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17-hydroxysteroid dehydrogenases - antagonists & inhibitors (274) 274
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molecular structure (43) 43
pregnancy (43) 43
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cells, cultured (31) 31
substrate specificity (31) 31
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rats, wistar (30) 30
3-hydroxysteroid dehydrogenases - antagonists & inhibitors (29) 29
breast neoplasms - enzymology (29) 29
androstenedione - metabolism (28) 28
drug design (28) 28
estradiol dehydrogenases - antagonists & inhibitors (28) 28
rats, sprague-dawley (28) 28
cell line (27) 27
estrogens - metabolism (26) 26
rna, messenger - metabolism (26) 26
toxicology (26) 26
testosterone - biosynthesis (25) 25
aromatase (24) 24
breast neoplasms - drug therapy (24) 24
dehydrogenase (24) 24
dehydrogenases (24) 24
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estrogen antagonists - pharmacology (24) 24
oncology (24) 24
physiological aspects (24) 24
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gene-expression (23) 23
microsomes - enzymology (23) 23
steroidogenesis (23) 23
adult (22) 22
aromatase inhibitors (22) 22
breast-cancer (22) 22
hormones, hormone substitutes, and hormone antagonists (22) 22
inhibitory concentration 50 (22) 22
oxidation-reduction (22) 22
steroids (22) 22
17β-hydroxysteroid dehydrogenase (21) 21
metabolism (21) 21
analysis (20) 20
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enzyme inhibitors - therapeutic use (19) 19
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breast neoplasms - pathology (18) 18
endocrine system (18) 18
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pharmacology & pharmacy (18) 18
progesterone (18) 18
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article (17) 17
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cell proliferation - drug effects (17) 17
cytochrome p-450 (17) 17
estrone - pharmacology (17) 17
gene expression (17) 17
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1. Full Text Human dehydrogenase/reductase (SDR family) member 11 is a novel type of 17β-hydroxysteroid dehydrogenase
by Endo, Satoshi and Miyagi, Namiki and Matsunaga, Toshiyuki and Hara, Akira and Ikari, Akira
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 03/2016, Volume 472, Issue 1, pp. 231 - 236
We report characterization of a member of the short-chain dehydrogenase/reductase superfamily encoded in a human gene, . The recombinant protein (DHRS11)... 
Dehydroepiandrosterone | Neurosteroid | DHRS11 | 17β-Hydroxysteroid dehydrogenase | Isolithocholic acid | 3β-Hydroxysteroid dehydrogenase | MAMMALIAN REDUCTASES | BIOCHEMISTRY & MOLECULAR BIOLOGY | SHORT-CHAIN DEHYDROGENASE/REDUCTASE | ISOFORM | IDENTIFICATION | 3 beta-Hydroxysteroid dehydrogenase | KETO REDUCTASE FAMILY | NOMENCLATURE | BIOPHYSICS | METABOLISM | PATHWAY | ENZYMES | 17 beta-Hydroxysteroid dehydrogenase | Oxidoreductases - antagonists & inhibitors | Alternative Splicing | Humans | Substrate Specificity | Male | RNA, Messenger - metabolism | Tissue Distribution | Isoenzymes - metabolism | Female | NADP - metabolism | Ketosteroids - chemistry | Recombinant Proteins - metabolism | Oxidoreductases - metabolism | Isoenzymes - genetics | Oxidoreductases - genetics | 17-Hydroxysteroid Dehydrogenases - antagonists & inhibitors | RNA, Messenger - genetics | Enzyme Inhibitors - pharmacology | Enzyme Stability | Recombinant Proteins - genetics | Hot Temperature | 17-Hydroxysteroid Dehydrogenases - genetics | Ketosteroids - metabolism | Kinetics | 17-Hydroxysteroid Dehydrogenases - metabolism | Isoenzymes - antagonists & inhibitors | Hydrogen-Ion Concentration
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2. Full Text 17β-Hydroxysteroid dehydrogenases (17β-HSDs) as therapeutic targets: Protein structures, functions, and recent progress in inhibitor development
by Marchais-Oberwinkler, Sandrine and Henn, Claudia and Möller, Gabriele and Klein, Tobias and Negri, Matthias and Oster, Alexander and Spadaro, Alessandro and Werth, Ruth and Wetzel, Marie and Xu, Kuiying and Frotscher, Martin and Hartmann, Rolf W and Adamski, Jerzy
Journal of Steroid Biochemistry and Molecular Biology, ISSN 0960-0760, 2011, Volume 125, Issue 1, pp. 66 - 82
17β-Hydroxysteroid dehydrogenases (17β-HSDs) are oxidoreductases, which play a key role in estrogen and androgen steroid metabolism by catalyzing final steps... 
