AKR1C3 (type 5 17β-hydroxysteroid dehydrogenase/prostaglandin F synthase): Roles in malignancy and endocrine disorders

Abiraterone and Increased Survival in Metastatic Prostate Cancer

de Bono, J. S., Logothetis, C. J., Molina, A., Fizazi, K., North, S., Chu, L., Chi, K. N., Jones, R. J., Goodman, O. B., Saad, F., et al. (2011) · New England Journal of Medicine · doi:10.1056/nejmoa1014618 · Cited by 4,407

A prostaglandin J2 metabolite binds peroxisome proliferator-activated receptor γ and promotes adipocyte differentiation

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9-cis retinoic acid is a high affinity ligand for the retinoid X receptor

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9-Cis retinoic acid stereoisomer binds and activates the nuclear receptor RXRα

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Increased Expression of Genes Converting Adrenal Androgens to Testosterone in Androgen-Independent Prostate Cancer

Stanbrough, M., Bubley, G. J., Ross, K., Golub, T. R., Rubin, M. A., Penning, T. M., Febbo, P. G., & Balk, S. P. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4000 · Cited by 1,082

Antitumour activity of MDV3100 in castration-resistant prostate cancer: a phase 1–2 study

Scher, H. I., Beer, T. M., Higano, C. S., Anand, A., Taplin, M., Efstathiou, E., Rathkopf, D. E., Shelkey, J., Yu, E. Y., Alumkal, J. J., et al. (2010) · The Lancet · doi:10.1016/s0140-6736(10)60172-9 · Cited by 1,063

Phase I Clinical Trial of a Selective Inhibitor of CYP17, Abiraterone Acetate, Confirms That Castration-Resistant Prostate Cancer Commonly Remains Hormone Driven

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Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease

Tebay, L. E., Robertson, H., Durant, S. T., Vitale, S. R., Penning, T. M., Dinkova-Kostova, A. T., & Hayes, J. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.021 · Cited by 837

Human 3α-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones

PENNING, T. M., BURCZYNSKI, M. E., JEZ, J. M., HUNG, C.-F., LIN, H.-K., MA, H., MOORE, M., PALACKAL, N., & RATNAM, K. (2000) · Biochemical Journal · doi:10.1042/bj3510067 · Cited by 649

Comparative anatomy of the aldo–keto reductase superfamily

Jez, J. M., BENNETT, M. J., Schlegel, B. P., Lewis, M., & Penning, T. M. (1997) · Biochemical Journal · doi:10.1042/bj3260625 · Cited by 603

Targeting the Androgen Signaling Axis in Prostate Cancer

Dai, C. S., Dehm, S. M., & Sharifi, N. (2023) · Journal of Clinical Oncology · doi:10.1200/jco.23.00433 · Cited by 182

Aldo-Keto Reductases and Cancer Drug Resistance

Penning, T. M., Jonnalagadda, S. K., Trippier, P. C., & Rižner, T. L. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000122 · Cited by 158

The Role of Prostaglandins in Different Types of Cancer

Jara-Gutiérrez, Á., & Baladrón, V. (2021) · Cells · doi:10.3390/cells10061487 · Cited by 111

Overview of AKR1C3: Inhibitor Achievements and Disease Insights

Liu, Y., He, S., Chen, Y., Liu, Y., Feng, F., Liu, W., Guo, Q., Zhao, L., & Sun, H. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b02138 · Cited by 105

Conversion of Classical and 11-Oxygenated Androgens by Insulin-Induced AKR1C3 in a Model of Human PCOS Adipocytes

Paulukinas, R. D., Mesaros, C., & Penning, T. M. (2022) · Endocrinology · doi:10.1210/endocr/bqac068 · Cited by 63

Identification and Validation of a Prognostic Signature for Prostate Cancer Based on Ferroptosis-Related Genes

Liu, H., Gao, L., Li, J., Zhai, T., Xie, T., & Xu, Y. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.623313 · Cited by 53

Unraveling the differential impact of PAHs and dioxin-like compounds on AKR1C3 reveals the EGFR extracellular domain as a critical determinant of the AHR response

Vogeley, C., Sondermann, N. C., Woeste, S., Momin, A. A., Gilardino, V., Hartung, F., Heinen, M., Maaß, S. K., Mescher, M., Pollet, M., et al. (2021) · Environment International · doi:10.1016/j.envint.2021.106989 · Cited by 55

