, D.J.1    Mao, C.2    Cherian, M.T.3
  • 5
    • 82655174048 scopus 로고    scopus 로고
    • Steroid receptor coactivators 1, 2, and 3: Critical regulators of nuclear receptor activity and steroid receptor modulator (SRM)-based cancer therapy
    • Johnson AB, O'Malley BW. Steroid receptor coactivators 1, 2, and 3: critical regulators of nuclear receptor activity and steroid receptor modulator (SRM)-based cancer therapy. Mol Cell Endocrinol. 2012;348(2):430-439.
    • (2012) Mol Cell Endocrinol. , vol.348 , Issue.2 , pp. 430-439
    • Johnson, A.B.1    O'Malley, B.W.2
  • 6
    • 84885711476 scopus 로고    scopus 로고
    • Cross-talk between the ligand-and DNA-binding domains of estrogen receptor
    • Huang W, Greene GL, Ravikumar KM, Yang S. Cross-talk between the ligand-and DNA-binding domains of estrogen receptor. Proteins. 2013;81(11):1909-1919.
    • (2013) Proteins. , vol.81 , Issue.11 , pp. 1909-1919
    • Huang, W.1    Greene, G.L.2    Ravikumar, K.M.3    Yang, S.4
  • 7
    • 0030667676 scopus 로고    scopus 로고
    • Molecular basis of agonism and antagonism in the oestrogen receptor
    • Brzozowski AM, Pike AC, Dauter Z, et al. Molecular basis of agonism and antagonism in the oestrogen receptor. Nature. 1997;389(6652):753-758.
    • (1997) Nature. , vol.389 , Issue.6652 , pp. 753-758
    • Brzozowski, A.M.1    Pike, A.C.2    Dauter, Z.3
  • 8
    • 18944381947 scopus 로고    scopus 로고
    • Structural basis for an unexpected mode of SERM-mediated ER antagonism
    • Wu YL, Yang X, Ren Z, et al. Structural basis for an unexpected mode of SERM-mediated ER antagonism. Mol Cell. 2005;18(4): 413-424.
    • (2005) Mol Cell. , vol.18 , Issue.4 , pp. 413-424
    • Wu, Y.L.1    Yang, X.2    Ren, Z.3
  • 9
    • 34547653666 scopus 로고    scopus 로고
    • Structural plasticity in the oestrogen receptor ligand-binding domain
    • Nettles KW, Bruning JB, Gil G, et al. Structural plasticity in the oestrogen receptor ligand-binding domain. EMBO Rep. 2007;8(6): 563-568.
    • (2007) EMBO Rep. , vol.8 , Issue.6 , pp. 563-568
    • Nettles, K.W.1    Bruning, J.B.2    Gil, G.3
  • 10
    • 0023794190 scopus 로고
    • Multiple and cooperative trans-activation domains of the human glucocorticoid receptor
    • Hollenberg SM, Evans RM. Multiple and cooperative trans-activation domains of the human glucocorticoid receptor. Cell. 1988;55(5):899-906.
    • (1988) Cell. , vol.55 , Issue.5 , pp. 899-906
    • Hollenberg, S.M.1    Evans, R.M.2
  • 11
    • 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, et al. 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. 1998;273(20):12101-12108.
    • (1998) J Biol Chem. , vol.273 , Issue.20 , pp. 12101-12108
    • Onate, S.A.1    Boonyaratanakornkit, V.2    Spencer, T.E.3
  • 12
    • 18344380994 scopus 로고    scopus 로고
    • Ligand-selective potentiation of rat mineralocorticoid receptor activation function 1 by a CBP-containing histone acetyltransferase complex
    • Kitagawa H, Yanagisawa J, Fuse H, et al. Ligand-selective potentiation of rat mineralocorticoid receptor activation function 1 by a CBP-containing histone acetyltransferase complex. Mol Cell Biol. 2002;22(11):3698-3706.
    • (2002) Mol Cell Biol. , vol.22 , Issue.11 , pp. 3698-3706
    • Kitagawa, H.1    Yanagisawa, J.2    Fuse, H.3
  • 14
    • 78149497463 scopus 로고    scopus 로고
    • Drugs for 'protein clouds': Targeting intrinsically disordered transcription factors
    • Dunker AK, Uversky VN. Drugs for 'protein clouds': targeting intrinsically disordered transcription factors. Curr Opin Pharmacol. 2010;10(6):782-788.
    • (2010) Curr Opin Pharmacol. , vol.10 , Issue.6 , pp. 782-788
    • Dunker, A.K.1    Uversky, V.N.2
  • 15
    • 84879327823 scopus 로고    scopus 로고
    • Modulation of allostery by protein intrinsic disorder
    • Ferreon AC, Ferreon JC, Wright PE, Deniz AA. Modulation of allostery by protein intrinsic disorder. Nature. 2013;498(7454): 390-394.
    • (2013) Nature. , vol.498 , Issue.7454 , pp. 390-394
    • Ferreon, A.C.1    Ferreon, J.C.2    Wright, P.E.3    Deniz, A.A.4
  • 16
    • 0037203771 scopus 로고    scopus 로고
    • Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators
    • Demarest SJ, Martinez-Yamout M, Chung J, et al. Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. Nature. 2002;415(6871):549-553.
    • (2002) Nature. , vol.415 , Issue.6871 , pp. 549-553
    • Demarest, S.J.1    Martinez-Yamout, M.2    Chung, J.3
  • 17
    • 34250815165 scopus 로고    scopus 로고
    • Characterization of molecular recognition features, MoRFs, and their binding partners
    • Vacic V, Oldfield CJ, Mohan A, et al. Characterization of molecular recognition features, MoRFs, and their binding partners. J Proteome Res. 2007;6(6):2351-2366.
