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Volumn 36, Issue 1, 2015, Pages 3-23

Androgen receptor: Structure, role in prostate cancer and drug discovery

Author keywords

androgen; androgen receptor; antiandrogen; castration resistance; drug discovery; nuclear receptor; prostate cancer; rational drug design; structural biology

Indexed keywords

ANDROGEN; ANDROGEN RECEPTOR; ANDROGEN RECEPTOR AGONIST; ANTIANDROGEN; BICALUTAMIDE; ENZALUTAMIDE; FLUDROCORTISONE; HORMONE RECEPTOR AFFECTING AGENT; UNCLASSIFIED DRUG;

EID: 84920394601     PISSN: 16714083     EISSN: 17457254     Source Type: Journal    
DOI: 10.1038/aps.2014.18     Document Type: Review
Times cited : (613)

References (206)
  • 2
    • 0028283503 scopus 로고
    • Molecular mechanisms of action of steroid/thyroid receptor superfamily members
    • Tsai MJ, O'Malley BW. Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu Rev Biochem 1994; 63: 451-86.
    • (1994) Annu Rev Biochem , vol.63 , pp. 451-486
    • Tsai, M.J.1    O'Malley, B.W.2
  • 3
    • 0033574663 scopus 로고    scopus 로고
    • A unified nomenclature system for the nuclear receptor superfamily
    • Nuclear Receptors Nomenclature Committee
    • Nuclear Receptors Nomenclature Committee. A unified nomenclature system for the nuclear receptor superfamily. Cell 1999; 97: 161-3.
    • (1999) Cell , vol.97 , pp. 161-163
  • 5
    • 0036803797 scopus 로고    scopus 로고
    • Albumin, steroid hormones and the origin of vertebrates
    • Baker ME. Albumin, steroid hormones and the origin of vertebrates. J Endocrinol 2002; 175: 121-7.
    • (2002) J Endocrinol , vol.175 , pp. 121-127
    • Baker, M.E.1
  • 7
    • 0036208492 scopus 로고    scopus 로고
    • Formation of the androgen receptor transcription complex
    • Shang Y, Myers M, Brown M. Formation of the androgen receptor transcription complex. Mol Cell 2002; 9: 601-10.
    • (2002) Mol Cell , vol.9 , pp. 601-610
    • Shang, Y.1    Myers, M.2    Brown, M.3
  • 8
    • 33746623315 scopus 로고    scopus 로고
    • Molecular regulation of androgen action in prostate cancer
    • Dehm SM, Tindall DJ. Molecular regulation of androgen action in prostate cancer. J Cell Biochem 2006; 99: 333-44.
    • (2006) J Cell Biochem , vol.99 , pp. 333-344
    • Dehm, S.M.1    Tindall, D.J.2
  • 9
    • 24044540381 scopus 로고    scopus 로고
    • Spatial and temporal recruitment of androgen receptor and its coactivators involves chromosomal looping and polymerase tracking
    • Wang Q, Carroll JS, Brown M. Spatial and temporal recruitment of androgen receptor and its coactivators involves chromosomal looping and polymerase tracking. Mol Cell 2005; 19: 631-42.
    • (2005) Mol Cell , vol.19 , pp. 631-642
    • Wang, Q.1    Carroll, J.S.2    Brown, M.3
  • 11
    • 2342558431 scopus 로고    scopus 로고
    • Androgen receptor in prostate cancer
    • Heinlein CA, Chang C. Androgen receptor in prostate cancer. Endocr Rev 2004; 25: 276-308.
    • (2004) Endocr Rev , vol.25 , pp. 276-308
    • Heinlein, C.A.1    Chang, C.2
  • 12
    • 0029618368 scopus 로고
    • Steroid hormone receptors: Many actors in search of a plot
    • Beato M, Herrlich P, Schutz G. Steroid hormone receptors: many actors in search of a plot. Cell 1995; 83: 851-7.
    • (1995) Cell , vol.83 , pp. 851-857
    • Beato, M.1    Herrlich, P.2    Schutz, G.3
  • 13
    • 0035919213 scopus 로고    scopus 로고
    • Molecular basis of androgen insensitivity
    • Brinkmann AO. Molecular basis of androgen insensitivity. Mol Cell Endocrinol 2001; 179: 105-9.
    • (2001) Mol Cell Endocrinol , vol.179 , pp. 105-109
    • Brinkmann, A.O.1
  • 17
    • 0024555077 scopus 로고
    • Androgen receptor locus on the human X chromosome: Regional localization to Xq11-12 and description of a DNA polymorphism
    • Brown CJ, Goss SJ, Lubahn DB, Joseph DR, Wilson EM, French FS, et al. Androgen receptor locus on the human X chromosome: regional localization to Xq11-12 and description of a DNA polymorphism. Am J Hum Genet 1989; 44: 264-9.
    • (1989) Am J Hum Genet , vol.44 , pp. 264-269
    • Brown, C.J.1    Goss, S.J.2    Lubahn, D.B.3    Joseph, D.R.4    Wilson, E.M.5    French, F.S.6
  • 18
    • 0019806262 scopus 로고
    • Studies of the locus for androgen receptor: Localization on the human X chromosome and evidence for homology with the Tfm locus in the mouse
    • Migeon BR, Brown TR, Axelman J, Migeon CJ. Studies of the locus for androgen receptor: localization on the human X chromosome and evidence for homology with the Tfm locus in the mouse. Proc Natl Acad Sci USA 1981; 78: 6339-43.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 6339-6343
    • Migeon, B.R.1    Brown, T.R.2    Axelman, J.3    Migeon, C.J.4
  • 19
    • 0036645414 scopus 로고    scopus 로고
    • Molecular biology of the androgen receptor
    • Gelmann EP. Molecular biology of the androgen receptor. J Clin Oncol 2002; 20: 3001-15.
    • (2002) J Clin Oncol , vol.20 , pp. 3001-3015
    • Gelmann, E.P.1
  • 20
    • 3042540196 scopus 로고    scopus 로고
    • Molecular mechanisms of androgen receptor-mediated gene regulation: Structure-function analysis of the AF-1 domain
    • McEwan IJ. Molecular mechanisms of androgen receptor-mediated gene regulation: structure-function analysis of the AF-1 domain. Endocr Relat Cancer 2004; 11: 281-93.
    • (2004) Endocr Relat Cancer , vol.11 , pp. 281-293
    • McEwan, I.J.1
  • 21
    • 0033601249 scopus 로고    scopus 로고
    • Activation function 2 in the human androgen receptor ligand binding domain mediates interdomain communication with the NH2-terminal domain
    • He B, Kemppainen JA, Voegel JJ, Gronemeyer H, Wilson EM. Activation function 2 in the human androgen receptor ligand binding domain mediates interdomain communication with the NH2-terminal domain. J Biol Chem 1999; 274: 37219-25.
    • (1999) J Biol Chem , vol.274 , pp. 37219-37225
    • He, B.1    Kemppainen, J.A.2    Voegel, J.J.3    Gronemeyer, H.4    Wilson, E.M.5
  • 22
    • 0344495261 scopus 로고    scopus 로고
    • The polyglycine and polyglutamine repeats in the androgen receptor gene in Japanese and Caucasian populations
    • Sasaki M, Kaneuchi M, Sakuragi N, Fujimoto S, Carroll PR, Dahiya R. The polyglycine and polyglutamine repeats in the androgen receptor gene in Japanese and Caucasian populations. Biochem Biophys Res Commun 2003; 312: 1244-7.
    • (2003) Biochem Biophys Res Commun , vol.312 , pp. 1244-1247
    • Sasaki, M.1    Kaneuchi, M.2    Sakuragi, N.3    Fujimoto, S.4    Carroll, P.R.5    Dahiya, R.6
  • 23
    • 0034665359 scopus 로고    scopus 로고
    • Polymorphic CAG and GGN repeat lengths in the androgen receptor gene and prostate cancer risk: A population-based case-control study in China
    • Hsing AW, Gao YT, Wu G, Wang X, Deng J, Chen YL, et al. Polymorphic CAG and GGN repeat lengths in the androgen receptor gene and prostate cancer risk: a population-based case-control study in China. Cancer Res 2000; 60: 5111-6.
    • (2000) Cancer Res , vol.60 , pp. 5111-5116
    • Hsing, A.W.1    Gao, Y.T.2    Wu, G.3    Wang, X.4    Deng, J.5    Chen, Y.L.6
  • 24
    • 0042770258 scopus 로고
    • Structural analysis of complementary DNA and amino acid sequences of human and rat androgen receptors
    • Chang CS, Kokontis J, Liao ST. Structural analysis of complementary DNA and amino acid sequences of human and rat androgen receptors. Proc Natl Acad Sci USA 1988; 85: 7211-5.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7211-7215
    • Chang, C.S.1    Kokontis, J.2    Liao, S.T.3
  • 25
    • 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. Consequences of poly-glutamine repeat length for the conformation and folding of the androgen receptor amino-terminal domain. J Mol Endocrinol 2008; 41: 301-14.
    • (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
  • 26
    • 33748752321 scopus 로고    scopus 로고
    • The A645D mutation in the hinge region of the human androgen receptor (AR) gene modulates AR activity, depending on the context of the polymorphic glutamine and glycine repeats
    • Werner R, Holterhus PM, Binder G, Schwarz HP, Morlot M, Struve D, et al. The A645D mutation in the hinge region of the human androgen receptor (AR) gene modulates AR activity, depending on the context of the polymorphic glutamine and glycine repeats. J Clin Endocrinol Metab 2006; 91: 3515-20.
    • (2006) J Clin Endocrinol Metab , vol.91 , pp. 3515-3520
    • Werner, R.1    Holterhus, P.M.2    Binder, G.3    Schwarz, H.P.4    Morlot, M.5    Struve, D.6
  • 27
    • 0029856398 scopus 로고    scopus 로고
    • Reduced androgen receptor gene expression with first exon CAG repeat expansion
    • Choong CS, Kemppainen JA, Zhou ZX, Wilson EM. Reduced androgen receptor gene expression with first exon CAG repeat expansion. Mol Endocrinol 1996; 10: 1527-35.
    • (1996) Mol Endocrinol , vol.10 , pp. 1527-1535
    • Choong, C.S.1    Kemppainen, J.A.2    Zhou, Z.X.3    Wilson, E.M.4
  • 29
    • 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. 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 2008; 47: 3360-9.
    • (2008) Biochemistry , vol.47 , pp. 3360-3369
    • Lavery, D.N.1    McEwan, I.J.2
  • 30
    • 0037205522 scopus 로고    scopus 로고
    • Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and proteinprotein 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 proteinprotein interactions. J Biol Chem 2002; 277: 20079-86.