Statins and prostate cancer—hype or hope? The epidemiological perspective

Craig, E. L., Stopsack, K. H., Evergren, E., Penn, L. Z., Freedland, S. J., Hamilton, R. J., & Allott, E. H. (2022) · Prostate Cancer and Prostatic Diseases · doi:10.1038/s41391-022-00554-1 · Cited by 48

AKR1C3 regulated by NRF2/MAFG complex promotes proliferation via stabilizing PARP1 in hepatocellular carcinoma

Pan, D., Yang, W., Zeng, Y., Qin, H., Xu, Y., Gui, Y., Fan, X., Tian, G., Wu, Y., Sun, H., et al. (2022) · Oncogene · doi:10.1038/s41388-022-02379-7 · Cited by 37

Targeting Pharmacokinetic Drug Resistance in Acute Myeloid Leukemia Cells with CDK4/6 Inhibitors

Sorf, A., Sucha, S., Morell, A., Novotná, E., Štaud, F., Zavřelová, A., Víšek, B., Wsól, V., & Čečková, M. (2020) · Cancers · doi:10.3390/cancers12061596 · Cited by 34

AKR1C3 in carcinomas: from multifaceted roles to therapeutic strategies

Li, M., Zhang, L., Yu, J., Wang, X., Cheng, L., Ma, Z., Chen, X., Wang, L., & Goh, B. C. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1378292 · Cited by 36

Diagnostic and prognostic values of AKR1C3 and AKR1D1 in hepatocellular carcinoma

Zhu, P., Feng, R., Lu, X., Liao, Y., Du, Z., Zhai, W., & Chen, K. (2021) · Aging · doi:10.18632/aging.202380 · Cited by 32

Aldo-Keto Reductase 1C3 Mediates Chemotherapy Resistance in Esophageal Adenocarcinoma via ROS Detoxification

Zhou, C., Wang, Z., Li, J., Wu, X., Fan, N., Li, D., Liu, F., Plum, P. S., Hoppe, S., Hillmer, A. M., et al. (2021) · Cancers · doi:10.3390/cancers13102403 · Cited by 32

Evaluation of 17β-hydroxysteroid dehydrogenase activity using androgen receptor-mediated transactivation

Yazawa, T., Imamichi, Y., Uwada, J., Sekiguchi, T., Mikami, D., Kitano, T., Ida, T., Sato, T., Nemoto, T., Nagata, S., et al. (2019) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2019.105493 · Cited by 30

Development of highly potent and specific AKR1C3 inhibitors to restore the chemosensitivity of drug-resistant breast cancer

Liu, Y., Chen, Y., Jiang, J., Chu, X., Guo, Q., Zhao, L., Feng, F., Liu, W., Zhang, X., He, S., et al. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.115013 · Cited by 28

Targeting sex steroid biosynthesis for breast and prostate cancer therapy

POUTANEN, M. H., Thulin, M. H., & Härkönen, P. L. (2023) · Nature reviews. Cancer · doi:10.1038/s41568-023-00609-y · Cited by 31

AKR1C3 Is Associated with Better Survival of Patients with Endometrial Carcinomas

Hojnik, M., Šuster, N. K., Smrkolj, Š., Grazio, S. F., Verdenik, I., & Rižner, T. L. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9124105 · Cited by 26

Advances in ferroptosis for castration-resistant prostate cancer treatment: novel drug targets and combination therapy strategies

Chen, H., Lyu, F., & Gao, X. (2024) · Prostate Cancer and Prostatic Diseases · doi:10.1038/s41391-024-00933-w · Cited by 29

Novel inhibition of AKR1C3 and androgen receptor axis by PTUPB synergizes enzalutamide treatment in advanced prostate cancer

Yang, J. C., Xu, P., Ning, S., Wasielewski, L. J., Adomat, H. H., Hwang, S. H., Morisseau, C. H. P., Gleave, M. E., Corey, E., Gao, A. C., et al. (2023) · Oncogene · doi:10.1038/s41388-022-02566-6 · Cited by 23

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

Endo, S., Morikawa, Y., Kudo, Y., Suenami, K., Matsunaga, T., Ikari, A., & Hara, A. (2020) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2020.105586 · Cited by 21

New aldo-keto reductase 1C3 (AKR1C3) inhibitors based on the hydroxytriazole scaffold

Pippione, A. C., Kılıç-Kurt, Z., Kovachka, S., Sainas, S., Rolando, B., Denasio, E., Pors, K., Adinolfi, S., Zonari, D., Bagnati, R., et al. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114366 · Cited by 20

Molecular Mechanism Study on Stereo-Selectivity of α or β Hydroxysteroid Dehydrogenases

