The DOI matches its Crossref record; 168 of the 176 references it cites were found in a registry or an index.
Integrated view on 17beta-hydroxysteroid dehydrogenases
Abstract
17beta-Hydroxysteroid dehydrogenases (17beta-HSDs) are important enzymes in steroid metabolism. Long known members of the protein family seemed to be well characterised concerning their role in the regulation of the biological potency of steroid hormones, but today more and more evidence points to pivotal contributions of these enzymes in a variety of other metabolic pathways. Therefore, studies on 17beta-HSDs develop towards metabolomic survey. Latest research results give new insights into the complex metabolic interconnectivity of the 17beta-HSDs. In this paper metabolic activities of 17beta-HSDs will be compared, their interplay with endogenous substrates summarised, and interlacing pathways depicted. Strategies on deciphering the physiological role of 17beta-HSDs and the genetic predisposition for associated diseases will be presented.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
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?
In the citing paper
“Mutations in CYP11B2 selectively impair aldosterone synthesis, causing hyponatremia and hyperkalemia with normal cortisol production (39,90).”
From Congenital Adrenal Hyperplasia—Current Insights in Pathophysiology, Diagnostics, and Management (2022) · cites this paper as [90]
In the citing paper
“Generally, these enzymes are multi-functional and often have overlapping substrate specificities and expression patterns, allowing for redundant enzymes to cover in case of deficiency of another enzyme [107,114].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [114]
In the citing paper
“To date, 14 human enzymes with 17β-HSD/oxoreductase activities have been identified [105,106,113].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [106]
In the citing paper
“The majority of 5α/β-3α-metabolites of testosterone and DHT, which contain a 17β-hydroxy, are converted to 17-keto steroids by the action of the oxidative 17β-HSDs, HSD17B2 and HSD17B4 [106].”
From Human steroid biosynthesis, metabolism and excretion are differentially reflected by serum and urine steroid metabolomes: a comprehensive review (2019) · cites this paper as [106]
Citations
Cites
ABAD Directly Links Aß to Mitochondrial Toxicity in Alzheimer's Disease
Lustbader, J. W., Cirilli, M., Lin, C., Xu, H. W., Takuma, K., Wang, N., Caspersen, C., Chen, X., Pollak, S., Chaney, M., et al. (2004) · Science · doi:10.1126/science.1091230 · Cited by 1,303
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
Short-chain dehydrogenases/reductases (SDR): the 2002 update
Oppermann, U. C. T., Filling, C., Hult, M., Shafqat, N., Wu, X., Lindh, M., Shafqat, J., Nordling, E., Kallberg, Y., Persson, B., et al. (2003) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00164-3 · Cited by 633
Male pseudohermaphroditism caused by mutations of testicular 17β-hydroxysteroid dehydrogenase 3
Geissler, W. M., Davis, D. L., Wu, L., Bradshaw, K. D., Patel, S., Mendonca, B. B., Elliston, K. O., Wilson, J. D., Russell, D. W., & Andersson, S. (1994) · Nature Genetics · doi:10.1038/ng0594-34 · Cited by 570
Wu, L., Einstein, M., Geissler, W. M., Chan, H. K., Elliston, K. O., & Andersson, S. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31480-7 · Cited by 437
The 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
Du Yan, S., Fu, J., Soto, C., Chen, X., Zhu, H., Al-Mohanna, F., Collison, K., Zhu, A., Stern, E., Saido, T., et al. (1997) · Nature · doi:10.1038/39522 · Cited by 379
Endometriosis: The pathophysiology as an estrogen-dependent disease
Kitawaki, J., Kado, N., Ishihara, H., Koshiba, H., Kitaoka, Y., & Honjo, H. (2002) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(02)00260-1 · Cited by 370
Polymorphisms Associated With Circulating Sex Hormone Levels in Postmenopausal Women
Dunning, A. M., Dowsett, M., Healey, C. S., Tee, L. J., Luben, R., Folkerd, E. J., Novik, K. L., Kelemen, L., Ogata, S., Pharoah, P. D. P., et al. (2004) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djh167 · Cited by 346
Fujimoto, Y., Itabe, H., Sakai, J., Makita, M., Noda, J., Mori, M., Higashi, Y., Kojima, S., & Takano, T. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2003.10.018 · Cited by 331
Flagged first, then by citations
8 of the 176 references couldn’t be matched to a known paper.
