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Identification of a Principal mRNA Species for Human 3 -Hydroxysteroid Dehydrogenase Isoform (AKR1C3) That Exhibits High Prostaglandin D2 11-Ketoreductase Activity

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Type 5 17β-hydroxysteroid dehydrogenase (AKR1C3) contributes to testosterone production in the adrenal reticularis

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In situ production of sex steroids in human breast carcinoma

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Expression of AKR1B1, AKR1C3 and other genes of prostaglandin F2α biosynthesis and action in ovarian endometriosis tissue and in model cell lines

Sinreih, M., Anko, M., Hevir, N., Kocbek, V., & Rižner, T. L. (2014) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2014.11.009 · Cited by 39

Altered expression of genes involved in progesterone biosynthesis, metabolism and action in endometrial cancer

Sinreih, M., Hevir, N., & Rižner, T. L. (2012) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2012.11.012 · Cited by 38

11β-Prostaglandin F2α, a bioactive metabolite catalyzed by AKR1C3, stimulates prostaglandin F receptor and induces slug expression in breast cancer

Yoda, T., Kikuchi, K., Miki, Y., Onodera, Y., Hata, S., Takagi, K., Nakamura, Y., Hirakawa, H., Ishida, T., Suzuki, T., et al. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.07.008 · Cited by 36

The Steroidogenic Enzyme AKR1C3 Regulates Stability of the Ubiquitin Ligase Siah2 in Prostate Cancer Cells

Fan, L., Peng, G., Hussain, A., Fazli, L., Guns, E. S. T., Gleave, M. E., & Qi, J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.662155 · Cited by 36

Promiscuity and diversity in 3-ketosteroid reductases

Penning, T. M., Chen, M., & Jin, Y. (2014) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2014.12.003 · Cited by 36

Selective AKR1C3 inhibitors do not recapitulate the anti-leukaemic activities of the pan-AKR1C inhibitor medroxyprogesterone acetate

Khanim, F. L., Davies, N., Veliça, P., Hayden, R., Ride, J. P., Pararasa, C., Chong, M., Günther, U. L., Veerapen, N., Winn, P. J., et al. (2014) · British Journal of Cancer · doi:10.1038/bjc.2014.83 · Cited by 35

Prostaglandin 15d-PGJ2 Inhibits Androgen Receptor Signaling in Prostate Cancer Cells

Kaikkonen, S., Paakinaho, V., Sutinen, P., Levonen, A., & Palvimo, J. J. (2012) · Molecular Endocrinology · doi:10.1210/me.2012-1313 · Cited by 34

Expression of the 17β-hydroxysteroid dehydrogenase type 5 mRNA in the human brain

Steckelbroeck, S., Watzka, M., Stoffel‐Wagner, B., Hans, V., Redel, L., Clusmann, H., Elger, C. E., BIDLINGMAIER, F., & Klingmüller, D. (2001) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(00)00432-9 · Cited by 33

Molecular Markers in Sex Hormone Pathway Genes Associated with the Efficacy of Androgen-Deprivation Therapy for Prostate Cancer

Yu, C.-C., Huang, S.-P., Lee, Y.-C., Huang, C., Liu, C.-C., Hour, T., Huang, C.-N., You, B.-J., Chang, T.-Y., Huang, C.-H., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054627 · Cited by 31

Impact of nonsynonymous single nucleotide polymorphisms on in-vitro metabolism of exemestane by hepatic cytosolic reductases

Platt, A., Xia, Z., Liu, Y., Chen, G., & Lazarus, P. J. (2016) · Pharmacogenetics and Genomics · doi:10.1097/fpc.0000000000000226 · Cited by 31

Quality of life effects of androgen deprivation therapy in a prostate cancer cohort in New Zealand: can we minimize effects using a stratification based on the aldo-keto reductase family 1, member C3 rs12529 gene polymorphism?

