REFERENCES
2. Huggins CB, Hodges CV. Studies on prostatic cancer 1. Effect of castration, estrogen and androgen injection on serum phosphatases in metatstatic carcinoma of the prostate. Cancer Res 1941;1:293-397.
3. Huggins CB. Two principles in endocrine therapy of cancers: Hormone deprival and hormone interference. Cancer Res 1965;25:1163-7.
4. Santen RJ, Demers L, Max DT, et al. Long term effects of administration of a gonadotropin-releasing hormone superagonist analog in men with prostatic carcinoma. J Clin Endocrinol Metab 1984;58:397-400.
6. Sharifi R, Soloway M. Clinical study of leuprolide depot formulation in the treatment of advanced prostate cancer. The Leuprolide Study Group. J Urol 1990;143:68-71.
7. Schellhammer PF, Sharifi R, Block NL, et al. A controlled trial of bicalutamide versus flutamide, each in combination with luteinizing hormone-releasing hormone analogue therapy, in patients with advanced prostate carcinoma. Analysis of time to progression. CASODEX Combination Study Group. Cancer 1996;78:2164-9.
8. Shah H, Vaishampayan U. Therapy of advanced prostate cancer: targeting the androgen receptor axis in earlier lines of treatment. Target Oncol 2018;13:679-89.
9. Yuan X, Cai C, Chen S, et al. Androgen receptor functions in castration-resistant prostate cancer and mechanisms of resistance to new agents targeting the androgen axis. Oncogene 2014;33:2815-25.
10. Cannata DH, Kirschenbaum A, Levine AC. Androgen deprivation therapy as primary treatment for prostate cancer. J Clin Endcorinol Metab 2012;97:360-5.
11. Attard G, Reid AHM, Yap TA, et al. Phase 1 clinical trial of a selective inhibitor of CYP17, abiraterone acetate, confirms that castration-resistant prostate cancer commonly remains hormone driven. J Clin Oncol 2008;28:4563-71.
12. Knudsen K, Scher HI. Starving the addiction: new opportunities for durable suppression of AR signaling in prostate cancer. Clin Cancer Res 2009;15:4792-8.
13. Knudsen K, Penning TM. Partners in crime: deregulation of AR activity and androgen synthesis in prostate cancer. Trends Endocrinol Metab 2010;21:315-24.
14. Visakorpi T, Hyytinen E, Koivisto P, et al. In vivo amplification of the androgen receptor gene and progression of human prostate cancer. Nat Genet 1995;9:401-6.
15. Buchanan G, Greenberg NM, Scher HI, et al. Collocation of androgen receptor gene mutations in prostate cancer. Clin Cancer Res 2001;7:1273-81.
16. Taplin ME, Bubley GJ, Shuster TD, et al. Mutation of the androgen-receptor gene in metastatic androgen-independent prostate cancer. N Engl J Med 1995;332:1393-8.
17. Taplin ME, Bubley GJ, Ko YJ, et al. Selection for androgen receptor mutations in prostate cancers treated with androgen antagonist. Cancer Res 1999;59:2511-5.
18. Dehm SM, Tindall DJ. Alternatively spliced androgen receptor variants. Endocr Relat Cancer 2011;18:R183-96.
19. Chen S, Xu Y, Yuan X, Bubley GJ, Balk SP. Androgen receptor phosphorylation and stabilization in prostate cancer by cyclin-dependent kinase 1. Proc Natl Acad Sci U S A 2006;103:15969-74.
20. Kemppainen JA, Lane MV, Sar M, Wilson EM. Androgen receptor phosphorylation, turnover, nuclear transport, and transcriptional activation. Specificity for steroids and antihormones. J Biol Chem 1992;267:968-74.
21. Labrie F, Belanger A, Simard J, et al. DHEA and peripheral androgen and estrogen formation: intracrinology. Ann N Y Acad Sci 1995;774:16-28.
22. Labrie F, Belanger A, Luu-The V, et al. DHEA and the intracrine formation of androgens and estrogens in peripheral target tissues: its role during aging. Steroids 1998;63:322-8.