Research works printed but not linked: 2
- Lenski, 2007, The reduced expression of the HADH2 protein causes X-linked mental retardation, choreoathetosis, and abnormal behavior, Am. J. Hum. Genet., 80, 372, 10.1086/511527 · DOI
- Nagasaki, S., Suzuki, T., Miki, Y., Akahira, J., Kitada, K., Ishida, T., Handa, H., Ohuchi, N., Sasano, H., in press. 17β-hydroxysteroid dehydrogenase type12 in human breast carcinoma: a prognostic factor via potential regulation of fatty acids synthesis. Cancer Res.
Cited by
Sorted by citations
A Protein-Truncating HSD17B13 Variant and Protection from Chronic Liver Disease
Abul-Husn, N. S., Cheng, X., Li, A. H., Xin, Y., Schurmann, C., Stevis, P., Liu, Y., Kozlitina, J., Stender, S., Wood, G. C., et al. (2018) · New England Journal of Medicine · doi:10.1056/nejmoa1712191 · Cited by 827
Congenital Adrenal Hyperplasia—Current Insights in Pathophysiology, Diagnostics, and Management
Claahsen - van der Grinten, H. L., Speiser, P. W., Ahmed, S. F., Arlt, W., Auchus, R. J., Falhammar, H., Flück, C. E., Guasti, L., Huebner, A., Kortmann, B. B. M., et al. (2022) · Endocrine Reviews · doi:10.1210/endrev/bnab016 · Cited by 556
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
“20 enzymes to cover in case of deficiency of another enzyme [107,114].”
Genome-wide association study identifies 143 loci associated with 25 hydroxyvitamin D concentration
Revez, J. A., Lin, T., Qiao, Z., Xue, A., Holtz, Y., Zhu, Z., Zeng, J., Wang, H., Sidorenko, J., Kemper, K. E., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15421-7 · Cited by 416
An ADIOL-ERβ-CtBP Transrepression Pathway Negatively Regulates Microglia-Mediated Inflammation
Saijo, K., Collier, J. G., Li, A. C., Katzenellenbogen, J. A., & Glass, C. K. (2011) · Cell · doi:10.1016/j.cell.2011.03.050 · Cited by 295
“However, there are at least 14 different members of the 17β-HSD family identified in humans and mice, and some of them could also potentially convert DHEA to ADIOL (Moeller and Adamski, 2009).”
Steroids in teleost fishes: A functional point of view
Tokarz, J., Möller, G., de Angelis, M. H., & Adamski, J. (2015) · Steroids · doi:10.1016/j.steroids.2015.06.011 · Cited by 258
Su, W., Wang, Y., Jia, X., Wu, W., Li, L., Tian, X., Li, S., Wang, C., Xu, H.-M., Cao, J., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1410741111 · Cited by 222
“The family of 17β-HSDs consists of 14 enzymes responsible for reduction or oxidation of sex hormones, fatty acids, and bile acids in vivo (35).”
BackgroundIntracrine androgen biosynthesis, metabolism and action revisited
Schiffer, L., Arlt, W., & Storbeck, K.-H. (2018) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.08.016 · Cited by 217
“Several HSD17B isoforms are active in the liver (Moeller and Adamski, 2009) as well as HSD11B1, which oxidises 11-keto-ste-”
InfluentialMarchais-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
Self-citationKaserer, T., Beck, K. R., Akram, M., Odermatt, A., & Schuster, D. (2015) · Molecules · doi:10.3390/molecules201219880 · Cited by 214
Storbeck, K.-H., Bloem, L. M., Africander, D., Schloms, L., Swart, P., & Swart, A. C. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.07.006 · Cited by 198
“In humans, the primary function of 17bHSD3 is the production of T in the testes, however, its expression has also been detected in the prostate (Montgomery et al., 2008; Mindnich et al., 2004; Moeller and Adamski, 2009).”