Karunasinghe, N., Zhu, Y., Han, D. Y., Lange, K., Zhu, S., Wang, A., Ellett, S., Masters, J., Goudie, M., Keogh, J., et al. (2016) · BMC Urology · doi:10.1186/s12894-016-0164-4 · Cited by 30

Substrate Specificity, Inhibitor Selectivity and Structure-Function Relationships of Aldo-Keto Reductase 1B15: A Novel Human Retinaldehyde Reductase

Giménez-Dejoz, J., Kolář, M. H., Ruiz, F. X., Crespo, I., Cousido-Siah, A., PODJARNY, A. D., Barski, O. A., Fanfrlík, J., Parés, X., Farrés, J., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0134506 · Cited by 29

Association analysis between the polymorphisms of HSD17B5 and HSD17B6 and risk of polycystic ovary syndrome in Chinese population

Ju, R., Wu, W., Fei, J., Qin, Y., Tang, Q., Wu, D., Xia, Y., Wu, J., & Wang, X. (2014) · European Journal of Endocrinology · doi:10.1530/eje-14-0615 · Cited by 27

Structure and activity of the murine type 5 17β-hydroxysteroid dehydrogenase gene

Rheault, P., Charbonneau, A., & Luu-The, V. (1999) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(99)00106-2 · Cited by 25

Genome-Wide Analysis of Human Disease Alleles Reveals That Their Locations Are Correlated in Paralogous Proteins

Yandell, M. D., Moore, B., Salas, F., Mungall, C., MacBride, A. R., White, C., & Reese, M. G. (2008) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000218 · Cited by 25

Fine mapping analysis confirms and strengthens linkage of four chromosomal regions in familial hypospadias

Söderhäll, C., Körberg, I. B., Thai, H. T. T., Cao, J., Chen, Y., Zhang, X., Zu, S., van der Zanden, L. F. M., van Rooij, I. A. L. M., Frisén, L., et al. (2014) · European Journal of Human Genetics · doi:10.1038/ejhg.2014.129 · Cited by 22

Knockdown of AKR1C3 exposes a potential epigenetic susceptibility in prostate cancer cells

Doig, C. L., Battaglia, S., Khanim, F. L., Bunce, C. M., & Campbell, M. J. (2015) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2015.09.037 · Cited by 21

15-Deoxy-Δ12,14-prostaglandin J2 induces growth inhibition, cell cycle arrest and apoptosis in human endometrial cancer cell lines

Li, H., & Narahara, H. (2013) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2013.1268 · Cited by 13

Progestin effects on expression of AKR1C1–AKR1C3, SRD5A1 and PGR in the Z-12 endometriotic epithelial cell line

Beranič, N., & Rižner, T. L. (2012) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2012.10.028 · Cited by 12

Positive biopsy (bx) rates for prostate cancer (PCA) based on prostate specific antigen (PSA) grouping in a large cancer screening trial: Prostate, Lung, Colorectal, and Ovarian Cancer Screening Trial (PLCO).

Reding, D. J., McCarty, C. A., Riley, T. L., Hickey, T., & Hocking, W. G. (2010) · Journal of Clinical Oncology · doi:10.1200/jco.2010.28.15_suppl.4563 · Cited by 9

Generation of human endometrial knockout cell lines with the CRISPR/Cas9 system confirms the prostaglandin F2 synthase activity of aldo-ketoreductase 1B1

Lacroix‐Pepin, N., Chapdelaine, P., Rodriguez, Y., Tremblay, J. P., & Fortier, M. A. (2014) · Molecular Human Reproduction · doi:10.1093/molehr/gau023 · Cited by 9

Functional Significance May Underlie the Taxonomic Utility of Single Amino Acid Substitutions in Conserved Proteins

Tyler, K. M., Wagner, G. K., Wu, Q., & Huber, K. T. (2010) · Journal of Molecular Evolution · doi:10.1007/s00239-010-9338-y · Cited by 8

A Single Nucleotide Variant in the Promoter Region of 17β-HSD Type 5 Gene Influences External Genitalia Virilization in Females with 21-Hydroxylase Deficiency

Kaupert, L. C., Gomes, L. G., Brito, V. N., de Lemos‐Marini, S. H. V., de Mello, M. P., Longui, C. A., Kochi, C., de Castro, M., Guerra‐Júnior, G., Mendonca, B. B., et al. (2016) · Hormone Research in Paediatrics · doi:10.1159/000445684 · Cited by 7

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

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