Human hydroxysteroid dehydrogenases and pre-receptor regulation: Insights into inhibitor design and evaluation

Relationship between the inhibition constant (KI) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction

Yung-Chi, C., & Prusoff, W. H. (1973) · Biochemical Pharmacology · doi:10.1016/0006-2952(73)90196-2 · Cited by 12,922 · 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

MINERALOCORTICOID ACTIVITY OF LIQUORICE: 11-BETA-HYDROXYSTEROID DEHYDROGENASE DEFICIENCY COMES OF AGE

Stewart, P., Valentino, R., Wallace, A. M., Burt, D., Shackleton, C., & Edwards, C. R. W. (1987) · The Lancet · doi:10.1016/s0140-6736(87)91014-2 · Cited by 798 · see citing works

11β-Hydroxysteroid Dehydrogenase

Stewart, P. M., & Krozowski, Z. S. (1997) · Vitamins and hormones · doi:10.1016/s0083-6729(08)60646-9 · Cited by 716 · see citing works

Minireview: 11β-Hydroxysteroid Dehydrogenase Type 1— A Tissue-Specific Amplifier of Glucocorticoid Action1

Seckl, J. R., & Walker, B. R. (2001) · Endocrinology · doi:10.1210/endo.142.4.8114 · Cited by 714 · see citing works

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

PENNING, T. M., BURCZYNSKI, M. E., JEZ, J. M., HUNG, C.-F., LIN, H.-K., MA, H., MOORE, M., PALACKAL, N., & RATNAM, K. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3510067 · Cited by 649 · see citing works

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

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

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 · see citing works

Critical Residues for Structure and Catalysis in Short-chain Dehydrogenases/Reductases

Filling, C., Berndt, K. D., Benach, J., Knapp, S., Prozorovski, T., Nordling, E., Ladenstein, R., Jörnvall, H., & Oppermann, U. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202160200 · Cited by 583 · see citing works

The 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 · see citing works

RU486 (MIFEPRISTONE): Mechanisms of Action and Clinical Uses

Cadepond, F., Ulmann, A., & Baulieu, E. E. (1997) · Annual Review of Medicine · doi:10.1146/annurev.med.48.1.129 · Cited by 424 · see citing works

Intracrinology: Role of the family of 17 beta-hydroxysteroid dehydrogenases in human physiology and disease

Labrie, 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

Human Cytosolic 3α-Hydroxysteroid Dehydrogenases of the Aldo-keto Reductase Superfamily Display Significant 3β-Hydroxysteroid Dehydrogenase Activity

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

THE ENZYMATIC TRANSFER OF HYDROGEN

Fisher, H. F., Conn, E. E., Vennesland, B., & Westheimer, F. H. (1953) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66181-2 · Cited by 240 · see citing works

Structure of human estrogenic 17β-hydroxysteroid dehydrogenase at 2.20 å resolution

Ghosh, D., Pletnev, V. Z., Zhu, D.-W., Wawrzak, Z., Duax, W. L., Pangborn, W., Labrie, F., & Lin, S.-X. (1995) · Structure · doi:10.1016/s0969-2126(01)00183-6 · Cited by 239 · see citing works

Three-dimensional structure of holo 3 alpha,20 beta-hydroxysteroid dehydrogenase: a member of a short-chain dehydrogenase family.

Ghosh, D., Weeks, C. M., Grochulski, P., Duax, W. L., Erman, M., Rimsay, R. L., & Orr, J. C. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.22.10064 · Cited by 231 · see citing works

Expression cloning and characterization of oxidative 17β- and 3α-hydroxysteroid dehydrogenases from rat and human prostate

Biswas, M. G., & Russell, D. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.25.15959 · Cited by 224 · see citing works

17β-Hydroxysteroid dehydrogenases (17β-HSDs) as therapeutic targets: Protein structures, functions, and recent progress in inhibitor development

Marchais-Oberwinkler, S., Henn, C., Möller, G., Klein, T., Negri, M., Oster, A., Spadaro, A., Werth, R., Wetzel, M., Xu, K., et al. (2011) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.12.013 · Cited by 216 · see citing works

Molecular cloning of a novel widely expressed human 80 kDa 17 <i>β</i> -hydroxysteroid dehydrogenase IV

Adamski, J., Normand, T., Leenders, F., Monté, D., Begue, A., Stéhelin, D., Jungblut, P. W., & de Launoit, Y. (1995) · Biochemical Journal · doi:10.1042/bj3110437 · Cited by 214 · see citing works

17 beta-Hydroxysteroid dehydrogenase type 2: chromosomal assignment and progestin regulation of gene expression in human endometrium.

Casey, M. L., MacDonald, P. C., & Andersson, S. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117569 · Cited by 212 · see citing works

The refined three-dimensional structure of 3α, 20β-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases

Ghosh, D., Wawrzak, Z., Weeks, C. M., Duax, W. L., & Erman, M. (1994) · Structure · doi:10.1016/s0969-2126(00)00064-2 · Cited by 202 · see citing works

Purification and properties of a 3α-hydroxysteroid dehydrogenase of rat liver cytosol and its inhibition by anti-inflammatory drugs

Penning, T. M., Mukharji, I., Barrows, S., & Talalay, P. (1984) · Biochemical Journal · doi:10.1042/bj2220601 · Cited by 187 · see citing works

Evidence 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

Tyrosine-48 Is the Proton Donor and Histidine-110 Directs Substrate Stereochemical Selectivity in the Reduction Reaction of Human Aldose Reductase: Enzyme Kinetics and Crystal Structure of the Y48H Mutant Enzyme

Bohren, K. M., Grimshaw, C. E., Lai, C.-J., Harrison, D. H. T., Ringe, D., Petsko, G. A., & Gabbay, K. H. (1994) · Biochemistry · doi:10.1021/bi00174a007 · Cited by 171 · see citing works