BackgroundThe structural biology of oestrogen metabolism
THOMAS, M. P., & Potter, B. V. L. (2013) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2012.12.014 · Cited by 181
Carlsson, B., Lindén, D., Brolén, G., Liljeblad, M., Bjursell, M., Romeo, S., & Loomba, R. (2020) · Alimentary Pharmacology & Therapeutics · doi:10.1111/apt.15738 · Cited by 169
Structural and functional biology of aldo-keto reductase steroid transforming enzymes
Penning, T. M., Wangtrakuldee, P., & Auchus, R. J. (2019) · Endocrine Reviews · doi:10.1210/er.2018-00089 · Cited by 164
Sex hormone metabolism in lung development and maturation
Seaborn, T., Simard, M., Provost, P. R., Piedbœuf, B., & Tremblay, Y. (2010) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2010.09.001 · Cited by 152
Hydroxysteroid dehydrogenases (HSDs) in bacteria – A bioinformatic perspective
Kisiela, M., Skarka, A., Ebert, B., & Maser, E. (2011) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2011.08.002 · Cited by 141
Steroidogenesis and its regulation in teleost-a review
Anbazhagan, R., & Senthilkumaran, B. (2020) · Fish Physiology and Biochemistry · doi:10.1007/s10695-019-00752-0 · Cited by 131
Saloniemi, T., Jokela, H., Strauss, L., Pakarinen, P., & POUTANEN, M. H. (2011) · Journal of Endocrinology · doi:10.1530/joe-11-0315 · Cited by 116
“…sequence homology, expression pattern (Table 1), cofactor preference, substrate specificity and subcellular localisation (Peltoketo et al. 1999a, Lukacik et al. 2006, Möeller & Adamski 2006, Wu et al. 2007, Meier et al. 2009, Mindnich & Adamski 2009, Möeller & Adamski 2009, Persson et al. 2009).”
BackgroundEstrogen biosynthesis and signaling in endometriosis
Huhtinen, K., Ståhle, M., Perheentupa, A., & Poutanen, M. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.08.022 · Cited by 107
Ma, W., Cojocaru, R. I., Gotoh, N., Gieser, L. M., Villasmil, R., Cogliati, T., Swaroop, A., & Wong, W. T. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.03.022 · Cited by 108
“A down-regulated gene, Hsd17b1, codes for 11b-hydroxysteroid dehydrogenase type 1, which activates the glucocorticoid cortisone (Seckl and Walker, 2001) and induces the production of steroid hormone 5androsten-3b, 17b-diol (ADIOL) (Moeller and Adamski, 2009), a key factor in limiting microglial activation (Gottfried-B…”
BackgroundBaker, M. E., Nelson, D. R., & Studer, R. A. (2014) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2014.10.020 · Cited by 99
The Clinical and Molecular Heterogeneity of 17βHSD-3 Enzyme Deficiency
George, M. M., New, M. I., Ten, S., Sultan, C., & Bhangoo, A. (2010) · Hormone Research in Paediatrics · doi:10.1159/000318004 · Cited by 102
Origin and diversification of steroids: Co-evolution of enzymes and nuclear receptors
Baker, M. E. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2010.07.013 · Cited by 93
“Important in the orgins and evolution of vertebrate steroids are two important classes of enzymes, cytochrome P450s [CYP450s] [10] [11] [12] and hydroxysteroid dehydrogenases [HSDs] [13] [14] [15], which are involved in the synthesis of biologically active steroids from cholesterol.”
Steroidogenic Enzymes in the Brain: Morphological Aspects
Pelletier, G. (2010) · Progress in brain research · doi:10.1016/s0079-6123(08)81011-4 · Cited by 101
Schloms, L., Storbeck, K., Swart, P., Gelderblom, W. C. A., & Swart, A. C. (2011) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2011.11.003 · Cited by 89
Kemiläinen, H., Adam, M., Mäki-Jouppila, J. H., Damdimopoulou, P., Damdimopoulos, A. E., Kere, J., Hovatta, O., Laajala, T. D., Aittokallio, T. A., Adamski, J., et al. (2016) · Endocrinology · doi:10.1210/en.2016-1252 · Cited by 89
Mazumdar, M., Fournier, D., Zhu, D., Cadot, C., Poirier, D., & Lin, S. (2009) · Biochemical Journal · doi:10.1042/bj20091020 · Cited by 84
17β-Hydroxysteroid dehydrogenase inhibitors: a patent review
Poirier, D. (2010) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2010.505604 · Cited by 83
“In fact, there is a significant 1000-fold difference in catalytic efficiencies of 17b-HSD types 1, 7 and 12 and a great difference in tissue-expression of each type [30,41-45].”