    • (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
  • 31
    • 34248649845 scopus 로고    scopus 로고
    • The human androgen receptor AF1 transactivation domain: Interactions with transcription factor IIF and molten-globule-like structural characteristics
    • Lavery DN, McEwan IJ. The human androgen receptor AF1 transactivation domain: interactions with transcription factor IIF and molten-globule-like structural characteristics. Biochem Soc Trans 2006; 34: 1054-7.
    • (2006) Biochem Soc Trans , vol.34 , pp. 1054-1057
    • Lavery, D.N.1    McEwan, I.J.2
  • 32
    • 27744511919 scopus 로고    scopus 로고
    • Structure and function of steroid receptor AF1 transactivation domains: Induction of active conformations
    • Lavery DN, McEwan IJ. Structure and function of steroid receptor AF1 transactivation domains: induction of active conformations. Biochem J 2005; 391: 449-64.
    • (2005) Biochem J , vol.391 , pp. 449-464
    • Lavery, D.N.1    McEwan, I.J.2
  • 33
    • 56749130032 scopus 로고    scopus 로고
    • Structure of the intact PPAR-gamma-RXR-nuclear receptor complex on DNA
    • Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, et al. Structure of the intact PPAR-gamma-RXR-nuclear receptor complex on DNA. Nature 2008; 456: 350-6.
    • (2008) Nature , vol.456 , pp. 350-356
    • Chandra, V.1    Huang, P.2    Hamuro, Y.3    Raghuram, S.4    Wang, Y.5    Burris, T.P.6
  • 34
    • 84875363845 scopus 로고    scopus 로고
    • Multidomain integration in the structure of the HNF-4alpha nuclear receptor complex
    • Chandra V, Huang P, Potluri N, Wu D, Kim Y, Rastinejad F. Multidomain integration in the structure of the HNF-4alpha nuclear receptor complex. Nature 2013; 495: 394-8.
    • (2013) Nature , vol.495 , pp. 394-398
    • Chandra, V.1    Huang, P.2    Potluri, N.3    Wu, D.4    Kim, Y.5    Rastinejad, F.6
  • 35
    • 79951905332 scopus 로고    scopus 로고
    • Multitude of binding modes attainable by intrinsically disordered proteins: A portrait gallery of disorder-based complexes
    • Uversky VN. Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes. Chem Soc Rev 2011; 40: 1623-34.
    • (2011) Chem Soc Rev , vol.40 , pp. 1623-1634
    • Uversky, V.N.1
  • 36
    • 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. The AF1 and AF2 domains of the androgen receptor interact with distinct regions of SRC1. Mol Cell Biol 1999; 19: 8383-92.
    • (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
  • 37
    • 0030790495 scopus 로고    scopus 로고
    • Interaction of the human androgen receptor transactivation function with the general transcription factor TFIIF
    • McEwan IJ, Gustafsson J. Interaction of the human androgen receptor transactivation function with the general transcription factor TFIIF. Proc Natl Acad Sci USA 1997; 94: 8485-90.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8485-8490
    • McEwan, I.J.1    Gustafsson, J.2
  • 38
    • 0025957233 scopus 로고
    • Transcriptional activation and nuclear targeting signals of the human androgen receptor
    • Simental JA, Sar M, Lane MV, French FS, Wilson EM. Transcriptional activation and nuclear targeting signals of the human androgen receptor. J Biol Chem 1991; 266: 510-8.
    • (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
  • 39
    • 31544451068 scopus 로고    scopus 로고
    • Interplay between two hormone-independent activation domains in the androgen receptor
    • Callewaert L, Van Tilborgh N, Claessens F. Interplay between two hormone-independent activation domains in the androgen receptor. Cancer Res 2006; 66: 543-53.
    • (2006) Cancer Res , vol.66 , pp. 543-553
    • Callewaert, L.1    Van Tilborgh, N.2    Claessens, F.3
  • 40
    • 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, et al. Functional in vivo interaction between the amino-terminal, transactivation domain and the ligand binding domain of the androgen receptor. Biochemistry 1997; 36: 1052-64.
    • (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
  • 41
    • 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. FXXLF and WXXLF sequences mediate the NH2-terminal interaction with the ligand binding domain of the androgen receptor. J Biol Chem 2000; 275: 22986-94.
    • (2000) J Biol Chem , vol.275 , pp. 22986-22994
    • He, B.1    Kemppainen, J.A.2    Wilson, E.M.3
  • 42
    • 80052957801 scopus 로고    scopus 로고
    • Analysis of interdomain interactions of the androgen receptor
    • Wilson EM. Analysis of interdomain interactions of the androgen receptor. Methods Mol Biol 2011; 776: 113-29.
    • (2011) Methods Mol Biol , vol.776 , pp. 113-129
    • Wilson, E.M.1
  • 43
    • 0028809317 scopus 로고
    • Specificity of ligand-dependent androgen receptor stabilization: Receptor domain interactions influence ligand dissociation and receptor stability
    • Zhou ZX, Lane MV, Kemppainen JA, French FS, Wilson EM. Specificity of ligand-dependent androgen receptor stabilization: receptor domain interactions influence ligand dissociation and receptor stability. Mol Endocrinol 1995; 9: 208-18.
    • (1995) Mol Endocrinol , vol.9 , pp. 208-218
    • Zhou, Z.X.1    Lane, M.V.2    Kemppainen, J.A.3    French, F.S.4    Wilson, E.M.5
  • 44
    • 0031594713 scopus 로고    scopus 로고
    • Intermolecular NH2-/carboxylterminal interactions in androgen receptor dimerization revealed by mutations that cause androgen insensitivity
    • Langley E, Kemppainen JA, Wilson EM. Intermolecular NH2-/carboxylterminal interactions in androgen receptor dimerization revealed by mutations that cause androgen insensitivity. J Biol Chem 1998; 273: 92-101.
    • (1998) J Biol Chem , vol.273 , pp. 92-101
    • Langley, E.1    Kemppainen, J.A.2    Wilson, E.M.3
  • 46
    • 0029778413 scopus 로고    scopus 로고
    • The androgen-specific probasin response element 2 interacts differentially with androgen and glucocorticoid receptors
    • Claessens F, Alen P, Devos A, Peeters B, Verhoeven G, Rombauts W. The androgen-specific probasin response element 2 interacts differentially with androgen and glucocorticoid receptors. J Biol Chem 1996; 271: 19013-6.
    • (1996) J Biol Chem , vol.271 , pp. 19013-19016
    • Claessens, F.1    Alen, P.2    Devos, A.3    Peeters, B.4    Verhoeven, G.5    Rombauts, W.6
  • 47
    • 0034697359 scopus 로고    scopus 로고
    • Change of specificity mutations in androgenselective enhancers. Evidence for a role of differential DNA binding by the androgen receptor
    • Verrijdt G, Schoenmakers E, Haelens A, Peeters B, Verhoeven G, Rombauts W, et al. Change of specificity mutations in androgenselective enhancers. Evidence for a role of differential DNA binding by the androgen receptor. J Biol Chem 2000; 275: 12298-305.
    • (2000) J Biol Chem , vol.275 , pp. 12298-12305
    • Verrijdt, G.1    Schoenmakers, E.2    Haelens, A.3    Peeters, B.4    Verhoeven, G.5    Rombauts, W.6
  • 48
    • 0034697122 scopus 로고    scopus 로고
    • Differences in DNA binding characteristics of the androgen and glucocorticoid receptors can determine hormonespecific responses
    • Schoenmakers E, Verrijdt G, Peeters B, Verhoeven G, Rombauts W, Claessens F. Differences in DNA binding characteristics of the androgen and glucocorticoid receptors can determine hormonespecific responses. J Biol Chem 2000; 275: 12290-7.
    • (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
  • 50
    • 0027283705 scopus 로고
    • Nuclear import of the human androgen receptor
    • Jenster G, Trapman J, Brinkmann AO. Nuclear import of the human androgen receptor. Biochem J 1993; 293: 761-8.
    • (1993) Biochem J , vol.293 , pp. 761-768
    • Jenster, G.1    Trapman, J.2    Brinkmann, A.O.3
  • 51
    • 0028225858 scopus 로고
    • A liganddependent bipartite nuclear targeting signal in the human androgen receptor. Requirement for the DNA-binding domain and modulation by NH2-terminal and carboxyl-terminal sequences
    • Zhou ZX, Sar M, Simental JA, Lane MV, Wilson EM. A liganddependent bipartite nuclear targeting signal in the human androgen receptor. Requirement for the DNA-binding domain and modulation by NH2-terminal and carboxyl-terminal sequences. J Biol Chem 1994; 269: 13115-23.
    • (1994) J Biol Chem , vol.269 , pp. 13115-13123
    • Zhou, Z.X.1    Sar, M.2    Simental, J.A.3    Lane, M.V.4    Wilson, E.M.5
  • 52
    • 0034965056 scopus 로고    scopus 로고
    • Passage through the nuclear pore
    • Marte B. Passage through the nuclear pore. Nat Cell Biol 2001; 3: E135.
    • (2001) Nat Cell Biol , vol.3 , pp. E135
    • Marte, B.1
  • 53
    • 84893050752 scopus 로고    scopus 로고
    • Androgen induces a switch in the androgen receptor from cytoplasmic retention to nuclear import
    • Ni L, Llewellyn R, Kesler CT, Kelley JB, Spencer A, Snow CJ, et al. Androgen induces a switch in the androgen receptor from cytoplasmic retention to nuclear import. Mol Cell Biol 2013; 33: 4766-78.
    • (2013) Mol Cell Biol , vol.33 , pp. 4766-4778
    • Ni, L.1    Llewellyn, R.2    Kesler, C.T.3    Kelley, J.B.4    Spencer, A.5    Snow, C.J.6
  • 54
  • 55
    • 34249307492 scopus 로고    scopus 로고
    • The hinge region regulates DNA binding, nuclear translocation, and transactivation of the androgen receptor
    • Haelens A, Tanner T, Denayer S, Callewaert L, Claessens F. The hinge region regulates DNA binding, nuclear translocation, and transactivation of the androgen receptor. Cancer Res 2007; 67: 4514-23.
    • (2007) Cancer Res , vol.67 , pp. 4514-4523
    • Haelens, A.1    Tanner, T.2    Denayer, S.3    Callewaert, L.4    Claessens, F.5
  • 57
    • 0034714276 scopus 로고    scopus 로고
    • Structural evidence for ligand specificity in the binding domain of the human androgen receptor. Implications for pathogenic gene mutations
    • Matias PM, Donner P, Coelho R, Thomaz M, Peixoto C, Macedo S, et al. Structural evidence for ligand specificity in the binding domain of the human androgen receptor. Implications for pathogenic gene mutations. J Biol Chem 2000; 275: 26164-71.