Animal models | 17β-Hydroxysteroid dehydrogenases | Inhibitors | Protein structures | Therapeutic targets | Humans | Molecular Sequence Data | Male | Isoenzymes - chemistry | Phylogeny | Isoenzymes - classification | 17-Hydroxysteroid Dehydrogenases - classification | Breast Neoplasms - enzymology | Estrogens - chemistry | Isoenzymes - metabolism | Enzyme Inhibitors - chemistry | Female | Molecular Structure | Estrogens - metabolism | Prostatic Neoplasms - drug therapy | Amino Acid Sequence | Catalytic Domain | Enzyme Inhibitors - metabolism | Isoenzymes - genetics | 17-Hydroxysteroid Dehydrogenases - antagonists & inhibitors | Models, Molecular | Breast Neoplasms - drug therapy | Sequence Alignment | Animals | Prostatic Neoplasms - enzymology | Androgens - chemistry | Protein Conformation | Androgens - metabolism | 17-Hydroxysteroid Dehydrogenases - chemistry | 17-Hydroxysteroid Dehydrogenases - metabolism
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3. Full Text Estrogen and androgen-converting enzymes 17β-hydroxysteroid dehydrogenase and their involvement in cancer: With a special focus on 17β-hydroxysteroid dehydrogenase type 1, 2, and breast cancer
by Hilborn, Erik and Stål, Olle and Jansson, Agneta and Medicinska fakulteten and Region Östergötland and Linköpings universitet and Institutionen för klinisk och experimentell medicin and Onkologiska kliniken US and Centrum för kirurgi, ortopedi och cancervård and Avdelningen för Kirurgi, Ortopedi och Onkologi
Oncotarget, ISSN 1949-2553, 2017, Volume 8, Issue 18, pp. 30552 - 30562
Sex steroid hormones such as estrogens and androgens are involved in the development and differentiation of the breast tissue. The activity and concentration... 
Androgens | Breast cancer | Estrogens | HSD17B1 | HSD17B2 | TAMOXIFEN RESPONSE | androgens | estrogens | RECEPTOR EXPRESSION | breast cancer | CELL BIOLOGY | CELL LUNG-CANCER | HUMAN PROSTATE-CANCER | METABOLISM | HYDROXYSTEROID 17-BETA DEHYDROGENASE-1 | COLONIC-CANCER | GENE-EXPRESSION | ESTRADIOL LEVELS | PROGNOSTIC-SIGNIFICANCE | Multigene Family | 17-Hydroxysteroid Dehydrogenases - antagonists & inhibitors | Humans | Breast Neoplasms - etiology | Enzyme Inhibitors - pharmacology | Gene Expression Regulation, Neoplastic | Breast Neoplasms - drug therapy | Enzyme Inhibitors - therapeutic use | Breast Neoplasms - metabolism | Animals | Breast Neoplasms - pathology | 17-Hydroxysteroid Dehydrogenases - genetics | Female | Androgens - metabolism | Estrogens - metabolism | 17-Hydroxysteroid Dehydrogenases - metabolism | Clinical Medicine | Medical and Health Sciences | Medicin och hälsovetenskap | Cancer and Oncology | Klinisk medicin | breast cancer; estrogens; androgens; HSD17B1; HSD17B2 | Cancer och onkologi
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4. Full Text Expression and regulation of CYP17A1 and 3β-hydroxysteroid dehydrogenase in cells of the nervous system: Potential effects of vitamin D on brain steroidogenesis
by Emanuelsson, Ida and Almokhtar, Mokhtar and Wikvall, Kjell and Grönbladh, Alfhild and Nylander, Erik and Svensson, Anne-Lie and Fex Svenningsen, Åsa and Norlin, Maria and Medicinska och farmaceutiska vetenskapsområdet and Institutionen för farmaceutisk biovetenskap and Uppsala universitet and Farmaceutiska fakulteten
Neurochemistry International, ISSN 0197-0186, 02/2018, Volume 113, pp. 46 - 55
Steroids are reported to have diverse functions in the nervous system. Enzymatic production of steroid hormones has been reported in different cell types,... 