BackgroundRoles of 17β-hydroxysteroid dehydrogenase type 10 in neurodegenerative disorders
Yang, S., He, X., Isaacs, C. E., Dobkin, C., Miller, D. L., & Philipp, M. (2014) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2014.07.001 · Cited by 85
Nakamoto, M., Shibata, Y., Ohno, K., Usami, T., Kamei, Y., Taniguchi, Y., Todo, T., Sakamoto, T., Young, G., Swanson, P., et al. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.07.013 · Cited by 82
Kazeto, Y., Tosaka, R., Matsubara, H., Ijiri, S., & Adachi, S. (2011) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2011.03.013 · Cited by 76
Minireview: Androgen Metabolism in Castration-Resistant Prostate Cancer
Sharifi, N. (2013) · Molecular Endocrinology · doi:10.1210/me.2013-1007 · Cited by 78
Estrogen biosynthesis, phase I and phase II metabolism, and action in endometrial cancer
Rižner, T. L. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.07.026 · Cited by 76
Cornel, K. M. C., Kruitwagen, R. F. P. M., Delvoux, B., Visconti, L. M., de Vijver, K. K. V., Day, J. M., Gorp, T. V., Hermans, R. J. J., Dunselman, G. A. J., & Romano, A. (2012) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2011-2994 · Cited by 64
Konings, G. F. J., Brentjens, L. S., Delvoux, B., Linnanen, T., Cornel, K. M. C., Koskimies, P., Bongers, M. Y., Kruitwagen, R. F. P. M., Xanthoulea, S., & Romano, A. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00940 · Cited by 66
“Fourteen 17βHSDs exist, whose specificity is determined by tissue distribution, intracellular localization and biochemistry (Table 2); reviewed thoroughly in (Mindnich et al., 2004; Moeller and Adamski, 2006, 2009; Prehn et al., 2009; Miller and Auchus, 2011).”
BackgroundZou, C., Wang, L., Zou, Y., Wu, Z., Wang, W., Liang, S., Wang, L., & You, F. (2020) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2020.105597 · Cited by 61
Engineering Mycobacterium smegmatis for testosterone production
Fernández‐Cabezón, L., Galán, B., & García, J. L. (2016) · Microbial Biotechnology · doi:10.1111/1751-7915.12433 · Cited by 58
“They catalyse NAD(P)H/NAD(P)+dependent reductions/oxidations at the C-17 position of different steroids (Peltoketo et al., 1999; Moeller and Adamski, 2006, 2009; Marchais-Oberwinkler et al., 2011).”
BackgroundHydroxysteroid (17β) Dehydrogenase 12 Is Essential for Mouse Organogenesis and Embryonic Survival
Rantakari, P., Lagerbohm, H., Kaimainen, M., Suomela, J., Strauss, L., Sainio, K., Pakarinen, P., & POUTANEN, M. H. (2010) · Endocrinology · doi:10.1210/en.2009-0929 · Cited by 57
Chen, Z., Kastaniotis, A. J., Miinalainen, I., Venkatesan, R., Wierenga, R. K., & Hiltunen, J. K. (2009) · The FASEB Journal · doi:10.1096/fj.09-133587 · Cited by 56
Recent advances in 17beta-hydroxysteroid dehydrogenases
Prehn, C. P., Möller, G., & Adamski, J. (2009) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2008.12.024 · Cited by 56
A tale of two steroids: The importance of the androgens DHEA and DHEAS for early neurodevelopment
Greaves, R. F., Wudy, S. A., Badoer, E., Zacharin, M., Hirst, J. J., Quinn, T., & Walker, D. W. (2018) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2018.12.007 · Cited by 54
The Adrenal Cortex and its Disorders
Miller, W. L. (2009) · Wiley eBooks · doi:10.1002/9781444316728.ch13 · Cited by 51
Beilstein, F., Bouchoux, J., Rousset, M., & Demignot, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053017 · Cited by 50
Tokarz, J., Mindnich, R., Norton, W., Möller, G., Hrabé de Angelis, M., & Adamski, J. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.10.022 · Cited by 48
“Other 17beta-HSDs, e.g. types 4, 7, 8, 10, and 12, can be denoted as multifunctional 17beta-HSDs regarding their broad substrate specificities ranging from very long chain fatty acids, branched fatty acids, and bile acids to sterols (Mindnich and Adamski, 2009; Moeller and Adamski, 2009).”