    • (2000) J Biol Chem , vol.275 , pp. 26164-26171
    • Matias, P.M.1    Donner, P.2    Coelho, R.3    Thomaz, M.4    Peixoto, C.5    MacEdo, S.6
  • 58
    • 10744231103 scopus 로고    scopus 로고
    • Study of 202 natural, synthetic, and environmental chemicals for binding to the androgen receptor
    • Fang H, Tong W, Branham WS, Moland CL, Dial SL, Hong H, et al. Study of 202 natural, synthetic, and environmental chemicals for binding to the androgen receptor. Chem Res Toxicol 2003; 16: 1338-58.
    • (2003) Chem Res Toxicol , vol.16 , pp. 1338-1358
    • Fang, H.1    Tong, W.2    Branham, W.S.3    Moland, C.L.4    Dial, S.L.5    Hong, H.6
  • 59
    • 0344844462 scopus 로고    scopus 로고
    • Pharmacological uncoupling of androgen receptor-mediated prostate cancer cell proliferation and prostate-specific antigen secretion
    • Sathya G, Chang CY, Kazmin D, Cook CE, McDonnell DP. Pharmacological uncoupling of androgen receptor-mediated prostate cancer cell proliferation and prostate-specific antigen secretion. Cancer Res 2003; 63: 8029-36.
    • (2003) Cancer Res , vol.63 , pp. 8029-8036
    • Sathya, G.1    Chang, C.Y.2    Kazmin, D.3    Cook, C.E.4    McDonnell, D.P.5
  • 60
    • 0034121290 scopus 로고    scopus 로고
    • Androgen receptor antagonists (antiandrogens): Structure-activity relationships
    • Singh SM, Gauthier S, Labrie F. Androgen receptor antagonists (antiandrogens): structure-activity relationships. Curr Med Chem 2000; 7: 211-47.
    • (2000) Curr Med Chem , vol.7 , pp. 211-247
    • Singh, S.M.1    Gauthier, S.2    Labrie, F.3
  • 61
    • 25444496757 scopus 로고    scopus 로고
    • Chemistry and structural biology of androgen receptor
    • Gao W, Bohl CE, Dalton JT. Chemistry and structural biology of androgen receptor. Chem Rev 2005; 105: 3352-70.
    • (2005) Chem Rev , vol.105 , pp. 3352-3370
    • Gao, W.1    Bohl, C.E.2    Dalton, J.T.3
  • 62
    • 35648970526 scopus 로고    scopus 로고
    • Structural characterization of the human androgen receptor ligand-binding domain complexed with EM5744, a rationally designed steroidal ligand bearing a bulky chain directed toward helix 12
    • Cantin L, Faucher F, Couture JF, de Jesus-Tran KP, Legrand P, Ciobanu LC, et al. Structural characterization of the human androgen receptor ligand-binding domain complexed with EM5744, a rationally designed steroidal ligand bearing a bulky chain directed toward helix 12. J Biol Chem 2007; 282: 30910-9.
    • (2007) J Biol Chem , vol.282 , pp. 30910-30919
    • Cantin, L.1    Faucher, F.2    Couture, J.F.3    De Jesus-Tran, K.P.4    Legrand, P.5    Ciobanu, L.C.6
  • 64
    • 0014414093 scopus 로고
    • Metabolism of testosterone and action of metabolites on prostate glands grown in organ culture
    • Baulieu EE, Lasnizki I, Robel P. Metabolism of testosterone and action of metabolites on prostate glands grown in organ culture. Nature 1968; 219: 1155-6.
    • (1968) Nature , vol.219 , pp. 1155-1156
    • Baulieu, E.E.1    Lasnizki, I.2    Robel, P.3
  • 65
    • 0014429464 scopus 로고
    • The conversion of testosterone to 5-alphaandrostan-17-beta-ol-3-one by rat prostate in vivo and in vitro
    • Bruchovsky N, Wilson JD. The conversion of testosterone to 5-alphaandrostan-17-beta-ol-3-one by rat prostate in vivo and in vitro. J Biol Chem 1968; 243: 2012-21.
    • (1968) J Biol Chem , vol.243 , pp. 2012-2021
    • Bruchovsky, N.1    Wilson, J.D.2
  • 66
    • 0025037581 scopus 로고
    • Testosterone at high concentrations interacts with the human androgen receptor similarly to dihydrotestosterone
    • Grino PB, Griffin JE, Wilson JD. Testosterone at high concentrations interacts with the human androgen receptor similarly to dihydrotestosterone. Endocrinology 1990; 126: 1165-72.
    • (1990) Endocrinology , vol.126 , pp. 1165-1172
    • Grino, P.B.1    Griffin, J.E.2    Wilson, J.D.3
  • 67
    • 0035942197 scopus 로고    scopus 로고
    • Crystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosterone
    • Sack JS, Kish KF, Wang C, Attar RM, Kiefer SE, An Y, et al. Crystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosterone. Proc Natl Acad Sci USA 2001; 98: 4904-9.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4904-4909
    • Sack, J.S.1    Kish, K.F.2    Wang, C.3    Attar, R.M.4    Kiefer, S.E.5    An, Y.6
  • 68
    • 33646138016 scopus 로고    scopus 로고
    • Comparison of crystal structures of human androgen receptor ligand-binding domain complexed with various agonists reveals molecular determinants responsible for binding affinity
    • Pereira de Jesus-Tran K, Cote PL, Cantin L, Blanchet J, Labrie F, Breton R. Comparison of crystal structures of human androgen receptor ligand-binding domain complexed with various agonists reveals molecular determinants responsible for binding affinity. Protein Sci 2006; 15: 987-99.
    • (2006) Protein Sci , vol.15 , pp. 987-999
    • Pereira De Jesus-Tran, K.1    Cote, P.L.2    Cantin, L.3    Blanchet, J.4    Labrie, F.5    Breton, R.6
  • 69
    • 0030113441 scopus 로고    scopus 로고
    • Transcriptional control: How nuclear receptors get turned on
    • Schwabe JW. Transcriptional control: how nuclear receptors get turned on. Curr Biol 1996; 6: 372-4.
    • (1996) Curr Biol , vol.6 , pp. 372-374
    • Schwabe, J.W.1
  • 70
    • 0038646966 scopus 로고    scopus 로고
    • Activation of nuclear receptors: A perspective from structural genomics
    • Li Y, Lambert MH, Xu HE. Activation of nuclear receptors: a perspective from structural genomics. Structure 2003; 11: 741-6.
    • (2003) Structure , vol.11 , pp. 741-746
    • Li, Y.1    Lambert, M.H.2    Xu, H.E.3
  • 71
    • 0034306499 scopus 로고    scopus 로고
    • Nuclear receptor ligandbinding domains: Three-dimensional structures, molecular interactions and pharmacological implications
    • Bourguet W, Germain P, Gronemeyer H. Nuclear receptor ligandbinding domains: three-dimensional structures, molecular interactions and pharmacological implications. Trends Pharmacol Sci 2000; 21: 381-8.
    • (2000) Trends Pharmacol Sci , vol.21 , pp. 381-388
    • Bourguet, W.1    Germain, P.2    Gronemeyer, H.3
  • 72
    • 0038526314 scopus 로고    scopus 로고
    • Structure and function of Nurr1 identifies a class of ligand-independent nuclear receptors
    • Wang Z, Benoit G, Liu J, Prasad S, Aarnisalo P, Liu X, et al. Structure and function of Nurr1 identifies a class of ligand-independent nuclear receptors. Nature 2003; 423: 555-60.
    • (2003) Nature , vol.423 , pp. 555-560
    • Wang, Z.1    Benoit, G.2    Liu, J.3    Prasad, S.4    Aarnisalo, P.5    Liu, X.6
  • 73
    • 84875051349 scopus 로고    scopus 로고
    • Mini-review: Foldosome regulation of androgen receptor action in prostate cancer
    • Cano LQ, Lavery DN, Bevan CL. Mini-review: Foldosome regulation of androgen receptor action in prostate cancer. Mol Cell Endocrinol 2013; 369: 52-62.
    • (2013) Mol Cell Endocrinol , vol.369 , pp. 52-62
    • Cano, L.Q.1    Lavery, D.N.2    Bevan, C.L.3
  • 74
    • 0029643780 scopus 로고
    • Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid
    • Renaud JP, Rochel N, Ruff M, Vivat V, Chambon P, Gronemeyer H, et al. Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid. Nature 1995; 378: 681-9.
    • (1995) Nature , vol.378 , pp. 681-689
    • Renaud, J.P.1    Rochel, N.2    Ruff, M.3    Vivat, V.4    Chambon, P.5    Gronemeyer, H.6
  • 76
    • 33745670369 scopus 로고    scopus 로고
    • Structural rearrangements in the thyroid hormone receptor hinge domain and their putative role in the receptor function
    • Nascimento AS, Dias SM, Nunes FM, Aparicio R, Ambrosio AL, Bleicher L, et al. Structural rearrangements in the thyroid hormone receptor hinge domain and their putative role in the receptor function. J Mol Biol 2006; 360: 586-98.
    • (2006) J Mol Biol , vol.360 , pp. 586-598
    • Nascimento, A.S.1    Dias, S.M.2    Nunes, F.M.3    Aparicio, R.4    Ambrosio, A.L.5    Bleicher, L.6
  • 77
    • 0035923672 scopus 로고    scopus 로고
    • Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors
    • Xu HE, Lambert MH, Montana VG, Plunket KD, Moore LB, Collins JL, et al. Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors. Proc Natl Acad Sci USA 2001; 98: 13919-24.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 13919-13924
    • Xu, H.E.1    Lambert, M.H.2    Montana, V.G.3    Plunket, K.D.4    Moore, L.B.5    Collins, J.L.6
  • 78
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery DM, Kalkhoven E, Hoare S, Parker MG. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 1997; 387: 733-6.
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 79
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 1996; 87: 953-9.
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 80
    • 20044394709 scopus 로고    scopus 로고
    • The molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptor
    • Estebanez-Perpina E, Moore JM, Mar E, Delgado-Rodrigues E, Nguyen P, Baxter JD, et al. The molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptor. J Biol Chem 2005; 280: 8060-8.
    • (2005) J Biol Chem , vol.280 , pp. 8060-8068
    • Estebanez-Perpina, E.1    Moore, J.M.2    Mar, E.3    Delgado-Rodrigues, E.4    Nguyen, P.5    Baxter, J.D.6
  • 81
    • 77950556674 scopus 로고    scopus 로고
    • Identification of SRC3/AIB1 as a preferred coactivator for hormoneactivated androgen receptor
    • Zhou XE, Suino-Powell KM, Li J, He Y, Mackeigan JP, Melcher K, et al. Identification of SRC3/AIB1 as a preferred coactivator for hormoneactivated androgen receptor. J Biol Chem 2010; 285: 9161-71.
