The DOI matches its Crossref record; 37 of the 38 references it cites were found in a registry or an index.
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
Open accessAbstract
The kinetic parameters, steroid substrate specificity and identities of reaction products were determined for four homogeneous recombinant human 3α-hydroxysteroid dehydrogenase (3α-HSD) isoforms of the aldo-keto reductase (AKR) superfamily. The enzymes correspond to type 1 3α-HSD (AKR1C4), type 2 3α(17β)-HSD (AKR1C3), type 3 3α-HSD (AKR1C2) and 20α(3α)-HSD (AKR1C1), and share at least 84% amino acid sequence identity. All enzymes acted as NAD(P)(H)-dependent 3-, 17- and 20-ketosteroid reductases and as 3α-, 17β- and 20α-hydroxysteroid oxidases. The functional plasticity of these isoforms highlights their ability to modulate the levels of active androgens, oestrogens and progestins. Salient features were that AKR1C4 was the most catalytically efficient, with kcat/Km values for substrates that exceeded those obtained with other isoforms by 10–30-fold. In the reduction direction, all isoforms inactivated 5α-dihydrotestosterone (17β-hydroxy-5α-androstan-3-one; 5α-DHT) to yield 5α-androstane-3α,17β-diol (3α-androstanediol). However, only AKR1C3 reduced ∆4-androstene-3,17-dione to produce significant amounts of testosterone. All isoforms reduced oestrone to 17β-oestradiol, and progesterone to 20α-hydroxy-pregn-4-ene-3,20-dione (20α-hydroxyprogesterone). In the oxidation direction, only AKR1C2 converted 3α-androstanediol to the active hormone 5α-DHT. AKR1C3 and AKR1C4 oxidized testosterone to ∆4-androstene-3,17-dione. All isoforms oxidized 17β-oestradiol to oestrone, and 20α-hydroxy…
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“17HSD5 may account for much of the extratesticular, peripheral conversion of androstenedione to testosterone, although its catalytic efficiency as a 17HSD is poor (528) compared with its 20␣HSD activity with progesterone and DOC (520) or its prostaglandin dehydrogenase activity, reducing prostaglandin H 2 to prostaglandin F 2␣ (529).”
From The Molecular Biology, Biochemistry, and Physiology of Human Steroidogenesis and Its Disorders (2011) · cites this paper as [528]
Experimental — accuracy not yet measuredIn the citing paper
“AKR1C1-AKR1C4 act as 3-keto, 17-keto and 20-ketosteroid reductases to varying extents”
From Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism (2014) · cites this paper as [14]
In the citing paper
“AKR1C enzymes (AKR1C1-AKR1C4) function in vivo as 3-keto-, 17-keto- and 20-ketosteroid reductases to form 3α/β, 17β- and 20α-hydroxy-metabolites to varying extents and thus metabolize a broad spectrum of natural and synthetic therapeutic steroids”
From Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism (2014) · cites this paper as [14]
In the citing paper
“These enzymes are expressed in different tissues, while AKR1C4 is mainly liver specific”
From Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism (2014) · cites this paper as [14]
In the citing paper
“AKR1C1, but also AKR1C2 and AKR1C3 catalyze progesterone reduction to form the less potent progestagen 20α-hydroxy-pregn-4-ene-3-one”
From Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism (2014) · cites this paper as [14]
In the citing paper
“AKR1C3 is the most efficient enzyme for this reaction (KM = 9 μM, kcat = 0.068 mM−1; kcat/KM = 76 min−1 mm−1).”
From Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism (2014) · cites this paper as [14]
In the citing paper
“AKR1C enzymes also act as 17-ketosteroid reductases to reduce the weak estrogen, estrone to form the potent estrogen, 17β-estradiol in peripheral tissues”
From Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism (2014) · cites this paper as [14]
In the citing paper
“Other AKR1C enzymes have much lower activities for 17β-estradiol formation”
From Role of aldo-keto reductase family 1 (AKR1) enzymes in human steroid metabolism (2014) · cites this paper as [14]
In the citing paper
“AKR1C enzymes are multifunctional and also function as 20α- and 17β-HSDs, with different efficiencies, stereoselectivities and tissue specific expression [104].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [104]
In the citing paper
“the direct 20α-reduction of progesterone terminates its progestogenic activity”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [104]
In the citing paper
“is predominantly catalyzed by AKR1C1 [104,115].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [104]
In the citing paper
“AKR1C1 is the predominant 20-ketosteroid reductase in human [104].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [104]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Statistical estimations in enzyme kinetics
Wilkinson, G. (1961) · Biochemical Journal · doi:10.1042/bj0800324 · Cited by 3,535
Steroid hormone metabolites are barbiturate-like modulators of the GABA receptor
Majewska, M. D., Harrison, N. L., Schwartz, R. D., Barker, J. L., & Paul, S. M. (1986) · Science · doi:10.1126/science.2422758 · Cited by 2,225
Majewska, M. D. (1992) · Progress in Neurobiology · doi:10.1016/0301-0082(92)90025-a · Cited by 1,089
Neurosteroids and GABAA receptor function
Lambert, J. J., Belelli, D., Hill-Venning, C., & Peters, J. A. (1995) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(00)89058-6 · Cited by 746
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
Self-citationThe key role of 17β-hydroxysteroid dehydrogenases in sex steroid biology
Labrie, F., Luu-The, V., Lin, S.-X., Claude, L., Simard, J., Breton, R., & Bélanger, A. (1997) · Steroids · doi:10.1016/s0039-128x(96)00174-2 · Cited by 480
Selective 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
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
Self-citationDanielsson, H., & Sjövall, J. (1975) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.44.070175.001313 · Cited by 272
Steroid Structure and Androgenic Activity
Liao, S., Liang, T., Fang, S., Castañeda, E., & Shao, T.-C. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43521-7 · Cited by 265
Research works printed but not linked: 2
- 29 Leatherbarrow, R. J. (1987) ENZFITTER: A non-linear regression data analysis program for the IBM PC (and true compatibles), BioSoft, Cambridge, U.K.
- 33 Lin, H.-K., Jez, J. M., Overby, A. M., Burczynski, M. E., Peehl, D. M. and Penning, T. M. (2000) Type 3 3 a -hydroxysteroid dehydrogenase (3 a -HSD) accumulates 5 a -DHT and activates the androgen receptor in human prostate cancer PC3 cells. Proc. Am. Assoc. Cancer. Res. 41 , Abstract 1510
Cited by
Sorted by citations
Items 201–300 of 671
The Adrenal Cortex and its Disorders
Miller, W. L. (2009) · Wiley eBooks · doi:10.1002/9781444316728.ch13 · Cited by 51
Jin, Y., Duan, L., Lee, S. H., Kloosterboer, H. J., Blair, I. A., & Penning, T. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809465200 · Cited by 50
Self-citationAdeniji, A. O., Twenter, B. M., Byrns, M. C., Jin, Y., Winkler, J. D., & Penning, T. M. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.01.010 · Cited by 51
Self-citationLyon, R. C., Li, D., McGarvie, G. M., & Ellis, E. M. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.10.007 · Cited by 52
Aldo-keto reductase 1C3—Assessment as a new target for the treatment of endometriosis
Rižner, T. L., & Penning, T. M. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104446 · Cited by 53
Self-citationMinireview: Modulation of Hormone Receptor Signaling by Dietary Anticancer Indoles