23. Cai C, Chen S, Ng P, et al. Intratumoral de novo steroid synthesis activates androgen receptor in castration-resistant prostate cancer and is upregulated by treatment with CYP17A1 inhibitors. Cancer Res 2011;71:6503-13.
24. Wright JL, Kwon EM, Ostrander EA, et al. Expression of SLCO transport genes in castration-resistant prostate cancer and impact of genetic variation in SLCO1B3 and SLCO2B1 on prostate cancer outcomes. Cancer Epidemiol Biomarkers Prev 2011;20:619-27.
25. Clegg NJ, Wongvipat J, Joseph JD, et al. ARN-509: a novel antiandrogen for prostate cancer treatment. Cancer Res 2012;72:1494-503.
26. Fizazi K, Shore N, Tammela TL, et al. Darolutamide in nonmetastatic, castration-resistant prostate cancer. N Engl J Med 2019;380:1235-46.
27. Fizazi K, Smith MR, Tombal B. Clinical development of darolutamide: a novel androgen receptor antagonist for the treatment of prostate cancer. Clin Genitourin Cancer 2018;16:332-40.
28. Tran C, Ouk S, Clegg NJ, et al. Development of a second-generation antiandrogen for treatment of advanced prostate cancer. Science 2009;324:787-90.
29. de Bono JS, Logothetis CJ, Molina A, et al. Abiraterone and increased survival in metastatic prostate cancer. N Engl J Med 2011;364:1995-2005.
30. Fizazi K, Scher HI, Molina A, et al; COU-AA-301 Investigators. Abiraterone acetate for treatment of metastatic castration-resistant prostate cancer: final overall survival analysis of the COU-AA-301 randomised, double-blind, placebo-controlled phase 3 study. Lancet Oncol 2012;13:983-92.
31. Kwegyir-Afful AK, Ramaligam S, Ramamurthy VP, et al. Galeterone and the next generation galeterone analogs, VNPP414 and VNPP433-3beta exert potent therapeutic effects in castration-/drug-resistant prostate cancer preclinical models in vitro and in vivo. Cancers (Basel) 2019;11:1637.
32. Njar VC, Brodie AM. Discovery and development of Galeterone (TOK-001 or VN/124-1) for the treatment of all stages of prostate cancer. J Med Chem 2015;58:2077-87.
33. Rege J, Turcu AF, Kasa-Vubu JZ, et al. 11-Ketotestosterone is the dominant circulating bioactive androgen during normal and premature adrenarche. J Clin Endocrinol Metab 2018;103:4589-98.
34. Penning TM. Dehydroepiandrosterone (DHEA)-SO4 depot and castration-resistant prostate cancer. Vitam Horm 2018;108:309-31.
35. Locke JA, Nelson CC, Adomat HH, et al. Steroidogenesis inhibitors alter but do not eliminate androgen synthesis mechanisms during progression to castration-resistance in LNCaP prostate xenografts. J Steroid Biochem Mol Biol 2009;115:126-36.
36. Locke JA, Guns E, Lubik AA, et al. Androgen levels increase by intratumoral de novo steroidogenesis during progression of castration-resistant prostate cancer. Cancer Res 2008;68:6407-15.
37. Kumagai J, Hofland J, Erkens-Schulze S, et al. Intratumoral conversion of adrenal androgen precursors drives androgen receptor-activated cell growth in prostate cancer more potently than de novo steroidogenesis. Prostate 2013;73:1636-50.
38. Fankhauser M, Tan Y, Macintyre G, et al. Canonical androstenedione reduction is the predominant source of signaling androgens in hormone-refractory prostate cancer. Clin Cancer Res 2014;20:5547-57.
39. Mitsiades N, Sung CC, Schultz N, 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.
40. Chang KH, Li R, Papari-Zareei M, et al. Dihydrotestosterone synthesis bypasses testosterone to drive castration-resistant prostate cancer. Proc Natl Acad Sci U S A 2011;108:13728-33.
41. Sharifi N, Auchus RJ. Androstenedione is the preferred androgen source in hormone refractory prostate cancer--letter. Clin Cancer Res 2014;20:4971.