    • (2010) J Biol Chem , vol.285 , pp. 9161-9171
    • Zhou, X.E.1    Suino-Powell, K.M.2    Li, J.3    He, Y.4    MacKeigan, J.P.5    Melcher, K.6
  • 83
    • 0037155790 scopus 로고    scopus 로고
    • The FXXLF motif mediates androgen receptor-specific interactions with coregulators
    • He B, Minges JT, Lee LW, Wilson EM. The FXXLF motif mediates androgen receptor-specific interactions with coregulators. J Biol Chem 2002; 277: 10226-35.
    • (2002) J Biol Chem , vol.277 , pp. 10226-10235
    • He, B.1    Minges, J.T.2    Lee, L.W.3    Wilson, E.M.4
  • 84
    • 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 RT Jr, Kole AJ, Hnat AT, Stanley TB, An G, et al. Structural basis for androgen receptor interdomain and coactivator interactions suggests a transition in nuclear receptor activation function dominance. Mol Cell 2004; 16: 425-38.
    • (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
  • 85
    • 0033773337 scopus 로고    scopus 로고
    • Mutational analysis of the androgen receptor AF-2 (activation function 2) core domain reveals functional and mechanistic differences of conserved residues compared with other nuclear receptors
    • Slagsvold T, Kraus I, Bentzen T, Palvimo J, Saatcioglu F. Mutational analysis of the androgen receptor AF-2 (activation function 2) core domain reveals functional and mechanistic differences of conserved residues compared with other nuclear receptors. Mol Endocrinol 2000; 14: 1603-17.
    • (2000) Mol Endocrinol , vol.14 , pp. 1603-1617
    • Slagsvold, T.1    Kraus, I.2    Bentzen, T.3    Palvimo, J.4    Saatcioglu, F.5
  • 89
    • 0034465595 scopus 로고    scopus 로고
    • Dynamics of intracellular movement and nucleocytoplasmic recycling of the ligand-activated androgen receptor in living cells
    • Tyagi RK, Lavrovsky Y, Ahn SC, Song CS, Chatterjee B, Roy AK. Dynamics of intracellular movement and nucleocytoplasmic recycling of the ligand-activated androgen receptor in living cells. Mol Endocrinol 2000; 14: 1162-74.
    • (2000) Mol Endocrinol , vol.14 , pp. 1162-1174
    • Tyagi, R.K.1    Lavrovsky, Y.2    Ahn, S.C.3    Song, C.S.4    Chatterjee, B.5    Roy, A.K.6
  • 90
    • 0142211276 scopus 로고    scopus 로고
    • Identification and characterization of a ligand-regulated nuclear export signal in androgen receptor
    • Saporita AJ, Zhang Q, Navai N, Dincer Z, Hahn J, Cai X, et al. Identification and characterization of a ligand-regulated nuclear export signal in androgen receptor. J Biol Chem 2003; 278: 41998-2005.
    • (2003) J Biol Chem , vol.278 , pp. 41998-42005
    • Saporita, A.J.1    Zhang, Q.2    Navai, N.3    Dincer, Z.4    Hahn, J.5    Cai, X.6
  • 91
    • 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, Cheng L, Kushner PJ, Agard DA, et al. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 1998; 95: 927-37.
    • (1998) Cell , vol.95 , pp. 927-937
    • Shiau, A.K.1    Barstad, D.2    Loria, P.M.3    Cheng, L.4    Kushner, P.J.5    Agard, D.A.6
  • 92
    • 0038265311 scopus 로고    scopus 로고
    • The three-dimensional structures of antagonistic and agonistic forms of the glucocorticoid receptor ligand-binding domain: RU-486 induces a transconformation that leads to active antagonism
    • Kauppi B, Jakob C, Farnegardh M, Yang J, Ahola H, Alarcon M, et al. The three-dimensional structures of antagonistic and agonistic forms of the glucocorticoid receptor ligand-binding domain: RU-486 induces a transconformation that leads to active antagonism. J Biol Chem 2003; 278: 22748-54.
    • (2003) J Biol Chem , vol.278 , pp. 22748-22754
    • Kauppi, B.1    Jakob, C.2    Farnegardh, M.3    Yang, J.4    Ahola, H.5    Alarcon, M.6
  • 93
    • 18244393501 scopus 로고    scopus 로고
    • Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARalpha
    • Xu HE, Stanley TB, Montana VG, Lambert MH, Shearer BG, Cobb JE, et al. Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARalpha. Nature 2002; 415: 813-7.
    • (2002) Nature , vol.415 , pp. 813-817
    • Xu, H.E.1    Stanley, T.B.2    Montana, V.G.3    Lambert, M.H.4    Shearer, B.G.5    Cobb, J.E.6
  • 94
    • 55749094858 scopus 로고    scopus 로고
    • Structural basis for nuclear receptor corepressor recruitment by antagonist-liganded androgen receptor
    • Hodgson MC, Shen HC, Hollenberg AN, Balk SP. Structural basis for nuclear receptor corepressor recruitment by antagonist-liganded androgen receptor. Mol Cancer Ther 2008; 7: 3187-94.
    • (2008) Mol Cancer Ther , vol.7 , pp. 3187-3194
    • Hodgson, M.C.1    Shen, H.C.2    Hollenberg, A.N.3    Balk, S.P.4
  • 95
    • 79955831117 scopus 로고    scopus 로고
    • Mechanism of androgen receptor antagonism by bicalutamide in the treatment of prostate cancer
    • Osguthorpe DJ, Hagler AT. Mechanism of androgen receptor antagonism by bicalutamide in the treatment of prostate cancer. Biochemistry 2011; 50: 4105-13.
    • (2011) Biochemistry , vol.50 , pp. 4105-4113
    • Osguthorpe, D.J.1    Hagler, A.T.2
  • 96
    • 0028237201 scopus 로고
    • Mechanism of antiandrogen action: Conformational changes of the receptor
    • Kuil CW, Mulder E. Mechanism of antiandrogen action: conformational changes of the receptor. Mol Cell Endocrinol 1994; 102: R1-5.
    • (1994) Mol Cell Endocrinol , vol.102 , pp. R1-5
    • Kuil, C.W.1    Mulder, E.2
  • 97
    • 32044448683 scopus 로고    scopus 로고
    • Macrophage/cancer cell interactions mediate hormone resistance by a nuclear receptor derepression pathway
    • Zhu P, Baek SH, Bourk EM, Ohgi KA, Garcia-Bassets I, Sanjo H, et al. Macrophage/cancer cell interactions mediate hormone resistance by a nuclear receptor derepression pathway. Cell 2006; 124: 615-29.
    • (2006) Cell , vol.124 , pp. 615-629
    • Zhu, P.1    Baek, S.H.2    Bourk, E.M.3    Ohgi, K.A.4    Garcia-Bassets, I.5    Sanjo, H.6
  • 102
    • 84875416683 scopus 로고    scopus 로고
    • Clinical and molecular aspects of androgen insensitivity
    • Hiort O. Clinical and molecular aspects of androgen insensitivity. Endocr Dev 2013; 24: 33-40.
    • (2013) Endocr Dev , vol.24 , pp. 33-40
    • Hiort, O.1
  • 103
    • 0037203514 scopus 로고    scopus 로고
    • Androgen receptor mutations and androgen insensitivity
    • McPhaul MJ. Androgen receptor mutations and androgen insensitivity. Mol Cell Endocrinol 2002; 198: 61-7.
    • (2002) Mol Cell Endocrinol , vol.198 , pp. 61-67
    • McPhaul, M.J.1
  • 105
    • 0025800526 scopus 로고
    • Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy
    • La Spada AR, Wilson EM, Lubahn DB, Harding AE, Fischbeck KH. Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy. Nature 1991; 352: 77-9.
    • (1991) Nature , vol.352 , pp. 77-79
    • La Spada, A.R.1    Wilson, E.M.2    Lubahn, D.B.3    Harding, A.E.4    Fischbeck, K.H.5
  • 106
    • 84934441995 scopus 로고    scopus 로고
    • Kennedy's disease: Clinical significance of tandem repeats in the androgen receptor
    • Zajac JD, Fui MN. Kennedy's disease: clinical significance of tandem repeats in the androgen receptor. Adv Exp Med Biol 2012; 769: 153-68.
    • (2012) Adv Exp Med Biol , vol.769 , pp. 153-168
    • Zajac, J.D.1    Fui, M.N.2
  • 107
    • 64149099061 scopus 로고    scopus 로고
    • Bulbar and spinal muscular atrophy (Kennedy's disease): A review
    • Finsterer J. Bulbar and spinal muscular atrophy (Kennedy's disease): a review. Eur J Neurol 2009; 16: 556-61.
    • (2009) Eur J Neurol , vol.16 , pp. 556-561
    • Finsterer, J.1
  • 109
    • 84865446644 scopus 로고    scopus 로고
    • Androgen receptor in laryngeal carcinoma: Could there be an androgen-refractory tumor?
    • Goulioumis AK, Varakis J, Goumas P, Papadaki H. Androgen receptor in laryngeal carcinoma: could there be an androgen-refractory tumor? ISRN Oncol 2011; 2011: 180518.
    • (2011) ISRN Oncol , vol.2011 , pp. 180518
    • Goulioumis, A.K.1    Varakis, J.2    Goumas, P.3    Papadaki, H.4
  • 110
    • 84984588392 scopus 로고    scopus 로고
    • Androgen pathway stimulates microRNA-216a transcription to suppress the tumor suppressor in lung cancer-1 gene in early hepatocarcinogenesis
    • Chen PJ, Yeh SH, Liu WH, Lin CC, Huang HC, Chen CL, et al. Androgen pathway stimulates microRNA-216a transcription to suppress the tumor suppressor in lung cancer-1 gene in early hepatocarcinogenesis. Hepatology 2012; 56: 632-43.
    • (2012) Hepatology , vol.56 , pp. 632-643
    • Chen, P.J.1    Yeh, S.H.2    Liu, W.H.3    Lin, C.C.4    Huang, H.C.5    Chen, C.L.6
  • 113
    • 81855227033 scopus 로고    scopus 로고
    • Clinical practice. Screening for prostate cancer
    • Hoffman RM. Clinical practice. Screening for prostate cancer. N Engl J Med 2011; 365: 2013-9.
    • (2011) N Engl J Med , vol.365 , pp. 2013-2019
    • Hoffman, R.M.1
  • 115
    • 37849017532 scopus 로고    scopus 로고
    • Polymorphic CAG and GGC repeat lengths in the androgen receptor gene and prostate cancer risk: Analysis of a Brazilian population
    • Silva Neto B, Koff WJ, Biolchi V, Brenner C, Biolo KD, Spritzer PM, et al. Polymorphic CAG and GGC repeat lengths in the androgen receptor gene and prostate cancer risk: analysis of a Brazilian population. Cancer Invest 2008; 26: 74-80.
    • (2008) Cancer Invest , vol.26 , pp. 74-80
    • Silva Neto, B.1    Koff, W.J.2    Biolchi, V.3    Brenner, C.4    Biolo, K.D.5    Spritzer, P.M.6
  • 116
    • 84864004900 scopus 로고    scopus 로고
    • Polymorphisms in androgen signaling pathway predisposing to prostate cancer
    • Schleutker J. Polymorphisms in androgen signaling pathway predisposing to prostate cancer. Mol Cell Endocrinol 2012; 360: 25-37.