Firestone, G. L., & Sundar, S. N. (2009) · Molecular Endocrinology · doi:10.1210/me.2009-0149 · Cited by 50
Characterization of the 5 -Reductase-3 -Hydroxysteroid Dehydrogenase Complex in the Human Brain
Steckelbroeck, S., Watzka, M., Reichelt, R., Hans, V., Stoffel‐Wagner, B., Heidrich, D. D., Schramm, J., BIDLINGMAIER, F., & Klingmüller, D. (2001) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.86.3.7325 · Cited by 56
Jin, Y., Mesaros, A. C., Blair, I. A., & Penning, T. M. (2011) · Biochemical Journal · doi:10.1042/bj20101804 · Cited by 49
Self-citationEndo, S., Matsunaga, T., Kanamori, A., Otsuji, Y., Nagai, H., Sundaram, K., El-Kabbani, O. A. L., Toyooka, N., Ohta, S., & Hara, A. (2012) · Journal of Natural Products · doi:10.1021/np201002x · Cited by 49
Bremer, A. A., & Miller, W. L. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-408134-5.00013-5 · Cited by 54
Xiong, W., Zhao, J., Yu, H., Li, X., Sun, S., Li, Y., Xia, Q., Zhang, C., He, Q., Gao, X., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111911 · Cited by 50
Moore, S. G., Scully, S., Browne, J. A., Fair, T., & Butler, S. T. (2014) · Journal of Dairy Science · doi:10.3168/jds.2014-8133 · Cited by 49
Hevir, 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
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
Enzymes of the AKR1B and AKR1C Subfamilies and Uterine Diseases
Rižner, T. L. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00034 · Cited by 50
Romero‐Ramírez, L., & Mey, J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25179279 · Cited by 50
Androgen synthesis in prostate cancer: do all roads lead to Rome?
Stuchbery, R., McCoy, P. J., Hovens, C. M., & Corcoran, N. M. (2016) · Nature Reviews Urology · doi:10.1038/nrurol.2016.221 · Cited by 46
Iino, T., 真由子, 田., Takikawa, S.-I., Sawada, H., Shintaku, H., Ishikura, S., & Hara, A. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(03)00295-9 · Cited by 48
Phytoestrogens as inhibitors of the human progesterone metabolizing enzyme AKR1C1
Brožič, P., Šmuc, T., Gobec, S., & Rižner, T. L. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2006.08.001 · Cited by 46
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
Self-citationMarcos, J., Guo, L., Wilson, W. K., Porter, F. D., & Shackleton, C. H. L. (2003) · Steroids · doi:10.1016/j.steroids.2003.09.013 · Cited by 46
Matsunaga, T., Arakaki, M., Kamiya, T., Endo, S., El-Kabbani, O. A. L., & Hara, A. (2009) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2009.05.005 · Cited by 45
Gobec, S., Brožič, P., & Rižner, T. L. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.08.063 · Cited by 46
Yee, D. J., Balšánek, V., Bauman, D. R., Penning, T. M., & Sameš, D. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604672103 · Cited by 45
Self-citationEbert, B., Kisiela, M., & Maser, E. (2014) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12108 · Cited by 49
Cinnamic acids as new inhibitors of 17β-hydroxysteroid dehydrogenase type 5 (AKR1C3)
Brožič, P., Golob, B., Gomboc, N., Rižner, T. L., & Gobec, S. (2005) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2005.10.020 · Cited by 44
Nongenomic Action of Steroids in Myometrial Contractility
Perusquı́a, M. (2001) · Endocrine · doi:10.1385/endo:15:1:063 · Cited by 45
Jamieson, S. M. F., Gu, Y., Manesh, D. M., El‐Hoss, J., Jing, D., MacKenzie, K. L., Guise, C. P., Foehrenbacher, A., Pullen, S. M., Benito, J., et al. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.019 · Cited by 42
Androgen biosynthesis in castration-resistant prostate cancer
Penning, T. M. (2014) · Endocrine Related Cancer · doi:10.1530/erc-14-0109 · Cited by 48
Self-citationAdrenal cortex and its disorders
Miller, W. L., & Flück, C. E. (2014) · Elsevier eBooks · doi:10.1016/b978-1-4557-4858-7.00022-6 · Cited by 45
Grindflek, E. H., Berget, I., Moe, M., Oeth, P. A., & Lien, S. (2010) · BMC Genetics · doi:10.1186/1471-2156-11-4 · Cited by 42
5α‐reductase type 3 enzyme in benign and malignant prostate
Titus, M. A., Li, Y., Kozyreva, O. G., Maher, V., Godoy, A., Smith, G. J., & Mohler, J. L. (2013) · The Prostate · doi:10.1002/pros.22745 · Cited by 40
Can genes for mammographic density inform cancer aetiology?