Gao, M., Nie, K., Qin, M., Xu, H.-J., Wang, F., & Liu, L. (2021) · Crystals · doi:10.3390/cryst11030224 · Cited by 22

Insulin-Induced AKR1C3 Induces Fatty Acid Synthase in a Model of Human PCOS Adipocytes

Paulukinas, R. D., & Penning, T. M. (2023) · Endocrinology · doi:10.1210/endocr/bqad033 · Cited by 19

Hepatotoxicity of AKR1C3 Inhibitor BAY1128688: Findings from an Early Terminated Phase IIa Trial for the Treatment of Endometriosis

Hilpert, J., Groettrup‐Wolfers, E., Kosturski, H., Bennett, L., Barnes, C. L. K., Gude, K., Gashaw, I., Reif, S., Steger‐Hartmann, T., Scheerans, C., et al. (2023) · Drugs in R&D · doi:10.1007/s40268-023-00427-5 · Cited by 18

Future directions in endometriosis treatment: discovery and development of novel inhibitors of estrogen biosynthesis

Barra, F., Romano, A., Grandi, G., Facchinetti, F., & Ferrero, S. (2019) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2019.1618269 · Cited by 18

Hydroxyazoles as acid isosteres and their drug design applications—Part 1: Monocyclic systems

Sainas, S., Pippione, A. C., Boschi, D., & Lolli, M. L. (2021) · Advances in heterocyclic chemistry · doi:10.1016/bs.aihch.2020.12.001 · Cited by 18

Reinke crystals: Hallmarks of adult Leydig cells in humans

Planinić, A., Marić, T., Bojanac, A. K., & Ježek, D. (2022) · Andrology · doi:10.1111/andr.13201 · Cited by 16

X-ray structure of human aldo–keto reductase 1C3 in complex with a bile acid fused tetrazole inhibitor: experimental validation, molecular docking and structural analysis

Marinović, M. A., Bekić, S. S., Kugler, M., Brynda, J., Škerlová, J., Škorić, D., Řezáčová, P., Petri, E. T., & Ćelić, A. S. (2022) · RSC Medicinal Chemistry · doi:10.1039/d2md00387b · Cited by 17

A Targeted-Covalent Inhibitor of 17β-HSD1 Blocks Two Estrogen-Biosynthesis Pathways: In Vitro (Metabolism) and In Vivo (Xenograft) Studies in T-47D Breast Cancer Models

Poirier, D., Roy, J., & Maltais, R. (2021) · Cancers · doi:10.3390/cancers13081841 · Cited by 20

AKR1C3 expression in T acute lymphoblastic leukemia/lymphoma for clinical use as a biomarker

Reddi, D., Seaton, B. W., Woolston, D. W., Aicher, L. D., Monroe, L. D., Mao, Z. J., Harrell, J. C., Radich, J. P., Advani, A. S., Papadantonakis, N., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-09697-6 · Cited by 17

Roles of AKR1C3 in malignancy

Xiao, X., Lin, L., Zhuang, M., Zhong, C., & Chen, F. (2021) · Chinese Medical Journal · doi:10.1097/cm9.0000000000001379 · Cited by 16

Polymorphisms in androgen metabolism genes with serum testosterone levels and prognosis in androgen-deprivation therapy.

Shiota, M., Endo, S., Fujimoto, N., Tsukahara, S., Ushijima, M., Kashiwagi, E., Takeuchi, A., Inokuchi, J., Uchiumi, T., & Eto, M. (2020) · Urologic oncology · doi:10.1016/j.urolonc.2020.06.033 · Cited by 16

Analogues of Natural Chalcones as Efficient Inhibitors of AKR1C3

Möller, G., Temml, V., Cala, A., Gruet, O., Richomme, P., Séraphin, D., Viault, G., Kraus, L., Huber‐Cantonati, P., Schopfhauser, E., et al. (2022) · Metabolites · doi:10.3390/metabo12020099 · Cited by 16

Sex steroid metabolism and action in colon health and disease

Banibakhsh, A., Sidhu, D., Khan, S., Haime, H., & Foster, P. (2023) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2023.106371 · Cited by 13

AKR1C3 Converts Castrate and Post-Abiraterone DHEA-S into Testosterone to Stimulate Growth of Prostate Cancer Cells via 5-Androstene-3β,17β-Diol

Detlefsen, A. J., Mesaros, C., Duan, L., & Penning, T. M. (2023) · Cancer Research Communications · doi:10.1158/2767-9764.crc-23-0235 · Cited by 14