    • (2012) Mol Cell Endocrinol , vol.360 , pp. 25-37
    • Schleutker, J.1
  • 117
    • 78349310918 scopus 로고    scopus 로고
    • Androgen receptor CAG repeat length and association with prostate cancer risk: Results from the prostate cancer prevention trial
    • Price DK, Chau CH, Till C, Goodman PJ, Baum CE, Ockers SB, et al. Androgen receptor CAG repeat length and association with prostate cancer risk: results from the prostate cancer prevention trial. J Urol 2010; 184: 2297-302.
    • (2010) J Urol , vol.184 , pp. 2297-2302
    • Price, D.K.1    Ch, C.2    Till, C.3    Goodman, P.J.4    Baum, C.E.5    Ockers, S.B.6
  • 118
    • 0029873670 scopus 로고    scopus 로고
    • Role of programmed (apoptotic) cell death during the progression and therapy for prostate cancer
    • Denmeade SR, Lin XS, Isaacs JT. Role of programmed (apoptotic) cell death during the progression and therapy for prostate cancer. Prostate 1996; 28: 251-65.
    • (1996) Prostate , vol.28 , pp. 251-265
    • Denmeade, S.R.1    Lin, X.S.2    Isaacs, J.T.3
  • 119
    • 0014151337 scopus 로고
    • Endocrine-induced regression of cancers
    • Huggins C. Endocrine-induced regression of cancers. Cancer Res 1967; 27: 1925-30.
    • (1967) Cancer Res , vol.27 , pp. 1925-1930
    • Huggins, C.1
  • 120
    • 0036636871 scopus 로고
    • Studies on prostatic cancer: I. The effect of castration, of estrogen and of androgen injection on serum phosphatases in metastatic carcinoma of the prostate
    • Huggins C, Hodges CV. Studies on prostatic cancer: I. The effect of castration, of estrogen and of androgen injection on serum phosphatases in metastatic carcinoma of the prostate. 1941. J Urol 2002; 168: 9-12.
    • (1941) J Urol , vol.2002 , Issue.168 , pp. 9-12
    • Huggins, C.1    Hodges, C.V.2
  • 122
    • 80053078529 scopus 로고    scopus 로고
    • Common gene rearrangements in prostate cancer
    • Rubin MA, Maher CA, Chinnaiyan AM. Common gene rearrangements in prostate cancer. J Clin Oncol 2011; 29: 3659-68.
    • (2011) J Clin Oncol , vol.29 , pp. 3659-3668
    • Rubin, M.A.1    Maher, C.A.2    Chinnaiyan, A.M.3
  • 123
    • 27344442125 scopus 로고    scopus 로고
    • Medicine Fused genes may help explain the origins of prostate cancer
    • Marx J. Medicine. Fused genes may help explain the origins of prostate cancer. Science 2005; 310: 603.
    • (2005) Science , vol.310 , pp. 603
    • Marx, J.1
  • 124
    • 27344451557 scopus 로고    scopus 로고
    • Recurrent fusion of TMPRSS2 and ETS transcription factor genes in prostate cancer
    • Tomlins SA, Rhodes DR, Perner S, Dhanasekaran SM, Mehra R, Sun XW, et al. Recurrent fusion of TMPRSS2 and ETS transcription factor genes in prostate cancer. Science 2005; 310: 644-8.
    • (2005) Science , vol.310 , pp. 644-648
    • Tomlins, S.A.1    Rhodes, D.R.2    Perner, S.3    Dhanasekaran, S.M.4    Mehra, R.5    Sun, X.W.6
  • 125
    • 71249101060 scopus 로고    scopus 로고
    • Nuclear receptor-induced chromosomal proximity and DNA breaks underlie specific translocations in cancer
    • Lin C, Yang L, Tanasa B, Hutt K, Ju BG, Ohgi K, et al. Nuclear receptor-induced chromosomal proximity and DNA breaks underlie specific translocations in cancer. Cell 2009; 139: 1069-83.
    • (2009) Cell , vol.139 , pp. 1069-1083
    • Lin, C.1    Yang, L.2    Tanasa, B.3    Hutt, K.4    Ju, B.G.5    Ohgi, K.6
  • 126
    • 77955069195 scopus 로고    scopus 로고
    • Androgen-induced TOP2B-mediated double-strand breaks and prostate cancer gene rearrangements
    • Haffner MC, Aryee MJ, Toubaji A, Esopi DM, Albadine R, Gurel B, et al. Androgen-induced TOP2B-mediated double-strand breaks and prostate cancer gene rearrangements. Nat Genet 2010; 42: 668-75.
    • (2010) Nat Genet , vol.42 , pp. 668-675
    • Haffner, M.C.1    Aryee, M.J.2    Toubaji, A.3    Esopi, D.M.4    Albadine, R.5    Gurel, B.6
  • 128
    • 84879447404 scopus 로고    scopus 로고
    • Non-castrate metastatic prostate cancer: Have the treatment options changed?
    • Palmbos PL, Hussain M. Non-castrate metastatic prostate cancer: have the treatment options changed? Semin Oncol 2013; 40: 337-46.
    • (2013) Semin Oncol , vol.40 , pp. 337-346
    • Palmbos, P.L.1    Hussain, M.2
  • 129
    • 84862767296 scopus 로고    scopus 로고
    • Gonadotropin-releasing hormone: An update review of the antagonists versus agonists
    • Van Poppel H, Klotz L. Gonadotropin-releasing hormone: an update review of the antagonists versus agonists. Int J Urol 2012; 19: 594-601.
    • (2012) Int J Urol , vol.19 , pp. 594-601
    • Van Poppel, H.1    Klotz, L.2
  • 131
    • 0036112592 scopus 로고    scopus 로고
    • The current state of hormonal therapy for prostate cancer
    • Hellerstedt BA, Pienta KJ. The current state of hormonal therapy for prostate cancer. CA Cancer J Clin 2002; 52: 154-79.
    • (2002) CA Cancer J Clin , vol.52 , pp. 154-179
    • Hellerstedt, B.A.1    Pienta, K.J.2
  • 132
    • 78149489985 scopus 로고    scopus 로고
    • Research in castration-resistant prostate cancer: What does the future hold?
    • Macfarlane RJ, Chi KN. Research in castration-resistant prostate cancer: what does the future hold? Curr Oncol 2010; 17: S80-6.
    • (2010) Curr Oncol , vol.17 , pp. S80-S86
    • MacFarlane, R.J.1    Chi, K.N.2
  • 133
    • 60149089419 scopus 로고    scopus 로고
    • Androgen deprivation therapy: Progress in understanding mechanisms of resistance and optimizing androgen depletion
    • Harris WP, Mostaghel EA, Nelson PS, Montgomery B. Androgen deprivation therapy: progress in understanding mechanisms of resistance and optimizing androgen depletion. Nat Clin Pract Urol 2009; 6: 76-85.
    • (2009) Nat Clin Pract Urol , vol.6 , pp. 76-85
    • Harris, W.P.1    Mostaghel, E.A.2    Nelson, P.S.3    Montgomery, B.4
  • 134
    • 4744337716 scopus 로고    scopus 로고
    • Docetaxel and estramustine compared with mitoxantrone and prednisone for advanced refractory prostate cancer
    • Petrylak DP, Tangen CM, Hussain MH, Lara PN Jr, Jones JA, Taplin ME, et al. Docetaxel and estramustine compared with mitoxantrone and prednisone for advanced refractory prostate cancer. N Engl J Med 2004; 351: 1513-20.
    • (2004) N Engl J Med , vol.351 , pp. 1513-1520
    • Petrylak, D.P.1    Tangen, C.M.2    Hussain, M.H.3    Lara, Jr.P.N.4    Jones, J.A.5    Taplin, M.E.6
  • 135
    • 4744366279 scopus 로고    scopus 로고
    • Docetaxel plus prednisone or mitoxantrone plus prednisone for advanced prostate cancer
    • Tannock IF, de Wit R, Berry WR, Horti J, Pluzanska A, Chi KN, et al. Docetaxel plus prednisone or mitoxantrone plus prednisone for advanced prostate cancer. N Engl J Med 2004; 351: 1502-12.
    • (2004) N Engl J Med , vol.351 , pp. 1502-1512
    • Tannock, I.F.1    De Wit, R.2    Berry, W.R.3    Horti, J.4    Pluzanska, A.5    Chi, K.N.6
  • 136
    • 0035496220 scopus 로고    scopus 로고
    • The development of androgen-independent prostate cancer
    • Feldman BJ, Feldman D. The development of androgen-independent prostate cancer. Nat Rev Cancer 2001; 1: 34-45.
    • (2001) Nat Rev Cancer , vol.1 , pp. 34-45
    • Feldman, B.J.1    Feldman, D.2
  • 137
    • 84874426546 scopus 로고    scopus 로고
    • Interplay between genomic alterations and androgen receptor signaling during prostate cancer development and progression
    • Nyquist MD, Dehm SM. Interplay between genomic alterations and androgen receptor signaling during prostate cancer development and progression. Horm Cancer 2013; 4: 61-9.
    • (2013) Horm Cancer , vol.4 , pp. 61-69
    • Nyquist, M.D.1    Dehm, S.M.2
  • 138
    • 84886534301 scopus 로고    scopus 로고
    • Mechanisms of androgen receptor activation in castrationresistant prostate cancer
    • Sharifi N. Mechanisms of androgen receptor activation in castrationresistant prostate cancer. Endocrinology 2013; 154: 4010-7.
    • (2013) Endocrinology , vol.154 , pp. 4010-4017
    • Sharifi, N.1
  • 140
    • 15644368237 scopus 로고    scopus 로고
    • Androgen receptor gene amplification: A possible molecular mechanism for androgen deprivation therapy failure in prostate cancer
    • Koivisto P, Kononen J, Palmberg C, Tammela T, Hyytinen E, Isola J, et al. Androgen receptor gene amplification: a possible molecular mechanism for androgen deprivation therapy failure in prostate cancer. Cancer Res 1997; 57: 314-9.
    • (1997) Cancer Res , vol.57 , pp. 314-319
    • Koivisto, P.1    Kononen, J.2    Palmberg, C.3    Tammela, T.4    Hyytinen, E.5    Isola, J.6
  • 141
    • 49249119358 scopus 로고    scopus 로고
    • Maintenance of intratumoral androgens in metastatic prostate cancer: A mechanism for castration-resistant tumor growth
    • Montgomery RB, Mostaghel EA, Vessella R, Hess DL, Kalhorn TF, Higano CS, et al. Maintenance of intratumoral androgens in metastatic prostate cancer: a mechanism for castration-resistant tumor growth. Cancer Res 2008; 68: 4447-54.