    • (2007) J Proteome Res. , vol.6 , Issue.6 , pp. 2351-2366
    • Vacic, V.1    Oldfield, C.J.2    Mohan, A.3
  • 18
    • 40949105259 scopus 로고    scopus 로고
    • Signal transduction via unstructured protein conduits
    • Dunker AK, Uversky VN. Signal transduction via unstructured protein conduits. Nat Chem Biol. 2008;4(4):229-230.
    • (2008) Nat Chem Biol. , vol.4 , Issue.4 , pp. 229-230
    • Dunker, A.K.1    Uversky, V.N.2
  • 20
    • 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. Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure. Mol Endocrinol. 2010;24(10):1935-1948.
    • (2010) Mol Endocrinol. , vol.24 , Issue.10 , pp. 1935-1948
    • Fischer, K.1    Kelly, S.M.2    Watt, K.3    Price, N.C.4    McEwan, I.J.5
  • 21
    • 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. The conformation of the glucocorticoid receptor af1/tau1 domain induced by osmolyte binds co-regulatory proteins. J Biol Chem. 2001;276(21):18146-18152.
    • (2001) J Biol Chem. , vol.276 , Issue.21 , pp. 18146-18152
    • Kumar, R.1    Lee, J.C.2    Bolen, D.W.3    Thompson, E.B.4
  • 22
    • 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. The N-terminal region of human progesterone B-receptors: biophysical and biochemical comparison to A-receptors. J Biol Chem. 2001;276(26):23825-23831.
    • (2001) J Biol Chem. , vol.276 , Issue.26 , pp. 23825-23831
    • Bain, D.L.1    Franden, M.A.2    McManaman, J.L.3    Takimoto, G.S.4    Horwitz, K.B.5
  • 23
    • 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. The N-terminal regions of estrogen receptor α and β are unstructured in vitro and show different TBP binding properties. J Biol Chem. 2001;276(49):45939-45944.
    • (2001) J Biol Chem. , vol.276 , Issue.49 , pp. 45939-45944
    • Wärnmark, A.1    Wikström, A.2    Wright, A.P.3    Gustafsson, J.A.4    Härd, T.5
  • 24
    • 0037205522 scopus 로고    scopus 로고
    • Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions
    • Reid J, Kelly SM, Watt K, Price NC, McEwan IJ. Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions. J Biol Chem. 2002;277(22):20079-20086.
    • (2002) J Biol Chem. , vol.277 , Issue.22 , pp. 20079-20086
    • Reid, J.1    Kelly, S.M.2    Watt, K.3    Price, N.C.4    McEwan, I.J.5
  • 25
    • 84871741777 scopus 로고    scopus 로고
    • Binding of the N-terminal region of coactivator TIF2 to the intrinsically disordered AF1 domain of the glucocorticoid receptor is accompanied by conformational reorganizations
    • Khan SH, Awasthi S, Guo C, et al. Binding of the N-terminal region of coactivator TIF2 to the intrinsically disordered AF1 domain of the glucocorticoid receptor is accompanied by conformational reorganizations. J Biol Chem. 2012;287(53):44546-44560.
    • (2012) J Biol Chem. , vol.287 , Issue.53 , pp. 44546-44560
    • Khan, S.H.1    Awasthi, S.2    Guo, C.3
  • 26
    • 33144462544 scopus 로고    scopus 로고
    • Probing protein ligand interactions by automated hydrogen/deuterium exchange mass spectrometry
    • Chalmers MJ, Busby SA, Pascal BD, et al. Probing protein ligand interactions by automated hydrogen/deuterium exchange mass spectrometry. Anal Chem. 2006;78(4):1005-1014.
    • (2006) Anal Chem. , vol.78 , Issue.4 , pp. 1005-1014
    • Chalmers, M.J.1    Busby, S.A.2    Pascal, B.D.3
  • 27
    • 35148887302 scopus 로고    scopus 로고
    • Partial agonists activate PPARγ using a helix 12 independent mechanism
    • Bruning JB, Chalmers MJ, Prasad S, et al. Partial agonists activate PPARγ using a helix 12 independent mechanism. Structure. 2007;15(10):1258-1271.
    • (2007) Structure. , vol.15 , Issue.10 , pp. 1258-1271
    • Bruning, J.B.1    Chalmers, M.J.2    Prasad, S.3
  • 28
    • 56749130032 scopus 로고    scopus 로고
    • Structure of the intact PPAR-γ-RXR-nuclear receptor complex on DNA
    • Chandra V, Huang P, Hamuro Y, et al. Structure of the intact PPAR-γ-RXR-nuclear receptor complex on DNA. Nature. 2008; 456(7220):350-356.
    • (2008) Nature. , vol.456 , Issue.7220 , pp. 350-356
    • Chandra, V.1    Huang, P.2    Hamuro, Y.3
  • 29
    • 84886930646 scopus 로고    scopus 로고
    • Regulation of the structurally dynamic amino-terminal domain of progesterone receptor by protein induced folding
    • Kumar R, Moure CM, Khan SH, et al. Regulation of the structurally dynamic amino-terminal domain of progesterone receptor by protein induced folding. J Biol Chem. 2013.
    • (2013) J Biol Chem.
    • Kumar, R.1    Moure, C.M.2    Khan, S.H.3
  • 30
    • 84866607246 scopus 로고    scopus 로고
    • Nuclear receptor coregulators: Modulators of pathology and therapeutic targets
    • Lonard DM, O'Malley BW. Nuclear receptor coregulators: modulators of pathology and therapeutic targets. Nat Rev Endocrinol. 2012;8(10):598-604.