Brain | Vitamin D | Neurosteroids | Metabolism | Neurons | Astrocytes | BIOCHEMISTRY & MOLECULAR BIOLOGY | STEROID-METABOLISM | MECHANISMS | NEUROSCIENCES | NEUROPROTECTION | NEUROSTEROID BIOSYNTHESIS | PROGESTERONE SYNTHESIS | ESTROGEN | RAT-BRAIN | CULTURES | Gene Expression Regulation, Enzymologic - drug effects | Steroid 17-alpha-Hydroxylase - antagonists & inhibitors | 17-Hydroxysteroid Dehydrogenases - antagonists & inhibitors | Humans | Cells, Cultured | Brain - enzymology | Rats | Vitamin D - pharmacology | Steroids - antagonists & inhibitors | Rats, Sprague-Dawley | Brain - drug effects | 17-Hydroxysteroid Dehydrogenases - biosynthesis | Animals | 17-Hydroxysteroid Dehydrogenases - genetics | Cell Line, Tumor | Steroid 17-alpha-Hydroxylase - genetics | Steroid 17-alpha-Hydroxylase - biosynthesis | Steroids - biosynthesis | Biological Sciences | neurosteroids | vitamin D | Biokemi | Biochemistry | brain | neurons | Naturvetenskap | Biokemi och molekylärbiologi | Biologiska vetenskaper | Biochemistry and Molecular Biology | metabolism | Natural Sciences | astrocytes
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5. Full Text First Dual Inhibitors of Steroid Sulfatase (STS) and 17β-Hydroxysteroid Dehydrogenase Type 1 (17β-HSD1): Designed Multiple Ligands as Novel Potential Therapeutics for Estrogen-Dependent Diseases
by Salah, Mohamed and Abdelsamie, Ahmed S and Frotscher, Martin
Journal of Medicinal Chemistry, ISSN 0022-2623, 05/2017, Volume 60, Issue 9, pp. 4086 - 4092
STS and 17β-HSD1 are attractive targets for the treatment of estrogen-dependent diseases like endometriosis and breast cancer. The simultaneous inhibition of... 
HUMAN BREAST-CARCINOMA | CANCER PATIENTS | CELLS | CHEMISTRY, MEDICINAL | THERAPY | MCF-7 | IN-VIVO | MICE | ENDOMETRIOSIS | DISCOVERY | SULFOTRANSFERASE | Cell Proliferation | Steryl-Sulfatase - antagonists & inhibitors | Breast Neoplasms - pathology | 17-Hydroxysteroid Dehydrogenases - antagonists & inhibitors | Humans | Enzyme Inhibitors - pharmacology | Female | Ligands | Endometriosis - drug therapy | Breast Neoplasms - drug therapy | Enzyme Inhibitors - therapeutic use
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6. Full Text Inhibition of human and rat testicular steroidogenic enzyme activities by bisphenol A
by Ye, Leping and Zhao, Binghai and Hu, Guoxin and Chu, Yanhui and Ge, Ren-Shan
Toxicology Letters, ISSN 0378-4274, 11/2011, Volume 207, Issue 2, pp. 137 - 142
► BPA inhibited 3β-hydroxysteroid dehydrogenase activity. ► BPA inhibited CYP17A1 activity. ► BPA inhibited 17β-hydroxysteroid dehydrogenase 3 activity in... 