An indomethacin analogue, N-(4-chlorobenzoyl)-melatonin, is a selective inhibitor of aldo-keto reductase 1C3 (type 2 3α-HSD, type 5 17β-HSD, and prostaglandin F synthase), a potential target for the treatment of hormone dependent and hormone independent malignancies

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

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

Byrns, M. C., Jin, Y., & Penning, T. M. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.11.004 · Cited by 144 · see citing works

Mutagenesis of 3α-Hydroxysteroid Dehydrogenase Reveals a “Push−Pull” Mechanism for Proton Transfer in Aldo−Keto Reductases

Schlegel, B. P., Jez, J. M., & Penning, T. M. (1998) · Biochemistry · doi:10.1021/bi9723055 · 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

Human type 3 3α-hydroxysteroid dehydrogenase (aldo-keto reductase 1C2) and androgen metabolism in prostate cells

Rižner, 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

Structure of the Human Type II 3β-Hydroxysteroid Dehydrogenase/Δ 5 -Δ 4 Isomerase (3β-HSD) Gene: Adrenal and Gonadal Specificity

Lachance, Y., LUU-THE, V., Verreault, H., Dumont, M., Rhéaume, É., Leblanc, G., & Labrie, F. (1991) · DNA and Cell Biology · doi:10.1089/dna.1991.10.701 · Cited by 130 · see citing works

Increased expression of type 2 3α-hydroxysteroid dehydrogenase/type 5 17β-hydroxysteroid dehydrogenase (AKR1C3) and its relationship with androgen receptor in prostate carcinoma

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

Development of Nonsteroidal Anti-Inflammatory Drug Analogs and Steroid Carboxylates Selective for Human Aldo-Keto Reductase Isoforms: Potential Antineoplastic Agents That Work Independently of Cyclooxygenase Isozymes

Bauman, D. R., Rudnick, S. I., Szewczuk, L. M., Jin, Y., Gopishetty, S. R., & Penning, T. M. (2004) · Molecular Pharmacology · doi:10.1124/mol.104.006569 · Cited by 124 · see citing works

Design and validation of specific inhibitors of 17 -hydroxysteroid dehydrogenases for therapeutic application in breast and prostate cancer, and in endometriosis

Day, J. M., Tutill, H. J., Purohit, A., & Reed, M. J. (2008) · Endocrine Related Cancer · doi:10.1677/erc-08-0042 · Cited by 123 · see citing works

Identification of the Major Oxidative 3α-Hydroxysteroid Dehydrogenase in Human Prostate That Converts 5α-Androstane-3α,17β-diol to 5α-Dihydrotestosterone: A Potential Therapeutic Target for Androgen-Dependent Disease

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

Minireview: Cellular Redox State Regulates Hydroxysteroid Dehydrogenase Activity and Intracellular Hormone Potency

Agarwal, A. K., & Auchus, R. J. (2005) · Endocrinology · doi:10.1210/en.2005-0061 · Cited by 112 · see citing works

11β-Hydroxysteroid dehydrogenase type 1 in obesity and the metabolic syndrome

Wake, D. J., & Walker, B. R. (2004) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2003.11.015 · Cited by 111 · see citing works

Design, Synthesis, Biological Evaluation and Pharmacokinetics of Bis(hydroxyphenyl) substituted Azoles, Thiophenes, Benzenes, and Aza-Benzenes as Potent and Selective Nonsteroidal Inhibitors of 17β-Hydroxysteroid Dehydrogenase Type 1 (17β-HSD1)

Bey, E., Marchais‐Oberwinkler, S., Werth, R., Negri, M., Al‐Soud, Y. A., Kruchten, P., Oster, A., Frotscher, M., Birk, B., & Hartmann, R. W. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm8006917 · Cited by 109 · see citing works

17β‐hydroxysteroid dehydrogenase Type 1, and not Type 12, is a target for endocrine therapy of hormone‐dependent breast cancer

Day, J. M., Foster, P., Tutill, H. J., Parsons, M. F. C., Newman, S. P., Chander, S. K., Allan, G. M., Lawrence, H. R., Vicker, N., Potter, B. V. L., et al. (2008) · International Journal of Cancer · doi:10.1002/ijc.23350 · Cited by 107 · see citing works

Structure-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

Structure of 3α-Hydroxysteroid/Dihydrodiol Dehydrogenase Complexed with NADP⁺

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

THE ENZYMATIC TRANSFER OF HYDROGEN

Loewus, F. A., Ofner, P., Fisher, H. F., Westheimer, F. H., & Vennesland, B. (1953) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66182-4 · Cited by 91 · see citing works

Design, Synthesis, and Biological Evaluation of (Hydroxyphenyl)naphthalene and -quinoline Derivatives: Potent and Selective Nonsteroidal Inhibitors of 17β-Hydroxysteroid Dehydrogenase Type 1 (17β-HSD1) for the Treatment of Estrogen-Dependent Diseases

Frotscher, M., Ziegler, E., Marchais‐Oberwinkler, S., Kruchten, P., Neugebauer, A., Fetzer, L., Scherer, C., Müller‐Vieira, U., Messinger, J., Thole, H., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm701447v · Cited by 89 · see citing works

Inhibition of a major NAD(P)-linked oxidoreductase from rat liver cytosol by steroidal and nonsteroidal anti-inflammatory agents and by prostaglandins.

