Structural and functional biology of aldo-keto reductase steroid transforming enzymes
Open accessAbstract
Aldo-keto reductases (AKRs) are monomeric NAD(P)(H)-dependent oxidoreductases that play pivotal roles in the biosynthesis and metabolism of steroids in humans. AKR1C enzymes acting as 3-ketosteroid, 17-ketosteroid, and 20-ketosteroid reductases are involved in the prereceptor regulation of ligands for the androgen, estrogen, and progesterone receptors and are considered drug targets to treat steroid hormone-dependent malignancies and endocrine disorders. In contrast, AKR1D1 is the only known steroid 5β-reductase and is essential for bile-acid biosynthesis, the generation of ligands for the farnesoid X receptor, and the 5β-dihydrosteroids that have their own biological activity. In this review we discuss the crystal structures of these AKRs, their kinetic and catalytic mechanisms, AKR genomics (gene expression, splice variants, polymorphic variants, and inherited genetic deficiencies), distribution in steroid target tissues, roles in steroid hormone action and disease, and inhibitor design.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
DHEA can be converted to A4 by peripheral HSD3B1, with A4 serving as substrate for production of testosterone by AKR1C3.
“More specifically, DHEA can be converted to A4 by peripheral HSD3B1, with A4 serving as the substrate for the production of testosterone by AKR1C3 [54].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [54]
Androgens and precursors that escape tissue-specific activation via 5α-reduction are metabolized within the liver, which expresses both 5α- and 5β-reductases.
“Those androgens and precursors that escape the tissue specific activation via 5α-reduction are metabolized within the liver, which expresses both 5α- and 5β-reductases [54,94,100].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [54]
Following 5α/5β-reduction, androgen metabolites are subject to reduction of the 3-keto group with predominant 3α-stereoselectivity.
“Following 5α/5β-reduction, androgen metabolites are subject to reduction of the 3-keto group with predominant 3α-stereoselectivity [54].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [54]
Even 5β-DHT, the product of the 5β-reduction of testosterone, is an inactive androgen metabolite.
“Even 5β-DHT, the product of the 5β-reduction of testosterone, is an inactive androgen metabolite [54].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [54]
Cites
Kumar, P., Henikoff, S., & Ng, P. C. (2009) · Nature Protocols · doi:10.1038/nprot.2009.86 · Cited by 6,521 · see citing works
Increased Survival with Enzalutamide in Prostate Cancer after Chemotherapy
Scher, H. I., Fizazi, K., Saad, F., Taplin, M.-E., Sternberg, C. N., Miller, K., de Wit, R., Mulders, P., Chi, K. N., Shore, N. D., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1207506 · Cited by 4,586 · see citing works
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 · see citing works
Advanced Organic Chemistry: Reactions, Mechanisms, and Structure
March, J. (1977) · Andalas University Repository (Andalas University) · Cited by 4,029 · see citing works
Development of a second-generation antiandrogen for treatment of advanced prostate cancer.
Tran, C., Ouk, S., Clegg, N. J., Chen, Y., Watson, P. A., Arora, V., Wongvipat, J., Smith-Jones, P. M., Yoo, D., Kwon, A., et al. (2009) · Science · doi:10.1126/science.1168175 · Cited by 2,292 · see citing works
The Enzymes, Regulation, and Genetics of Bile Acid Synthesis
Russell, D. W. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161712 · Cited by 2,069 · see citing works
Mineralocorticoid action: target tissue specificity is enzyme, not receptor, mediated
Funder, J. W., Pearce, P. T., Smith, R., & Smith, A. I. (1988) · Science · doi:10.1126/science.2845584 · Cited by 1,628 · see citing works
Short-chain dehydrogenases/reductases (SDR)
Jörnvall, H., Persson, B., Krook, M., Atrian, S., Gonzàlez‐Duarte, R., Jeffery, J., & Ghosh, D. (1995) · Biochemistry · doi:10.1021/bi00018a001 · Cited by 1,241 · see citing works
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 · see citing works
Self-citationKavanagh, K. L., Jörnvall, H., Persson, B., & Oppermann, U. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8588-y · Cited by 908 · see citing works
Attard, G., Reid, A. H. M., Yap, T. A., Raynaud, F., Dowsett, M., Settatree, S., Barrett, M., Parker, C., Martins, V., Folkerd, E., et al. (2008) · Journal of Clinical Oncology · doi:10.1200/jco.2007.15.9749 · Cited by 903 · see citing works
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 · see citing works
Self-citationLabrie, F. (1991) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(91)90116-a · Cited by 685 · see citing works
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:10.1042/0264-6021:3510067 · Cited by 649 · see citing works
Self-citationPENNING, 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 · see citing works
Self-citationComparative 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 · see citing works
Self-citationThe Aldo-Keto Reductase Superfamily and its Role in Drug Metabolism and Detoxification
Barski, O. A., Tipparaju, S. M., & Bhatnagar, A. (2008) · Drug Metabolism Reviews · doi:10.1080/03602530802431439 · Cited by 543 · see citing works
Wilson, D. K., Bohren, K. M., Gabbay, K. H., & Quiocho, F. A. (1992) · Science · doi:10.1126/science.1621098 · Cited by 434 · see citing works
Short‐chain dehydrogenases/reductases (SDRs)
Kallberg, Y., Oppermann, U. C. T., Jörnvall, H., & Persson, B. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03130.x · Cited by 432 · see citing works
Danila, D. C., Morris, M. J., de Bono, J. S., Ryan, C. J., Denmeade, S. R., Smith, M. R., Taplin, M.-E., Bubley, G. J., Kheoh, T., Haqq, C., et al. (2010) · Journal of Clinical Oncology · doi:10.1200/jco.2009.25.9259 · Cited by 410 · see citing works
Nelson, V. L., Qin, K.-N., Rosenfield, R. L., Wood, J. R., Penning, T. M., Legro, R. S., Strauss, J. F., & McAllister, J. M. (2001) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.86.12.8088 · Cited by 405 · see citing works
Self-citationThe SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative
Persson, B., Kallberg, Y., Bray, J. E., Bruford, E. A., Dellaporta, S. L., Favia, A. D., Duarte, R. G., Jörnvall, H., Kavanagh, K. L., Kedishvili, N. Y., et al. (2008) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2008.10.040 · Cited by 397 · see citing works
Self-citationSelective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes
Griffin, L. D., & Mellon, S. H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.23.13512 · Cited by 387 · see citing works
Aldo-Keto Reductases and Bioactivation/Detoxication
Jin, Y., & Penning, T. M. (2006) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105337 · Cited by 386 · see citing works
Self-citation11β-Hydroxysteroid dehydrogenase and the pre-receptor regulation of corticosteroid hormone action
Draper, N., & Stewart, P. M. (2005) · Journal of Endocrinology · doi:10.1677/joe.1.06019 · Cited by 375 · see citing works
Wang, M., Seippel, L., Purdy, R. H., & Bäckström, T. C. (1996) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.81.3.8772579 · Cited by 353 · see citing works
A new nomenclature for the aldo-keto reductase superfamily