Self-citationWetzel, M., Marchais‐Oberwinkler, S., Perspicace, E., Möller, G., Adamski, J., & Hartmann, R. W. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm2008453 · Cited by 47
Delvoux, B., D'Hooghe, T., Kyama, C., Koskimies, P., Hermans, R. J. J., Dunselman, G. A., & Romano, A. (2014) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2013-2851 · Cited by 59
“These findings confirm previous data of our laboratory and other research teams indicating that 17 -HSD type 1 plays one of the major roles in estrogen metabolism (16, 17) and specifically in the endometrium (21).”
BackgroundResultKimoto, T., Ishii, H., Higo, S., Hojo, Y., & Kawato, S. (2010) · Endocrinology · doi:10.1210/en.2010-0581 · Cited by 46
Ayan, D. P., Maltais, R., & Poirier, D. (2012) · ChemMedChem · doi:10.1002/cmdc.201200129 · Cited by 46
Möller, G., Deluca, D., Gege, C., Rosinus, A., Kowalik, D., Peters, O., Droescher, P., Elger, W. A. G., Adamski, J., & Hillisch, A. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.09.113 · Cited by 45
Hydroxysteroid (17β) dehydrogenase X in human health and disease
Yang, S., He, X., & Miller, D. L. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.06.011 · Cited by 45
Poirier, D. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.12.007 · Cited by 44
17B-hydroxysteroid dehydrogenases as acyl thioester metabolizing enzymes
Hiltunen, J. K., Kastaniotis, A. J., Autio, K. J., Jiang, G., Chen, Z., & Glumoff, T. (2019) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2018.11.012 · Cited by 43
Steroid metabolism in cnidarians: Insights from Nematostella vectensis
Tarrant, A. M., Reitzel, A. M., Blomquist, C. H., Haller, F., Tokarz, J., & Adamski, J. (2008) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2008.09.037 · Cited by 45
Seasonal expression and cellular distribution of star and steroidogenic enzymes in quail testis
Rosati, L., Fiore, M. M. D., Prisco, M., Russo, F. D. G., Venditti, M., Andreuccetti, P., Baccari, G. C., & Santillo, A. (2019) · Journal of Experimental Zoology Part B Molecular and Developmental Evolution · doi:10.1002/jez.b.22896 · Cited by 41
Zemanová, L., & Wsól, V. (2011) · Drug Metabolism Reviews · doi:10.3109/03602532.2011.638304 · Cited by 41
“17β-HSDs can be grouped into oxidative NAD+-dependent enzymes (e.g., 17β-HSD types 2, 4, 6, 8, 9, 10, 11, and 14) and reductive NADPH-dependent enzymes (e.g., 17β-HSD types 1, 3, 5, 7, and 12) (Lukacik et al., 2006; Moeller and Adamski, 2006, 2009).”