Penning, T. M., & Talalay, P. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.14.4504 · Cited by 84 · see citing works

Binary and ternary crystal structure analyses of a novel inhibitor with 17β-HSD type 1: a lead compound for breast cancer therapy

Mazumdar, M., Fournier, D., Zhu, D., Cadot, C., Poirier, D., & Lin, S. (2009) · Biochemical Journal · doi:10.1042/bj20091020 · Cited by 84 · see citing works

17β-Hydroxysteroid dehydrogenase inhibitors: a patent review

Poirier, D. (2010) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2010.505604 · Cited by 83 · see citing works

Targeting the pre-receptor metabolism of cortisol as a novel therapy in obesity and diabetes

Gathercole, L., & Stewart, P. M. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.03.060 · Cited by 82 · see citing works

Lack of functional and expression homology between human and mouse aldo-keto reductase 1C enzymes: implications for modelling human cancers

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

New Insights into the SAR and Binding Modes of Bis(hydroxyphenyl)thiophenes and -benzenes: Influence of Additional Substituents on 17β-Hydroxysteroid Dehydrogenase Type 1 (17β-HSD1) Inhibitory Activity and Selectivity

Bey, E., Marchais‐Oberwinkler, S., Negri, M., Kruchten, P., Oster, A., Klein, T., Spadaro, A., Werth, R., Frotscher, M., Birk, B., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm901195w · Cited by 77 · see citing works

The kinetic mechanism catalysed by homogeneous rat liver 3 α -hydroxysteroid dehydrogenase. Evidence for binary and ternary dead-end complexes containing non-steroidal anti-inflammatory drugs

Askonas, L. J., Ricigliano, J. W., & Penning, T. M. (1991) · Biochemical Journal · doi:10.1042/bj2780835 · Cited by 73 · see citing works

11B-Hydroxysteroid Dehydrogenase Type 1 Inhibitors as Promising Therapeutic Drugs for Diabetes: Status and Development

Ge, R., Huang, Y., Liang, G., & Li, X. (2010) · Current Medicinal Chemistry · doi:10.2174/092986710790226147 · Cited by 73 · see citing works

The roles of aldo-keto reductases in steroid hormone action

Bauman, D. R., Steckelbroeck, S., & Penning, T. M. (2004) · Drug News & Perspectives · doi:10.1358/dnp.2004.17.9.872570 · Cited by 71 · see citing works

The arginine 276 anchor for NADP(H) dictates fluorescence kinetic transients in 3α-hydroxysteroid dehydrogenase, a representative aldo-keto reductase

Ratnam, K., Ma, H., & Penning, T. M. (1999) · Biochemistry · doi:10.1021/bi982838t · Cited by 68 · see citing works

Substituted 6-Phenyl-2-naphthols. Potent and Selective Nonsteroidal Inhibitors of 17β-Hydroxysteroid Dehydrogenase Type 1 (17β-HSD1): Design, Synthesis, Biological Evaluation, and Pharmacokinetics

Marchais‐Oberwinkler, S., Kruchten, P., Frotscher, M., Ziegler, E., Neugebauer, A., Bhoga, U., Bey, E., Müller‐Vieira, U., Messinger, J., Thole, H., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800367k · Cited by 64 · see citing works

Human Hydroxysteroid (17-β) Dehydrogenase 1 Expression Enhances Estrogen Sensitivity of MCF-7 Breast Cancer Cell Xenografts

Husen, B., Huhtinen, K., Saloniemi, T., Messinger, J., Thole, H., & POUTANEN, M. H. (2006) · Endocrinology · doi:10.1210/en.2006-0778 · Cited by 63 · see citing works

Characterization of the structure-activity relationships of rat types I and II 3 beta-hydroxysteroid dehydrogenase/delta 5 -delta 4 isomerase by site-directed mutagenesis and expression in HeLa cells

Simard, J., de Launoit, Y., & Labrie, F. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98548-0 · Cited by 62 · see citing works

Discovery of Nonsteroidal 17β-Hydroxysteroid Dehydrogenase 1 Inhibitors by Pharmacophore-Based Screening of Virtual Compound Libraries

Schuster, D., Nashev, L. G., Kirchmair, J., Laggner, C., Wolber, G., Langer, T., & Odermatt, A. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800054h · Cited by 61 · see citing works

Characterization of activity and binding mode of glycyrrhetinic acid derivatives inhibiting 11β-hydroxysteroid dehydrogenase type 2

Kratschmar, D. V., Vuorinen, A., Cunha, T. D., Wolber, G., Classen-Houben, D., Doblhoff, O., Schuster, D., & Odermatt, A. (2011) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.12.019 · Cited by 61 · see citing works

Multiple steps determine the overall rate of the reduction of 5α-dihydrotestosterone catalyzed by human type 3 3α-hydroxysteroid dehydrogenase: implications for the elimination of androgens

Jin, Y., & Penning, T. M. (2006) · Biochemistry · doi:10.1021/bi060591r · Cited by 60 · see citing works

Novel and Potent 17β-Hydroxysteroid Dehydrogenase Type 1 Inhibitors

Lawrence, H. R., Vicker, N., Allan, G. M., Smith, A., Mahon, M. F., Tutill, H. J., Purohit, A., Reed, M. J., & Potter, B. V. L. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm049045r · Cited by 60 · see citing works

Elucidation of a Complete Kinetic Mechanism for a Mammalian Hydroxysteroid Dehydrogenase (HSD) and Identification of All Enzyme Forms on the Reaction Coordinate

Cooper, W. C., Jin, Y., & Penning, T. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703414200 · Cited by 58 · see citing works

Mechanism of inhibition of 3α,20β-hydroxysteroid dehydrogenaseby a licorice-derived steroidal inhibitor

Ghosh, D., Erman, M., Wawrzak, Z., Duax, W. L., & Pangborn, W. A. (1994) · Structure · doi:10.1016/s0969-2126(94)00099-9 · Cited by 56 · see citing works

Selective Inhibition of the Tumor Marker AKR1B10 by Antiinflammatory N-Phenylanthranilic Acids and Glycyrrhetic Acid

Endo, S., Matsunaga, T., Soda, M., Tajima, K., Zhao, H.-T., El-Kabbani, O. A. L., & Hara, A. (2010) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.33.886 · Cited by 54 · see citing works

Estradiol−Adenosine Hybrid Compounds Designed to Inhibit Type 1 17β-Hydroxysteroid Dehydrogenase

Poirier, D., Boivin, R. P., Tremblay, M. R., Bérubé, M., Qiu, W., & Lin, S. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm058235e · Cited by 54 · see citing works