Jez, J. M., Flynn, T. G., & Penning, T. M. (1997) · Biochemical Pharmacology · doi:10.1016/s0006-2952(97)84253-0 · Cited by 350 · see citing works
Self-citationThe backdoor pathway to dihydrotestosterone
Auchus, R. J. (2004) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2004.09.004 · Cited by 347 · see citing works
Self-citationDihydrotestosterone synthesis bypasses testosterone to drive castration-resistant prostate cancer
Chang, K.-H., Li, R., Papari-Zareei, M., Watumull, L., Zhao, Y. D., Auchus, R. J., & Sharifi, N. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107898108 · Cited by 346 · see citing works
Self-citationAnticonvulsant profile of the progesterone metabolite 5α-pregnan-3α-ol-20-one
Belelli, D., Bolger, M. B., & Gee, K. W. (1989) · European Journal of Pharmacology · doi:10.1016/0014-2999(89)90077-0 · Cited by 323 · see citing works
The aldo-keto reductase superfamily homepage
Hyndman, D., Bauman, D. R., Heredia, V. V., & Penning, T. M. (2003) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00193-x · Cited by 317 · see citing works
Self-citationLabrie, F., Luu-The, V, Lin, S., Simard, J., Labrie, C., El-Alfy, M., Pelletier, G., & Belanger, A. (2000) · Journal of Molecular Endocrinology · doi:10.1677/jme.0.0250001 · Cited by 278 · see citing works
Steckelbroeck, S., Jin, Y., Gopishetty, S., Oyesanmi, B., & Penning, T. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313308200 · Cited by 270 · see citing works
Self-citation11-Oxygenated C19 steroids are the predominant androgens in polycystic ovary syndrome
O’Reilly, M. W., Kempegowda, P., Jenkinson, C., Taylor, A. E., Quanson, J. L., Storbeck, K.-H., & Arlt, W. (2017) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2016-3285 · Cited by 267 · see citing works
Human aldo–keto reductases: Function, gene regulation, and single nucleotide polymorphisms
Penning, T. M., & Drury, J. E. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.04.024 · Cited by 266 · see citing works
Self-citationCharacteristics of a Highly Labile Human Type 5 17β-Hydroxysteroid Dehydrogenase1
Dufort, I., Rheault, P., Huang, X.-F., Soucy, P., & Luu-The, V. (1999) · Endocrinology · doi:10.1210/endo.140.2.6531 · Cited by 255 · see citing works
Setchell, K. D. R., Suchy, F. J., Welsh, M. B., Zimmer-Nechemias, L., Heubi, J. E., & Balistreri, W. F. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113837 · Cited by 254 · see citing works
Agyeman, A. S., Chaerkady, R., Shaw, P. G., Davidson, N. E., Visvanathan, K., Pandey, A., & Kensler, T. W. (2011) · Breast Cancer Research and Treatment · doi:10.1007/s10549-011-1536-9 · Cited by 252 · see citing works
Flück, C. E., Meyer-Böni, M., Pandey, A. V., Kempná, P., Miller, W. L., Schoenle, E. J., & Biason-Lauber, A. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.06.009 · Cited by 248 · see citing works
Intracrine Androgens and AKR1C3 Activation Confer Resistance to Enzalutamide in Prostate Cancer
Liu, C., Lou, W., Zhu, Y., Yang, J. C., Nadiminty, N., Gaikwad, N. W., Evans, C. P., & Gao, A. C. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-3080 · Cited by 245 · see citing works
Turcu, A. F., Nanba, A. T., Chomic, R., Upadhyay, S. K., Giordano, T. J., Shields, J. J., Merke, D. P., Rainey, W. E., & Auchus, R. J. (2016) · European Journal of Endocrinology · doi:10.1530/eje-15-1181 · Cited by 231 · see citing works
Self-citationRege, J., Nakamura, Y., Satoh, F., Morimoto, R., Kennedy, M. R., Layman, L. C., Honma, S., Sasano, H., & Rainey, W. E. (2013) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2012-2912 · Cited by 227 · see citing works
Biswas, M. G., & Russell, D. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.25.15959 · Cited by 224 · see citing works
Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism
Rižner, T. L., & Penning, T. M. (2014) · Steroids · doi:10.1016/j.steroids.2013.10.012 · Cited by 217 · see citing works
Self-citationO’Reilly, M. W., Kempegowda, P., Walsh, M., Taylor, A. E., Manolopoulos, K. N., Allwood, J. W., Semple, R. K., Hebenstreit, D., Dunn, W. B., Tomlinson, J. W., et al. (2017) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2017-00947 · Cited by 215 · see citing works
Integrated view on 17beta-hydroxysteroid dehydrogenases
Moeller, G., & Adamski, J. (2009) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2008.10.040 · Cited by 214 · see citing works
Mitsiades, N., Sung, C. C., Schultz, N. D., Danila, D. C., He, B., Eedunuri, V. K., Fleisher, M., Sander, C., Sawyers, C. L., & Scher, H. I. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-1335 · Cited by 196 · see citing works
Lin, H.-K., Jez, J. M., Schlegel, B. P., Peehl, D. M., Pachter, J. A., & Penning, T. M. (1997) · Molecular Endocrinology · doi:10.1210/mend.11.13.0026 · Cited by 194 · see citing works
Self-citationStructure and function of human 17β-hydroxysteroid dehydrogenases
Lukacik, P., Kavanagh, K. L., & Oppermann, U. C. T. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2005.12.007 · Cited by 192 · see citing works
Burczynski, M. E., Gopishetty, S. R., Palackal, N. T., & Penning, T. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006655200 · Cited by 191 · see citing works
Self-citationBurczynski, M. E., Hseuh-Kung, L. I. N., & Penning, T. M. (1999) · PubMed · Cited by 189 · see citing works
Self-citationEvidence of limited contributions for intratumoral steroidogenesis in prostate cancer
Hofland, J., van Weerden, W. M., Dits, N. F. J., Steenbergen, J., van Leenders, G. J. L. H., Jenster, G., Schröder, F. H., & de Jong, F. H. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-2092 · Cited by 176 · see citing works
Khanna, M., Qin, K.-N., Wang, R. W., & Cheng, K.-C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.34.20162 · Cited by 174 · see citing works
Wilson, J. D., Auchus, R. J., Leihy, M. W., Guryev, O. L., Estabrook, R. W., Osborn, S. M., Shaw, G., & Renfree, M. B. (2003) · Endocrinology · doi:10.1210/en.2002-220721 · Cited by 172 · see citing works
Self-citationAllegra, J. C., Lippman, M. E., Thompson, E. B., Simon, R., Barlock, A., Green, L., Kk, H., Do, H. M., & Aitken, S. C. (1979) · PubMed · Cited by 162 · see citing works
AKR1C1 and AKR1C3 may determine progesterone and estrogen ratios in endometrial cancer
Rižner, T. L., Šmuc, T., Rupreht, R., Šinkovec, J., & Penning, T. M. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2005.10.009 · Cited by 159 · see citing works
Self-citationWood, S. H., Mortola, J. F., Chan, Y., Moossazadeh, F., & Yen, S. S. C. (1992) · PubMed · Cited by 155 · see citing works
A MAMMALIAN 3α-HYDROXYSTEROID DEHYDROGENASE
Tomkins, G. M. (1956) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65907-1 · Cited by 151 · see citing works
Byrns, M. C., Steckelbroeck, S., & Penning, T. M. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.09.008 · Cited by 145 · see citing works
Self-citationInhibitors 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 144 · see citing works
Self-citationA new dawn for androgens: novel lessons from 11-oxygenated C19 steroids
Pretorius, E., Arlt, W., & Storbeck, K.-H. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.08.014 · Cited by 142 · see citing works
KONDO, K., KAI, M., SETOGUCHI, Y., EGGERTSEN, G., SJÖBLOM, P., SETOGUCHI, T., OKUDA, K., & BJÖRKHEM, I. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb19947.x · Cited by 139 · see citing works