17β-Hydroxysteroid dehydrogenase 3 | Leydig cells | 3β-Hydroxysteroid dehydrogenase | CYP17A1 | TESTOSTERONE SYNTHESIS | 17 beta-Hydroxysteroid dehydrogenase 3 | REGULATORY STAR PROTEIN | TOXICOLOGY | OCTYLPHENOL | 3 beta-Hydroxysteroid dehydrogenase | DEHYDROGENASE | Steroid 17-alpha-Hydroxylase - antagonists & inhibitors | Testis - metabolism | Benzhydryl Compounds | Leydig Cells - enzymology | 17-Hydroxysteroid Dehydrogenases - antagonists & inhibitors | Humans | Rats | Testosterone - biosynthesis | Male | Leydig Cells - drug effects | Rats, Sprague-Dawley | Testis - drug effects | 3-Hydroxysteroid Dehydrogenases - antagonists & inhibitors | Animals | Leydig Cells - metabolism | Testis - enzymology | 3-Hydroxysteroid Dehydrogenases - metabolism | Steroid 17-alpha-Hydroxylase - metabolism | 17-Hydroxysteroid Dehydrogenases - metabolism | Phenols - pharmacology | Bisphenol-A | Cytochrome P-450
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7. Full Text Reductive 17beta-hydroxysteroid dehydrogenases which synthesize estradiol and inactivate dihydrotestosterone constitute major and concerted players in ER+ breast cancer cells
by Zhang, Chen-Yan and Wang, Wei-Qi and Chen, Jiong and Lin, Sheng-Xiang
Journal of Steroid Biochemistry and Molecular Biology, ISSN 0960-0760, 06/2015, Volume 150, pp. 24 - 34
The reductive 17β-hydroxysteroid dehydrogenases which catalyze the last step in estrogen activation for estrogen dependent breast cancer cells were studied.... 
Reductive 17β-HSDs | Estrogen activation | Cell viability | Breast cancer | Androgen reduction | RNA, Small Interfering - genetics | Cell Proliferation | Signal Transduction | Cell Survival | 17-Hydroxysteroid Dehydrogenases - antagonists & inhibitors | Humans | Gene Expression Regulation, Neoplastic | Estrogen Receptor alpha - antagonists & inhibitors | Estradiol Dehydrogenases - antagonists & inhibitors | Feedback, Physiological | Estrogen Receptor alpha - genetics | Cell Cycle | MCF-7 Cells | Estradiol Dehydrogenases - genetics | 17-Hydroxysteroid Dehydrogenases - genetics | Estradiol Dehydrogenases - metabolism | Cell Line, Tumor | Estrogen Receptor alpha - metabolism | 17-Hydroxysteroid Dehydrogenases - metabolism | Estradiol - biosynthesis | Dihydrotestosterone - metabolism | RNA, Small Interfering - metabolism | Estradiol | Oxidoreductases
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8. Full Text First Structure–Activity Relationship of 17β-Hydroxysteroid Dehydrogenase Type 14 Nonsteroidal Inhibitors and Crystal Structures in Complex with the Enzyme
by Braun, Florian and Bertoletti, Nicole and Möller, Gabriele and Adamski, Jerzy and Steinmetzer, Torsten and Salah, Mohamed and Abdelsamie, Ahmed S and van Koppen, Chris J and Heine, Andreas and Klebe, Gerhard and Marchais-Oberwinkler, Sandrine
Journal of Medicinal Chemistry, ISSN 0022-2623, 12/2016, Volume 59, Issue 23, pp. 10719 - 10737
17β-HSD14 belongs to the SDR family and oxidizes the hydroxyl group at position 17 of estradiol and 5-androstenediol using NAD+ as cofactor. The goal of this... 