Structure-guided optimization of 3-hydroxybenzoisoxazole derivatives as inhibitors of Aldo-keto reductase 1C3 (AKR1C3) to target prostate cancer

Pippione, A. C., Kovachka, S., Vigato, C., Bertarini, L., Mannella, I., Sainas, S., Rolando, B., Denasio, E., Piercy-Mycock, H., Romalho, L., et al. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116193 · Cited by 13

Microproteomics and Immunohistochemistry Reveal Differences in Aldo‐Keto Reductase Family 1 Member C3 in Tissue Specimens of Ulcerative Colitis and Crohn's Disease

Arafah, K., Kriegsmann, M., Renner, M., Lasitschka, F., Fresnais, M., Kriegsmann, K., von Winterfeld, M., Goeppert, B. F., Kriegsmann, J., Casadonte, R., et al. (2020) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201900110 · Cited by 13

Identification of Featured Metabolism-Related Genes in Patients with Acute Myocardial Infarction

Xie, H., Zhao, E., & Zhang, Y. (2020) · Disease Markers · doi:10.1155/2020/8880004 · Cited by 12

Androgen and Estrogen β Receptor Expression Enhances Efficacy of Antihormonal Treatments in Triple-Negative Breast Cancer Cell Lines

Crespo, B., Illera, J. C., Silván, G., Lopez-Plaza, P., de la Muela, M. H., Yagüe, M. D. L. P., del Arco, C. D., Illera, M. J., & Cáceres, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031471 · Cited by 11

Potential biomarkers of acute myocardial infarction based on co‑expression network analysis

Hu, Z., Liu, R., Hu, H., Ding, X., Ji, Y., Li, G., Wang, Y., Xie, S., Liu, X., & Ding, Z. (2021) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2021.11085 · Cited by 11

Characterization of the major single nucleotide polymorphic variants of aldo-keto reductase 1C3 (type 5 17β-hydroxysteroid dehydrogenase)

Detlefsen, A. J., Wangtrakuldee, P., & Penning, T. M. (2022) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2022.106121 · Cited by 12

Genome-scale CRISPR screens identify PTGES3 as a direct modulator of androgen receptor function in advanced prostate cancer

Li, H., Melnyk, J. E., Fu, B. X. H., Shrestha, R., Zhang, M., Sjöström, M., Feng, S., Anderson, J. A., Han, W., Chesner, L. N., et al. (2025) · Nature Genetics · doi:10.1038/s41588-025-02388-8 · Cited by 10

Aldo-keto reductase family 1 member C3 (AKR1C3) gene polymorphism (rs12529) is associated with breast cancer in Bangladeshi population: A case-control study and computational investigation

Shaon, M. A., Ansari, F., Mahmud, Z., Tamanna, S., Ibrahim, M. N. B., Alam, N. F., Hossain, M. N., & Howlader, M. Z. H. (2025) · PLoS ONE · doi:10.1371/journal.pone.0318079 · Cited by 11

Small molecules as products of evolution

Markov, G. V., & Laudet, V. (2022) · Current Biology · doi:10.1016/j.cub.2021.12.038 · Cited by 10

Quantitative Systems Toxicology Identifies Independent Mechanisms for Hepatotoxicity and Bilirubin Elevations Due to AKR1C3 Inhibitor BAY1128688

Battista, C., Shoda, L. K. M., Watkins, P. B., Groettrup‐Wolfers, E., Rottmann, A., Raschke, M., & Generaux, G. T. (2023) · Clinical Pharmacology & Therapeutics · doi:10.1002/cpt.3010 · Cited by 10

Inhibitory Interplay of SULT2B1b Sulfotransferase with AKR1C3 Aldo-keto Reductase in Prostate Cancer

Park, S.-G., Song, C.-S., Lin, C.-L., Jiang, S., Osmulski, P. A., Wang, C., Marck, B. T., Matsumoto, A. M., Morrissey, C. M., Gaczynska, M. E., et al. (2020) · Endocrinology · doi:10.1210/endocr/bqz042 · Cited by 10

Canonical and Noncanonical Androgen Metabolism and Activity

Storbeck, K., & Mostaghel, E. A. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-32656-2_11 · Cited by 10

Influence of Indomethacin on Steroid Metabolism: Endocrine Disruption and Confounding Effects in Urinary Steroid Profiling of Anti-Doping Analyses

Stoll, A., Iannone, M., Gregorio, G. D., Molaioni, F., de la Torre, X., Botrè, F., & Parr, M. K. (2020) · Metabolites · doi:10.3390/metabo10110463 · Cited by 10