    • (2012) Nat Rev Endocrinol. , vol.8 , Issue.10 , pp. 598-604
    • Lonard, D.M.1    O'Malley, B.W.2
  • 31
    • 33344459086 scopus 로고    scopus 로고
    • MED14 and MED1 differentially regulate target-specific gene activation by the glucocorticoid receptor
    • Chen W, Rogatsky I, Garabedian MJ. MED14 and MED1 differentially regulate target-specific gene activation by the glucocorticoid receptor. Mol Endocrinol. 2006;20(3):560-572.
    • (2006) Mol Endocrinol. , vol.20 , Issue.3 , pp. 560-572
    • Chen, W.1    Rogatsky, I.2    Garabedian, M.J.3
  • 32
    • 33747860031 scopus 로고    scopus 로고
    • The role of the general transcription factor IIF in androgen receptor-dependent transcription
    • Choudhry MA, Ball A, McEwan IJ. The role of the general transcription factor IIF in androgen receptor-dependent transcription. Mol Endocrinol. 2006;20(9):2052-2061.
    • (2006) Mol Endocrinol. , vol.20 , Issue.9 , pp. 2052-2061
    • Choudhry, M.A.1    Ball, A.2    McEwan, I.J.3
  • 33
    • 84858234186 scopus 로고    scopus 로고
    • Agonism/antagonism switching in allosteric ensembles
    • Motlagh HN, Hilser VJ. Agonism/antagonism switching in allosteric ensembles. Proc Natl Acad Sci USA. 2012;109(11):4134-4139.
    • (2012) Proc Natl Acad Sci USA. , vol.109 , Issue.11 , pp. 4134-4139
    • Motlagh, H.N.1    Hilser, V.J.2
  • 34
    • 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. TBP binding-induced folding of the glucocorticoid receptor AF1 domain facilitates its interaction with steroid receptor coactivator-1. PLoS One. 2011;6(7):e21939.
    • (2011) PLoS One. , vol.6 , Issue.7
    • Khan, S.H.1    Ling, J.2    Kumar, R.3
  • 35
    • 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. TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain. Proc Natl Acad Sci USA. 2004;101(47):16425-16430.
    • (2004) Proc Natl Acad Sci USA. , vol.101 , Issue.47 , 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
  • 36
    • 1542743970 scopus 로고    scopus 로고
    • Induced alpha-helix structure in AF1 of the androgen receptor upon binding transcription factor TFIIF
    • Kumar R, Betney R, Li J, Thompson EB, McEwan IJ. Induced alpha-helix structure in AF1 of the androgen receptor upon binding transcription factor TFIIF. Biochemistry. 2004;43(11):3008-3013.
    • (2004) Biochemistry. , vol.43 , Issue.11 , pp. 3008-3013
    • Kumar, R.1    Betney, R.2    Li, J.3    Thompson, E.B.4    McEwan, I.J.5
  • 37
    • 0032766843 scopus 로고    scopus 로고
    • Multiple signal input and output domains of the 160-kilodalton nuclear receptor coactivator proteins
    • Ma H, Hong H, Huang SM, et al. Multiple signal input and output domains of the 160-kilodalton nuclear receptor coactivator proteins. Mol Cell Biol. 1999;19(9):6164-6173.
    • (1999) Mol Cell Biol. , vol.19 , Issue.9 , pp. 6164-6173
    • Ma, H.1    Hong, H.2    Huang, S.M.3
  • 38
    • 22344452245 scopus 로고    scopus 로고
    • Corepressor binding to progesterone and glucocorticoid receptors involves the activation function-1 domain and is inhibited by molybdate
    • Wang D, Simons SS Jr. Corepressor binding to progesterone and glucocorticoid receptors involves the activation function-1 domain and is inhibited by molybdate. Mol Endocrinol. 2005;19(6):1483-1500.
    • (2005) Mol Endocrinol. , vol.19 , Issue.6 , pp. 1483-1500
    • Wang, D.1    Simons Jr., S.S.2
  • 39
    • 14644401720 scopus 로고    scopus 로고
    • Role of activation function domain-1, DNA binding, and coactivator GRIP1 in the expression of partial agonist activity of glucocorticoid receptor-antagonist complexes
    • Cho S, Blackford JA Jr, Simons SS Jr. Role of activation function domain-1, DNA binding, and coactivator GRIP1 in the expression of partial agonist activity of glucocorticoid receptor-antagonist complexes. Biochemistry. 2005;44(9):3547-3561.
    • (2005) Biochemistry. , vol.44 , Issue.9 , pp. 3547-3561
    • Cho, S.1    Blackford Jr., J.A.2    Simons Jr., S.S.3
  • 40
    • 82655172410 scopus 로고    scopus 로고
    • Structural and functional analysis of domains of the progesterone receptor
    • Hill KK, Roemer SC, Churchill ME, Edwards DP. Structural and functional analysis of domains of the progesterone receptor. Mol Cell Endocrinol. 2012;348(2):418-429.
    • (2012) Mol Cell Endocrinol. , vol.348 , Issue.2 , pp. 418-429
    • Hill, K.K.1    Roemer, S.C.2    Churchill, M.E.3    Edwards, D.P.4
  • 41
    • 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. Site-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor. Mol Cell Biol. 2010;30(1):220-230.