    • (2008) Cancer Res , vol.68 , pp. 4447-4454
    • Montgomery, R.B.1    Mostaghel, E.A.2    Vessella, R.3    Hess, D.L.4    Kalhorn, T.F.5    Higano, C.S.6
  • 142
    • 84879604525 scopus 로고    scopus 로고
    • Targeting the adrenal gland in castration-resistant prostate cancer: A case for orteronel, a selective CYP-17 17,20-lyase inhibitor
    • Zhu H, Garcia JA. Targeting the adrenal gland in castration-resistant prostate cancer: a case for orteronel, a selective CYP-17 17,20-lyase inhibitor. Curr Oncol Rep 2013; 15: 105-12.
    • (2013) Curr Oncol Rep , vol.15 , pp. 105-112
    • Zhu, H.1    Garcia, J.A.2
  • 143
    • 84870336847 scopus 로고    scopus 로고
    • Distinct patterns of dysregulated expression of enzymes involved in androgen synthesis and metabolism in metastatic prostate cancer tumors
    • Mitsiades N, Sung CC, Schultz N, Danila DC, He B, Eedunuri VK, et al. Distinct patterns of dysregulated expression of enzymes involved in androgen synthesis and metabolism in metastatic prostate cancer tumors. Cancer Res 2012; 72: 6142-52.
    • (2012) Cancer Res , vol.72 , pp. 6142-6152
    • Mitsiades, N.1    Sung, C.C.2    Schultz, N.3    Danila, D.C.4    He, B.5    Eedunuri, V.K.6
  • 145
    • 0033152164 scopus 로고    scopus 로고
    • Selection for androgen receptor mutations in prostate cancers treated with androgen antagonist
    • Taplin ME, Bubley GJ, Ko YJ, Small EJ, Upton M, Rajeshkumar B, et al. Selection for androgen receptor mutations in prostate cancers treated with androgen antagonist. Cancer Res 1999; 59: 2511-5.
    • (1999) Cancer Res , vol.59 , pp. 2511-2515
    • Taplin, M.E.1    Bubley, G.J.2    Ko, Y.J.3    Small, E.J.4    Upton, M.5    Rajeshkumar, B.6
  • 146
    • 0033921978 scopus 로고    scopus 로고
    • Ligand-independent activation of the androgen receptor in prostate cancer by growth factors and cytokines
    • Jenster G. Ligand-independent activation of the androgen receptor in prostate cancer by growth factors and cytokines. J Pathol 2000; 191: 227-8.
    • (2000) J Pathol , vol.191 , pp. 227-228
    • Jenster, G.1
  • 147
    • 0028113415 scopus 로고
    • Androgen receptor activation in prostatic tumor cell lines by insulin-like growth factor-I, keratinocyte growth factor, and epidermal growth factor
    • Culig Z, Hobisch A, Cronauer MV, Radmayr C, Trapman J, Hittmair A, et al. Androgen receptor activation in prostatic tumor cell lines by insulin-like growth factor-I, keratinocyte growth factor, and epidermal growth factor. Cancer Res 1994; 54: 5474-8.
    • (1994) Cancer Res , vol.54 , pp. 5474-5478
    • Culig, Z.1    Hobisch, A.2    Cronauer, M.V.3    Radmayr, C.4    Trapman, J.5    Hittmair, A.6
  • 148
    • 7944234374 scopus 로고    scopus 로고
    • HER2/neu kinase-dependent modulation of androgen receptor function through effects on DNA binding and stability
    • Mellinghoff IK, Vivanco I, Kwon A, Tran C, Wongvipat J, Sawyers CL. HER2/neu kinase-dependent modulation of androgen receptor function through effects on DNA binding and stability. Cancer Cell 2004; 6: 517-27.
    • (2004) Cancer Cell , vol.6 , pp. 517-527
    • Mellinghoff, I.K.1    Vivanco, I.2    Kwon, A.3    Tran, C.4    Wongvipat, J.5    Sawyers, C.L.6
  • 149
    • 34347263425 scopus 로고    scopus 로고
    • Activated Cdc42-associated kinase Ack1 promotes prostate cancer progression via androgen receptor tyrosine phosphorylation
    • Mahajan NP, Liu Y, Majumder S, Warren MR, Parker CE, Mohler JL, et al. Activated Cdc42-associated kinase Ack1 promotes prostate cancer progression via androgen receptor tyrosine phosphorylation. Proc Natl Acad Sci USA 2007; 104: 8438-43.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8438-8443
    • Mahajan, N.P.1    Liu, Y.2    Majumder, S.3    Warren, M.R.4    Parker, C.E.5    Mohler, J.L.6
  • 150
    • 77953229511 scopus 로고    scopus 로고
    • Dasatinib inhibits site-specific tyrosine phosphorylation of androgen receptor by Ack1 and Src kinases
    • Liu Y, Karaca M, Zhang Z, Gioeli D, Earp HS, Whang YE. Dasatinib inhibits site-specific tyrosine phosphorylation of androgen receptor by Ack1 and Src kinases. Oncogene 2010; 29: 3208-16.
    • (2010) Oncogene , vol.29 , pp. 3208-3216
    • Liu, Y.1    Karaca, M.2    Zhang, Z.3    Gioeli, D.4    Earp, H.S.5    Whang, Y.E.6
  • 151
    • 33845298019 scopus 로고    scopus 로고
    • Receptor for activated C kinase 1 (RACK1) and Src regulate the tyrosine phosphorylation and function of the androgen receptor
    • Kraus S, Gioeli D, Vomastek T, Gordon V, Weber MJ. Receptor for activated C kinase 1 (RACK1) and Src regulate the tyrosine phosphorylation and function of the androgen receptor. Cancer Res 2006; 66: 11047-54.
    • (2006) Cancer Res , vol.66 , pp. 11047-11054
    • Kraus, S.1    Gioeli, D.2    Vomastek, T.3    Gordon, V.4    Weber, M.J.5
  • 152
    • 84883132550 scopus 로고    scopus 로고
    • LncRNA-dependent mechanisms of androgen-receptor-regulated gene activation programs
    • Yang L, Lin C, Jin C, Yang JC, Tanasa B, Li W, et al. lncRNA-dependent mechanisms of androgen-receptor-regulated gene activation programs. Nature 2013; 500: 598-602.
    • (2013) Nature , vol.500 , pp. 598-602
    • Yang, L.1    Lin, C.2    Jin, C.3    Yang, J.C.4    Tanasa, B.5    Li, W.6
  • 153
    • 65549168746 scopus 로고    scopus 로고
    • A novel androgen receptor splice variant is up-regulated during prostate cancer progression and promotes androgen depletion-resistant growth
    • Guo Z, Yang X, Sun F, Jiang R, Linn DE, Chen H, et al. A novel androgen receptor splice variant is up-regulated during prostate cancer progression and promotes androgen depletion-resistant growth. Cancer Res 2009; 69: 2305-13.
    • (2009) Cancer Res , vol.69 , pp. 2305-2313
    • Guo, Z.1    Yang, X.2    Sun, F.3    Jiang, R.4    Linn, D.E.5    Chen, H.6
  • 154
    • 77949379050 scopus 로고    scopus 로고
    • B-cellderived lymphotoxin promotes castration-resistant prostate cancer
    • Ammirante M, Luo JL, Grivennikov S, Nedospasov S, Karin M. B-cellderived lymphotoxin promotes castration-resistant prostate cancer. Nature 2010; 464: 302-5.
    • (2010) Nature , vol.464 , pp. 302-305
    • Ammirante, M.1    Luo, J.L.2    Grivennikov, S.3    Nedospasov, S.4    Karin, M.5
  • 155
    • 26844569717 scopus 로고    scopus 로고
    • Current thoughts on the role of the androgen receptor and prostate cancer progression
    • Setlur SR, Rubin MA. Current thoughts on the role of the androgen receptor and prostate cancer progression. Adv Anat Pathol 2005; 12: 265-70.
    • (2005) Adv Anat Pathol , vol.12 , pp. 265-270
    • Setlur, S.R.1    Rubin, M.A.2
  • 156
    • 84890078624 scopus 로고    scopus 로고
    • Glucocorticoid receptor confers resistance to antiandrogens by bypassing androgen receptor blockade
    • Arora VK, Schenkein E, Murali R, Subudhi SK, Wongvipat J, Balbas MD, et al. Glucocorticoid receptor confers resistance to antiandrogens by bypassing androgen receptor blockade. Cell 2013; 155: 1309-22.
    • (2013) Cell , vol.155 , pp. 1309-1322
    • Arora, V.K.1    Schenkein, E.2    Murali, R.3    Subudhi, S.K.4    Wongvipat, J.5    Balbas, M.D.6
  • 157
    • 84881403991 scopus 로고    scopus 로고
    • A road map to comprehensive androgen receptor axis targeting for castration-resistant prostate cancer
    • Mitsiades N. A road map to comprehensive androgen receptor axis targeting for castration-resistant prostate cancer. Cancer Res 2013; 73: 4599-605.
    • (2013) Cancer Res , vol.73 , pp. 4599-4605
    • Mitsiades, N.1
  • 158
    • 66249135684 scopus 로고    scopus 로고
    • Treatment-dependent androgen receptor mutations in prostate cancer exploit multiple mechanisms to evade therapy
    • Steinkamp MP, O'Mahony OA, Brogley M, Rehman H, Lapensee EW, Dhanasekaran S, et al. Treatment-dependent androgen receptor mutations in prostate cancer exploit multiple mechanisms to evade therapy. Cancer Res 2009; 69: 4434-42.
    • (2009) Cancer Res , vol.69 , pp. 4434-4442
    • Steinkamp, M.P.1    O'Mahony, O.A.2    Brogley, M.3    Rehman, H.4    Lapensee, E.W.5    Dhanasekaran, S.6
  • 159
    • 84883741726 scopus 로고    scopus 로고
    • Overview of the latest treatments for castrationresistant prostate cancer
    • Bishr M, Saad F. Overview of the latest treatments for castrationresistant prostate cancer. Nat Rev Urol 2013; 10: 522-8.
    • (2013) Nat Rev Urol , vol.10 , pp. 522-528
    • Bishr, M.1    Saad, F.2
  • 161
    • 79957497548 scopus 로고    scopus 로고
    • Expanding treatment options for metastatic prostate cancer
    • Antonarakis ES, Eisenberger MA. Expanding treatment options for metastatic prostate cancer. N Engl J Med 2011; 364: 2055-8.
    • (2011) N Engl J Med , vol.364 , pp. 2055-2058
    • Antonarakis, E.S.1    Eisenberger, M.A.2
  • 162
    • 65649090203 scopus 로고    scopus 로고
    • Development of a second-generation antiandrogen for treatment of advanced prostate cancer
    • Tran C, Ouk S, Clegg NJ, Chen Y, Watson PA, Arora V, et al. Development of a second-generation antiandrogen for treatment of advanced prostate cancer. Science 2009; 324: 787-90.