LIBRARIES | DEHYDROGENASES | POTENT | CHEMISTRY, MEDICINAL | CATALYZED REACTIONS | BIOLOGICAL EVALUATION | ESTRONE | DERIVATIVES | EXPRESSION | BINDING | DISCOVERY | Dose-Response Relationship, Drug | 17-Hydroxysteroid Dehydrogenases - antagonists & inhibitors | Enzyme Inhibitors - chemistry | Humans | Drug Design | Enzyme Inhibitors - pharmacology | Models, Molecular | Crystallography, X-Ray | Molecular Structure | Structure-Activity Relationship | Enzyme Inhibitors - chemical synthesis | 17-Hydroxysteroid Dehydrogenases - metabolism
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9. Full Text A Chemical Genomics Approach to Drug Reprofiling in Oncology: Antipsychotic Drug Risperidone as a Potential Adenocarcinoma Treatment
by Dilly, Suzanne J and Clark, Andrew J and Marsh, Andrew and Mitchell, Daniel A and Cain, Ricky and Fishwick, Colin W.G and Taylor, Paul C
Cancer Letters, ISSN 0304-3835, 2017, Volume 393, pp. 16 - 21
Abstract Drug reprofiling is emerging as an effective paradigm for discovery of cancer treatments. Herein, an antipsychotic drug is immobilised using the Magic... 
Hematology, Oncology and Palliative Medicine | Adenocarcinoma | Chemical genomics | Drug reprofiling | 17-β-Hydroxysteroid dehydrogenase 10 | Drosophila melanogaster | THERAPEUTICS | CELLS | 17-beta-Hydroxysteroid dehydrogenase 10 | ALZHEIMERS-DISEASE | GLIDE | IDENTIFICATION | CANCER | DROSOPHILA | DISCOVERY | ONCOLOGY | ACCURATE DOCKING | INHIBITOR | Humans | 3-Hydroxyacyl CoA Dehydrogenases - metabolism | Male | Structure-Activity Relationship | 3-Hydroxyacyl CoA Dehydrogenases - genetics | Molecular Targeted Therapy | Drosophila melanogaster - genetics | Dose-Response Relationship, Drug | Prostatic Neoplasms - genetics | Time Factors | Enzyme Inhibitors - chemistry | Drug Compounding | Adenocarcinoma - genetics | Antineoplastic Agents - pharmacology | 3-Hydroxyacyl CoA Dehydrogenases - chemistry | Genomics - methods | Prostatic Neoplasms - drug therapy | Bacteriophage T7 - genetics | 3-Hydroxyacyl CoA Dehydrogenases - antagonists & inhibitors | Gene Library | 17-Hydroxysteroid Dehydrogenases - antagonists & inhibitors | Adenocarcinoma - enzymology | Enzyme Inhibitors - pharmacology | Risperidone - pharmacology | Risperidone - chemistry | Antineoplastic Agents - chemistry | Adenocarcinoma - drug therapy | Drosophila melanogaster - drug effects | Xenograft Model Antitumor Assays | Animals | Antipsychotic Agents - chemistry | Tumor Burden - drug effects | Mice, Nude | 17-Hydroxysteroid Dehydrogenases - genetics | Drug Repositioning - methods | Cell Line, Tumor | Drosophila melanogaster - enzymology | Linoleic Acids, Conjugated - chemistry | Prostatic Neoplasms - enzymology | Protein Conformation | Cell Proliferation - drug effects | Molecular Docking Simulation | Antipsychotic Agents - pharmacology | 17-Hydroxysteroid Dehydrogenases - chemistry | 17-Hydroxysteroid Dehydrogenases - metabolism | Enzymes | Antipsychotic drugs | Analysis | Genomics | Genetic research | Genetic aspects | Drug therapy | Prostate cancer | Cancer | Drugs | Medical colleges | Fruit-flies | Drug discovery | Polypeptides | Multiple myeloma | Oncology | Breast cancer | Genomes | Experiments | Fatty acids | Cancer therapies | Psychotropic drugs | Organic chemicals | Enzyme kinetics | Drug dosages