Kelemen, L. E., Sellers, T. A., & Vachon, C. M. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2466 · Cited by 41
El-Kabbani, O. A. L., Scammells, P. J., Gosling, J., Dhagat, U., Endo, S., Matsunaga, T., Soda, M., & Hara, A. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm9001633 · Cited by 42
Inhibitors of human 20α-hydroxysteroid dehydrogenase (AKR1C1)
El-Kabbani, O. A. L., Dhagat, U., & Hara, A. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.10.006 · Cited by 43
Lemley, C. O., Vonnahme, K. A., Tager, L. R., Krause, K. M., & Wilson, M. E. (2010) · Journal of Endocrinology · doi:10.1677/joe-10-0042 · Cited by 39
Enzymology and Molecular Biology of Glucocorticoid Metabolism in Humans
Blum, A., & Maser, E. (2003) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(03)75006-5 · Cited by 44
Heinosalo, T., Saarinen, N., & POUTANEN, M. H. (2018) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2018.08.004 · Cited by 40
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 41
Flanagan, J. U., Atwell, G. J., Heinrich, D. M., Brooke, D. G., Silva, S., Rigoreau, L. J. M., Trivier, E., Turnbull, A. P., Raynham, T. M., Jamieson, S. M. F., et al. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.12.050 · Cited by 40
Li, Y., He, X., Yang, X., Huang, K., Luo, Y., Zhu, L., Li, Y., & Xu, W. (2015) · Scientific Reports · doi:10.1038/srep14277 · Cited by 40
Sharifi, N., McPhaul, M. J., & Auchus, R. J. (2010) · Journal of Investigative Medicine · doi:10.2310/jim.0b013e3181ff6bb8 · Cited by 36
PTHrP stimulates prostate cancer cell growth and upregulates aldo–keto reductase 1C3
Downs, T. M., Burton, D. W., Araiza, F., Hastings, R. H., & Deftos, L. J. (2011) · Cancer Letters · doi:10.1016/j.canlet.2011.02.027 · Cited by 40
Mantel, A., Carpenter-Mendini, A. B., VanBuskirk, J., Benedetto, A. D., Beck, L. A., & Pentland, A. P. (2011) · Journal of Investigative Dermatology · doi:10.1038/jid.2011.412 · Cited by 40
Schuster, D., Kowalik, D., Kirchmair, J., Laggner, C., Markt, P., Aebischer-Gumy, C., Ströhle, F., Möller, G., Wolber, G., Wilckens, T., et al. (2011) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2011.01.016 · Cited by 39
Proposed mechanism for sperm chromatin condensation/decondensation in the male rat
Chapman, J. C., & Michael, S. D. (2003) · Reproductive Biology and Endocrinology · doi:10.1186/1477-7827-1-20 · Cited by 42
Evolution of a novel adrenal cell type that promotes parental care
Niepoth, N., Merritt, J. R., Uminski, M., Lei, E., Esquibies, V. S., Bando, I. B., Hernandez, K. A., Gebhardt, C., Wacker, S., Lutzu, S., et al. (2024) · Nature · doi:10.1038/s41586-024-07423-y · Cited by 36
Milivojevic, V., Kranzler, H. R., Gelernter, J. E., Burian, L. C., & Covault, J. (2011) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2010.01425.x · Cited by 37
Sinreih, M., Hevir, N., & Rižner, T. L. (2012) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2012.11.012 · Cited by 38
Jamieson, S. M. F., Brooke, D. G., Heinrich, D. M., Atwell, G. J., Silva, S., Hamilton, E. J., Turnbull, A. P., Rigoreau, L. J. M., Trivier, E., Soudy, C., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm3007867 · Cited by 39
Steroid metabolism in breast cancer: Where are we and what are we missing?