    • (2009) Science , vol.324 , pp. 787-790
    • Tran, C.1    Ouk, S.2    Clegg, N.J.3    Chen, Y.4    Watson, P.A.5    Arora, V.6
  • 165
    • 0025644325 scopus 로고
    • A mutation in the ligand binding domain of the androgen receptor of human LNCaP cells affects steroid binding characteristics and response to anti-androgens
    • Veldscholte J, Ris-Stalpers C, Kuiper GG, Jenster G, Berrevoets C, Claassen E, et al. A mutation in the ligand binding domain of the androgen receptor of human LNCaP cells affects steroid binding characteristics and response to anti-androgens. Biochem Biophys Res Commun 1990; 173: 534-40.
    • (1990) Biochem Biophys Res Commun , vol.173 , pp. 534-540
    • Veldscholte, J.1    Ris-Stalpers, C.2    Kuiper, G.G.3    Jenster, G.4    Berrevoets, C.5    Claassen, E.6
  • 166
    • 0027427321 scopus 로고
    • Threonine on amino-acid position-868 in the human androgen receptor is essential for androgen-binding specificity and functionalactivity
    • Risstalpers C, Verleunmooijman MCT, Trapman J, Brinkmann AO. Threonine on amino-acid position-868 in the human androgen receptor is essential for androgen-binding specificity and functionalactivity. Biochem Biophys Res Commun 1993; 196: 173-80.
    • (1993) Biochem Biophys Res Commun , vol.196 , pp. 173-180
    • Risstalpers, C.1    McT, V.2    Trapman, J.3    Brinkmann, A.O.4
  • 167
    • 0034125195 scopus 로고    scopus 로고
    • Glucocorticoids can promote androgen-independent growth of prostate cancer cells through a mutated androgen receptor
    • Zhao XY, Malloy PJ, Krishnan AV, Swami S, Navone NM, Peehl DM, et al. Glucocorticoids can promote androgen-independent growth of prostate cancer cells through a mutated androgen receptor. Nat Med 2000; 6: 703.
    • (2000) Nat Med , vol.6 , pp. 703
    • Zhao, X.Y.1    Malloy, P.J.2    Krishnan, A.V.3    Swami, S.4    Navone, N.M.5    Peehl, D.M.6
  • 168
    • 0037187408 scopus 로고    scopus 로고
    • Structural basis for the glucocorticoid response in a mutant human androgen receptor (AR(ccr)) derived from an androgenindependent prostate cancer
    • Matias PM, Carrondo MA, Coelho R, Thomaz M, Zhao XY, Wegg A, et al. Structural basis for the glucocorticoid response in a mutant human androgen receptor (AR(ccr)) derived from an androgenindependent prostate cancer. J Med Chem 2002; 45: 1439-46.
    • (2002) J Med Chem , vol.45 , pp. 1439-1446
    • Matias, P.M.1    Carrondo, M.A.2    Coelho, R.3    Thomaz, M.4    Zhao, X.Y.5    Wegg, A.6
  • 169
    • 85003173512 scopus 로고
    • Mutant androgen receptor detected in an advancedstage prostatic-carcinoma Is activated by adrenal androgens and progesterone
    • Culig Z, Hobisch A, Cronauer MV, Cato ACB, Hittmair A, Radmayr C, et al. Mutant androgen receptor detected in an advancedstage prostatic-carcinoma Is activated by adrenal androgens and progesterone. Mol Endocrinol 1993; 7: 1541-50.
    • (1993) Mol Endocrinol , vol.7 , pp. 1541-1550
    • Culig, Z.1    Hobisch, A.2    Cronauer, M.V.3    Acb, C.4    Hittmair, A.5    Radmayr, C.6
  • 171
    • 69249110003 scopus 로고    scopus 로고
    • Normal and cancer-related functions of the p160 steroid receptor co-activator (SRC) family
    • Xu J, Wu RC, O'Malley BW. Normal and cancer-related functions of the p160 steroid receptor co-activator (SRC) family. Nat Rev Cancer 2009; 9: 615-30.
    • (2009) Nat Rev Cancer , vol.9 , pp. 615-630
    • Xu, J.1    Wu, R.C.2    O'Malley, B.W.3
  • 172
    • 0037226103 scopus 로고    scopus 로고
    • Novel mutations of androgen receptor: A possible mechanism of bicalutamide withdrawal syndrome
    • Hara T, Miyazaki J, Araki H, Yamaoka M, Kanzaki N, Kusaka M, et al. Novel mutations of androgen receptor: a possible mechanism of bicalutamide withdrawal syndrome. Cancer Res 2003; 63: 149-53.
    • (2003) Cancer Res , vol.63 , pp. 149-153
    • Hara, T.1    Miyazaki, J.2    Araki, H.3    Yamaoka, M.4    Kanzaki, N.5    Kusaka, M.6
  • 173
    • 17844376217 scopus 로고    scopus 로고
    • Structural basis for antagonism and resistance of bicalutamide in prostate cancer
    • Bohl CE, Gao W, Miller DD, Bell CE, Dalton JT. Structural basis for antagonism and resistance of bicalutamide in prostate cancer. Proc Natl Acad Sci USA 2005; 102: 6201-6.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 6201-6206
    • Bohl, C.E.1    Gao, W.2    Miller, D.D.3    Bell, C.E.4    Dalton, J.T.5
  • 174
    • 84876265987 scopus 로고    scopus 로고
    • Enzalutamide: An evidence-based review of its use in the treatment of prostate cancer
    • Golshayan AR, Antonarakis ES. Enzalutamide: an evidence-based review of its use in the treatment of prostate cancer. Core Evid 2013; 8: 27-35.
    • (2013) Core Evid , vol.8 , pp. 27-35
    • Golshayan, A.R.1    Antonarakis, E.S.2
  • 175
    • 84885210324 scopus 로고    scopus 로고
    • A clinically relevant androgen receptor mutation confers resistance to second-generation antiandrogens enzalutamide and ARN-509
    • Joseph JD, Lu N, Qian J, Sensintaffar J, Shao G, Brigham D, et al. A clinically relevant androgen receptor mutation confers resistance to second-generation antiandrogens enzalutamide and ARN-509. Cancer Discov 2013; 3: 1020-9.
    • (2013) Cancer Discov , vol.3 , pp. 1020-1029
    • Joseph, J.D.1    Lu, N.2    Qian, J.3    Sensintaffar, J.4    Shao, G.5    Brigham, D.6
  • 177
    • 33846609681 scopus 로고    scopus 로고
    • Androgen receptor decoy molecules block the growth of prostate cancer
    • Quayle SN, Mawji NR, Wang J, Sadar MD. Androgen receptor decoy molecules block the growth of prostate cancer. Proc Natl Acad Sci USA 2007; 104: 1331-6.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1331-1336
    • Quayle, S.N.1    Mawji, N.R.2    Wang, J.3    Sadar, M.D.4
  • 178
    • 77953280591 scopus 로고    scopus 로고
    • Regression of castrate-recurrent prostate cancer by a small-molecule inhibitor of the amino-terminus domain of the androgen receptor
    • Andersen RJ, Mawji NR, Wang J, Wang G, Haile S, Myung JK, et al. Regression of castrate-recurrent prostate cancer by a small-molecule inhibitor of the amino-terminus domain of the androgen receptor. Cancer Cell 2010; 17: 535-46.
    • (2010) Cancer Cell , vol.17 , pp. 535-546
    • Andersen, R.J.1    Mawji, N.R.2    Wang, J.3    Wang, G.4    Haile, S.5    Myung, J.K.6
  • 180
    • 84862963669 scopus 로고    scopus 로고
    • Niphatenones, glycerol ethers from the sponge niphates digitalis block androgen receptor transcriptional activity in prostate cancer cells: Structure elucidation, synthesis, and biological activity
    • Meimetis LG, Williams DE, Mawji NR, Banuelos CA, Lal AA, Park JJ, et al. Niphatenones, glycerol ethers from the sponge niphates digitalis block androgen receptor transcriptional activity in prostate cancer cells: structure elucidation, synthesis, and biological activity. J Med Chem 2012; 55: 503-14.
    • (2012) J Med Chem , vol.55 , pp. 503-514
    • Meimetis, L.G.1    Williams, D.E.2    Mawji, N.R.3    Banuelos, C.A.4    Lal, A.A.5    Park, J.J.6
  • 181
    • 34547496561 scopus 로고    scopus 로고
    • Suppression of androgen receptor-mediated gene expression by a sequence-specific DNA-binding polyamide
    • Nickols NG, Dervan PB. Suppression of androgen receptor-mediated gene expression by a sequence-specific DNA-binding polyamide. Proc Natl Acad Sci USA 2007; 104: 10418-23.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 10418-10423
    • Nickols, N.G.1    Dervan, P.B.2
  • 182
    • 70149095918 scopus 로고    scopus 로고
    • Cyclic pyrrole-imidazole polyamides targeted to the androgen response element
    • Chenoweth DM, Harki DA, Phillips JW, Dose C, Dervan PB. Cyclic pyrrole-imidazole polyamides targeted to the androgen response element. J Am Chem Soc 2009; 131: 7182-8.
    • (2009) J Am Chem Soc , vol.131 , pp. 7182-7188
    • Chenoweth, D.M.1    Harki, D.A.2    Phillips, J.W.3    Dose, C.4    Dervan, P.B.5
  • 183
    • 84863631223 scopus 로고    scopus 로고
    • A competitive inhibitor that reduces recruitment of androgen receptor to androgen-responsive genes
    • Cherian MT, Wilson EM, Shapiro DJ. A competitive inhibitor that reduces recruitment of androgen receptor to androgen-responsive genes. J Biol Chem 2012; 287: 23368-80.
    • (2012) J Biol Chem , vol.287 , pp. 23368-23380
    • Cherian, M.T.1    Wilson, E.M.2    Shapiro, D.J.3
  • 184
    • 1542380019 scopus 로고    scopus 로고
    • Ligand-selective inhibition of the interaction of steroid receptor coactivators and estrogen receptor isoforms
    • Geistlinger TR, McReynolds AC, Guy RK. Ligand-selective inhibition of the interaction of steroid receptor coactivators and estrogen receptor isoforms. Chem Biol 2004; 11: 273-81.
    • (2004) Chem Biol , vol.11 , pp. 273-281
    • Geistlinger, T.R.1    McReynolds, A.C.2    Guy, R.K.3
  • 185
    • 25444478057 scopus 로고    scopus 로고
    • Development of peptide antagonists for the androgen receptor using combinatorial peptide phage display
    • Chang CY, Abdo J, Hartney T, McDonnell DP. Development of peptide antagonists for the androgen receptor using combinatorial peptide phage display. Mol Endocrinol 2005; 19: 2478-90.