Aberrant epigenetic regulation of estrogen and progesterone signaling at the level of endometrial/endometriotic tissue in the pathomechanism of endometriosis

Szukiewicz, D. (2022) · Vitamins and hormones · doi:10.1016/bs.vh.2022.11.005 · Cited by 10

A Mansonone Derivative Coupled with Monoclonal Antibody 4D5-Modified Chitosan Inhibit AKR1C3 to Treat Castration-Resistant Prostate Cancer

Zhou, M., Wang, X., Xia, J., Cheng, Y., Xiao, L., Yu, B., Tang, J., Huang, Y., Xiang, Q., & Huang, S. (2020) · International Journal of Nanomedicine · doi:10.2147/ijn.s241324 · Cited by 9

Network Pharmacological Study of the Active Ingredient of Panax Notoginseng Saponins for the Treatment of Lung Cancer by Inhibiting AKR1C3

Wei, Y.-Z., Yang, M.-Z., & Yuan, W. (2023) · Letters in Drug Design & Discovery · doi:10.2174/1570180820666230914104206 · Cited by 8

The third generation AKR1C3-activated prodrug, ACHM-025, eradicates disease in preclinical models of aggressive T-cell acute lymphoblastic leukemia

Toscan, C. E., McCalmont, H., Ashoorzadeh, A., Lin, X., Fu, Z., Doculara, L., Kosasih, H. J., Cadiz, R., Zhou, A., Williams, S., et al. (2024) · Blood Cancer Journal · doi:10.1038/s41408-024-01180-x · Cited by 8

Recent advances in the development of 17beta-hydroxysteroid dehydrogenase inhibitors

Poirier, D. (2024) · Steroids · doi:10.1016/j.steroids.2024.109529 · Cited by 12

Ferroptosis-related gene signature predicts prognosis in kidney renal papillary cell carcinoma

Yin, H., Mei, L., Liang, S., Wei, M., Huang, C., Qin, F., Nong, J., Zeng, X., Nong, C., & Qin, H. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.988867 · Cited by 8

Dynamics of HSD17B3 expression in human fetal testis: implications for the role of Sertoli cells in fetal testosterone biosynthesis

Planinić, A., Marić, T., Himelreich-Perić, M., Ježek, D., & Bojanac, A. K. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1429292 · Cited by 8

Human AKR1C3 binds agonists of GPR84 and participates in an expanded polyamine pathway

Dudkina, N., Park, H. B., Song, D., Jain, A., Khan, S. A., Flavell, R. A., Johnson, C. H., Palm, N. W., & Crawford, J. M. (2024) · Cell chemical biology · doi:10.1016/j.chembiol.2024.07.011 · Cited by 7

A novel AKR1C3 specific prodrug AST-3424 and its combination therapy in hepatocellular carcinoma

Chen, X., Zhang, Y., Zheng, X., & Qin, S. (2023) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2023.03.004 · Cited by 7

In Silico Analysis to Identify Molecular Targets for Chemicals of Concern: The Case Study of Flocoumafen, an Anticoagulant Pesticide

Coronado‐Posada, N., Mercado‐Camargo, J., & Olivero‐Verbel, J. (2021) · Environmental Toxicology and Chemistry · doi:10.1002/etc.5042 · Cited by 7

Protocadherin 19 Clustering Epilepsy and Neurosteroids: Opportunities for Intervention

de Nys, R., Kumar, R., & Gécz, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22189769 · Cited by 7

AI Based Discovery of a New AKR1C3 Inhibitor for Anticancer Applications.

Pippione, A. C., Vigato, C., Tucciarello, C., Hussain, S., Salladini, E., Truong, H. H., Henriksen, N. M., Vanzetti, G., Giordano, G., Zonari, D., et al. (2024) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.4c00150 · Cited by 7

AKR1C3 mediates gastric cancer cell invasion and metastasis via the AKT and JNK/p-NF-κB signaling pathways

Lin, L., Xiao, X., Guo, X., Zhong, C., Zhuang, M., Xu, J., Wang, Y., & Chen, F. (2024) · Scientific Reports · doi:10.1038/s41598-024-82039-w · Cited by 8

Entinostat overcomes cisplatin resistance in bladder cancer by promoting H3K18la-mediated DHRS2 expression and nuclear translocation to suppress the AKR1C3-androgen axis

Xu, G., Zheng, M., Wu, Z., Xie, T., Li, Y., Hu, G., Fang, S., Zhang, J., Diao, W., Zhao, W., et al. (2025) · Drug Resistance Updates · doi:10.1016/j.drup.2025.101343 · Cited by 6