42. Montgomery RB, Mostaghel E, Vessella R, et al. Maintenance of intratumoral androgens in metastatic prostate cancer: a mechanism for castration-resistant tumor growth. Cancer Res 2008;68:4447-54.
44. Bauman DR, Steckelbroeck S, Williams MV, et al. Identification of the major oxidative 3a-hydroxysteroid dehydrogenase in human prostate that converts 5a-andostane-3a,17b-diol to 5a-dihydrotestosterone. A potential therapeutic target for androgen dependent disease. Mol Endocrinol 2006;20:444-58.
45. Mohler JL, Titus MA, Bai S, et al. Activation of the androgen receptor by intratumoral bioconversion of androstanediol to dihydrotestosterone in prostate cancer. Cancer Res 2011;71:1486-96.
46. Pretorius E, Africander DJ, Vlok M, et al. 11-Ketotestosterone and 11-Ketodihydrotestosterone in castration resistant prostate cancer: potent androgens which can no longer be ignored. PLoS One 2016;11:e0159867.
47. Pretorius E, Arlt W, Storbeck KH. A new dawn for androgens: novel lessons from 11-oxygenated C19 steroids. Mol Cell Endocrinol 2017;441:76-85.
48. Schiffer L, Arlt W, Storbeck KH. Intracrine androgen biosynthesis, metabolism and action revisited. Mol Cell Endocrinol 2018;465:4-26.
49. Barnard M, Quanson J L, Mostaghel E, et al. 11-Oxygenated androgen precursors are the preferred substrates for aldo-keto reductase 1C3 (AKR1C3): implications for castration resistant prostate cancer. J Steroid Biochem Mol Biol 2018;183:192-201.
50. Endo S, Morikawa Y, Kudo Y, et al. Human dehydrogenase/reductase SDR family member 11 (DHRS11) and aldo-keto reductase 1C isoforms in comparison: substrate and reaction specificity in the reduction of 11-keto-C19-steroids. J Steroid Biochem Mol Biol 2020;199:105586.
51. Penning TM, Jin Y, Rizner TL, Bauman DR. Pre-receptor regulation of the androgen receptor. Mol Cell Endocrinol 2008;281:1-8.
52. Steckelbroeck S, Jin Y, Gopishetty S, Oyesanmi B, Penning TM. Human cytosolic 3a-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display significant 3b-hydroxysteroid dehydrogenase activity: Implications for steroid hormone metabolism and action. J Biol Chem 2003;279:10784-95.
53. Penning TM, Bauman DR, Jin Y, Rizner TL. Identification of the molecular switch that regulates access of 5a-DHT to the androgen receptor. Mol Cell Endocrinol 2007;265-266:77-82.
54. Gao X, Dai C, Huang S, et al. Functional silencing of HSD17B2 in prostate cancer promotes disease progression. Clin Cancer Res 2019;25:1291-301.
55. Ko H, Berk M, Chung YM, et al. Loss of an androgen-inactivating and isoform-specific HSD17B4 splice form enables emergence of castration-resistant prostate cancer. Cell Rep 2018;22:809-19.
56. Chouinard S, Barbier O, Bélanger A. UDP-glucuronosyltransferase 2B15 (UGT2B15) and UGT2B17 enzymes are major determinants of the androgen response in prostate cancer LNCaP cells. J Biol Chem 2007;282:33466-74.
57. Pâquet S, Fazil L, Grosse L, et al. Differential expression of the androgen-conjugating UGT2B15 and UGT2B17 enzymes in prostate tumor cells during cancer progression. J Clin Endcrinol Metab 2012;97:E428-32.
58. Tamae D, Mostaghel E, Montgomery B, Nelson PS, Balk SP. The DHEA-sulfate depot following P450c17 inhibition supports the case for AKR1C3 inhibition in high risk localized and advanced castration resistant prostate cancer. Chem Biol Interact 2015;234:332-8.
59. Taplin ME, Montgomery B, Logothetis CJ, et al. Intense androgen-deprivation therapy with abiraterone acetate plus leuprolide acetate in patients with localized high-risk prostate cancer: results of a randomized phase II neoadjuvant study. J Clin Oncol 2014;32:3705-15.