Selective estrogen receptor modulators (SERMs): A first step in the development of perfect hormone replacement therapy regimen

McDonnell, D. P. (2000) · Journal of the Society for Gynecologic Investigation · doi:10.1016/s1071-5576(99)00055-6 · Cited by 53 · see citing works

Human Aldose Reductase: pK of Tyrosine 48 Reveals the Preferred Ionization State for Catalysis and Inhibition

Grimshaw, C. E., Bohren, K. M., Lai, C.-J., & Gabbay, K. H. (1995) · Biochemistry · doi:10.1021/bi00044a014 · Cited by 52 · see citing works

Selective inhibition of 11β-hydroxysteroid dehydrogenase 1 by 18α-glycyrrhetinic acid but not 18β-glycyrrhetinic acid

Classen-Houben, D., Schuster, D., Cunha, T. D., Odermatt, A., Wolber, G., Jordis, U., & Kueenburg, B. (2009) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2009.01.009 · Cited by 51 · see citing works

17β-Hydroxysteroid dehydrogenase: isozymes and mutations

Andersson, S. (1995) · Journal of Endocrinology · doi:10.1677/joe.0.1460197 · Cited by 51 · see citing works

Discovery of substituted 3-(phenylamino)benzoic acids as potent and selective inhibitors of type 5 17β-hydroxysteroid dehydrogenase (AKR1C3)

Adeniji, 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 50 · see citing works

2-Amino-1,3-thiazol-4(5H)-ones as Potent and Selective 11β-Hydroxysteroid Dehydrogenase Type 1 Inhibitors: Enzyme−Ligand Co-Crystal Structure and Demonstration of Pharmacodynamic Effects in C57Bl/6 Mice

Johansson, L., Fotsch, C. H., Bartberger, M. D., Castro, V. M., Chen, M., Emery, M. G., Gustafsson, S., Hale, C., Hickman, D., Homan, E. J., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm701551j · Cited by 49 · see citing works

N-(Pyridin-2-yl) arylsulfonamide inhibitors of 11β-hydroxysteroid dehydrogenase type 1: Discovery of PF-915275

Siu, M., Johnson, T., Wang, Y., Nair, S. K., Taylor, W. D., Cripps, S. J., Matthews, J. J., Edwards, M. P., Pauly, T. A., Ermolieff, J., et al. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.05.011 · Cited by 46 · see citing works

Contribution to the development of inhibitors of 17β-hydroxysteroid dehydrogenase types 1 and 7: Key tools for studying and treating estrogen-dependent diseases

Poirier, D. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.12.007 · Cited by 44 · see citing works

Structure-Guided Design, Synthesis, and Evaluation of Salicylic Acid-Based Inhibitors Targeting a Selectivity Pocket in the Active Site of Human 20α-Hydroxysteroid Dehydrogenase (AKR1C1)

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 41 · see citing works

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 41 · see citing works

11β-Hydroxysteroid dehydrogenase activity and corticosteroid hormone action

Stewart, P. M., & Whorwood, C. B. (1994) · Steroids · doi:10.1016/0039-128x(94)90082-5 · Cited by 41 · see citing works

Novel inhibitors of 17β-hydroxysteroid dehydrogenase type 1: Templates for design

Allan, G. M., Vicker, N., Lawrence, H. R., Tutill, H. J., Day, J. M., Huchet, M., Ferrandis, E., Reed, M. J., Purohit, A., & Potter, B. V. L. (2008) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2008.02.059 · Cited by 40 · see citing works

Identification of a novel series of tetrahydrodibenzazocines as inhibitors of 17β-hydroxysteroid dehydrogenase type 3

Fink, B. E., Gavai, A. V., Tokarski, J. S., Goyal, B., Misra, R. N., Xiao, H., Kimball, S. D., Han, W.-C., Norris, D. J., Spires, T. E., et al. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.12.039 · Cited by 40 · see citing works

Identification of chemically diverse, novel inhibitors of 17β-hydroxysteroid dehydrogenase type 3 and 5 by pharmacophore-based virtual screening

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 · see citing works

Focused Libraries of 16‐Substituted Estrone Derivatives and Modified E‐Ring Steroids: Inhibitors of 17ß‐Hydroxysteroid Dehydrogenase Type 1

Vicker, N., Lawrence, H. R., Allan, G. M., Bubert, C., Smith, A., Tutill, H. J., Purohit, A., Day, J. M., Mahon, M. F., Reed, M. J., et al. (2006) · ChemMedChem · doi:10.1002/cmdc.200500087 · Cited by 38 · see citing works

Structure-based virtual screening for identification of novel 11β-HSD1 inhibitors

Yang, H., Shen, Y., Chen, J., Jiang, Q., Leng, Y., & Shen, J. (2008) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2008.06.005 · Cited by 37 · see citing works

Design and synthesis of bisubstrate inhibitors of type 1 17β-hydroxysteroid dehydrogenase: Overview and perspectives

Fournier, D., Poirier, D., Mazumdar, M., & Lin, S. (2008) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2008.01.044 · Cited by 34 · see citing works

A Salicylic Acid-Based Analogue Discovered from Virtual Screening as a Potent Inhibitor of Human 20α-Hydroxysteroid Dehydrogenase

Dhagat, U., Carbone, V., Chung, R. P. ‐., Matsunaga, T., Endo, S., Hara, A., & El-Kabbani, O. A. L. (2007) · Medicinal Chemistry · doi:10.2174/157340607782360399 · Cited by 34 · see citing works

Site specificity and mechanism of human placental 17β-hydroxysteroid dehydrogenase

Warren, J. C., & Crist, R. D. (1967) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(67)90392-x · Cited by 33 · see citing works

Novel estrone mimetics with high 17β-HSD1 inhibitory activity

Oster, A., Klein, T., Werth, R., Kruchten, P., Bey, E., Negri, M., Marchais‐Oberwinkler, S., Frotscher, M., & Hartmann, R. W. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.03.065 · Cited by 32 · see citing works