Saloniemi, T., Järvensivu, P., Koskimies, P., Jokela, H., Lamminen, T., Ghaem‐Maghami, S., Dina, R. E., Damdimopoulou, P., Mäkelä, S., Perheentupa, A. H., et al. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.090325 · Cited by 40
Heinosalo, T., Saarinen, N., & POUTANEN, M. H. (2018) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2018.08.004 · Cited by 40
Effects of novel brominated flame retardants on steroidogenesis in primary porcine testicular cells
Mankidy, R., Ranjan, B., Honaramooz, A., & Giesy, J. P. (2013) · Toxicology Letters · doi:10.1016/j.toxlet.2013.10.018 · Cited by 40
Sharifi, N., McPhaul, M. J., & Auchus, R. J. (2010) · Journal of Investigative Medicine · doi:10.2310/jim.0b013e3181ff6bb8 · Cited by 36
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
Yin, J., Lu, J., Peng, L., He, M., Huang, S., Lv, J., Zhu, Y., Liu, Z., & Jiang, M. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.671708 · Cited by 39
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
Local estrogen metabolism (intracrinology) in endometrial cancer: A systematic review
Cornel, K. M. C., Bongers, M. Y., Kruitwagen, R. F. P. M., & Romano, A. (2018) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2018.10.004 · Cited by 37
“Finally, AKRs (that also include HSD17B5) are enzymes that posses various 3, 17, 20 steroid keto-reductase/hydroxyl-dehydrogenase activities and can use various substrates like androgens, progesterone (and other 21carbon derivatives), thus making the intracrine network extremely flexible (Konings et al., 2018a; Moelle…”
Endo, S., Miyagi, N., Matsunaga, T., Hara, A., & Ikari, A. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.01.190 · Cited by 35
Zhang, C., Chen, J., Yin, D., & Lin, S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0029835 · Cited by 35
Omic studies reveal the pathogenic lipid droplet proteins in non-alcoholic fatty liver disease
Zhang, X., Wang, Y., & Liu, P. (2016) · Protein & Cell · doi:10.1007/s13238-016-0327-9 · Cited by 36
“Since more than half of all known types of 17β-HSDs have been found in the liver (Moeller and Adamski, 2009), it is reasonable to speculate that the liver can also generate intracrine sex steroid signaling.”
BackgroundPerimenopausal regulation of steroidogenesis in the nonhuman primate
Sorwell, K. G., Kohama, S. G., & Urbanski, H. F. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.05.004 · Cited by 35
“Of the isozymes of 17BHSD, type 5 was chosen because of its confirmed expression in the brain and its primary direction of action, namely the conversion of androstenedione to testosterone (Labrie et al., 2000; Luu-The and Labrie, 2010; Moeller and Adamski, 2009).”
BackgroundChen, X., Xu, S., Yu, Z., Guo, L., Yang, S., Liu, L., Yang, X., & Liu, J. (2013) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2013.12.002 · Cited by 35
“…gene 82 (hsp82), which are usually used for phylogenetic analysis in insects and mites, and 17-beta-hydroxysteroid dehydrogenase (17b-HSD), which is hypothetically responsible for catalyzing the sex hormone and involved in fatty acid elongation (Moeller and Adamski, 2009), were also amplified.”
BackgroundMethodKonings, G. F. J., Reynaert, N. L., Delvoux, B., Verhamme, F. M., Bracke, K. R., Brusselle, G., Romano, A., & Vernooy, J. H. J. (2016) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.12.001 · Cited by 35
Subcellular localization and membrane topology of 17β-hydroxysteroid dehydrogenases
Tsachaki, M., & Odermatt, A. (2018) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2018.07.003 · Cited by 35
Liu, L., Bai, Y.-X., Zhou, J.-H., Sun, X.-W., Sui, H., Zhang, W.-J., Yuan, H.-H., Xie, R., Wei, X.-L., Zhang, T.-T., et al. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140918973 · Cited by 34
“These are the aromatase gene (CYP19A1) and the type 1 17-β hydroxysteroid dehydrogenase (17-β-HSD-1) gene encoding the bidirectional enzyme that converts estrone (E1) to estradiol (E2) [17,18].”
Maltais, R., Ayan, D. P., Trottier, A., Barbeau, X., Lagüe, P., Bouchard, J., & Poirier, D. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm401639v · Cited by 33
Genetic Risk Factors and Disease Modifiers of Nonalcoholic Steatohepatitis
Kozlitina, J. (2020) · Gastroenterology Clinics of North America · doi:10.1016/j.gtc.2019.09.001 · Cited by 33
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
Maltais, R., Fournier, M.-A., & Poirier, D. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.06.003 · Cited by 33
New agents and strategies for the hormonal treatment of castration-resistant prostate cancer
Sharifi, N. (2010) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2010.494178 · Cited by 32
“DHEA may be converted to D(5)-androstenediol (A5diol) by a member of the 17b-hydroxysteroid dehydrogenase (17bHSD) family [45,46].”