60. Arakawa H, Nakanishi T, Yanagihara C, et al. Enhanced expression of organic anion transporting polypeptides (OATPs) in androgen receptor-positive prostate cancer cells: possible role of OATP1A2 in adaptive cell growth under androgen-depleted conditions. Biochem Pharmacol 2012;84:1070-7.
61. Green SM, Kaipainen A, Bullock K, et al. Role of OATP transporters in steroid uptake by prostate cancer cells in vivo. Prostate Cancer Prostatic Dis 2017;84:20-7.
62. Yang M, Xie W, Mostaghel E, et al. SLCO2B1 and SLCO1B3 may determine time to progression for patients receiving androgen deprivation therapy for prostate cancer. J Clin Oncol 2012;29:2565-73.
64. Hettel D, Zhang A, Alyamani M, Berk M, Sharifi N. AR signaling in prostate cancer regulates a feed-forward mechanism of androgen synthesis by way of HSD3B1 upregulation. Endocrinology 2018;159:2884-90.
65. Chang KH, Li R, Kuri B, et al. A gain-of-function mutation in DHT synthesis in castration-resistant prostate cancer. Cell 2013;154:1074-84.
66. Hearn JWD, AbuAli G, Reichard CA, et al. HSD3B1 and resistance to androgen-deprivation therapy in prostate cancer: a retrospective, multicohort study. Lancet Oncol 2016;17:1435-44.
67. Hearn JWD, Xie W, Nakabayashi M, et al. Association of HSD3B1 genotype with response to androgen-deprivation therapy for biochemical recurrence after radiotherapy for localized prostate cancer. JAMA Oncol 2018;4:558-62.
68. Li R, Evaul K, Sharma KK, et al. Abiraterone inhibits 3β-hydroxysteroid dehydrogenase: a rationale for increasing drug exposure in castration-resistant prostate cancer. Clin Cancer Res 2012;18:3571-9.
69. Li Z, Bishop AC, Alyamani M, et al. Conversion of abiraterone to D4A drives anti-tumour activity in prostate cancer. Nature 2015;523:347-51.
70. Stanbrough M, Bubley GJ, Ross K, et al. Increased expression of genes converting adrenal androgens to testosterone in androgen-independent prostate cancer. Cancer Res 2006;66:2815-25.
71. Hofland J, van Weerden WM, Dits NFJ, et al. Evidence of limited contributions for intratumoral steroidogenesis in prostate cancer. Cancer Res 2010;70:1256-64.
72. Hamid AR, Pfeiffer MJ, Verhaegh GW, et al. Aldo-keto reductase family 1 member C3 (AKR1C3) is a biomarker and therapeutic target for castration-resistant prostate cancer. Mol Med 2012;18:1449-55.
73. Pfeiffer MJ, Smit FP, Sedelaar JP, Schalken JA. Steroidogenic enzymes and stem cell markers are upregulated during androgen deprivation in prostate cancer. Mol Med 2011;17:657-64.
74. Knuuttila M, Yatkin E, Kallio J, et al. Castration induces up-regulation of intratumoral androgen biosynthesis and androgen receptor expression in an orthotopic VCaP human prostate cancer xenograft model. Am J Pathol 2014;184:2163-73.
75. Powell K, Semaan L, Conley-LaComb MK, et al. ERG/AKR1C3/AR constitutes a feed-forward loop for AR signaling in prostate Cancer Cells. Clin Cancer Res 2015;21:2569-79.
76. Tian Y, Zhao L, Zhang H, et al. AKR1C3 overexpression may serve as a promising biomarker for prostate cancer progression. Diagnostic Pathol 2014;9:42-8.
77. Zhao J, Zhang M, Liu J, et al. AKR1C3 expression in primary lesion rebiopsy at the time of metastatic castration-resistant prostate cancer is strongly associated with poor efficacy of abiraterone as a first-line therapy. Prostate 2019;79:1553-62.
78. Miyazaki Y, Teramoto Y, Shibuya S, et al. Consecutive prostate cancer specimens revealed increased Aldo-Keto reductase family 1 member C3 expression with progression to castration-resistant prostate cancer. J Clin Med 2019;8:E601.