    • (2010) Mol Cell Biol. , vol.30 , Issue.1 , pp. 220-230
    • Garza, A.M.1    Khan, S.H.2    Kumar, R.3
  • 42
    • 84875363845 scopus 로고    scopus 로고
    • Multidomain integration in the structure of the HNF-4α nuclear receptor complex
    • Chandra V, Huang P, Potluri N, Wu D, Kim Y, Rastinejad F. Multidomain integration in the structure of the HNF-4α nuclear receptor complex. Nature. 2013;495(7441):394-398.
    • (2013) Nature. , vol.495 , Issue.7441 , pp. 394-398
    • Chandra, V.1    Huang, P.2    Potluri, N.3    Wu, D.4    Kim, Y.5    Rastinejad, F.6
  • 43
    • 84876925215 scopus 로고    scopus 로고
    • Disorder guides protein function
    • Whitford PC. Disorder guides protein function. Proc Natl Acad Sci USA. 2013;110(18):7114-7115.
    • (2013) Proc Natl Acad Sci USA. , vol.110 , Issue.18 , pp. 7114-7115
    • Whitford, P.C.1
  • 44
    • 26444526919 scopus 로고    scopus 로고
    • Regulation of the amino-terminal transcription activation domain of progesterone receptor by a cofactor-induced protein folding mechanism
    • Wardell SE, Kwok SC, Sherman L, Hodges RS, Edwards DP. Regulation of the amino-terminal transcription activation domain of progesterone receptor by a cofactor-induced protein folding mechanism. Mol Cell Biol. 2005;25(20):8792-8808.
    • (2005) Mol Cell Biol. , vol.25 , Issue.20 , pp. 8792-8808
    • Wardell, S.E.1    Kwok, S.C.2    Sherman, L.3    Hodges, R.S.4    Edwards, D.P.5
  • 45
    • 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. A progesterone receptor co-activator (JDP2) mediates activity through interaction with residues in the carboxyl-terminal extension of the DNA binding domain. J Biol Chem. 2009;284(36): 24415-24424.
    • (2009) J Biol Chem. , vol.284 , Issue.36 , pp. 24415-24424
    • Hill, K.K.1    Roemer, S.C.2    Jones, D.N.3    Churchill, M.E.4    Edwards, D.P.5
  • 46
    • 80053898470 scopus 로고    scopus 로고
    • Bindingfolding induced regulation of AF1 transactivation domain of the glucocorticoid receptor by a cofactor that binds to its DNA binding domain
    • Garza AS, Khan SH, Moure CM, Edwards DP, Kumar R. Bindingfolding induced regulation of AF1 transactivation domain of the glucocorticoid receptor by a cofactor that binds to its DNA binding domain. PLoS One. 2011;6(10):e25875.
    • (2011) PLoS One. , vol.6 , Issue.10
    • Garza, A.S.1    Khan, S.H.2    Moure, C.M.3    Edwards, D.P.4    Kumar, R.5
  • 48
    • 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. 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. 2005;34(3):603-615.
    • (2005) J Mol Endocrinol. , vol.34 , Issue.3 , pp. 603-615
    • Brodie, J.1    McEwan, I.J.2
  • 49
    • 0033609855 scopus 로고    scopus 로고
    • Interdomain signaling in a two-domain fragment of the human glucocorticoid receptor
    • Kumar R, Baskakov IV, Srinivasan G, Bolen DW, Lee JC, Thompson EB. Interdomain signaling in a two-domain fragment of the human glucocorticoid receptor. J Biol Chem. 1999;274(35): 24737-24741.
    • (1999) J Biol Chem. , vol.274 , Issue.35 , pp. 24737-24741
    • Kumar, R.1    Baskakov, I.V.2    Srinivasan, G.3    Bolen, D.W.4    Lee, J.C.5    Thompson, E.B.6
  • 50
    • 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. DNA binding site sequence directs glucocorticoid receptor structure and activity. Science. 2009;324(5925):407-410.
    • (2009) Science. , vol.324 , Issue.5925 , 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
  • 51
    • 79955581636 scopus 로고    scopus 로고
    • Common architecture of nuclear receptor heterodimers on DNA direct repeat elements with different spacings
    • Rochel N, Ciesielski F, Godet J, et al. Common architecture of nuclear receptor heterodimers on DNA direct repeat elements with different spacings. Nat Struct Mol Biol. 2011;18(5):564-570.
    • (2011) Nat Struct Mol Biol. , vol.18 , Issue.5 , pp. 564-570
    • Rochel, N.1    Ciesielski, F.2    Godet, J.3
  • 53
    • 84857183093 scopus 로고    scopus 로고
    • Structure of the full human RXR/VDR nuclear receptor heterodimer complex with its DR3 target DNA
    • Orlov I, Rochel N, Moras D, Klaholz BP. Structure of the full human RXR/VDR nuclear receptor heterodimer complex with its DR3 target DNA. EMBO J. 2012;31(2):291-300.
    • (2012) EMBO J. , vol.31 , Issue.2 , pp. 291-300
    • Orlov, I.1    Rochel, N.2    Moras, D.3    Klaholz, B.P.4
  • 54
    • 44449102870 scopus 로고    scopus 로고
    • Prediction of the tissuespecificity of selective estrogen receptor modulators by using a single biochemical method
    • Dai SY, Chalmers MJ, Bruning J, et al. Prediction of the tissuespecificity of selective estrogen receptor modulators by using a single biochemical method. Proc Natl Acad Sci USA. 2008;105(20): 7171-7176.