BackgroundBellavance, É., Luu-The, V., & Poirier, D. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900921c · Cited by 31
Testosterone synthesis in patients with 17β-hydroxysteroid dehydrogenase 3 deficiency
Werner, R., Kulle, A., Sommerfeld, I., Riepe, F. G., Wudy, S., Hartmann, M. F., Merz, H., Döhnert, U., Bertelloni, S., Holterhus, P.-M., et al. (2012) · Sexual Development · doi:10.1159/000336605 · Cited by 29
“…different isoenzymes of the 17 - HSD fulfill specific roles in sex steroid metabolism by catalyzing the conversion of low-activity 17-ketosteroids, such as androstenedione and estrone to their more potent 17 -hydroxysteroid forms, testosterone or estradiol and reverse [Moeller and Adamski, 2009].”
BackgroundInfluentialLiu, J., Zhang, Z., Ma, X., Liang, S., & Yang, D. (2014) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2014.01.008 · Cited by 29
Sex hormone levels in the brain of d-aspartate-treated rats
Fiore, M. M. D., Santillo, A., Falvo, S., Baccari, G. C., Venditti, M., Russo, F. D. G., Lispi, M., & D’Aniello, A. (2017) · Comptes Rendus Biologies · doi:10.1016/j.crvi.2017.11.002 · Cited by 29
Scheiner, B., Stättermayer, A. F., Schwabl, P., Bucsics, T., Paternostro, R., Bauer, D. J. M., Simbrunner, B., Schmidt, R. L. J., Marculescu, R., Ferlitsch, A., et al. (2019) · Liver International · doi:10.1111/liv.14304 · Cited by 28
“well as MELD scores (12 (10-15) vs 11 (9-13) points; P = .”
Anbazhagan, R., & Senthilkumaran, B. (2014) · Steroids · doi:10.1016/j.steroids.2014.09.009 · Cited by 29
Li, S., Li, J., Mao, G., Hu, Y., Ye, X., Ding, T., Linhardt, R. J., & Chen, S. (2018) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2018.08.020 · Cited by 29
Genomic and neural analysis of the estradiol-synthetic pathway in the zebra finch
London, S. E., & Clayton, D. F. (2010) · BMC Neuroscience · doi:10.1186/1471-2202-11-46 · Cited by 28
“Perhaps then the complement of HSD17B enzymes in zebra finches can perform all of the necessary reactions represented in the fourteen mammalian enzymes [32,39,63-66].”
Testicular steroidogenic enzymes in the lizard Podarcis sicula during the spermatogenic cycle
Rosati, L., Santillo, A., Fiore, M. M. D., Andreuccetti, P., & Prisco, M. (2017) · Comptes Rendus Biologies · doi:10.1016/j.crvi.2017.10.001 · Cited by 27
Naganuma, T., & Kihara, A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101823 · Cited by 29
Konings, G. F., Cornel, K. M., Xanthoulea, S., Delvoux, B., Skowron, M. A., Kooreman, L., Koskimies, P., Krakstad, C., Salvesen, H. B., van Kuijk, K., et al. (2018) · The Journal of Pathology · doi:10.1002/path.5004 · Cited by 26
Cassetta, A., Stojan, J., Krastanova, I. B., Kristan, K., Brunskole, M., Lamba, D., & Rižner, T. L. (2017) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2017.02.020 · Cited by 27
Järvensivu, P., Saloniemi-Heinonen, T., Awosanya, M., Koskimies, P., Saarinen, N., & POUTANEN, M. H. (2015) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2015.01.008 · Cited by 23
Combined Biophysical Chemistry Reveals a New Covalent Inhibitor with a Low-Reactivity Alkyl Halide
Li, T., Maltais, R., Poirier, D., & Lin, S. (2018) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.8b02225 · Cited by 25
Lima, D., Machado, A., Reis-Henriques, M. A., Rocha, E., Santos, M. M., & Castro, L. F. C. (2012) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2012.10.005 · Cited by 24
Genetic polymorphisms and obesity influence estradiol decline during the menopause
Sowers, M. R., Randolph, J. F., Zheng, H. T., Jannausch, M. L., McConnell, D. S., Kardia, S. R., Crandall, C. J., & Nan, B. (2010) · Clinical Endocrinology · doi:10.1111/j.1365-2265.2010.03968.x · Cited by 24
Möller, G., Husen, B., Kowalik, D., Hirvelä, L., Plewczyński, D., Rychlewski, L., Messinger, J., Thole, H., & Adamski, J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010969 · Cited by 23
“Several druggable targets were defined in humans [1,2] including steroid metabolizing enzymes like 17b-hydroxysteroid dehydrogenases (17b-HSDs) controlling the biological potency of steroid hormones by redox reactions at position 17 of the steroid scaffold [3,4,5,6,7].”