Schlegel, B. P., Jez, J. M., & Penning, T. M. (1998) · Biochemistry · doi:10.1021/bi9723055 · Cited by 139 · see citing works
Self-citationGuerini, V., Sau, D., Scaccianoce, E., Rusmini, P., Ciana, P., Maggi, A. C., Martini, P. G. V., Katzenellenbogen, B. S., Martini, L., Motta, M., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-1941 · Cited by 139 · see citing works
Hydroxysteroid dehydrogenases and pre-receptor regulation of steroid hormone action
Penning, T. M. (2003) · Human Reproduction Update · doi:10.1093/humupd/dmg022 · Cited by 137 · see citing works
Self-citationRižner, T. L., Lin, H. K., Peehl, D. M., Steckelbroeck, S., Bauman, D. R., & Penning, T. M. (2003) · Endocrinology · doi:10.1210/en.2002-0032 · Cited by 132 · see citing works
Self-citationcDNA cloning, expression and characterization of human prostaglandin F synthase1
Suzuki-Yamamoto, T., Nishizawa, M., Fukui, M., Okuda‐Ashitaka, E., Nakajima, T., Ito, S., & Watanabe, K. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01551-3 · Cited by 131 · see citing works
Nakamura, Y., Hornsby, P. J., Casson, P., Morimoto, R., Satoh, F., Xing, Y., Kennedy, M. R., Sasano, H., & Rainey, W. E. (2009) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2008-2374 · Cited by 129 · see citing works
Fung, K.-M., Samara, E. N. S., Wong, C., Metwalli, A., Krlin, R., Bane, B., Liu, C. Z., Yang, J. T., Pitha, J. V., Culkin, D. J., et al. (2006) · Endocrine Related Cancer · doi:10.1677/erc.1.01048 · Cited by 129 · see citing works
Self-citationMartinez Botella, G., Salituro, F. G., Harrison, B. L., Beresis, R. T., Bai, Z., Blanco, M.-J., Belfort, G. M., Dai, J., Loya, C. M., Ackley, M. A., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00846 · Cited by 129 · see citing works
Lewis, M. J., Wiebe, J. P., & Heathcote, J. G. (2004) · BMC Cancer · doi:10.1186/1471-2407-4-27 · Cited by 127 · see citing works
Lemonde, H. A., Custard, E. J., Bouquet, J., Duran, M., Overmars, H., Scambler, P. J., & Clayton, P. T. (2003) · Gut · doi:10.1136/gut.52.10.1494 · Cited by 125 · see citing works
Inhibition of AKR1C3 Activation Overcomes Resistance to Abiraterone in Advanced Prostate Cancer
Liu, C., Armstrong, C. M., Lou, W., Lombard, A. P., Evans, C. P., & Gao, A. C. (2016) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-16-0186 · Cited by 124 · see citing works
Yepuru, M., Wu, Z., Kulkarni, A. L., Yin, F., Barrett, C. M., Kim, J.-H., Steiner, M. S., Miller, D. D., Dalton, J. T., & Narayanan, R. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-1151 · Cited by 122 · see citing works
Bauman, D. R., Steckelbroeck, S., Williams, M. V., Peehl, D. M., & Penning, T. M. (2006) · Molecular Endocrinology · doi:10.1210/me.2005-0287 · Cited by 120 · see citing works
Self-citationJi, Q., Aoyama, C., Nien, Y.-D., Liu, P. I., Chen, P. K., Chang, L., Stanczyk, F. Z., & Stolz, A. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1608 · Cited by 119 · see citing works
Bennett, M. J., Albert, R. H., Jez, J. M., Ma, H., Penning, T. M., & Lewis, M. (1997) · Structure · doi:10.1016/s0969-2126(97)00234-7 · Cited by 117 · see citing works
Self-citationByrns, M. C., Duan, L., Lee, S. H., Blair, I. A., & Penning, T. M. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2009.12.009 · Cited by 116 · see citing works
Self-citationLong-term adjuvant tamoxifen therapy for breast cancer
Jordan, V. C. (1990) · Breast Cancer Research and Treatment · doi:10.1007/bf01806350 · Cited by 116 · see citing works
3α-reduced neuroactive steroids and their precursors during pregnancy and the postpartum period
Evans, S. E. G., Ross, L. E., Sellers, E. M., Purdy, R. H., & Romach, M. K. (2005) · Gynecological Endocrinology · doi:10.1080/09513590500361747 · Cited by 114 · see citing works
Adeniji, A. O., Twenter, B. M., Byrns, M. C., Jin, Y., Chen, M., Winkler, J. D., & Penning, T. M. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm201547v · Cited by 113 · see citing works
Self-citationHara, A., Matsuura, K., Tamada, Y., Sato, K., Miyabe, Y., Deyashiki, Y., & ISHIDA, N. (1996) · Biochemical Journal · doi:10.1042/bj3130373 · Cited by 109 · see citing works
Characterization of a human 20alpha-hydroxysteroid dehydrogenase
Zhang, Y., Dufort, I., Rheault, P., & Luu-The, V. (2000) · Journal of Molecular Endocrinology · doi:10.1677/jme.0.0250221 · Cited by 109 · see citing works
Stolz, A., Hammond, L. E., Lou, H., Takikawa, H., Ronk, M., & Shively, J. E. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82220-7 · Cited by 108 · see citing works
Levere, R. D., Kappas, A., & Granick, S. (1967) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.58.3.985 · Cited by 108 · see citing works
Turcu, A. F., Mallappa, A., Elman, M. S., Avila, N. A., Marko, J., Rao, H., Tsodikov, A., Auchus, R. J., & Merke, D. P. (2017) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2016-3989 · Cited by 107 · see citing works
Self-citationLiedtke, A. J., Adeniji, A. O., Chen, M., Byrns, M. C., Jin, Y., Christianson, D. W., Marnett, L. J., & Penning, T. M. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm3017656 · Cited by 106 · see citing works
Self-citationKubiseski, T. J., Hyndman, D., Morjana, N. A., & Flynn, T. G. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50457-4 · Cited by 105 · see citing works
Whorwood, C. B., Franklyn, J. A., Sheppard, M. C., & Stewart, P. M. (1992) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/0960-0760(92)90220-d · Cited by 103 · see citing works
Prostate formation in a marsupial is mediated by the testicular androgen 5α-androstane-3α,17β-diol
Shaw, G., Renfree, M. B., Leihy, M. W., Shackleton, C. H. L., Roitman, E., & Wilson, J. D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.220412297 · Cited by 101 · see citing works
THE CRYSTAL STRUCTURE OF THE ALDOSE REDUCTASE NADPH BINARY COMPLEX
Borhani, D. W., Harter, T. M., & Petrash, J. M. (1992) · Worldwide Protein Data Bank · doi:10.2210/pdb1abn/pdb · Cited by 99 · see citing works
Jin, Y., Stayrook, S. E., Albert, R. H., Palackal, N. T., Penning, T. M., & Lewis, M. (2001) · Biochemistry · doi:10.1021/bi010919a · Cited by 99 · see citing works
Self-citationPartial reduction of steroid hormones and related substances
Norymberski, J. K., & Woods, G. F. (1955) · Journal of the Chemical Society (Resumed) · doi:10.1039/jr9550003426 · Cited by 96 · see citing works
Aldo-Keto Reductase (AKR) 1C3 inhibitors: a patent review
Penning, T. M. (2017) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2017.1379503 · Cited by 96 · see citing works
Self-citationStructure-function aspects and inhibitor design of type 5 17β-hydroxysteroid dehydrogenase (AKR1C3)
Penning, T. M., Burczynski, M. E., Jez, J. M., Lin, H.-K., Ma, H., Moore, M., Ratnam, K., & Palackal, N. T. (2001) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(00)00426-3 · Cited by 95 · see citing works
Self-citationGrimshaw, C. E., Bohren, K. M., Lai, C.-J., & Gabbay, K. H. (1995) · Biochemistry · doi:10.1021/bi00044a012 · Cited by 95 · see citing works
Structure of 3α-Hydroxysteroid/Dihydrodiol Dehydrogenase Complexed with NADP<sup>+</sup>
Bennett, M. J., Schlegel, B. P., Jez, J. M., Penning, T. M., & Lewis, M. (1996) · Biochemistry · doi:10.1021/bi9604688 · Cited by 92 · see citing works
Self-citationThe crystal structure of the aldose reductase.NADPH binary complex.