    • (2008) Proc Natl Acad Sci USA. , vol.105 , Issue.20 , pp. 7171-7176
    • Dai, S.Y.1    Chalmers, M.J.2    Bruning, J.3
  • 55
    • 79955586601 scopus 로고    scopus 로고
    • DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex
    • Zhang J, Chalmers MJ, Stayrook KR, et al. DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex. Nat Struct Mol Biol. 2011;18(5):556-563.
    • (2011) Nat Struct Mol Biol. , vol.18 , Issue.5 , pp. 556-563
    • Zhang, J.1    Chalmers, M.J.2    Stayrook, K.R.3
  • 56
    • 81755187015 scopus 로고    scopus 로고
    • Disorder-to-order transition underlies the structural basis for the assembly of a transcriptionally active PGC-1α/ERRγ complex
    • Devarakonda S, Gupta K, Chalmers MJ, et al. Disorder-to-order transition underlies the structural basis for the assembly of a transcriptionally active PGC-1α/ERRγ complex. Proc Natl Acad Sci USA. 2011;108(46):18678-18683.
    • (2011) Proc Natl Acad Sci USA. , vol.108 , Issue.46 , pp. 18678-18683
    • Devarakonda, S.1    Gupta, K.2    Chalmers, M.J.3
  • 57
    • 2542486258 scopus 로고    scopus 로고
    • Equilibrium interactions of corepressors and coactivators with agonist and antagonist complexes of glucocorticoid receptors
    • Wang Q, Blackford JA Jr, Song LN, Huang Y, Cho S, Simons SS Jr. Equilibrium interactions of corepressors and coactivators with agonist and antagonist complexes of glucocorticoid receptors. Mol Endocrinol. 2004;18(6):1376-1395.
    • (2004) Mol Endocrinol. , vol.18 , Issue.6 , pp. 1376-1395
    • Wang, Q.1    Blackford Jr., J.A.2    Song, L.N.3    Huang, Y.4    Cho, S.5    Simons Jr., S.S.6
  • 58
    • 0025062215 scopus 로고
    • Role of the two activating domains of the oestrogen receptor in the cell-type and promoter-context dependent agonistic activity of the anti-oestrogen 4-hydroxytamoxifen
    • Berry M, Metzger D, Chambon P. Role of the two activating domains of the oestrogen receptor in the cell-type and promoter-context dependent agonistic activity of the anti-oestrogen 4-hydroxytamoxifen. EMBO J. 1990;9(9):2811-2818.
    • (1990) EMBO J. , vol.9 , Issue.9 , pp. 2811-2818
    • Berry, M.1    Metzger, D.2    Chambon, P.3
  • 59
    • 78149495249 scopus 로고    scopus 로고
    • Glucocorticoid receptor cofactors as therapeutic targets
    • Simons SS Jr. Glucocorticoid receptor cofactors as therapeutic targets. Curr Opin Pharmacol. 2010;10(6):613-619.
    • (2010) Curr Opin Pharmacol. , vol.10 , Issue.6 , pp. 613-619
    • Simons Jr., S.S.1
  • 60
    • 0028233383 scopus 로고
    • Estrogen receptor-associated proteins: Possible mediators of hormone-induced transcription
    • Halachmi S, Marden E, Martin G, MacKay H, Abbondanza C, Brown M. Estrogen receptor-associated proteins: possible mediators of hormone-induced transcription. Science. 1994;264(5164): 1455-1458.
    • (1994) Science. , vol.264 , Issue.5164 , pp. 1455-1458
    • Halachmi, S.1    Marden, E.2    Martin, G.3    McKay, H.4    Abbondanza, C.5    Brown, M.6
  • 61
    • 0033347396 scopus 로고    scopus 로고
    • Opposing effects of corepressor and coactivators in determining the dose-response curve of agonists, and residual agonist activity of antagonists, for glucocorticoid receptor-regulated gene expression
    • Szapary D, Huang Y, Simons SS Jr. Opposing effects of corepressor and coactivators in determining the dose-response curve of agonists, and residual agonist activity of antagonists, for glucocorticoid receptor-regulated gene expression. Mol Endocrinol. 1999;13(12): 2108-2121.
    • (1999) Mol Endocrinol. , vol.13 , Issue.12 , pp. 2108-2121
    • Szapary, D.1    Huang, Y.2    Simons Jr., S.S.3
  • 62
    • 78751483455 scopus 로고    scopus 로고
    • Ligand binding domain mutations of the glucocorticoid receptor selectively modify the effects with, but not binding of, cofactors
    • Lee GS, Simons SS Jr. Ligand binding domain mutations of the glucocorticoid receptor selectively modify the effects with, but not binding of, cofactors. Biochemistry. 2011;50(3):356-366.
    • (2011) Biochemistry. , vol.50 , Issue.3 , pp. 356-366
    • Lee, G.S.1    Simons Jr., S.S.2
  • 63
    • 0033618510 scopus 로고    scopus 로고
    • Peptide antagonists of the human estrogen receptor
    • Norris JD, Paige LA, Christensen DJ, et al. Peptide antagonists of the human estrogen receptor. Science. 1999;285(5428):744-746.
    • (1999) Science. , vol.285 , Issue.5428 , pp. 744-746
    • Norris, J.D.1    Paige, L.A.2    Christensen, D.J.3
  • 64
    • 0023402249 scopus 로고
    • Mechanism of dexamethasone 21-mesylate antiglucocorticoid action: I. Receptor-antiglucocorticoid complexes do not competitively inhibit receptor-glucocorticoid complex activation of gene transcription in vivo
    • Sistare FD, Hager GL, Simons SS Jr. Mechanism of dexamethasone 21-mesylate antiglucocorticoid action: I. Receptor-antiglucocorticoid complexes do not competitively inhibit receptor-glucocorticoid complex activation of gene transcription in vivo. Mol Endocrinol. 1987;1(9):648-658.