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10. Full Text Identification of chemically diverse, novel inhibitors of 17β-hydroxysteroid dehydrogenase type 3 and 5 by pharmacophore-based virtual screening
by Schuster, Daniela and Kowalik, Dorota and Kirchmair, Johannes and Laggner, Christian and Markt, Patrick and Aebischer-Gumy, Christel and Ströhle, Fabian and Möller, Gabriele and Wolber, Gerhard and Wilckens, Thomas and Langer, Thierry and Odermatt, Alex and Adamski, Jerzy
Journal of Steroid Biochemistry and Molecular Biology, ISSN 0960-0760, 2011, Volume 125, Issue 1, pp. 148 - 161
17β-Hydroxysteroid dehydrogenase type 3 and 5 (17β-HSD3 and 17β-HSD5) catalyze testosterone biosynthesis and thereby constitute therapeutic targets for... 
Steroid-dependent disease | Pharmacophore screening | Androgens | Inhibitor development | Estrogens | KETO REDUCTASE AKR1C3 | IN-SILICO PHARMACOLOGY | BIOCHEMISTRY & MOLECULAR BIOLOGY | 20-ALPHA-HYDROXYSTEROID DEHYDROGENASE | CRYSTAL-STRUCTURES | 11-BETA-HYDROXYSTEROID DEHYDROGENASES | 4-HYDROXYPHENYL KETONES | DISCOVERY | NONSTEROIDAL ANTIINFLAMMATORY DRUGS | ENDOCRINOLOGY & METABOLISM | PROSTAGLANDIN-F-SYNTHASE | BIOCHEMICAL EVALUATION | Enzyme Inhibitors - metabolism | 17-Hydroxysteroid Dehydrogenases - antagonists & inhibitors | Humans | Crystallography, X-Ray | Drug Discovery | Hydroxyprostaglandin Dehydrogenases - metabolism | Hydroxyprostaglandin Dehydrogenases - genetics | 3-Hydroxysteroid Dehydrogenases - antagonists & inhibitors | Hydroxyprostaglandin Dehydrogenases - antagonists & inhibitors | Aldo-Keto Reductase Family 1 Member C3 | 17-Hydroxysteroid Dehydrogenases - genetics | Enzyme Inhibitors - chemistry | HEK293 Cells | 3-Hydroxysteroid Dehydrogenases - metabolism | Ligands | 3-Hydroxysteroid Dehydrogenases - chemistry | Molecular Structure | 3-Hydroxysteroid Dehydrogenases - genetics | Hydroxyprostaglandin Dehydrogenases - chemistry | 17-Hydroxysteroid Dehydrogenases - chemistry | 17-Hydroxysteroid Dehydrogenases - metabolism | Databases, Factual
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11. Full Text Discovery of a Non-Estrogenic Irreversible Inhibitor of 17β-Hydroxysteroid Dehydrogenase Type 1 from 3‑Substituted-16β‑(m‑carbamoylbenzyl)-estradiol Derivatives
by Maltais, René and Ayan, Diana and Trottier, Alexandre and Barbeau, Xavier and Lagüe, Patrick and Bouchard, Jean-Emmanuel and Poirier, Donald
Journal of Medicinal Chemistry, ISSN 0022-2623, 01/2014, Volume 57, Issue 1, pp. 204 - 222
17β-Hydroxysteroid dehydrogenase type 1 (17β-HSD1) is thought to play a pivotal role in the progression of estrogen-sensitive breast cancer by transforming... 