Borhani, D. W., Harter, T. M., & Petrash, J. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35840-x · Cited by 92 · see citing works
Hamid, A. R. A. H., Pfeiffer, M. J., Verhaegh, G. W. C. T., Schaafsma, E., Brandt, A. M., Sweep, F. C. G. J., Sedelaar, J. P. M., & Schalken, J. A. (2012) · Molecular Medicine · doi:10.2119/molmed.2012.00296 · Cited by 87 · see citing works
Selective reduction of AKR1C2 in prostate cancer and its role in DHT metabolism
Ji, Q., Chang, L., Vandenberg, D. J., Stanczyk, F. Z., & Stolz, A. (2003) · The Prostate · doi:10.1002/pros.10192 · Cited by 85 · see citing works
Steroid Modulation of the GABA A Receptor Complex: Electrophysiological Studies
Lambert, J. J., Peters, J. A., Sturgess, N. C., & Hales, T. G. (2007) · Novartis Foundation symposium · doi:10.1002/9780470513989.ch4 · Cited by 82 · see citing works
Trauger, J. W., Jiang, A., Stearns, B. A., & LoGrasso, P. V. (2002) · Biochemistry · doi:10.1021/bi026109w · Cited by 81 · see citing works
Veliça, P., Davies, N., Rocha, P. P., Schrewe, H., Ride, J. P., & Bunce, C. M. (2009) · Molecular Cancer · doi:10.1186/1476-4598-8-121 · Cited by 80 · see citing works
Di Costanzo, L., Drury, J. E., Penning, T. M., & Christianson, D. W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801778200 · Cited by 79 · see citing works
Self-citationCouture, J., Legrand, P., Cantin, L., Luu-The, V., Labrie, F., & Breton, R. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00762-9 · Cited by 76 · see citing works
Qiu, W., Zhou, M., Labrie, F., & Lin, S. (2004) · Molecular Endocrinology · doi:10.1210/me.2004-0032 · Cited by 76 · see citing works
Clayton, P. T., Mills, K. A., Johnson, A. W., Barabino, A. V., & Marazzi, M. G. (1996) · Gut · doi:10.1136/gut.38.4.623 · Cited by 75 · see citing works
Berséus, O. (1967) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1967.tb00163.x · Cited by 74 · see citing works
Human Types 1 and 3 3α-Hydroxysteroid Dehydrogenases: Differential Lability and Tissue Distribution1
Dufort, I., Labrie, F., & Luu-The, V. (2001) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.86.2.7216 · Cited by 73 · see citing works
Jansson, A., Gunnarsson, C., Cohen, M., Sivik, T., & Stål, O. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-1448 · Cited by 73 · see citing works
Bauman, D. R., Steckelbroeck, S., Peehl, D. M., & Penning, T. M. (2006) · Endocrinology · doi:10.1210/en.2006-0627 · Cited by 71 · see citing works
Self-citationERG/AKR1C3/AR Constitutes a Feed-Forward Loop for AR Signaling in Prostate Cancer Cells
Powell, K., Semaan, L., Conley‐LaComb, M. K., Asangani, I. A., Wu, Y.-M., Ginsburg, K., Williams, J. L., Squire, J. A., Maddipati, K. R., Cher, M. L., et al. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-2352 · Cited by 70 · see citing works
Ji, Q., Chang, L., Stanczyk, F. Z., Ookhtens, M., Sherrod, A. E., & Stolz, A. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-1593 · Cited by 69 · see citing works
Gonzales, E., Cresteil, D., Baussan, C., Dabadie, A., Gerhardt, M.-F., & Jacquemin, E. (2004) · Journal of Hepatology · doi:10.1016/j.jhep.2003.12.024 · Cited by 68 · see citing works
Ratnam, K., Ma, H., & Penning, T. M. (1999) · Biochemistry · doi:10.1021/bi982838t · Cited by 68 · see citing works
Self-citationPurification and characterization of delta 4-3-ketosteroid 5 beta-reductase.
Okuda, A., & Okuda, K. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42821-3 · Cited by 67 · see citing works
Loriot, Y., Fizazi, K. S., Jones, R. J., den Brande, J. V., Molife, R., Omlin, A. G., James, N. D., Baskin-Bey, E. S., Heeringa, M. J., Baron, B., et al. (2014) · Investigational New Drugs · doi:10.1007/s10637-014-0101-x · Cited by 65 · see citing works
Chen, M., Adeniji, A. O., Twenter, B. M., Winkler, J. D., Christianson, D. W., & Penning, T. M. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.03.085 · Cited by 65 · see citing works
Self-citationEngineering Steroid 5β-Reductase Activity into Rat Liver 3α-Hydroxysteroid Dehydrogenase
Jez, J. M., & Penning, T. M. (1998) · Biochemistry · doi:10.1021/bi980294p · Cited by 63 · see citing works
Self-citationKikuchi, A., Furutani, T., Azami, H., Watanabe, K., Niimi, T., Kamiyama, Y., Kuromitsu, S., Baskin-Bey, E. S., Heeringa, M. J., Ouatas, T., et al. (2014) · Investigational New Drugs · doi:10.1007/s10637-014-0130-5 · Cited by 63 · see citing works
O’Reilly, M., Gathercole, L., Capper, F., Arlt, W., & Tomlinson, J. (2015) · The Lancet · doi:10.1016/s0140-6736(15)60331-2 · Cited by 62 · see citing works
Jin, Y., & Penning, T. M. (2006) · Biochemistry · doi:10.1021/bi060591r · Cited by 60 · see citing works
Self-citationByrns, M. C., Mindnich, R., Duan, L., & Penning, T. M. (2012) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2011.12.012 · Cited by 60 · see citing works
Self-citationCooper, W. C., Jin, Y., & Penning, T. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703414200 · Cited by 58 · see citing works
Self-citationPre-receptor regulation of the androgen receptor
Penning, T. M., Jin, Y., Rižner, T. L., & Bauman, D. R. (2007) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2007.10.008 · Cited by 58 · see citing works
Self-citationDeoxycorticosterone inactivation by AKR1C3 in human mineralocorticoid target tissues
Sharma, K. K., Lindqvist, A., Zhou, X. J., Auchus, R. J., Penning, T. M., & Andersson, S. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2005.10.024 · Cited by 57 · see citing works
Self-citationAromatase inhibitors in breast cancer
Brodie, A. M. H. (2002) · Trends in Endocrinology and Metabolism · doi:10.1016/s1043-2760(01)00529-x · Cited by 57 · see citing works
Kumar, S., Suleski, M., Markov, G. J., Lawrence, S., Marco, A. D., & Filipski, A. J. (2009) · Genome Research · doi:10.1101/gr.091991.109 · Cited by 56 · see citing works
AKR1C3 overexpression may serve as a promising biomarker for prostate cancer progression
Tian, Y., Zhao, L., Zhang, H., Liu, X., Zhao, L., Zhao, X., Li, Y., & Li, J. (2014) · Diagnostic Pathology · doi:10.1186/1746-1596-9-42 · Cited by 54 · see citing works
Substrate specificity and inhibitor analyses of human steroid 5β-reductase (AKR1D1)
Chen, M., Drury, J. E., & Penning, T. M. (2011) · Steroids · doi:10.1016/j.steroids.2011.01.003 · Cited by 53 · see citing works
Self-citationBelelli, D., & Gee, K. W. (1989) · European Journal of Pharmacology · doi:10.1016/0014-2999(89)90760-7 · Cited by 52 · see citing works
Grimshaw, C. E., Bohren, K. M., Lai, C.-J., & Gabbay, K. H. (1995) · Biochemistry · doi:10.1021/bi00044a014 · Cited by 52 · see citing works
Sheehan, P. M., Rice, G. E., Moses, E. K., & Brennecke, S. P. (2005) · MHR: Basic science of reproductive medicine · doi:10.1093/molehr/gah201 · Cited by 52 · see citing works
Ma, H., & Penning, T. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11161 · Cited by 52 · see citing works