Africander, D., & Storbeck, K. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.05.016 · Cited by 40
Wanichwatanadecha, P., Sirisrimangkorn, S., Kaewprag, J., & Ponglikitmongkol, M. (2012) · Journal of General Virology · doi:10.1099/vir.0.038265-0 · Cited by 41
Adrenal androgens, adrenarche, and zona reticularis: A human affair?
Dumontet, T., & Martinez, A. (2021) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2021.111239 · Cited by 41
Lemley, C. O., Wilmoth, T. A., Tager, L. R., Krause, K. M., & Wilson, M. E. (2010) · Journal of Dairy Science · doi:10.3168/jds.2009-2539 · Cited by 37
Antineoplastic Effects of Gamma Linolenic Acid on Hepatocellular Carcinoma Cell Lines
Itoh, S., Taketomi, A., Harimoto, N., Tsujita, E., Rikimaru, T., Shirabe, K., Shimada, M., & Maehara, Y. (2010) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.10-24 · Cited by 36
Jin, Y., & Penning, T. M. (2006) · Steroids · doi:10.1016/j.steroids.2005.12.002 · Cited by 37
Self-citationLord, S. J., Mack, W. J., Berg, D. V. D., Pike, M. C., Ingles, S. A., Haiman, C. A., Wang, W., Parisky, Y. R., Hodis, H. N., & Ursin, G. (2005) · Breast Cancer Research · doi:10.1186/bcr999 · Cited by 37
Update on Adrenarche—Still a Mystery
Augsburger, P., Liimatta, J., & Flück, C. E. (2024) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgae008 · Cited by 44
Retinaldehyde is a substrate for human aldo–keto reductases of the 1C subfamily
Ruiz, F. X., Porté, S., Gallego, O., Moro, A., Ardèvol, A., Río-Espínola, A. D., Rovira, C., Farrés, J., & Parés, X. (2011) · Biochemical Journal · doi:10.1042/bj20111286 · Cited by 38
Aldo-keto reductase 1C3 may be a new radioresistance marker in non-small-cell lung cancer
Xie, L., Yu, J., Guo, W., Wei, L., Liu, Y., Wang, X., & Song, X. (2013) · Cancer Gene Therapy · doi:10.1038/cgt.2013.15 · Cited by 36
Marín, Y. E., Seiberg, M., & Lin, C. B. (2009) · Experimental Dermatology · doi:10.1111/j.1600-0625.2008.00839.x · Cited by 37
Wsól, V., Szotáková, B., Martin, H.-J., & Maser, E. (2007) · Toxicology · doi:10.1016/j.tox.2007.05.021 · Cited by 37
Zang, T., Verma, K., Chen, M., Jin, Y., Trippier, P. C., & Penning, T. M. (2014) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2014.12.015 · Cited by 37
Self-citationPromiscuity 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
Self-citationLi, M., Wu, Z., Zhao, K., Tao, J. Q., Tam, C., Zhang, S., Wang, C. C., & Teerds, K. J. (2020) · Antioxidants · doi:10.3390/antiox10010022 · Cited by 35
Jakobsson, J., Palonek, E., Lorentzon, M., Ohlsson, C., Rane, A., & Ekström, L. (2006) · The Pharmacogenomics Journal · doi:10.1038/sj.tpj.6500419 · Cited by 35
Roberts, R. O., Bergstralh, E. J., Farmer, S. A., Jacobson, D. J., Hebbring, S. J., Cunningham, J. M., Thibodeau, S. N., Lieber, M. M., & Jacobsen, S. J. (2005) · The Prostate · doi:10.1002/pros.20362 · Cited by 34
Interactions Between Ferroptosis and Oxidative Stress in Ischemic Stroke
Liu, D., Yang, S., & Yu, S. (2024) · Antioxidants · doi:10.3390/antiox13111329 · Cited by 37
Agapova, O. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(03)00101-3 · Cited by 34
Noureini, S. K. (2004) · World Journal of Gastroenterology · doi:10.3748/wjg.v10.i12.1716 · Cited by 34
Yin, Y. D., Fu, M., Brooke, D. G., Heinrich, D. M., Denny, W. A., & Jamieson, S. M. F. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00159 · Cited by 33