Discovery and optimization of piperidyl benzamide derivatives as a novel class of 11β-HSD1 inhibitors

Rew, Y., McMinn, D. L., Wang, Z., He, X., Hungate, R. W., Jaén, J. C., Sudom, A. M., Sun, D., Tu, H., Ursu, S., et al. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.01.058 · Cited by 30 · see citing works

17β-Hydroxysteroid Dehydrogenase from Cochliobolus lunatus: Model Structure and Substrate Specificity

Rižner, T. L., Adamski, J., & Stojan, J. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.2064 · Cited by 30 · see citing works

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 · see citing works

Selectivity Determinants of Inhibitor Binding to Human 20α-Hydroxysteroid Dehydrogenase: Crystal Structure of the Enzyme in Ternary Complex with Coenzyme and the Potent Inhibitor 3,5-Dichlorosalicylic Acid

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 · see citing works

4-Methyl-5-phenyl triazoles as selective inhibitors of 11β-hydroxysteroid dehydrogenase type I

Zhu, Y., Olson, S. H., Hermanowski‐Vosatka, A., Mundt, S. S., Shah, K., Springer, M. S., Thieringer, R., Wright, S. D., Xiao, J., Zokian, H. J., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.04.013 · Cited by 29 · see citing works

Insights in 17β-HSD1 Enzyme Kinetics and Ligand Binding by Dynamic Motion Investigation

Negri, M., Recanatini, M., & Hartmann, R. W. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012026 · Cited by 28 · see citing works

The role of the heterocycle in bis(hydroxyphenyl)triazoles for inhibition of 17β-Hydroxysteroid Dehydrogenase (17β-HSD) type 1 and type 2

Al‐Soud, Y. A., Bey, E., Oster, A., Marchais‐Oberwinkler, S., Werth, R., Kruchten, P., Frotscher, M., & Hartmann, R. W. (2008) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2008.09.012 · Cited by 27 · see citing works

Crystal Structure at 1.8 Å Resolution of CDP- d -Glucose 4,6-Dehydratase from Yersinia pseudotuberculosis,

Vogan, E. M., Bellamacina, C. R., He, X., Liu, H., Ringe, D., & Petsko, G. A. (2004) · Biochemistry · doi:10.1021/bi035547f · Cited by 26 · see citing works

Substrate activation in pyridine nucleotide-linked reactions: illustrations from the steroid field

Akhtar, M., Wilton, D. C., Watkinson, I. A., & Rahimtula, A. D. (1972) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.1972.0012 · Cited by 25 · see citing works

Synthesis and optimization of arylsulfonylpiperazines as a novel class of inhibitors of 11β-hydroxysteroid dehydrogenase type 1 (11β-HSD1)

Sun, D., Wang, Z., Cardozo, M. G., Choi, R. J., DeGraffenreid, M. R., Di, Y., He, X., Jaén, J. C., Labelle, M., Liu, J., et al. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.12.114 · Cited by 25 · see citing works

Termination of Early Pregnancy by the 3β-Hydroxysteroid Dehydrogenase Inhibitor Epostane

CROOIJ, M. J., Cc, D. N., Rao, B. R., Berends, G. T., Gooren, L. J., & Janssens, J. (1988) · New England Journal of Medicine · doi:10.1056/nejm198809293191301 · Cited by 25 · see citing works

Optimization of novel di-substituted cyclohexylbenzamide derivatives as potent 11β-HSD1 inhibitors

McMinn, D. L., Rew, Y., Sudom, A. M., Caille, S., DeGraffenreid, M. R., He, X., Hungate, R. W., Jiang, B., Jaén, J. C., Julian, L. D., et al. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.01.026 · Cited by 24 · see citing works

The evolving role of specific estrogen receptor modulators (SERMs)

Ibrahim, N. K., & Hortobágyi, G. N. (1999) · Surgical Oncology · doi:10.1016/s0960-7404(99)00047-x · Cited by 23 · see citing works

Modulation of 11β-hydroxysteroid dehydrogenase type 1 activity by 1,5-substituted 1H-tetrazoles

Webster, S. P., Binnie, M., McConnell, K. M. M., Sooy, K., Ward, P., Greaney, M. F., Vinter, A., Pallin, T. D., Dyke, H. J., Gill, M., et al. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.04.055 · Cited by 23 · see citing works

Arginine 276 controls the directional preference of AKR1C9 (rat liver 3α-hydroxysteroid dehydrogenase) in human embryonic kidney 293 cells

Papari-Zareei, M., Brandmaier, A., & Auchus, R. J. (2006) · Endocrinology · doi:10.1210/en.2005-1141 · Cited by 23 · see citing works

Selective inhibition of human 3β-hydroxysteroid dehydrogenase type 1 as a potential treatment for breast cancer

Thomas, J. L., Bucholtz, K. M., & Kacsoh, B. (2011) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.08.003 · Cited by 22 · see citing works

Mechanism-based inactivation of 17.beta.,20.alpha.-hydroxysteroid dehydrogenase by an acetylenic secoestradiol

Auchus, R. J., & Covey, D. F. (1986) · Biochemistry · doi:10.1021/bi00371a008 · Cited by 22 · see citing works

Selective Estrogen Receptor Modulators (SERMs): A First Step in the Development of Perfect Hormone Replacement Therapy Regimen

McDonnell, D. P. (2000) · Journal of the Society for Gynecologic Investigation · doi:10.1177/1071557600007001s05 · Cited by 22 · see citing works

Discovery and structure–activity relationships of pentanedioic acid diamides as potent inhibitors of 11β-hydroxysteroid dehydrogenase type I

Roche, D., Carniato, D., Leriche, C., Lepifre, F., Christmann‐Franck, S., Grädler, U., Charon, C., Hallakou‐Bozec, S., Doaré, L., Schmidlin, F., et al. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.03.140 · Cited by 20 · see citing works

["Intracrinology". Autonomy and freedom of peripheral tissues].