Self-citationDrury, J. E., Mindnich, R., & Penning, T. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.127779 · Cited by 51 · see citing works
Self-citationIdentification of the molecular switch that regulates access of 5α-DHT to the androgen receptor
Penning, T. M., Bauman, D. R., Jin, Y., & Rižner, T. L. (2007) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2006.12.007 · Cited by 50 · see citing works
Self-citationJin, Y., Mesaros, A. C., Blair, I. A., & Penning, T. M. (2011) · Biochemical Journal · doi:10.1042/bj20101804 · Cited by 49 · see citing works
Self-citationHevir, N., Vouk, K., Šinkovec, J., Ribič-Pucelj, M., & Lanišnik Rižner, T. (2011) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2011.01.003 · Cited by 48 · see citing works
Fankhauser, M., Tan, Y., Macintyre, G., Haviv, I., Hong, M. K. H., Nguyen, A., Pedersen, J. S., Costello, A. J., Hovens, C. M., & Corcoran, N. M. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-3483 · Cited by 48 · see citing works
Molecular cloning and sequence analysis of cDNA encoding δ4‐3‐ketosteroid 5β‐reductase of rat liver
Onishi, Y., Noshiro, M., SHIMOSATO, T., & Okuda, K. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80591-p · Cited by 45 · see citing works
Adeniji, A. O., Uddin, M. J., Zang, T., Tamae, D., Wangtrakuldee, P., Marnett, L. J., & Penning, T. M. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00160 · Cited by 45 · see citing works
Self-citationIn situ production of sex steroids in human breast carcinoma
Suzuki, T., Miki, Y., Moriya, T., Akahira, J., Hirakawa, H., Ohuchi, N., & Sasano, H. (2007) · Medical Molecular Morphology · doi:10.1007/s00795-007-0365-8 · Cited by 43 · see citing works
Progesterone metabolite and spontaneous myometrial contractions in vitro
Thornton, S., Terzidou, V., Clark, A., & Blanks, A. M. (1999) · The Lancet · doi:10.1016/s0140-6736(98)05247-7 · Cited by 42 · see citing works
Matsuura, K., Deyashiki, Y., Sato, K., ISHIDA, N., Miwa, G., & Hara, A. (1997) · Biochemical Journal · doi:10.1042/bj3230061 · Cited by 42 · see citing works
Ueki, I., Kimura, A., Chen, H., Yorifuji, T., Mori, J., Itoh, S., Maruyama, K., Ishige, T., Takei, H., Nittono, H., et al. (2009) · Journal of Gastroenterology and Hepatology · doi:10.1111/j.1440-1746.2008.05669.x · Cited by 41 · see citing works
Sinreih, M., Anko, M., Zukunft, S., Adamski, J., & Rižner, T. L. (2014) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2014.11.012 · Cited by 40 · see citing works
Age-dependent increases in adrenal cytochrome b5 and serum 5-androstenediol-3-sulfate
Rege, J., Karashima, S., Lerario, A. M., Smith, J. M., Auchus, R. J., Kasa-Vubu, J. Z., Sasano, H., Nakamura, Y., White, P. C., & Rainey, W. E. (2016) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2016-2864 · Cited by 40 · see citing works
Self-citationStructure and catalytic mechanism of human steroid 5β-reductase (AKR1D1)
Costanzo, L. D., Drury, J. E., Christianson, D. W., & Penning, T. M. (2008) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2008.09.013 · Cited by 39 · see citing works
Self-citationGene analysis in δ-3-oxosteroid 5β–reductase deficiency
Sumazaki, R., Nakamura, N., Shoda, J., Kurosawa, T., & Tohma, M. (1997) · The Lancet · doi:10.1016/s0140-6736(05)62828-0 · Cited by 37 · see citing works
Jin, Y., & Penning, T. M. (2006) · Steroids · doi:10.1016/j.steroids.2005.12.002 · Cited by 37 · see citing works
Self-citationUrabe, A., Sassa, S., & Kappas, A. (1979) · The Journal of Experimental Medicine · doi:10.1084/jem.149.6.1314 · Cited by 36 · see citing works
Aldo-keto Reductase 1B15 (AKR1B15)
Weber, S., Salabei, J. K., Möller, G., Kremmer, E., Bhatnagar, A., Adamski, J., & Barski, O. A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.610121 · Cited by 35 · see citing works
Bhatia, C., Oerum, S., Bray, J. E., Kavanagh, K. L., Shafqat, N., Yue, W. W., & Oppermann, U. C. T. (2014) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2014.12.013 · Cited by 35 · see citing works
Platt, A., Xia, Z., Liu, Y., Chen, G., & Lazarus, P. J. (2016) · Pharmacogenetics and Genomics · doi:10.1097/fpc.0000000000000226 · Cited by 31 · see citing works
Functional expression of novel human and murine AKR1B genes
Salabei, J. K., Li, X., Petrash, J. M., Bhatnagar, A., & Barski, O. A. (2011) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2011.01.020 · Cited by 30 · see citing works
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 · see citing works
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 · see citing works
Papari-Zareei, M., Brandmaier, A., & Auchus, R. J. (2006) · Endocrinology · doi:10.1210/en.2005-1141 · Cited by 23 · see citing works
Self-citationEl-Kabbani, O. A. L., Scammells, P. J., Day, T., Dhagat, U., Endo, S., Matsunaga, T., Soda, M., & Hara, A. (2010) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2010.08.052 · Cited by 21 · see citing works
Takahashi, R. H., Grigliatti, T. A., Reid, R. E., & Riggs, K. W. (2009) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.109.150995 · Cited by 21 · see citing works
Gonzales, E. M., Cresteil, D., Baussan, C., Dabadie, A., Gerhardt, M., & Jacquemin, E. (2004) · Journal of Pediatric Gastroenterology and Nutrition · doi:10.1097/00005176-200406001-00312 · Cited by 20 · see citing works
Heredia, V. V., Cooper, W. C., Kruger, R. G., Jin, Y., & Penning, T. M. (2004) · Biochemistry · doi:10.1021/bi0499563 · Cited by 19 · see citing works
Self-citationZhang, B., Zhu, D., Hu, X., Zhou, M., Shang, P., & Lin, S. (2014) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2014.01.003 · Cited by 16 · see citing works
The effect of disease associated point mutations on 5β-reductase (AKR1D1) enzyme function
Mindnich, R., Drury, J. E., & Penning, T. M. (2011) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.12.020 · Cited by 16 · see citing works
Self-citationEl-Kabbani, O. A. L., Dhagat, U., Soda, M., Endo, S., Matsunaga, T., & Hara, A. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.01.076 · Cited by 12 · see citing works
Chen, M., Jin, Y., & Penning, T. M. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00816 · Cited by 12 · see citing works
Self-citationTatuya, O. H. T. A., Ishikura, S., Shintani, S., Usami, N., & Hara, A. (2000) · Biochemical Journal · doi:10.1042/bj3520685 · Cited by 9 · see citing works
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 · see citing works
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 · see citing works
Flagged first, then by citations
2 of the 171 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Schiffer, L., Barnard, L., Baranowski, E. S., Gilligan, L. C., Taylor, A. E., Arlt, W., Shackleton, C. H. L., & Storbeck, K.-H. (2019) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2019.105439 · Cited by 450 · see citing works
“precursors that escape the tissue specific activation via 5α-reduction are metabolized within the liver, which expresses both 5α- and 5β-reductases [54,94,100].”