Recent data on intratumor estrogens in breast cancer
Lønning, P. E., Haynes, B. P., Straume, A. H., Dunbier, A. K., Helle, H., Knappskog, S., & Dowsett, M. (2011) · Steroids · doi:10.1016/j.steroids.2011.02.040 · Cited by 32
Stanczyk, F. Z., Azen, C. G., & Pike, M. C. (2013) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2013.02.015 · Cited by 33
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
Reduced Progesterone Metabolites in Human Late Pregnancy
Hill, M., Pařı́zek, A., Kancheva, R. L., & Jirasek, J. E. (2011) · Physiological Research · doi:10.33549/physiolres.932077 · Cited by 32
Tissue Distribution, Ontogeny, and Chemical Induction of Aldo-Keto Reductases in Mice
Pratt–Hyatt, M., Lickteig, A. J., & Klaassen, C. D. (2013) · Drug Metabolism and Disposition · doi:10.1124/dmd.113.051904 · Cited by 32
Chang, K., & Petrash, J. M. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-98788-0_13 · Cited by 35
Miller, V. L., Lin, H.-K., Murugan, P., Fan, M. D., Penning, T. M., Brame, L. S., Yang, Q., & Fung, K.-M. A. (2012) · Europe PMC (PubMed Central) · Cited by 32
Self-citationIsoquinoline alkaloids as a novel type of AKR1C3 inhibitors
Zemanová, L., Hofman, J., Chlebek, J., Havrankova, J., Kosanova, K., Skarka, A., Hošťálková, A., Plucha, T., Cahlíková, L., & Wsól, V. (2014) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2014.04.005 · Cited by 32
Platt, A., Xia, Z., Liu, Y., Chen, G., & Lazarus, P. J. (2016) · Pharmacogenetics and Genomics · doi:10.1097/fpc.0000000000000226 · Cited by 31
Regulation of Human 3α-Hydroxysteroid Dehydrogenase (AKR1C4) Expression by the Liver X Receptor α
Stayrook, K. R., Rogers, P. M., Savkur, R. S., Wang, Y., Chen, S., Varga, G., Bu, X., Wei, T., Nagpal, S., Liu, X. S., et al. (2007) · Molecular Pharmacology · doi:10.1124/mol.107.039099 · Cited by 30
Nonneman, D., Wise, T., Ford, J. J., Kuehn, L. A., & Rohrer, G. A. (2006) · BMC Veterinary Research · doi:10.1186/1746-6148-2-28 · Cited by 31
Ming, D., Pham, S., Deb, S., Chin, M. Y., Kharmate, G., Adomat, H. H., Beheshti, E. H., Locke, J. A., & Guns, E. T. (2014) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2014.02.006 · Cited by 31
Lemley, C. O., & Wilson, M. E. (2010) · Journal of Dairy Science · doi:10.3168/jds.2010-3165 · Cited by 30
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
Identification of novel epithelial ovarian cancer loci in women of African ancestry
Manichaikul, A. W., Peres, L. C., Wang, X., Barnard, M. E., Chyn, D., Sheng, X., Du, Z., Tyrer, J. P., Dennis, J., Schwartz, A. G., et al. (2019) · International Journal of Cancer · doi:10.1002/ijc.32653 · Cited by 28
Wangtrakuldee, P., Adeniji, A. O., Zang, T., Duan, L., Khatri, B. B., Twenter, B. M., Estrada, M. A., Higgins, T. F., Winkler, J. D., & Penning, T. M. (2019) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2019.01.001 · Cited by 29
Self-citation(2010) · Europe PMC (PubMed Central) · Cited by 29
Self-citationCouture, J., de Jesus-Tran, K. P., Roy, A., Cantin, L., Côté, P., Legrand, P., Luu‐The, V., Labrie, F., & Breton, R. (2005) · Protein Science · doi:10.1110/ps.051353205 · Cited by 29
New cyclopentane derivatives as inhibitors of steroid metabolizing enzymes AKR1C1 and AKR1C3
Štefane, B., Brožič, P., Vehovc, M., Rižner, T. L., & Gobec, S. (2009) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2009.01.028 · Cited by 30