    • (2005) Mol Endocrinol , vol.19 , pp. 2478-2490
    • Chang, C.Y.1    Abdo, J.2    Hartney, T.3    McDonnell, D.P.4
  • 186
    • 0034099382 scopus 로고    scopus 로고
    • Differential interaction of steroid hormone receptors with LXXLL motifs in SRC-1a depends on residues f?lanking the motif
    • Needham M, Raines S, McPheat J, Stacey C, Ellston J, Hoare S, et al. Differential interaction of steroid hormone receptors with LXXLL motifs in SRC-1a depends on residues f?lanking the motif. J Steroid Biochem Mol Biol 2000; 72: 35-46.
    • (2000) J Steroid Biochem Mol Biol , vol.72 , pp. 35-46
    • Needham, M.1    Raines, S.2    McPheat, J.3    Stacey, C.4    Ellston, J.5    Hoare, S.6
  • 187
    • 0036138806 scopus 로고    scopus 로고
    • Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs
    • Ko L, Cardona GR, Iwasaki T, Bramlett KS, Burris TP, Chin WW. Ser-884 adjacent to the LXXLL motif of coactivator TRBP defines selectivity for ERs and TRs. Mol Endocrinol 2002; 16: 128-40.
    • (2002) Mol Endocrinol , vol.16 , pp. 128-140
    • Ko, L.1    Cardona, G.R.2    Iwasaki, T.3    Bramlett, K.S.4    Burris, T.P.5    Chin, W.W.6
  • 188
    • 0035794168 scopus 로고    scopus 로고
    • Core LXXLL motif sequences in CREB-binding protein, SRC1, and RIP140 define affinity and selectivity for steroid and retinoid receptors
    • Heery DM, Hoare S, Hussain S, Parker MG, Sheppard H. Core LXXLL motif sequences in CREB-binding protein, SRC1, and RIP140 define affinity and selectivity for steroid and retinoid receptors. J Biol Chem 2001; 276: 6695-702.
    • (2001) J Biol Chem , vol.276 , pp. 6695-6702
    • Heery, D.M.1    Hoare, S.2    Hussain, S.3    Parker, M.G.4    Sheppard, H.5
  • 189
    • 0033928379 scopus 로고    scopus 로고
    • Specific structural motifs determine TRAP220 interactions with nuclear hormone receptors
    • Ren Y, Behre E, Ren Z, Zhang J, Wang Q, Fondell JD. Specific structural motifs determine TRAP220 interactions with nuclear hormone receptors. Mol Cell Biol 2000; 20: 5433-46.
    • (2000) Mol Cell Biol , vol.20 , pp. 5433-5446
    • Ren, Y.1    Behre, E.2    Ren, Z.3    Zhang, J.4    Wang, Q.5    Fondell, J.D.6
  • 190
    • 80052819425 scopus 로고    scopus 로고
    • Inhibitors of androgen receptor activation function-2 (AF2) site identified through virtual screening
    • Axerio-cilies P, Lack NA, Nayana MRS, Chan KH, Yeung A, Leblanc E, et al. Inhibitors of androgen receptor activation function-2 (AF2) site identified through virtual screening. J Med Chem 2011; 54: 6197-205.
    • (2011) J Med Chem , vol.54 , pp. 6197-6205
    • Axerio-Cilies, P.1    Lack, N.A.2    Mrs, N.3    Chan, K.H.4    Yeung, A.5    Leblanc, E.6
  • 191
    • 84055217577 scopus 로고    scopus 로고
    • Targeting the binding function 3 (BF3) site of the human androgen receptor through virtual screening
    • Lack NA, Axerio-Cilies P, Tavassoli P, Han FQ, Chan KH, Feau C, et al. Targeting the binding function 3 (BF3) site of the human androgen receptor through virtual screening. J Med Chem 2011; 54: 8563-73.
    • (2011) J Med Chem , vol.54 , pp. 8563-8573
    • Lack, N.A.1    Axerio-Cilies, P.2    Tavassoli, P.3    Han, F.Q.4    Chan, K.H.5    Feau, C.6
  • 193
    • 84871306277 scopus 로고    scopus 로고
    • Enzalutamide in prostate cancer after chemotherapy
    • Berruti A, Generali D, Tampellini M. Enzalutamide in prostate cancer after chemotherapy. N Engl J Med 2012; 367: 2448.
    • (2012) N Engl J Med , vol.367 , pp. 2448
    • Berruti, A.1    Generali, D.2    Tampellini, M.3
  • 194
    • 79951518634 scopus 로고    scopus 로고
    • Drug safety is a barrier to the discovery and development of new androgen receptor antagonists
    • Foster WR, Car BD, Shi H, Levesque PC, Obermeier MT, Gan J, et al. Drug safety is a barrier to the discovery and development of new androgen receptor antagonists. Prostate 2011; 71: 480-8.
    • (2011) Prostate , vol.71 , pp. 480-488
    • Foster, W.R.1    Car, B.D.2    Shi, H.3    Levesque, P.C.4    Obermeier, M.T.5    Gan, J.6
  • 196
    • 84891538656 scopus 로고    scopus 로고
    • Phase i study of ARN-509, a novel antiandrogen, in the treatment of castration-resistant prostate cancer
    • Rathkopf DE, Morris MJ, Fox JJ, Danila DC, Slovin SF, Hager JH, et al. Phase I study of ARN-509, a novel antiandrogen, in the treatment of castration-resistant prostate cancer. J Clin Oncol 2013; 31: 3525-30.
    • (2013) J Clin Oncol , vol.31 , pp. 3525-3530
    • Rathkopf, D.E.1    Morris, M.J.2    Fox, J.J.3    Danila, D.C.4    Slovin, S.F.5    Hager, J.H.6
  • 198
    • 84865798066 scopus 로고    scopus 로고
    • Structure-based virtual screening and identification of a novel androgen receptor antagonist
    • Song CH, Yang SH, Park E, Cho SH, Gong EY, Khadka DB, et al. Structure-based virtual screening and identification of a novel androgen receptor antagonist. J Biol Chem 2012; 287: 30769-80.
    • (2012) J Biol Chem , vol.287 , pp. 30769-30780
    • Ch, S.1    Yang, S.H.2    Park, E.3    Cho, S.H.4    Gong, E.Y.5    Khadka, D.B.6
  • 199
    • 84868089097 scopus 로고    scopus 로고
    • In silico discovery of androgen receptor antagonists with activity in castration resistant prostate cancer
    • Shen HC, Shanmugasundaram K, Simon NI, Cai C, Wang H, Chen S, et al. In silico discovery of androgen receptor antagonists with activity in castration resistant prostate cancer. Mol Endocrinol 2012; 26: 1836-46.
    • (2012) Mol Endocrinol , vol.26 , pp. 1836-1846
    • Shen, H.C.1    Shanmugasundaram, K.2    Simon, N.I.3    Cai, C.4    Wang, H.5    Chen, S.6
  • 200
    • 84862822261 scopus 로고    scopus 로고
    • Learning from estrogen receptor antagonism: Structure-based identification of novel antiandrogens effective against multiple clinically relevant androgen receptor mutants
    • Liu B, Geng G, Lin R, Ren C, Wu JH. Learning from estrogen receptor antagonism: structure-based identification of novel antiandrogens effective against multiple clinically relevant androgen receptor mutants. Chem Biol Drug Des 2012; 79: 300-12.
    • (2012) Chem Biol Drug des , vol.79 , pp. 300-312
    • Liu, B.1    Geng, G.2    Lin, R.3    Ren, C.4    Wu, J.H.5
  • 201
    • 84876869320 scopus 로고    scopus 로고
    • SAR based design of nicotinamides as a novel class of androgen receptor antagonists for prostate cancer
    • Yang SH, Song CH, Van HT, Park E, Khadka DB, Gong EY, et al. SAR based design of nicotinamides as a novel class of androgen receptor antagonists for prostate cancer. J Med Chem 2013; 56: 3414-8.
    • (2013) J Med Chem , vol.56 , pp. 3414-3418
    • Yang, S.H.1    Ch, S.2    Van Ht Park, E.3    Khadka, D.B.4    Gong, E.Y.5
  • 202
    • 84875635062 scopus 로고    scopus 로고
    • The discovery of novel human androgen receptor antagonist chemotypes using a combined pharmacophore screening procedure
    • Voet A, Helsen C, Zhang KY, Claessens F. The discovery of novel human androgen receptor antagonist chemotypes using a combined pharmacophore screening procedure. ChemMedChem 2013; 8: 644-51.
    • (2013) Chem Med Chem , vol.8 , pp. 644-651
    • Voet, A.1    Helsen, C.2    Zhang, K.Y.3    Claessens, F.4
  • 203
    • 34247159601 scopus 로고    scopus 로고
    • Circumventing anti-androgen resistance by molecular design
    • McGinley PL, Koh JT. Circumventing anti-androgen resistance by molecular design. J Am Chem Soc 2007; 129: 3822-3.
    • (2007) J Am Chem Soc , vol.129 , pp. 3822-3823
    • McGinley, P.L.1    Koh, J.T.2
  • 204
    • 77949876365 scopus 로고    scopus 로고
    • Study of the impact of the T877A mutation on ligand-induced helix-12 positioning of the androgen receptor resulted in design and synthesis of novel antiandrogens
    • Zhou J, Liu B, Geng G, Wu JH. Study of the impact of the T877A mutation on ligand-induced helix-12 positioning of the androgen receptor resulted in design and synthesis of novel antiandrogens. Proteins 2010; 78: 623-37.
    • (2010) Proteins , vol.78 , pp. 623-637
    • Zhou, J.1    Liu, B.2    Geng, G.3    Wu, J.H.4
  • 205
    • 84864622006 scopus 로고    scopus 로고
    • Evidence for DNA-binding domain-ligand-binding domain communications in the androgen receptor
    • Helsen C, Dubois V, Verfaillie A, Young J, Trekels M, Vancraenenbroeck R, et al. Evidence for DNA-binding domain-ligand-binding domain communications in the androgen receptor. Mol Cell Biol 2012; 32: 3033-43.
    • (2012) Mol Cell Biol , vol.32 , pp. 3033-3043
    • Helsen, C.1    Dubois, V.2    Verfaillie, A.3    Young, J.4    Trekels, M.5    Vancraenenbroeck, R.6
  • 206
    • 84864004802 scopus 로고    scopus 로고
    • High-resolution protein structure determination by serial femtosecond crystallography
    • Boutet S, Lomb L, Williams GJ, Barends TRM, Aquila A, Doak RB, et al. High-resolution protein structure determination by serial femtosecond crystallography. Science 2012; 337: 362-64.
    • (2012) Science , vol.337 , pp. 362-364
    • Boutet, S.1    Lomb, L.2    Williams, G.J.3    Trm, B.4    Aquila, A.5    Doak, R.B.6


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