Labrie, F., Bèlanger, A., Simard, J., Luu-The, V., & Labrie, C. (1995) · PubMed · Cited by 16 · see citing works

Discovery of Adamantyl Ethanone Derivatives as Potent 11β‐Hydroxysteroid Dehydrogenase Type 1 (11β‐HSD1) Inhibitors

Su, X., Pradaux, F., THOMAS, M. P., Szeto, M. W. Y., Halem, H. A., Culler, M. D., Vicker, N., & Potter, B. V. L. (2010) · ChemMedChem · doi:10.1002/cmdc.201000081 · Cited by 15 · see citing works

Stereochemistry of hydrogen transfer by rat ovary 20α-hydroxy steroid dehydrogenase

Kersey, W. H., & Wilcox, R. B. (1970) · Biochemistry · doi:10.1021/bi00807a033 · Cited by 15 · see citing works

Transient‐phase kinetic studies on the nucleotide binding to 3α‐hydroxysteroid dehydrogenase from Pseudomonas sp. B‐0831 using fluorescence stopped‐flow procedures

Ueda, S., Oda, M., Imamura, S., & Ohnishi, M. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04089.x · Cited by 14 · see citing works

Secosteroid Mechanism-Based Inactivators and Site-Directed Mutagenesis as Probes for Steroid Hormone Recognition by 3.alpha.-Hydroxysteroid Dehydrogenase

Schlegel, B. P., Pawlowski, J. E., Hu, Y., Scolnick, D. M., Covey, D. F., & Penning, T. M. (1994) · Biochemistry · doi:10.1021/bi00200a017 · Cited by 11 · see citing works

Discovery of new inhibitors of aldo-keto reductase 1C1 by structure-based virtual screening

Brožič, P., Turk, S., Rižner, T. L., & Gobec, S. (2008) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2008.08.002 · Cited by 11 · see citing works

Assay optimization and kinetic profile of the human and the rabbit isoforms of 11β-HSD1

Castro, A., Zhu, J. X., Alton, G., Rejto, P. A., & Ermolieff, J. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.04.005 · Cited by 10 · see citing works

Azabicyclic sulfonamides as potent 11β-HSD1 inhibitors

Shah, U., Boyle, C. D., Chackalamannil, S., Baker, H. E., Kowalski, T. J., Lee, J., Terracina, G., & Zhang, L. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.01.082 · Cited by 9 · see citing works

Termination of Early Pregnancy by the 3β-Hydroxysteroid Dehydrogenase Inhibitor Epostane

CROOIJ, M. J., Cc, D. N., Rao, B. R., Berends, G. T., Gooren, L. J., & Janssens, J. (1989) · Obstetrical & Gynecological Survey · doi:10.1097/00006254-198908000-00011 · Cited by 8 · see citing works

Derivatives of (phenylsulfonamido-methyl)nicotine and (phenylsulfonamido-methyl)thiazole as novel 11β-hydroxysteroid dehydrogenase type 1 inhibitors: synthesis and biological activities in vitro

Zhang, X., Zhou, Y., Shen, Y., Du, L., Chen, J., Leng, Y., & Shen, J. (2009) · Acta Pharmacologica Sinica · doi:10.1038/aps.2009.118 · Cited by 5 · see citing works

Clues to the development of mechanism-based inactivators of 3α-hydroxysteroid dehydrogenase: comparison of steroidal and nonsteroidal Michael acceptors and epoxides

Penning, T. M., Thornton, R. A., & Ricigliano, J. W. (1991) · Steroids · doi:10.1016/0039-128x(91)90030-y · Cited by 2 · see citing works

Biogenesis and functions of lipid droplets in plants

Chapman, K. D., Dyer, J. M., & Mullen, R. T. (2011) · Journal of Lipid Research · doi:10.1194/jlr.r021436 · Cited by 394 · see citing works

Revisiting the roles of progesterone and allopregnanolone in the nervous system: Resurgence of the progesterone receptors

Schumacher, M., Mattern, C., Ghoumari, A. M., Oudinet, J., Lière, P., Labombarda, F., Sitruk-Ware, R. L., Nicola, A. F. D., & Guennoun, R. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.09.004 · Cited by 353 · see citing works

Progesterone Synthesis in the Nervous System: Implications for Myelination and Myelin Repair

Schumacher, M., Hussain, R., Gago, N., Oudinet, J., Mattern, C., & Ghoumari, A. M. (2012) · Frontiers in Neuroscience · doi:10.3389/fnins.2012.00010 · Cited by 221 · 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

Enzymology of retinoic acid biosynthesis and degradation

Kedishvili, N. Y. (2013) · Journal of Lipid Research · doi:10.1194/jlr.r037028 · Cited by 196 · see citing works

The 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

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

Byrns, M. C., Jin, Y., & Penning, T. M. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.11.004 · Cited by 144 · see citing works

Completion of the gut microbial epi-bile acid pathway

Doden, H. L., Wolf, P. G., Gaskins, H. R., Anantharaman, K., Alves, J. M. P., & Ridlon, J. M. (2021) · Gut Microbes · doi:10.1080/19490976.2021.1907271 · Cited by 114 · see citing works

Retinoic Acid Synthesis and Degradation

Kedishvili, N. Y. (2016) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-024-0945-1_5 · Cited by 111 · see citing works

Allopregnanolone: An overview on its synthesis and effects

Diviccaro, S., Cioffi, L., Falvo, E., Giatti, S., & Melcangi, R. C. (2021) · Journal of Neuroendocrinology · doi:10.1111/jne.12996 · Cited by 110 · see citing works

Pharmacophore-based discovery of FXR agonists. Part I: Model development and experimental validation

Schuster, D., Markt, P., Grienke, U., Mihaly‐Bison, J., Binder, M., Noha, S. M., Rollinger, J. M., Stuppner, H., Bochkov, V. N., & Wolber, G. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.09.056 · Cited by 50 · see citing works