Dhagat, U., Endo, S., Sumii, R., Hara, A., & El-Kabbani, O. A. L. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm8003575 · Cited by 29
Brožič, P., Turk, S., Adeniji, A. O., Konc, J., Janežič, D., Penning, T. M., Rižner, T. L., & Gobec, S. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300841n · Cited by 30
Self-citationQuinn, A. M., & Penning, T. M. (2008) · Chemical Research in Toxicology · doi:10.1021/tx700345v · Cited by 32
Self-citationWang, T., Shah, Y. M., Matsubara, T., Zhen, Y., Tanabe, T., Nagano, T., Fotso, S., Krausz, K. W., Zabriskie, T. M., Idle, J. R., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.090175 · Cited by 27
Topography and function of androgen-metabolizing enzymes in the central nervous system
Tsuruo, Y. (2005) · Anatomical Science International · doi:10.1111/j.1447-073x.2005.00098.x · Cited by 29
Su, T., Yu, H., Luo, G., Wang, M., Zhou, C., Zhang, L., Hou, B., Zhang, C., Liu, M., & Xu, D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093232 · Cited by 28
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
The design of novel 17β-hydroxysteroid dehydrogenase type 3 inhibitors
Vicker, N., Sharland, C. M., Heaton, W. B., Ramos, A., Bailey, H. V., Smith, A. C., Springall, J. S., Day, J. M., Tutill, H. J., Reed, M. J., et al. (2008) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2008.08.005 · Cited by 30
Interleukin 1β Regulates Progesterone Metabolism in Human Cervical Fibroblasts
Roberson, A. E., Hyatt, K., Kenkel, C., Hanson, K. R., & Myers, D. A. (2011) · Reproductive Sciences · doi:10.1177/1933719111419246 · Cited by 29
Pallai, R., Simpkins, H., Chen, J., & Parekh, H. K. (2010) · Gene · doi:10.1016/j.gene.2010.03.006 · Cited by 29
Metadata
- Authors
- PENNING, T. M., BURCZYNSKI, M. E., JEZ, J. M., HUNG, C.-F., LIN, H.-K., MA, H., MOORE, M., PALACKAL, N., & RATNAM, K.
- Affiliations
- University of Pennsylvania (US)
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2000-09-26
- Volume
- 351
- Issue
- 1
- Pages
- 67-77
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1221336
- OpenAlex
- W2045040068
- Cited by
- 649
- References
- 38
- Citations by year
- 2026: 21 · 2025: 20 · 2024: 23 · 2023: 15 · 2022: 15 · 2021: 27 · 2020: 19 · 2019: 22 · 2018: 23 · 2017: 18 · 2016: 23 · 2015: 14 · 2014: 47 · 2013: 28 · 2012: 29
- FWCI
- 6.29
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-47015, R01DK047015)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Aldose Reductase and Taurine
- Physical Sciences › Chemistry › Organic Chemistry › Steroid Chemistry and Biochemistry
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Hormonal Regulation and Hypertension
- Keywords
- 3α-hydroxysteroid dehydrogenase, aldo-keto reductase superfamily, steroid hormone metabolism, dihydrotestosterone, testosterone, estradiol, progesterone, 20alpha-dihydroprogesterone, 3α-androstanediol, enzyme kinetic parameters, substrate specificity
- MeSH terms
- Androgens, Binding Sites, Catalysis, Cloning, Molecular, Estrogens, Female, Humans, Isoenzymes, Ketones, Kinetics, Male, Organ Specificity, Progestins, Recombinant Proteins, RNA, Messenger, Steroids, Substrate Specificity, 3-Hydroxysteroid Dehydrogenases, Reverse Transcriptase Polymerase Chain Reaction, Gene Expression Profiling, 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific)
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