79. Liu C, Lou W, Zhu Y, et al. Intracrine androgens and AKR1C3 activation confer resistance to Enzalutamide in prostate cancer. Cancer Res 2015;75:1413-22.
80. Liu C, Armstrong CM, Lou W, et al. Inhibition of AKR1C3 activation overcomes resistance to abiraterone in advanced prostate cancer. Mol Cancer Ther 2017;16:35-44.
81. Morsy A, Trippier PC. Reversal of apalutamide and darolutamide aldo-keto reductase 1C3-mediated resistance by a small molecule inhibitor. ACS Chem Biol 2020;15:646-50.
82. Platt A, Xia Z, Liu Y, Chen G, Lazarus P. Impact of nonsynomynous single nucleotide polymorphsims on in vitro metabolism of exemestane by hepatic cytosolic reductases. Genomics 2016;26:370-80.
83. Russell DW, Wilson JD. Steroid 5apha-reductase: two genes/two enzymes. Annu Rev Biochem 1994;63:25-61.
84. Ramos L, Vichis F, Chávez B, Mares L. Mutational analysis of SRD5A2: from gene to functional kinetics in individuals with steroid 5α-reductase 2 deficiency. J Steroid Biochem Mol Biol 2020;200:105691.
85. Makridakis N, Akalu A, Reichardt JK. Identification and characterization of somatic steroid 5alpha-reductase (SRD5A2) mutations in human prostate cancer tissue. Oncogene 2004;23:7399-405.
86. Cantagrel V, Lefeber DJ, Ng BG, et al. SRD5A3 is required for converting polyprenol to dolichol and is mutated in a congenital glycosylation disorder. Cell 2010;142:203-17.
87. Burczynski ME, Lin HK, Penning TM. Isoform-specific induction of a Human Aldo-Keto reductase by polycyclic aromatic hydrocarbons (PAHs), electrophiles, and oxidative stress: implications for the alternative pathway of PAH Activation catalyzed by human dihydrodiol dehydrogenase. Cancer Res 1999;59:607-14.
88. Takahashi RH, Grigliatti TA, Reid RE, Riggs KW. The effectc of allelic variation in aldo-keto-reductase 1C2 on the in vitro metabolism of dihydrotestosterone. J Pharmaco Exp Ther 2009;329:1032-9.
89. Zhu Z, Chung YM, Sergeeva O, et al. Loss of dihydrotestosterone-inactivation activity promotes prostate cancer castration resistance detectable by functional imaging. J Biol Chem 2018;293:17829-37.
90. Gauthier-Landry L, Bélanger A, Barbier O. Multiple roles for UDP-glucuronosyltransferase (UGT)2B15 and UGT2B17 enzymes in androgen metabolism and prostate cancer evolution. J Steroid Biochem Mol Biol 2015;145:187-92.
91. Liu LL, Xie N, Sun S, et al. Mechanisms of the androgen receptor splicing in prostate cancer cells. Oncogene 2014;33:3140-50.
92. Zhang A, Zhang J, Plymate S, Mostaghel EA. Classical and non-classical roles for pre-receptor control of DHT metabolism in prostate cancer progression. Horm Cancer 2016;7:104-13.
93. Vidal AC, Tucker C, Schildkraut JM, et al. Novel associations of UDP-glucuronosyltransferase 2B gene variants with prostate cancer risk in a multiethnic study. BMC Cancer 2013;13:556.
94. Yepuru M, Wu Z, Kyulkarni A, et al. Steroidogenic enzyme AKR1C3 is a novel androgen receptor-selective coactivator that promotes prostate cancer growth. Clin Cancer Res 2013;19:5613-25.
95. Culig Z, Comuzzi B, Steiner H, Bartsch G, Hobisch A. Expression and function of androgen receptor coactivators in prostate cancer. J Steroid Biochem Mol Biol 2004;92:265-71.
96. He B, Bowen NT, Minges JT, Wilson EM. Androgen-induced NH2- and COOH-terminal interaction inhibits p160 coactivator recruitment by activation function 2. J Biol Chem 2001;276:422293-301.