Selective Inhibition of Human Type-5 17β-Hydroxysteroid Dehydrogenase (AKR1C3) by Baccharin, a Component of Brazilian Propolis

Endo, 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 · 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

Virtual screening applications in short-chain dehydrogenase/reductase research

Beck, K. R., Kaserer, T., Schuster, D., & Odermatt, A. (2017) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2017.03.008 · Cited by 38 · 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

Synthesis and structure–activity relationships of 2- and/or 4-halogenated 13β- and 13α-estrone derivatives as enzyme inhibitors of estrogen biosynthesis

Bacsa, I., Herman, B. E., Jójárt, R., Herman, K. S., Woelfling, J., Schneider, G., Varga, M., Tömböly, C., Rižner, T. L., Szécsi, M., et al. (2018) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2018.1490731 · Cited by 33 · see citing works

Physiopathological role of the enzymatic complex 5α-reductase and 3α/β-hydroxysteroid oxidoreductase in the generation of progesterone and testosterone neuroactive metabolites

Giatti, S., Diviccaro, S., Falvo, E., García‐Segura, L. M., & Melcangi, R. C. (2020) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2020.100836 · Cited by 32 · see citing works

Fluoxetine elevates allopregnanolone in female rat brain but inhibits a steroid microsomal dehydrogenase rather than activating an aldo‐keto reductase

Fry, J. P., Li, K. Y., Devall, A., Cockcroft, S., Honour, J. W., & Lovick, T. A. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12891 · Cited by 31 · see citing works

Selective Inhibitors of Aldo-Keto Reductases AKR1C1 and AKR1C3 Discovered by Virtual Screening of a Fragment Library

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 · see citing works

Progesterone: Synthesis, Metabolism, Mechanism of Action, and Effects in the Nervous System

Schumacher, M., Zhu, X., & Guennoun, R. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803592-4.00054-7 · Cited by 28 · see citing works

Overview of human 20 alpha-hydroxysteroid dehydrogenase (AKR1C1): Functions, regulation, and structural insights of inhibitors

Chu, X., He, S., Liu, Y., Liu, Y., Feng, F., Guo, Q., Zhao, L., & Sun, H. (2021) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2021.109746 · Cited by 26 · see citing works

11β-hydroxysteroid dehydrogenase inhibition as a new potential therapeutic target for alcohol abuse

Sanna, P. P., Kawamura, T., Chen, J., Koob, G. F., Roberts, A. J., Vendruscolo, L. F., & Repunte‐Canonigo, V. (2016) · Translational Psychiatry · doi:10.1038/tp.2016.13 · Cited by 25 · see citing works

The effect of experimental low zearalenone intoxication on ovarian follicles in pre-pubertal bitches

Gajęcka, M. (2013) · Polish Journal of Veterinary Sciences · doi:10.2478/pjvs-2013-0007 · Cited by 23 · see citing works

DHEA – a precursor of ERβ ligands

Warner, M., & Gustafsson, J.-A. (2015) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2014.08.003 · Cited by 22 · see citing works

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

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

The Role of Androgens and Estrogens in Social Interactions and Social Cognition

Aspesi, D., Bass, N., Kavaliers, M., & Choleris, E. (2023) · Neuroscience · doi:10.1016/j.neuroscience.2023.03.028 · Cited by 18 · see citing works

Steroid Hormones and Other Lipid Molecules Involved in Human Reproduction

Strauss, J. F., & FitzGerald, G. A. (2019) · Elsevier eBooks · doi:10.1016/b978-0-323-47912-7.00004-4 · Cited by 18 · see citing works

Ovarian Endocrinology

Takae, S., & Suzuki, N. (2017) · Springer eBooks · doi:10.1007/978-3-319-53454-1_1 · Cited by 17 · see citing works

Ile258Met mutation of Brucella melitensis 7α-hydroxysteroid dehydrogenase significantly enhances catalytic efficiency, cofactor affinity, and thermostability

Liu, Z., Zhang, R., Zhang, W., & Xu, Y. (2021) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-021-11299-7 · Cited by 16 · see citing works

Identification of a binding protein for sesamin and characterization of its roles in plant growth

Tera, M., Koyama, T., Murata, J., Furukawa, A., Mori, S., Azuma, T., Watanabe, T., Hori, K., Okazawa, A., Kabe, Y., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-45003-7 · Cited by 16 · see citing works

Structure-based rational design of hydroxysteroid dehydrogenases for improving and diversifying steroid synthesis

Liu, Z., Zhang, R., Zhang, W., & Xu, Y. (2022) · Critical Reviews in Biotechnology · doi:10.1080/07388551.2022.2054770 · Cited by 13 · see citing works

Allopregnanolone Promotes Migration and Invasion of Human Glioblastoma Cells through the Protein Tyrosine Kinase c-Src Activation

Zamora-Sánchez, C. J., Bello‐Alvarez, C., Rodríguez‐Dorantes, M., & Camacho‐Arroyo, I. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094996 · Cited by 12 · see citing works

New enzymatic assay for the AKR1C enzymes

Beranič, N., Štefane, B., Brus, B., Gobec, S., & Rižner, T. L. (2012) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2012.12.003 · Cited by 10 · see citing works

Synthesis of 5α-Androstane-17-spiro-δ-lactones with a 3-Keto, 3-Hydroxy, 3-Spirocarbamate or 3-Spiromorpholinone as Inhibitors of 17β-Hydroxysteroid Dehydrogenases

Djigoué, G. B., Ngatcha, B. T., Roy, J., & Poirier, D. (2013) · Molecules · doi:10.3390/molecules18010914 · Cited by 10 · see citing works

Key players in progesterone and testosterone action: the metabolizing enzymes

Giatti, S., Diviccaro, S., & Melcangi, R. C. (2022) · Current Opinion in Endocrine and Metabolic Research · doi:10.1016/j.coemr.2022.100319 · Cited by 9 · see citing works