Influential11-Oxygenated androgens in health and disease
Turcu, A. F., Rege, J., Auchus, R. J., & Rainey, W. E. (2020) · Nature Reviews Endocrinology · doi:10.1038/s41574-020-0336-x · Cited by 217 · see citing works
Self-citationThe Biosynthesis of Enzymatically Oxidized Lipids
Hajeyah, A. A., Griffiths, W. J., Wang, Y., Finch, A. J., & O’Donnell, V. B. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.591819 · Cited by 192 · see citing works
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 152 · see citing works
Self-citationMicrobial Hydroxysteroid Dehydrogenases: From Alpha to Omega
Doden, H. L., & Ridlon, J. M. (2021) · Microorganisms · doi:10.3390/microorganisms9030469 · Cited by 110 · see citing works
AKR1C1 Protects Corneal Epithelial Cells Against Oxidative Stress-Mediated Ferroptosis in Dry Eye
Zuo, X., Zeng, H., Wang, B., Yang, X., He, D., Wang, L., Ouyang, H. W., & Yuan, J. (2022) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.63.10.3 · Cited by 109 · see citing works
Paulukinas, R. D., Mesaros, C., & Penning, T. M. (2022) · Endocrinology · doi:10.1210/endocr/bqac068 · Cited by 63 · see citing works
Self-citationEndo, S., Oguri, H., Segawa, J., Kawai, M., Hu, D., Xia, S., Okada, T., Irie, K., Fujii, S., Gouda, H., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00939 · Cited by 63 · see citing works
Gut feelings about bacterial steroid-17,20-desmolase
Ly, L. K., Doden, H. L., & Ridlon, J. M. (2021) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2021.111174 · Cited by 43 · see citing works
Pleiotropic Actions of Aldehyde Reductase (AKR1A)
Fujii, J., Homma, T., Miyata, S., & Takahashi, M. (2021) · Metabolites · doi:10.3390/metabo11060343 · Cited by 42 · see citing works
Pyridine Moiety: An Insight into Recent Advances in the Treatment of Cancer
Sahu, R., Mishra, R., Kumar, R., Salahuddin, S., Majee, C., Mazumder, A., & Kumar, A. (2021) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557521666210614162031 · Cited by 39 · see citing works
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 · see citing works
Niu, J., Yan, R., Zhou, H., Ma, B., Lu, Z., Meng, F., Lü, F., & Ping, Z. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.129512 · Cited by 32 · see citing works
Hormone-linked redox status and its modulation by antioxidants
Sahoo, D. K., & Chainy, G. B. N. (2023) · Vitamins and hormones · doi:10.1016/bs.vh.2022.10.007 · Cited by 33 · see citing works
Cytochrome P450 and Other Drug-Metabolizing Enzymes As Therapeutic Targets
Foti, R. (2023) · Drug Metabolism and Disposition · doi:10.1124/dmd.122.001011 · Cited by 30 · see citing works
Integration of androgen hormones in endometrial cancer biology
Gjorgoska, M., & Rižner, T. L. (2022) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2022.06.001 · Cited by 27 · see citing works
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 28 · see citing works
Martin, C., Crastin, A., Sagmeister, M. S., Kalirai, M. S., Turner, J. D., MacDonald, L., Kurowska‐Stolarska, M., Scheel‐Toellner, D., TAYLOR, A. E. R., Gilligan, L. C., et al. (2024) · Journal of Autoimmunity · doi:10.1016/j.jaut.2024.103263 · Cited by 26 · see citing works
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 · see citing works
Aldo-keto reductases: Role in cancer development and theranostics
Nagini, S., Kallamadi, P. R., Tanagala, K. K. K., & Reddy, G. B. (2024) · Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics · doi:10.32604/or.2024.049918 · Cited by 25 · see citing works
Nikolaou, N., Hodson, L., & Tomlinson, J. (2021) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2021.105808 · Cited by 24 · see citing works
Aldo-keto reductase (AKR) superfamily website and database: An update
Huacachino, A. A., Joo, J., Narayanan, N., Tehim, A., Himes, B. E., & Penning, T. M. (2024) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2024.111111 · Cited by 25 · see citing works
Self-citationPeripheral blood mononuclear cells preferentially activate 11-oxygenated androgens
Schiffer, L., Bossey, A., Kempegowda, P., TAYLOR, A. E. R., Akerman, İ., Scheel‐Toellner, D., Storbeck, K., & Arlt, W. (2021) · European Journal of Endocrinology · doi:10.1530/eje-20-1077 · Cited by 22 · see citing works
Detlefsen, A. J., Paulukinas, R. D., & Penning, T. M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031873 · Cited by 23 · see citing works
Self-citationWang, Y., Fan, J., Yu, T., Wang, L., Wang, L., Weng, C., Lai, C., Song, J., & Zhang, W. (2023) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2023.106740 · Cited by 21 · see citing works
Tripathy, S., Nallasamy, S., & Mahendroo, M. (2022) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2022.106137 · Cited by 19 · see citing works
Electrochemical Biosensing of Glucose Based on the Enzymatic Reduction of Glucose
Soranzo, T., Tahar, A. B., Chmayssem, A., Zelsmann, M., Vadgama, P. M., Lenormand, J., Cinquin, P., Martin, D. K., & Zebda, A. (2022) · Sensors · doi:10.3390/s22197105 · Cited by 19 · see citing works
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 · see citing works
Self-citationHepatic miR-378 modulates serum cholesterol levels by regulating hepatic bile acid synthesis
Sun, C., Liu, W., Lu, Z., Li, Y., Liu, S., Tang, Z., Yan, Y., Li, Z., Feng, H., Zhang, D., et al. (2021) · Theranostics · doi:10.7150/thno.53624 · Cited by 19 · see citing works
AKR1C1/2 inhibition by MPA sensitizes platinum resistant ovarian cancer towards carboplatin
Badmann, S., Mayr, D. C., Schmoeckel, E., Hester, A., Buschmann, C., Beyer, S., Kolben, T., Kraus, F. B. T., Chelariu-Raicu, A., Burges, A., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-05785-9 · Cited by 18 · see citing works
Dai, T., Ye, L., Yu, H., Li, K., Li, J., Liu, R., Lü, X. C., Deng, M., Li, R., Liu, W., et al. (2021) · Journal of Hepatocellular Carcinoma · doi:10.2147/jhc.s323743 · Cited by 17 · see citing works
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 · see citing works
Pyridine Moiety: Recent Advances in Cancer Treatment
Sahu, R., Mishra, R., Kumar, R., Majee, C., Salahuddin, S., MAZUMDER, A., & Kumar, A. (2021) · Indian Journal of Pharmaceutical Sciences · doi:10.36468/pharmaceutical-sciences.763 · Cited by 16 · see citing works
Progesterone Metabolism by Human and Rat Hepatic and Intestinal Tissue
Coombes, Z., Plant, K., Freire, C., Basit, A. W., Butler, P. J., Conlan, R. S., & González, D. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13101707 · Cited by 16 · see citing works
5β-Dihydrosteroids: Formation and Properties
Penning, T. M., & Covey, D. F. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25168857 · Cited by 15 · see citing works
Self-citationEndo, S., Morikawa, Y., Matsunaga, T., Hara, A., & Nishinaka, T. (2022) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2022.106113 · Cited by 16 · see citing works
Abramova, V., Alvarado, V. L., Hill, M., Smejkalová, T., Malý, M., Valeš, K., Dittert, I., Božíková, P., Kysilov, B., Krausová, B. H., et al. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00131 · Cited by 14 · see citing works