    • (1987) Mol Endocrinol. , vol.1 , Issue.9 , pp. 648-658
    • Sistare, F.D.1    Hager, G.L.2    Simons Jr., S.S.3
  • 65
    • 84879086561 scopus 로고    scopus 로고
    • Allosteric controls of nuclear receptor function in the regulation of transcription
    • Billas I, Moras D. Allosteric controls of nuclear receptor function in the regulation of transcription. J Mol Biol. 2013;425(13):2317-2329.
    • (2013) J Mol Biol. , vol.425 , Issue.13 , pp. 2317-2329
    • Billas, I.1    Moras, D.2
  • 66
    • 35348812462 scopus 로고    scopus 로고
    • A surface on the androgen receptor that allosterically regulates coactivator binding
    • Estébanez-Perpiñá E, Arnold LA, Arnold AA, et al. A surface on the androgen receptor that allosterically regulates coactivator binding. Proc Natl Acad Sci USA. 2007;104(41):16074-16079.
    • (2007) Proc Natl Acad Sci USA. , vol.104 , Issue.41 , pp. 16074-16079
    • Estébanez-Perpiñá, E.1    Arnold, L.A.2    Arnold, A.A.3
  • 67
    • 67749148219 scopus 로고    scopus 로고
    • Inhibition of prostate cancer cell growth by second-site androgen receptor antagonists
    • Joseph JD, Wittmann BM, Dwyer MA, et al. Inhibition of prostate cancer cell growth by second-site androgen receptor antagonists. Proc Natl Acad Sci USA. 2009;106(29):12178-12183.
    • (2009) Proc Natl Acad Sci USA. , vol.106 , Issue.29 , pp. 12178-12183
    • Joseph, J.D.1    Wittmann, B.M.2    Dwyer, M.A.3
  • 68
    • 64749094997 scopus 로고    scopus 로고
    • Differential presentation of protein interaction surfaces on the androgen receptor defines the pharmacological actions of bound ligands
    • Norris JD, Joseph JD, Sherk AB, et al. Differential presentation of protein interaction surfaces on the androgen receptor defines the pharmacological actions of bound ligands. Chem Biol. 2009;16(4): 452-460.
    • (2009) Chem Biol. , vol.16 , Issue.4 , pp. 452-460
    • Norris, J.D.1    Joseph, J.D.2    Sherk, A.B.3
  • 69
    • 82655162285 scopus 로고    scopus 로고
    • The road less traveled: New views of steroid receptor action from the path of dose-response curves
    • Simons SS, Jr, Chow CC. The road less traveled: new views of steroid receptor action from the path of dose-response curves. Mol Cell Endocrinol. 2012;348(2):373-382.
    • (2012) Mol Cell Endocrinol. , vol.348 , Issue.2 , pp. 373-382
    • Simons Jr., S.S.1    Chow, C.C.2
  • 71
    • 70349305108 scopus 로고    scopus 로고
    • Modulation of glucocorticoid receptor induction properties by cofactors in peripheral blood mononuclear cells
    • Luo M, Simons SS Jr. Modulation of glucocorticoid receptor induction properties by cofactors in peripheral blood mononuclear cells. Hum Immunol. 2009;70(10):785-789.
    • (2009) Hum Immunol. , vol.70 , Issue.10 , pp. 785-789
    • Luo, M.1    Simons Jr., S.S.2
  • 72
    • 84858745781 scopus 로고    scopus 로고
    • Separate regions of glucocorticoid receptor, coactivator TIF2, and comodulator STAMP modify different parameters of glucocorticoid-mediated gene induction
    • Awasthi S, Simons SS Jr. Separate regions of glucocorticoid receptor, coactivator TIF2, and comodulator STAMP modify different parameters of glucocorticoid-mediated gene induction. Mol Cell Endocrinol. 2012;355(1):121-134.
    • (2012) Mol Cell Endocrinol. , vol.355 , Issue.1 , pp. 121-134
    • Awasthi, S.1    Simons Jr., S.S.2
  • 73
    • 84855829727 scopus 로고    scopus 로고
    • Deducing the temporal order of cofactor function in ligand-regulated gene transcription: Theory and experimental verification
    • Dougherty EJ, Guo C, Simons SS Jr, Chow CC. Deducing the temporal order of cofactor function in ligand-regulated gene transcription: theory and experimental verification. PLoS One. 2012;7(1): e30225.
    • (2012) PLoS One. , vol.7 , Issue.1
    • Dougherty, E.J.1    Guo, C.2    Simons Jr., S.S.3    Chow, C.C.4
  • 74
    • 84870363100 scopus 로고    scopus 로고
    • Identification of location and kinetically defined mechanism of cofactors and reporter genes in the cascade of steroid-regulated transactivation
    • Blackford JA Jr, Guo C, Zhu R, Dougherty EJ, Chow CC, Simons SS Jr. Identification of location and kinetically defined mechanism of cofactors and reporter genes in the cascade of steroid-regulated transactivation. J Biol Chem. 2012;287(49):40982-40995.
    • (2012) J Biol Chem. , vol.287 , Issue.49 , pp. 40982-40995
    • Blackford Jr., J.A.1    Guo, C.2    Zhu, R.3    Dougherty, E.J.4    Chow, C.C.5    Simons Jr., S.S.6
  • 75
    • 84872069513 scopus 로고    scopus 로고
    • PA1 protein, a new competitive decelerator acting at more than one step to impede glucocorticoid receptor-mediated transactivation
    • Zhang Z, Sun Y, Cho YW, Chow CC, Simons SS Jr. PA1 protein, a new competitive decelerator acting at more than one step to impede glucocorticoid receptor-mediated transactivation. J Biol Chem. 2013;288(1):42-58.