Emerging small-molecule AKR1C3 inhibitors development for cancer therapy: Progress from 2021 to 2025

Gao, H.-N., Wu, X.-S., Pan, Z.-J., Liu, H.-M., Chen, K.-Q., Teng, M.-X., Zhao, J.-T., Zhou, J., You, Q.-D., & Zhang, C. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.118490 · Cited by 8

Establishment of Ferroptosis-Related Key Gene Signature and Its Validation in Compression-Induced Intervertebral Disc Degeneration Rats

Guo, J., Yang, Y.-L., Niu, J., Luo, Z., Shi, Q., & Yang, H. (2023) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2023/9020236 · Cited by 6

Mechanisms of action of Zishen Yutai pills in treating premature ovarian failure determined by integrating UHPLC-Q-TOF-MS and network pharmacology analysis

Dang, L., Zhang, C., Su, B., Ning, N., Huang, Q., Zhou, S., Wu, M., Ma, W., Wang, M., Cui, P., et al. (2022) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-022-03763-2 · Cited by 6

Proteomic analysis of tear film in canine diabetic patients with and without retinopathy

Winiarczyk, D., Winiarczyk, M., Balicki, I., Szadkowski, M., Michalak, K., Winiarczyk, S., & Adaszek, Ł. (2022) · Journal of Veterinary Research · doi:10.2478/jvetres-2022-0053 · Cited by 6

Deconstructing Intratumoral Heterogeneity through Multiomic and Multiscale Analysis of Serial Sections

Schupp, P. G., Shelton, S. J., Brody, D. J., Eliscu, R., Johnson, B., Mazor, T., Kelley, K. W., Potts, M. B., McDermott, M. W., Huang, E. J., et al. (2024) · Cancers · doi:10.3390/cancers16132429 · Cited by 5

Influence of aldo–keto reductase 1C3 polymorphisms in early-onset female psoriasis patients

Nojiri, Y., Nakamura, M., Magara, T., Yamamoto, A., Ikumi, K., Nakamura, R. M., Nishida, E., Haarmann‐Stemmann, T., & Morita, A. (2023) · Scientific Reports · doi:10.1038/s41598-023-30464-8 · Cited by 5

Transitional cell metaplasia of the uterine cervix: A histopathological and immunohistochemical analysis suggesting a possible role of androgenic conversion during urothelial-like differentiation in peri/postmenopausal women

Yoo, S. H., Kim, K.-R., & Park, J. Y. (2021) · Annals of Diagnostic Pathology · doi:10.1016/j.anndiagpath.2021.151839 · Cited by 5

Prostanoid Signaling in Cancers: Expression and Regulation Patterns of Enzymes and Receptors

Ershov, P. V., Yablokov, E. O., Kaluzhskiy, L. A., Mezentsev, Y. V., & Ivanov, A. S. (2022) · Biology · doi:10.3390/biology11040590 · Cited by 6

Intracrine androgen biosynthesis and drug resistance

Penning, T. M., Asangani, I. A., Sprenger, C. C. T., & Plymate, S. R. (2020) · Cancer Drug Resistance · doi:10.20517/cdr.2020.60 · Cited by 6

Identification of Pyroptosis-Related Molecular Subtypes and Diagnostic Model development in Major Depressive Disorder

Feng, L., Yuan, J., Li, L., & Tang, J. (2024) · Molecular Biotechnology · doi:10.1007/s12033-024-01252-0 · Cited by 4

In silico prediction of deleterious single nucleotide polymorphism in human AKR1C3 gene and identification of potent inhibitors using molecular docking approach

Aloyuni, S. (2021) · Journal of King Saud University - Science · doi:10.1016/j.jksus.2021.101514 · Cited by 4

Computational modeling studies reveal the origin of the binding preference of 3‐(3,4‐di hydroisoquinolin‐2( 1H )‐ylsulfonyl)benzoic acids for AKR1C3 over its isoforms

Kong, X., Xing, E., Wu, S., Zhuang, T., Li, P., Li, C., & Cheng, X. (2022) · Protein Science · doi:10.1002/pro.4499 · Cited by 4

Reversible downregulation of MYC in a spheroid model of metastatic epithelial ovarian cancer

Buensuceso, A. V., Borrelli, M. J., Valdés, Y. R., & Shepherd, T. G. (2024) · Cancer Gene Therapy · doi:10.1038/s41417-024-00850-z · Cited by 5