97. He B, Lee LW, Minges JT, Wilson EM. Dependence of selective gene activation on the androgen receptor NH2- and COOH-terminal interaction. J Biol Chem 2002;277:25631-9.
98. Liu C, Yang JC, Armstrong CM, et al. AKR1C3 promotes AR-V7 protein stabilization and confers resistance to AR-targeted therapies in advanced prostate cancer. Mol Cancer Ther 2019;18:1875-96.
99. Fan L, Peng G, Hussain A, et al. The steroidogenic enzyme AKR1C3 regulates stability of the ubiquitin ligase Siah2 in prostate cancer cells. J Biol Chem 2015;290:20865-79.
100. Penning T. AKR1C3 (Type 5 17β-hydroxysteroid Dehydrogenase/Prostaglandin F Synthase): roles in malignancy and endocrine disorders. Mol Cell Endcorinol 2019;489:82-91.
101. Thompson IM, Goodman PJ, Tangen CM, et al. The influence of finasteride on the development of prostate cancer. Engl J Med 2003;349:215-24.
102. Andriole GL, Bostwick DG, Brawley OW, et al; REDUCE Study Group. Effect of dutasteride on the risk of prostate cancer. N Engl J Med 2010;362:1192-202.
103. Penning TM, Wangtrakuldee P, Auchus RJ. Structural and functional biology of aldo-keto reductase steroid-transofrming enzymes. Endocrine Rev 2019;40:447-75.
104. Adeniji AO, Uddin MJ, Zang T, et al. Discovery of (R)-2-(6-Methoxynaphthalen-2-yl)butanoic acid as a potent and selective aldo-keto reductase 1C3 inhibitor. J Med Chem 2016;59:7431-44.
105. Adeniji AO, Twenter BM, Byrns MC, et al. Development of potent and selective inhibitors of aldo-keto reductase 1C3 (type 5 17β-hydroxysteroid dehydrogenase) based on N-phenyl-aminobenzoates and their structure-activity relationships. J Med Chem 2012;55:2311-23.
106. Liedtke AJ, Adeniji AO, Chen M, et al. Development of potent and selective indomethacin analogues for the inhibition of AKR1C3 (type 5 17b-hydroxysteroid dehydrogenase/prostaglandin F synthase) in castrate-resistant prostate cancer. J Med Chem 2013;56:2429-46.
107. Lolli ML, Carnovale I, Pippione AC, et al. Bioisosteres of indomethacin as inhibitors of aldo-keto reductase 1C3. ACS Med Chem Lett 2019;10:437-43.
108. Jamieson SM, Brooke D, Heinrich D, et al. 3-(3,4-Dihydroisoquinolin-2(1H)-ylsulfonyl)benzoic acids: highly potent and selective inhibitors of the type 5 17-β-hydroxysteroid dehydrogenase AKR1C3. J Med Chem 2012;55:7746-58.
109. Li C, Zhao Y, Zheng X, et al. In vitro CAPE inhibitory activity towards human AKR1C3 and the molecular basis. Chen Biol Inter 2016;253:60-5.
110. Tian Y, Zhao L, Wang Y, et al. Berberine inhibits androgen synthesis by interaction with aldo-keto reductase 1C3 in 22Rv1 prostate cancer cells. Asian J Androl 2016;18:607-12.
111. Heinrich DM, Flanagan J, Jamieson SM, et al. Synthesis and structure-activity relationships for 1-(4-(piperidin-1-ylsulfonyl)phenyl)pyrrolidin-2-ones as novel non-carboxylate inhibitors of the aldo-keto reductase enzyme AKR1C3. Eur J Med Chem 2013;62:738-44.
112. Gazvoda M, Beranic N, Turk S, et al. 2,3-diarylpropenoic acids as selective non-steroidal inhibitors of type-5 17β-hydroxysteroid dehydrogenase (AKR1C3). Eur J Med Chem 2013;62:89-97.
113. Kikuchi A, Furutani T, Azami H, et al. In vitro and in vivo characterization of ASP9521: a novel selective, orally bioavailable inhibitor of 17b-hydroxysteroid dehydrogenase type 5 (17b-HSD5; AKR1C3). Invest New Drugs 2014;32:860-70.