Defects in Ovarian Steroid Hormone Biosynthesis

Strauss, J. F., Modi, B. P., & McAllister, J. M. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-408134-5.00018-4 · Cited by 9 · see citing works

The first Pd-catalyzed Buchwald–Hartwig aminations at C-2 or C-4 in the estrone series

Bacsa, I., Szemerédi, D., Woelfling, J., Schneider, G., Fekete, L., & Mernyák, E. (2018) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.14.85 · Cited by 8 · see citing works

The Synthesis and Metabolism of Steroid Hormones

Strauss, J. F. (2013) · Elsevier eBooks · doi:10.1016/b978-1-4557-2758-2.00004-4 · Cited by 7 · see citing works

Therapeutic potential of targeting AKR1C2 in the treatment of prostate cancer

Nie, M., Li, T., Liu, P., & Wang, X. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-09917-4 · Cited by 4 · see citing works

Catalytic Mechanism and Engineering of Hydroxysteroid Dehydrogenases in the Biosynthesis of Ursodeoxycholic Acid

Feng, J., Xue, J., Hu, X., Ren, L., & Ren, L. (2025) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5c09495 · Cited by 4 · see citing works

Involvement of porcine and human carbonyl reductases in the metabolism of epiandrosterone, 11-oxygenated steroids, neurosteroids, and corticosteroids

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

Comparative multi‐omics in female mice reveals tissue‐specific vulnerabilities to chronic alcohol intake

Willis, C. R. G., Ganjayi, M. S., Brown, A. M., Moser, S. E., Szewczyk, N. J., Clark, B. C., & Baumann, C. W. (2026) · Alcoholism Clinical and Experimental Research · doi:10.1111/acer.70240 · Cited by 2 · see citing works

Characterization of transgenic mice expressing EGFP under the control of the monkey 20α-hydroxysteroid dehydrogenase promoter

Park, C., Jeong, S.-K., Nanjidsuren, T., Byambaragchaa, M., Kang, M., Sim, B., & Min, K. (2018) · Science China Life Sciences · doi:10.1007/s11427-017-9111-9 · Cited by 2 · see citing works

Problems in the use of chemical and functional nomenclatures for steroids in human physiology, biology and pharmacology

Honour, J. W. (2026) · RSC Advances · doi:10.1039/d5ra08275g · Cited by 1 · see citing works

Biochemical Characterization of 20α-Hydroxysteroid Dehydrogenase

Byambaragchaa, M., & Min, K. (2018) · Reproductive and developmental Biology · doi:10.12749/rdb.2018.42.2.7

Synthèse de dérivés stéroïdiens et non stéroïdiens comme inhibiteurs des 17b-hydroxystéroïdes déshydrogénases type 1 et type 3

Djigoué, G. B. (2014) · Corpus Université Laval (Université Laval)

Sex Differences, Progesterone, and Ischemic Stroke

Schumacher, M., & Guennoun, R. (2019) · ISGE series · doi:10.1007/978-3-030-11355-1_14

Regulation of alternative splicing of retinol metabolism in lipid abnormality of PCOS liver by Cyp4a32 and Hsd17b6

Chen, G., Zhang, J., Wang, J., Chen, W., Li, H., Su, H., Dai, S., Tao, Y., Cao, Y., Qiang, H., et al. (2025) · Genomics · doi:10.1016/j.ygeno.2025.111136

Reservatrol and Methoxy Derivatives Modulate Hydroxysteroid 17β-Dehydrogenases 1 and 2 Expression in Nontumorigenic and Cancer Breast Cells

Licznerska, B. E., Sobierajska, H., & Szaefer, H. (2026) · Acta Poloniae Pharmaceutica - Drug Research · doi:10.32383/appdr/220694

Effects of estrone-3-glucuronide on HSD gene expression in steroidogenesis of the sea urchin Mesocentrotus nudus

Hu, Y., Meng, W., Huang, X., Xiang, H., Cong, J., Chang, Y., & Sun, Z. (2026) · Aquaculture International · doi:10.1007/s10499-026-02658-0

BindingDB Entry 50039838: Selective inhibition of human type-5 17ß-hydroxysteroid dehydrogenase (AKR1C3) by baccharin, a component of Brazilian propolis.

BindingDB (2013) · UC San Diego · doi:10.7270/q2z320p2

BindingDB Entry 50040594: Selective inhibitors of aldo-keto reductases AKR1C1 and AKR1C3 discovered by virtual screening of a fragment library.

BindingDB (2013) · UC San Diego · doi:10.7270/q2125tr9

BindingDB Entry 50034235: Pharmacophore-based discovery of FXR agonists. Part I: Model development and experimental validation.

BindingDB (2012) · UC San Diego · doi:10.7270/q2cv4j6g

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

SDR-type human hydroxysteroid dehydrogenases involved in steroid hormone activation

Wu, X., Lukacik, P., Kavanagh, K. L., & Oppermann, U. C. T. (2007) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2006.12.006 · Cited by 54 · see citing works

Molecular Endocrinology of Hydroxysteroid Dehydrogenases

Penning, T. M. (1997) · Endocrine Reviews · doi:10.1210/edrv.18.3.0302 · Cited by 436 · see citing works

17β-Hydroxysteroid dehydrogenases (17β-HSDs) as therapeutic targets: Protein structures, functions, and recent progress in inhibitor development

Marchais-Oberwinkler, S., Henn, C., Möller, G., Klein, T., Negri, M., Oster, A., Spadaro, A., Werth, R., Wetzel, M., Xu, K., et al. (2011) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.12.013 · Cited by 216 · see citing works

Hydrohysteroid Dehydrogenases – Biological Role and Clinical Importance – Review

Atanassova, N. N., & Koev, Y. (2012) · InTech eBooks · doi:10.5772/54149 · Cited by 16 · see citing works