    • (2013) J Biol Chem. , vol.288 , Issue.1 , pp. 42-58
    • Zhang, Z.1    Sun, Y.2    Cho, Y.W.3    Chow, C.C.4    Simons Jr., S.S.5
  • 76
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
    • Shiau AK, Barstad D, Loria PM, et al. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell. 1998;95(7):927-937.
    • (1998) Cell. , vol.95 , Issue.7 , pp. 927-937
    • Shiau, A.K.1    Barstad, D.2    Loria, P.M.3
  • 77
    • 0026410042 scopus 로고
    • Differential DNA-binding abilities of estrogen receptor occupied with two classes of antiestrogens: Studies using human estrogen receptor overexpressed in mammalian cells
    • Reese JC, Katzenellenbogen BS. Differential DNA-binding abilities of estrogen receptor occupied with two classes of antiestrogens: studies using human estrogen receptor overexpressed in mammalian cells. Nucleic Acids Res. 1991;19(23):6595-6602.
    • (1991) Nucleic Acids Res. , vol.19 , Issue.23 , pp. 6595-6602
    • Reese, J.C.1    Katzenellenbogen, B.S.2
  • 78
    • 34748864669 scopus 로고    scopus 로고
    • A functional serine 118 phosphorylation site in estrogen receptor-α is required for down-regulation of gene expression by 17β-estradiol and 4-hydroxytamoxifen
    • Cheng J, Zhang C, Shapiro DJ. A functional serine 118 phosphorylation site in estrogen receptor-α is required for down-regulation of gene expression by 17β-estradiol and 4-hydroxytamoxifen. Endocrinology. 2007;148(10):4634-4641.
    • (2007) Endocrinology. , vol.148 , Issue.10 , pp. 4634-4641
    • Cheng, J.1    Zhang, C.2    Shapiro, D.J.3
  • 79
    • 77950634822 scopus 로고    scopus 로고
    • Fulvestrant-a novel endocrine therapy for breast cancer
    • Johnston SJ, Cheung KL. Fulvestrant-a novel endocrine therapy for breast cancer. Curr Med Chem. 2010;17(10):902-914.
    • (2010) Curr Med Chem. , vol.17 , Issue.10 , pp. 902-914
    • Johnston, S.J.1    Cheung, K.L.2
  • 80
    • 79958149945 scopus 로고    scopus 로고
    • The turnover of estrogen receptor α by the selective estrogen receptor degrader (SERD) fulvestrant is a saturable process that is not required for antagonist efficacy
    • Wardell SE, Marks JR, McDonnell DP. The turnover of estrogen receptor α by the selective estrogen receptor degrader (SERD) fulvestrant is a saturable process that is not required for antagonist efficacy. Biochem Pharmacol. 2011;82(2):122-130.
    • (2011) Biochem Pharmacol. , vol.82 , Issue.2 , pp. 122-130
    • Wardell, S.E.1    Marks, J.R.2    McDonnell, D.P.3
  • 81
    • 34548241775 scopus 로고    scopus 로고
    • Fulvestrant (Faslodex)-how to make a good drug better
    • Robertson JF. Fulvestrant (Faslodex)-how to make a good drug better. Oncologist. 2007;12(7):774-784.
    • (2007) Oncologist. , vol.12 , Issue.7 , pp. 774-784
    • Robertson, J.F.1
  • 82
    • 84877091558 scopus 로고    scopus 로고
    • Bazedoxifene exhibits antiestrogenic activity in animal models of tamoxifen-resistant breast cancer: Implications for treatment of advanced disease
    • Wardell SE, Nelson ER, Chao CA, McDonnell DP. Bazedoxifene exhibits antiestrogenic activity in animal models of tamoxifen-resistant breast cancer: implications for treatment of advanced disease. Clin Cancer Res. 2013;19(9):2420-2431.
    • (2013) Clin Cancer Res. , vol.19 , Issue.9 , pp. 2420-2431
    • Wardell, S.E.1    Nelson, E.R.2    Chao, C.A.3    McDonnell, D.P.4
  • 83
    • 78650657019 scopus 로고    scopus 로고
    • A noncompetitive small molecule inhibitor of estrogen-regulated gene expression and breast cancer cell growth that enhances proteasome-dependent degradation of estrogen receptor α
    • Kretzer NM, Cherian MT, Mao C, et al. A noncompetitive small molecule inhibitor of estrogen-regulated gene expression and breast cancer cell growth that enhances proteasome-dependent degradation of estrogen receptor α. J Biol Chem. 2010;285(53):41863-41873.
    • (2010) J Biol Chem. , vol.285 , Issue.53 , pp. 41863-41873
    • Kretzer, N.M.1    Cherian, M.T.2    Mao, C.3
  • 84
    • 66349124428 scopus 로고    scopus 로고
    • Non-competitive androgen receptor inhibition in vitro and in vivo
    • Jones JO, Bolton EC, Huang Y, et al. Non-competitive androgen receptor inhibition in vitro and in vivo. Proc Natl Acad Sci USA. 2009;106(17):7233-7238.