Downregulation of Dihydrotestosterone and Estradiol Levels by HEXIM1

Mozar, F. S., Sharma, V., Gorityala, S., Albert, J. M., Xu, Y., & Montano, M. M. (2021) · Endocrinology · doi:10.1210/endocr/bqab236 · Cited by 4

Localized high-risk prostate cancer harbors an androgen receptor low subpopulation susceptible to HER2 inhibitionPreprint

Wilkinson, S. C., Ku, A. T., Lis, R. T., King, I. M., Low, D., Trostel, S. Y., Bright, J. R., Terrigino, N. T., Baj, A., Fenimore, J. M., et al. (2024) · medRxiv · doi:10.1101/2024.02.09.24302395 · Cited by 4

Discovery of Highly Selective AKR1C3 Inhibitors to Overcome EGFR C797S-Mediated Osimertinib Resistance in Non-Small Cell Lung Cancer

Guo, C., Wang, X., Guan, Q., Zhong, S., Zhang, L., Liu, Y., Han, B., Shao, J., Liu, Z., Chen, Y., et al. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c03655 · Cited by 4

Androgen metabolism in prostate cancer: recent advances

Sharifi, N. (2026) · Endocrinology · doi:10.1210/endocr/bqag021 · Cited by 3

Visualizable, AKR1C3-Activated Small-Molecule Antitumor Drug Conjugates with Ultra-Low Systemic Toxicity

Kang, N., Liu, S., Li, X. Q., Luo, R., Chen, W.-T., Ran, C., Wang, P., & Yang, J. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c03834 · Cited by 3

Aldo-Keto reductase 1C3 reduces myocardial cell damage after acute myocardial infarction by activating the Kelch-like ECH-associated protein 1-nuclear factor erythroid 2-related factor 2-antioxidant response element pathway to inhibit ferroptosis

Wang, M. I. A. O., & Yun-Zhao, H. U. (2024) · 老年心脏病学杂志：英文版 · doi:10.26599/1671-5411.2024.09.001 · Cited by 3

AKR1C3 protects cardiomyocytes against hypoxia-induced cell apoptosis through the Nrf-2/NF-κB pathway

Zhang, W., Tian, W., Xia, X., Tian, H., & Sun, T. (2024) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2024230 · Cited by 3

Exploring the roles of AKR1C1, AKR1C2, and AKR1C3 in the nervous system: Mechanisms and perspectives

Chen, X., Gan, L., Huang, Y., Wei, S. H., Wang, W., & Huang, Y. (2025) · Experimental Neurology · doi:10.1016/j.expneurol.2025.115580 · Cited by 3

From Gene Function to Precision Intervention: CRISPR/Cas9 and Stem Cell-Based Strategies as Emerging Disease-Modifying Approaches in PMOS

Khatun, M., Lundin, K., Tuuri, T., Piltonen, T., Tapanainen, J. S., & Salumets, A. (2026) · Stem Cell Reviews and Reports · doi:10.1007/s12015-026-11188-4 · Cited by 2

Statins and adrenal androgen levels in prostate cancer: A new twist

Mostaghel, E. A. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103494 · Cited by 2

Characterization of AST‐001 non‐clinical pharmacokinetics: A novel selective AKR1C3‐activated prodrug in mice, rats, and cynomolgus monkeys

Meng, T., Jung, D. T., Cai, X., Lu, Z., Yu, J., Qi, T., Meng, F., Ruan, M., & Duan, J. (2024) · Biopharmaceutics & Drug Disposition · doi:10.1002/bdd.2385 · Cited by 2

Identification and validation of five ferroptosis-related molecular signatures in keloids based on multiple transcriptome data analysis

Sun, Z., Qin, Y., & Zhang, X. (2025) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1490745 · Cited by 3

Ferroptosis induction, androgen biosynthesis disruption and prostate cancer suppression by androgen and vitamin D combination

Park, B., Khadka, S., Ahn, J., Vaquiz, J., Igbekoyi, O., Song, C. S., & Chatterjee, B. (2025) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2025.130828 · Cited by 2

In silico study of novel alpha tocopheroids as effective inhibitors of aldo-keto reductase 1c3 (AKR1C3) enzyme

Basu, T., & Upadhyay, A. K. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2241543 · Cited by 1

Cancer-Associated fibroblasts regulate the development of cholangiocarcinoma through IL-6/STAT3/AKR1C3 signaling axis

Huang, T.-C., Feng, W.-D., Fang, G.-X., Zhang, Q.-H., Wei, G.-Y., Li, C.-Z., Wang, J.-M., & Liu, J.-F. (2026) · Scientific Reports · doi:10.1038/s41598-026-37583-y · Cited by 1