Advances in aldo-keto reductases immobilization for biocatalytic synthesis of chiral alcohols
Zhang, W., Shao, Z.-Q., Wang, Z., Ye, Y., Li, S., & Wang, Y. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.133264 · Cited by 14 · see citing works
Frankó, A., Berti, L., Hennenlotter, J., Rausch, S., Scharpf, M. O., de Angelis, M. H., Stenzl, A., Birkenfeld, A. L., Peter, A., Lutz, S. Z., et al. (2020) · Journal of Personalized Medicine · doi:10.3390/jpm10030124 · Cited by 14 · see citing works
Kudová, E., Mareš, P., Hill, M., Vondráková, K., Tsenov, G., Chodounská, H., Kubová, H., & Valeš, K. (2021) · Pharmaceuticals · doi:10.3390/ph15010049 · Cited by 14 · see citing works
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 15 · see citing works
Krishnaiah, M., Jonnalagadda, S. K., Morsy, A., Duan, L., Chhonker, Y. S., Murry, D. J., Penning, T. M., & Trippier, P. C. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00732 · Cited by 13 · see citing works
Self-citationKawai, S., & Hashimoto, W. (2022) · Molecules · doi:10.3390/molecules27020338 · Cited by 13 · see citing works
Relevance of Human Aldoketoreductases and Microbial β-Glucuronidases in Testosterone Disposition
Basit, A., Amory, J. K., Mettu, V. S., Li, C. Y., Heyward, S. A., Jariwala, P. B., Redinbo, M. R., & Prasad, B. (2023) · Drug Metabolism and Disposition · doi:10.1124/dmd.122.000975 · Cited by 13 · see citing works
Šestić, T. L., Ajduković, J. J., Bekić, S. S., Ćelić, A. S., Stojanović, S., Najman, S. J., Marinović, M. A., Petri, E. T., Škorić, D., & Savić, M. P. (2023) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2023.106362 · Cited by 12 · see citing works
Function, drug resistance and prognostic effect of AKR1C2 in human cancer
Wang, Z., Feng, Y., Song, J., Sun, D., & Zhang, Y. (2023) · Neoplasma · doi:10.4149/neo_2023_230206n66 · Cited by 12 · see citing works
The Role of Prostaglandins as Major Inflammatory Mediators in Colorectal Cancer
Macia-Guardado, M., Lutz, V., Hengstschläger, M., & Dolznig, H. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262412191 · Cited by 15 · see citing works
Saleem, N., Aziz, U., Ali, M., Liu, X., Alwutayd, K. M., Alshegaihi, R. M., Niedbała, G., Elkelish, A., & Zhang, M. (2023) · Frontiers in Plant Science · doi:10.3389/fpls.2023.1159394 · Cited by 11 · see citing works
Differential activity and expression of human 5β-reductase (AKR1D1) splice variants
Appanna, N., Gibson, H., Gangitano, E., Dempster, N. J., Morris, K., George, S., Arvaniti, A., Gathercole, L., Keevil, B. G., Penning, T. M., et al. (2021) · Journal of Molecular Endocrinology · doi:10.1530/jme-20-0160 · Cited by 11 · see citing works
Self-citationFunctional Protein Composition in Femoral Glands of Sand Lizards (Lacerta agilis)
Ibáñez, A., Skupień-Rabian, B., Jankowska, U., Kędracka–Krok, S., Zając, B., & Pabijan, M. (2022) · Molecules · doi:10.3390/molecules27072371 · Cited by 11 · see citing works
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 · see citing works
Self-citationMarinović, M., Petri, E. T., Grbović, L. M., Vasiljević, B., Jovanović-Šanta, S., Bekić, S. S., & Ćelić, A. S. (2022) · Molecular Informatics · doi:10.1002/minf.202100256 · Cited by 11 · see citing works
Tenjović, B., Bekić, S. S., Ćelić, A. S., Petri, E. T., Scholda, J., Kopp, F. B., Sakač, M. N., & Nikolić, A. R. (2024) · RSC Medicinal Chemistry · doi:10.1039/d4md00297k · Cited by 10 · see citing works
Sanchon-Sanchez, P., Herráez, E., Macı́as, R. I. R., Estiú, M. C., Fortes, P., Monte, M. J., Marı́n, J. J. G., & Romero, M. R. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166926 · Cited by 10 · see citing works
Synthesis and Medicinal Applications of Fenamic Acid Derivatives
Sharma, M., & Prasher, P. (2023) · Current Organic Chemistry · doi:10.2174/1385272827666230914113509 · Cited by 9 · see citing works
AKR1B10 and digestive tumors development: a review
Shen, Y., Qiu, A., Huang, X., Wen, X., Shehzadi, S., He, Y., Hu, Q., Zhang, J., Luo, D., & Yang, S. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1462174 · Cited by 9 · see citing works
Khan, M. N., Binli, M., Hu, J., Mengjia, S., Shunyao, W., & Li, X. (2025) · Discover Oncology · doi:10.1007/s12672-025-03017-w · Cited by 9 · see citing works
Liu, M., Lin, C., Huang, Q.-W., Jia, J., Guo, J., & Jia, R. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043872 · Cited by 9 · see citing works
Role of Human Aldo–Keto Reductases in the Nitroreduction of 1-Nitropyrene and 1,8-Dinitropyrene
Su, A. L., Mesaros, C., Krzeminski, J., El‐Bayoumy, K., & Penning, T. M. (2022) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.2c00271 · Cited by 10 · see citing works
Self-citationHardaway, A., Goudarzi, M., Berk, M. P., Chung, Y., Zhang, R., Li, J., Klein, E. A., & Sharifi, N. (2022) · Endocrinology · doi:10.1210/endocr/bqac191 · Cited by 9 · see citing works
Shi, T., Fan, Q., Liu, S., & Zhang, S. (2024) · Biochemical Pharmacology · doi:10.1016/j.bcp.2024.116309 · Cited by 8 · see citing works
Adaptive loss of shortwave-sensitive opsins during cartilaginous fish evolution
Zhang, B., Feng, Y., Lv, M., Jia, L., Liao, Y., Xu, X., Meyer, A., Sun, J., Fan, G., Li, Y., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-62544-w · Cited by 8 · see citing works
Lin, J., Wu, W., Nie, G., Li, J., Fang, X., Sheng, Y.-G., Wang, M., Zheng, Q.-Y., Guo, X., Huang, J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-64323-z · Cited by 8 · see citing works
Pharmacology and therapeutics of bile acid synthesis and modification enzymes in metabolic diseases
Ding, L., Jin, L., & Huang, W. (2026) · Pharmacological Reviews · doi:10.1016/j.pharmr.2026.100115 · Cited by 9 · see citing works
Manzella, F. M., Cabrera, O. H., Wilkey, D., Fine-Raquet, B., Klawitter, J., Krishnan, K., Covey, D. F., Jevtović‐Todorović, V., & Todorovic, S. M. (2022) · British Journal of Anaesthesia · doi:10.1016/j.bja.2022.09.025 · Cited by 8 · see citing works
Oakley, J., Hill, M., Giess, A. P., Tanguy, M., & Elgar, G. S. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04711-5 · Cited by 9 · see citing works
Huacachino, A. A., Chung, A., Sharp, K. A., & Penning, T. M. (2024) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2024.106641 · Cited by 8 · see citing works
Self-citationHirosawa, K., Fujioka, H., Morinaga, G., Fukami, T., Ishiguro, N., Kishimoto, W., Nakase, H., Mizuguchi, H., & Nakajima, M. (2023) · Drug Metabolism and Disposition · doi:10.1124/dmd.123.001402 · Cited by 8 · see citing works
A three-level regulatory mechanism of the aldo-keto reductase subfamily AKR12D
Xiao, Z., Zha, J., Yang, X., Huang, T., Huang, S., Liu, Q., Wang, X., Zhong, J., Zheng, J., Liang, R., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-46363-z · Cited by 7 · see citing works
Chemical Diversity of Ketosteroids as Potential Therapeutic Agents