BackgroundMaltais, R., Ayan, D. P., & Poirier, D. (2011) · ACS Medicinal Chemistry Letters · doi:10.1021/ml200093v · Cited by 23
Synthesis and Biological Evaluation of Triazolyl 13α-Estrone–Nucleoside Bioconjugates
Bodnár, B., Mernyák, E., Woelfling, J., Schneider, G., Herman, B. E., Szécsi, M., Sinka, I., Zupkó, I., Kupihár, Z., & Kovács, L. (2016) · Molecules · doi:10.3390/molecules21091212 · Cited by 22
“Molecules 2016, 21, 1212 2 of 17 t e re cti f estr e t 17 -estra i l, ic e a ces t e r liferati f certai ca cer cells [4].”
BackgroundSynthesis of novel 13α-estrone derivatives by Sonogashira coupling as potential 17β-HSD1 inhibitors
Bacsa, I., Jójárt, R., Woelfling, J., Schneider, G., Herman, B. E., Szécsi, M., & Mernyák, E. (2017) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.13.126 · Cited by 22
Liu, L., Chen, S., Yu, M., Ge, C., Ren, M., Liu, B., Yang, X. P., Christian, T., Hou, Y., Zou, J., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-02763-9 · Cited by 21
Genes linked to species diversity in a sexually dimorphic communication signal in electric fish
Smith, G. T., Proffitt, M. R., Smith, A. R., & Rusch, D. B. (2017) · Journal of Comparative Physiology A · doi:10.1007/s00359-017-1223-3 · Cited by 23
“…of androgens and estrogens to more inactive or active forms, and thus might have influence local availability of active ligands for androgen and estrogen receptors in the Pn. 17β-HSDs also have numerous other functions, however, including fatty acid/lipid metabolism (Moeller and Adamski 2009).”
Wang, T., He, K. F., Blaney, L. M., & Chung, J. S. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.962576 · Cited by 21
Visús, C., Ito, D., Dhir, R., Szczepański, M. J., Chang, Y. J., Latimer, J. J., Grant, S. G., & DeLeo, A. B. (2011) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-011-1001-y · Cited by 20
Metadata
- Authors
- Moeller, G., & Adamski, J.
- Affiliations
- Helmholtz Munich (DE)
- ORCID
- Adamski, Jerzy
- Venue
- Molecular and Cellular Endocrinology
- Publisher
- Elsevier BV
- Published
- 2009-03
- Volume
- 301
- Issue
- 1-2
- Pages
- 7-19
- ISSN
- 0303-7207 (ISSN-L)
- OpenAlex
- W2048714965
- Cited by
- 214
- References
- 176
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 12 · 2023: 8 · 2022: 6 · 2021: 8 · 2020: 11 · 2019: 8 · 2018: 17 · 2017: 12 · 2016: 14 · 2015: 12 · 2014: 11 · 2013: 16 · 2012: 11
- FWCI
- 1.52
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Molecular and Cellular Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- Site cant be reached (submittedVersion)
- Topics
- Physical Sciences › Chemistry › Organic Chemistry › Steroid Chemistry and Biochemistry
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adrenal Hormones and Disorders
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Hormonal Regulation and Hypertension
- Keywords
- 17β-hydroxysteroid dehydrogenase, steroid metabolism, steroid hormone regulation, metabolomics, endogenous substrates, genetic susceptibility, disease
- MeSH terms
- Animals, Disease, Humans, Polymorphism, Genetic, 17-Hydroxysteroid Dehydrogenases, Crystallography, X-Ray, Models, Animal
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