114. Loriot Y, Fizazi K, Jones RJ, Brand Van den J, Molife RL, et al. Safety, tolerability and anti- tumor activity of the androgen biosynthesis inhibitor ASP9521 in patients with metastatic castration-resistant prostate cancer: multi-centre phase I/II study. Invest New Drugs 2014;32:995-1004.
115. Verma K, Gupta N, Zang T, Wangtrakluldee P, Srivastava SK, et al. AKR1C3 Inhibitor KV-37 exhibits antineoplastic effects and potentiates enzalutamide in combination therapy in prostate adenocarcinoma cells. Mol Cancer Ther 2018;17:1833-45.
116. Hulcová D, Breiterová K, Zemanová L, et al. AKR1C3 inhibitory potency of naturally-occurring amaryllidaceae alkaloids of different structural types. Nat Prod Commun 2017;12:245-6.
117. Byrns MC, Jin Y, Penning TM. Inhibitors of type 5 17β-hydroxysteroid dehydrogenase (AKR1C3): overview and structural insights. J Steroid Biochem Mol Biol 2011;125:95-104.
118. Penning TM. Aldo-Keto Reductase (AKR) 1C3 inhibitors: a patent review. Expert Opin Ther Pat 2017;27:1329-40.
119. Lin HK, Steckelbroeck S, Fung KM, Jones AN, Penning TM. Characterization of a monoclonal antibody for human aldo-keto reductase AKR1C3 (type 2 3a-hydroxysteroid dehydrogenase/type 5 17b-hydroxysteroid dehydrogenase); immunohistochemical detection in breast and prostate. Steroids 2004;69:795-801.
120. Rizner TL, Penning TM. Aldo-keto reductase 1C3-assessment as a new target for the treatment of endometriosis. Pharmacol Res 2020;152:104446.
121. Chen M, Adeniji AO, Twenter BM, et al. Crystal structures of AKR1C3 containing an N-(aryl)amino-benzoate inhibitor and a bifunctional AKR1C3 inhibitor and androgen receptor antagonist. Therapeutic leads for castrate resistant prostate cancer. Bioorg Med Chem Lett 2012;22:3492-7.
122. Wangtrakuldee P, Adeniji AO, Zang T, et al. A 3-(4-nitronaphthen-1-yl) amino-benzoate analog as a bifunctional AKR1C3 inhibitor and AR antagonist: Head to head comparison with other advanced AKR1C3 targeted therapeutics. J Steroid Biochem & Mol Biol 2019;192:105283.
123. Schweizer MT, Plymate SR. Targeting constitutively active androgen receptor splice variants in castration resistant prostate cancer. Expert Opin Ther Targets 2016;20:903-6.
124. Antonarakis ES, Lu C, Wang H, et al. AR-V7 and resistance to enzalutamide and abiraterone in prostate cancer. N Engl J Med 2014;371:1028-38.
125. Antonarakis ES, Lu C, Luber B, et al. Androgen receptor splice variant 7 and efficacy of taxane chemotherapy in patients with metastatic castration-resistant prostate cancer. JAMA Oncol 2015;1:582-19.
126. Antonarakis ES, Lu C, Luber B, et al. Clinical significance of androgen receptor splice variant-7 mRNA detection in circulating tumor cells of men with metastatic castration-resistant prostate cancer treated with first- and second-line abiraterone and enzalutamide. J Clin Oncol 2017;35:2149-56.
127. Rasool RU, Natesan R, Deng Q, et al. A CDK7 inhibition suppresses castration-resistant prostate cancer through MED1 inactivation. Cancer Discov 2019;9:1538-55.
128. Russo JW, Liu X, Ye H, Calagua C, Chen S. Phosphorylation of androgen receptor serine 81 is associated with its reactivation in castration-resistant prostate cancer. Cancer Lett 2018;438:97-104.
129. Narayanan S, Srinivas S, Feldman D. Androgen-glucocorticoid interactions in the era of novel prostate cancer therapy. Nat Rev Urol 2016;13:47-60.