Single-cell and spatial transcriptomics reveal an arachidonic acid–related cellular atlas in lung adenocarcinoma

Sun, C., Zhang, Y., Pan, Y., 夏贵喜, Yang, G., Huang, C., Li, J., & Ma, P. (2026) · Inflammation Research · doi:10.1007/s00011-026-02251-4 · Cited by 1

Characterization of a highly specific monoclonal antibody against human aldo-keto reductase AKR1C3

Liu, J., He, P., Lin, L., Zhao, Y., Deng, W., Ding, H., Li, Q., & Wang, Z. (2019) · Steroids · doi:10.1016/j.steroids.2019.01.001 · Cited by 1

Molecular Docking of Phytomolecules of Grain Amaranth (Amaranthus hypochondriacus) with AKR1C3Protein Involved in Prostate Cancer in Human Beings

Pandey, D. K., Bharti, M., Rana, A., Prabhakaran, S., & Chauhan, R. (2024) · Letters in Organic Chemistry · doi:10.2174/0115701786275607231228094526 · Cited by 1

Steroids Static Postural Balance Changes After Exercise Intervention Correlate with Steroidome in Elderly Female

Kornatovská, Z., Hill, M., Jandová, D., Krejčí, M., & Zwierzchowska, A. (2025) · Metabolites · doi:10.3390/metabo15040239 · Cited by 1

Mechanisms of Action of Zishen Yutai pills in Treating Premature Ovarian Failure Determined by Integrating UHPLC-Q-TOF-MS and Network Pharmacology AnalysisPreprint

Dang, L., Zhang, C., Su, B., Na, N., Huang, Q., Zhou, S., Wu, M., Ma, W., Wang, M., Cui, P., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1176592/v1

Docking is not enough: 17-trifluoromethylphenyl trinor PGF2α is only a very weak ligand of neurokinin-1 receptor

Matalińska, J., & Lipiński, P. F. J. (2022) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2022.104849

Comprehensive clinical analysis of AKR1 expression profiles in the diagnosis of human colorectal cancerPreprint

Li, H., Duan, L., Li, S., He, R., Li, Z., Liao, X., Luo, D., & Zheng, L. (2023) · Research Square · doi:10.21203/rs.3.rs-2526991/v1

Research Progress of AR Gene Family in Prostate Cancer Therapy

Khan, M. (2024) · annals of urologic oncology · doi:10.32948/auo.2024.10.13

A Prognostic Survival Model Based on Endocrine-Related Gene Expression in Acute Myelogenous Leukemia

Lv, W., Wang, Y., Hu, F., Huang, H.-Y., Cui, Y., Song, Y., Chen, L., Wu, B., & Liang, Y. (2025) · Acta Haematologica · doi:10.1159/000543272

The Relationship between AKR1C3 and Diseases

袁, 大. (2025) · Hans Journal of Medicinal Chemistry · doi:10.12677/hjmce.2025.131008

Inhibitors of type 5 17β-hydroxysteroid dehydrogenase (AKR1C3): Overview and structural insights

Byrns, M. C., Jin, Y., & Penning, T. M. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.11.004 · Cited by 145

Aldo-keto reductase (AKR) 1C3 as an androgen receptor coactivator.

Narayanan, R., Yepuru, M., Wu, Z., Barrett, C. M., Kim, J., Penning, T. M., Steiner, M. S., Miller, D. D., & Dalton, J. T. (2013) · Journal of Clinical Oncology · doi:10.1200/jco.2013.31.6_suppl.100 · Cited by 2

Type 5 17β-hydroxysteroid dehydrogenase/prostaglandin F synthase (AKR1C3): Role in breast cancer and inhibition by non-steroidal anti-inflammatory drug analogs

Byrns, M. C., & Penning, T. M. (2008) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2008.10.024 · Cited by 82

Aldo-keto reductase (AKR) 1C3: Role in prostate disease and the development of specific inhibitors

Penning, T. M., Steckelbroeck, S., Bauman, D. R., Miller, M. W., Jin, Y., Peehl, D. M., Fung, K.-M. A., & Lin, H.-K. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2005.12.009 · Cited by 127

11-Oxygenated androgen precursors are the preferred substrates for aldo-keto reductase 1C3 (AKR1C3): implications for castration resistant prostate cancer

Barnard, M., Quanson, J. L., Mostaghel, E., Pretorius, E., Snoep, J. L., & Storbeck, K.-H. (2018) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2018.06.013 · Cited by 72