Dembitsky, V. M. (2024) · Microbiology Research · doi:10.3390/microbiolres15030103 · Cited by 6 · see citing works
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 7 · see citing works
Kettunen, K., Mathlin, J., Lamminen, T., Laiho, A., Häkkinen, M. R., Auriola, S. O. K., Elo, L. L., Boström, P. J., POUTANEN, M. H., & Taimen, P. (2024) · EBioMedicine · doi:10.1016/j.ebiom.2024.105359 · Cited by 6 · see citing works
Kędzierski, J., Allard, J. A., Odermatt, A., & Smieško, M. (2023) · Toxicology Letters · doi:10.1016/j.toxlet.2023.07.006 · Cited by 6 · see citing works
Mitsuizumi, H., & Mori, S. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c01751 · Cited by 6 · see citing works
Zhang, Z., Yun, Z., Zhao, H., Wu, Y., & Sun, L. (2023) · Chemical Communications · doi:10.1039/d3cc00850a · Cited by 5 · see citing works
Bose, H. S. (2024) · iScience · doi:10.1016/j.isci.2024.110039 · Cited by 5 · see citing works
Coumarin‐Based Aldo‐Keto Reductase Family 1C (AKR1C) 2 and 3 Inhibitors
Jonnalagadda, S. K., Duan, L., Dow, L. F., Boligala, G. P., Kosmacek, E. A., McCoy, K., Oberley‐Deegan, R. E., Chhonker, Y. S., Murry, D. J., Reynolds, C. P., et al. (2024) · ChemMedChem · doi:10.1002/cmdc.202400081 · Cited by 5 · see citing works
Self-citationGao, X., Yu, Z., Yang, J., Gao, Y., Li, S., & Zhang, W. (2020) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.13258 · Cited by 5 · see citing works
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 · see citing works
Self-citationŠtěrbová, K., Stuchlíková, L. R., Rychlá, N., Kohoutová, K., Babičková, M., Skálová, L., & Matoušková, P. (2024) · International Journal for Parasitology Drugs and Drug Resistance · doi:10.1016/j.ijpddr.2024.100555 · Cited by 4 · see citing works
Yang, F., Luo, J., Han, S., Zhang, Y., Liu, Z., Lan, J., Sun, Y., & Zhao, T. (2024) · Frontiers in Plant Science · doi:10.3389/fpls.2024.1480519 · Cited by 4 · see citing works
Bachhav, N., Subash, S., Ahire, D. S., Singh, D. K., & Prasad, B. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.117044 · Cited by 4 · see citing works
Zhou, L., Zhang, C., Xu, C., Chen, Z., Chen, R., Cao, L., & Jia, S. (2025) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2025.118497 · Cited by 4 · see citing works
Pawar, S., Mahajan, S., Sahu, P., & Bajaj, P. (2026) · Bioorganic chemistry (Print) · doi:10.1016/j.bioorg.2026.109620 · Cited by 4 · see citing works
Assessment of steroid enzymes action in children and adolescents with obesity
Sumińska, M., Podgórski, R., Fichna, P., Mazur, A., & Fichna, M. (2023) · Steroids · doi:10.1016/j.steroids.2023.109325 · Cited by 4 · see citing works
Cancer to Cataracts: The Mechanistic Impact of Aldo-Keto Reductases in Chronic Diseases
Shanbhag, A. P., & Bhowmik, P. (2024) · The Yale Journal of Biology and Medicine · doi:10.59249/vtbv6559 · Cited by 4 · see citing works
Niu, J., Ma, B., Zhu, H., Liu, H., Zhao, H., Bie, X., Lü, F., & Ping, Z. (2024) · Food Science and Human Wellness · doi:10.26599/fshw.2024.9250194 · Cited by 4 · see citing works
Adipocyte maturation impacts daunorubicin disposition and metabolism
Li, Z., Ngu, R., Naik, A. A., Trinh, K., Paharkova, V., Liao, H., Liu, Y., Zhuang, C., Le, D., Pei, H., et al. (2024) · European Journal of Clinical Investigation · doi:10.1111/eci.14307 · Cited by 4 · see citing works
Xing, S., Liu, Y., Xie, H., Guo, C., Wang, X., Lv, B., Li, X., Shao, J., Guo, Q., Feng, F., et al. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117413 · Cited by 5 · see citing works
Aldo keto-reductase family 1C members 1 through 4 recombinant enzyme purification and enzyme assay
Detlefsen, A. J. (2023) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2023.04.007 · Cited by 4 · see citing works
Šadibolová, M., Zárybnický, T., Smutný, T., Pávek, P., Šubrt, Z., Matoušková, P., Skálová, L., & Boušová, I. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184562 · Cited by 4 · see citing works
Ma, B., Niu, J., Zhu, H., Chi, H., Lu, Z., Lü, F., & Ping, Z. (2025) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.4c12497 · Cited by 3 · see citing works
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 · see citing works
AKR1B1 bridges metabolic pathways and disease progression
Zhang, Q., Cao, Z., Wang, T., Zhong, L., Sun, Z., & Cao, D. (2025) · Cellular Signalling · doi:10.1016/j.cellsig.2025.112324 · Cited by 5 · see citing works
Li, Z., Gu, B., Wang, Q., Liu, M., Ban, S., & Song, H. (2025) · ACS Catalysis · doi:10.1021/acscatal.5c06187 · Cited by 3 · see citing works
Endo, S., Morikawa, Y., Suenami, K., Sakai, Y., Abe, N., Matsunaga, T., Hara, A., & Takasu, M. (2024) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2024.106574 · Cited by 3 · see citing works
Cloning and characterization of steroid 5β-reductase from the venom gland of Bufo bufo gargarizans
Zhang, Y., Li, X., Xu, D., Wu, M., Dai, Y., Xia, M., & Wang, D. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.01.211 · Cited by 3 · see citing works
Honour, J. W. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-818124-9.00013-9 · Cited by 3 · see citing works
Endo, S., Matsunaga, T., & Hara, A. (2021) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2021.108755 · Cited by 3 · see citing works
Human xenobiotic metabolism proteins have full-length and split homologs in the gut microbiome
Rendina, M. C., Turnbaugh, P. J., & Bradley, P. H. (2025) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkaf131 · Cited by 2 · see citing works
- Authors
- Penning, T. M., Wangtrakuldee, P., & Auchus, R. J.
- Affiliations
- University of Pennsylvania (US)
- University of Michigan (US)
- Corresponding author
- Penning, Trevor M
- Venue
- Endocrine Reviews
- Publisher
- The Endocrine Society
- Published
- 2018-08-20
- Volume
- 40
- Issue
- 2
- Pages
- 447-475
- ISSN
- 0163-769X (ISSN-L)
- 1945-7189
- PMC
- PMC6405412
- OpenAlex
- W2888187525
- Cited by
- 164
- References
- 171
- Citations by year
- 2026: 30 · 2025: 28 · 2024: 34 · 2023: 27 · 2022: 19 · 2021: 16 · 2020: 7 · 2019: 3
- FWCI
- 0.76
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Endocrine Reviews (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Environmental Health Sciences (P30 ES013508)
- National Institute of General Medical Sciences (R01GM086596)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Aldose Reductase and Taurine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Steroid Chemistry and Biochemistry
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
- Keywords
- aldo-keto reductase, AKR1D1, steroid metabolism, androgen receptor, estrogen receptor, progesterone receptor, bile acid synthesis, farnesoid X receptor, enzyme crystal structure, catalytic mechanism, enzyme kinetics, splice variants, genetic polymorphism, enzyme inhibitors, endocrine disorders
- MeSH terms
- Aldo-Keto Reductases, Humans, Hydroxysteroid Dehydrogenases, Oxidoreductases, Steroids
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review