    • (2009) Proc Natl Acad Sci USA. , vol.106 , Issue.17 , pp. 7233-7238
    • Jones, J.O.1    Bolton, E.C.2    Huang, Y.3
  • 85
    • 45149088830 scopus 로고    scopus 로고
    • A new small molecule inhibitor of estrogen receptor α binding to estrogen response elements blocks estrogen-dependent growth of cancer cells
    • Mao C, Patterson NM, Cherian MT, et al. A new small molecule inhibitor of estrogen receptor α binding to estrogen response elements blocks estrogen-dependent growth of cancer cells. J Biol Chem. 2008;283(19):12819-12830.
    • (2008) J Biol Chem. , vol.283 , Issue.19 , pp. 12819-12830
    • Mao, C.1    Patterson, N.M.2    Cherian, M.T.3
  • 86
    • 84876665470 scopus 로고    scopus 로고
    • Lessons from the dissection of the activation functions (AF-1 and AF-2) of the estrogen receptor α in vivo
    • Arnal JF, Fontaine C, Abot A, et al. Lessons from the dissection of the activation functions (AF-1 and AF-2) of the estrogen receptor α in vivo. Steroids. 2013;78(6):576-582.
    • (2013) Steroids. , vol.78 , Issue.6 , pp. 576-582
    • Arnal, J.F.1    Fontaine, C.2    Abot, A.3
  • 87
    • 84871393540 scopus 로고    scopus 로고
    • Transactivating function (AF) 2-mediated AF-1 activity of estrogen receptor α is crucial to maintain male reproductive tract function
    • Arao Y, Hamilton KJ, Goulding EH, Janardhan KS, Eddy EM, Korach KS. Transactivating function (AF) 2-mediated AF-1 activity of estrogen receptor α is crucial to maintain male reproductive tract function. Proc Natl Acad Sci USA. 2012;109(51):21140-21145.
    • (2012) Proc Natl Acad Sci USA. , vol.109 , Issue.51 , pp. 21140-21145
    • Arao, Y.1    Hamilton, K.J.2    Goulding, E.H.3    Janardhan, K.S.4    Eddy, E.M.5    Korach, K.S.6
  • 88
    • 80052567302 scopus 로고    scopus 로고
    • Estrogen receptor α AF-2 mutation results in antagonist reversal and reveals tissue selective function of estrogen receptor modulators
    • Arao Y, Hamilton KJ, Ray MK, Scott G, Mishina Y, Korach KS. Estrogen receptor α AF-2 mutation results in antagonist reversal and reveals tissue selective function of estrogen receptor modulators. Proc Natl Acad Sci USA. 2011;108(36):14986-14991.
    • (2011) Proc Natl Acad Sci USA. , vol.108 , Issue.36 , pp. 14986-14991
    • Arao, Y.1    Hamilton, K.J.2    Ray, M.K.3    Scott, G.4    Mishina, Y.5    Korach, K.S.6
  • 89
    • 60549099919 scopus 로고    scopus 로고
    • The transactivating function 1 of estrogen receptor α is dispensable for the vasculoprotective actions of 17β-estradiol
    • Billon-Galés A, Fontaine C, Filipe C, et al. The transactivating function 1 of estrogen receptor α is dispensable for the vasculoprotective actions of 17β-estradiol. Proc Natl Acad Sci USA. 2009;106(6):2053-2058.
    • (2009) Proc Natl Acad Sci USA. , vol.106 , Issue.6 , pp. 2053-2058
    • Billon-Galés, A.1    Fontaine, C.2    Filipe, C.3
  • 90
    • 79955009428 scopus 로고    scopus 로고
    • Roles of transactivating functions 1 and 2 of estrogen receptor-α in bone
    • Börjesson AE, Windahl SH, Lagerquist MK, et al. Roles of transactivating functions 1 and 2 of estrogen receptor-α in bone. Proc Natl Acad Sci USA. 2011;108(15):6288-6293.
    • (2011) Proc Natl Acad Sci USA. , vol.108 , Issue.15 , pp. 6288-6293
    • Börjesson, A.E.1    Windahl, S.H.2    Lagerquist, M.K.3
  • 91
    • 80051954941 scopus 로고    scopus 로고
    • Activation function 2 (AF2) of estrogen receptor-α is required for the atheroprotective action of estradiol but not to accelerate endothelial healing
    • Billon-Galés A, Krust A, Fontaine C, et al. Activation function 2 (AF2) of estrogen receptor-α is required for the atheroprotective action of estradiol but not to accelerate endothelial healing. Proc Natl Acad Sci USA. 2011;108(32):13311-13316.
    • (2011) Proc Natl Acad Sci USA. , vol.108 , Issue.32 , pp. 13311-13316
    • Billon-Galés, A.1    Krust, A.2    Fontaine, C.3
  • 92
    • 77953280591 scopus 로고    scopus 로고
    • Regression of castraterecurrent prostate cancer by a small-molecule inhibitor of the amino-terminus domain of the androgen receptor
    • Andersen RJ, Mawji NR, Wang J, et al. Regression of castraterecurrent prostate cancer by a small-molecule inhibitor of the amino-terminus domain of the androgen receptor. Cancer Cell. 2010;17(6):535-546.
    • (2010) Cancer Cell. , vol.17 , Issue.6 , pp. 535-546
    • Andersen, R.J.1    Mawji, N.R.2    Wang, J.3
  • 93
    • 84879628727 scopus 로고    scopus 로고
    • An androgen receptor N-terminal domain antagonist for treating prostate cancer
    • Myung JK, Banuelos CA, Fernandez JG, et al. An androgen receptor N-terminal domain antagonist for treating prostate cancer. J Clin Invest. 2013;123(7):2948-2960.
    • (2013) J Clin Invest. , vol.123 , Issue.7 , pp. 2948-2960
    • Myung, J.K.1    Banuelos, C.A.2    Fernandez, J.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.