BREAST-CANCER | C-16 DERIVATIVES | DEHYDROGENASES | MAINTENANCE | CHEMISTRY, MEDICINAL | THERAPY | SODIUM-IODIDE SYMPORTER | ESTRADIOL DERIVATIVES | ESTRONE | AROMATASE | CARCINOMA | Estradiol - analogs & derivatives | 17-Hydroxysteroid Dehydrogenases - antagonists & inhibitors | Humans | Enzyme Inhibitors - pharmacology | HEK293 Cells | Models, Molecular | Cell Proliferation - drug effects | Structure-Activity Relationship | Enzyme Inhibitors - chemical synthesis | Drug Discovery
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12. Full Text Substrate inhibition of 17β-HSD1 in living cells and regulation of 17β-HSD7 by 17β-HSD1 knockdown
by Han, Hui and Thériault, Jean-François and Chen, Guang and Lin, Sheng-Xiang
Journal of Steroid Biochemistry and Molecular Biology, ISSN 0960-0760, 09/2017, Volume 172, pp. 36 - 45
This study addresses first the role of human 17β-hydroxysteroid dehydrogenase type 1 (17β-HSD1) in breast cancer (BC) cells. The enzyme has a high... 
Enzyme substrate inhibition | Reductive 17β-hydroxysteroid dehydrogenases | Breast cancer | Estradiol regulation of 17β-hydroxysteroid dehydrogenase type 7 | Enzymology | Reductive | CANCER CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | HUMAN ESTROGENIC 17-BETA-HYDROXYSTEROID-DEHYDROGENASE | 17 beta-hydroxysteroid dehydrogenases | PROLIFERATION | ESTRONE REDUCTION | Estradiol regulation of 17 beta-hydroxysteroid dehydrogenase type 7 | 3-DIMENSIONAL STRUCTURE | ENZYME | STEROID DEHYDROGENASE | ESTRADIOL | ENDOCRINOLOGY & METABOLISM | TYPE-1 17-BETA-HYDROXYSTEROID-DEHYDROGENASE | HUMAN-BREAST-CARCINOMA | RNA, Small Interfering - genetics | Epithelial Cells - metabolism | Epithelial Cells - drug effects | Humans | Substrate Specificity | 17-Hydroxysteroid Dehydrogenases - isolation & purification | MCF-7 Cells | Dihydrotestosterone - pharmacology | Female | Placenta - chemistry | Epithelial Cells - cytology | Binding Sites | Estradiol - pharmacology | Dihydrotestosterone - metabolism | Estradiol - metabolism | Gene Expression | Protein Structure, Secondary | 17-Hydroxysteroid Dehydrogenases - antagonists & inhibitors | Models, Molecular | Pregnancy | Feedback, Physiological | 17-Hydroxysteroid Dehydrogenases - genetics | Cell Line, Tumor | Protein Binding | Kinetics | 17-Hydroxysteroid Dehydrogenases - metabolism | RNA, Small Interfering - metabolism
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13. Full Text Structural basis for inhibition of 17β-hydroxysteroid dehydrogenases by phytoestrogens: The case of fungal 17β-HSDcl
by Cassetta, Alberto and Stojan, Jure and Krastanova, Ivet and Kristan, Katja and Brunskole Švegelj, Mojca and Lamba, Doriano and Lanišnik Rižner, Tea
Journal of Steroid Biochemistry and Molecular Biology, ISSN 0960-0760, 07/2017, Volume 171, pp. 80 - 93
Phytoestrogens are plant-derived compounds that functionally and structurally mimic mammalian estrogens. Phytoestrogens have broad inhibitory activities toward... 
Hydroxysteroid dehydrogenases | Phytoestrogens | Flavonoids | Structure–activity relationships | Structural biology | Enzyme inhibition kinetics | COENZYME | CONSTANTS | BIOCHEMISTRY & MOLECULAR BIOLOGY | CRYSTALLOGRAPHY | Structure-activity relationships | COCHLIOBOLUS-LUNATUS | GENISTEIN | SUBSTRATE-SPECIFICITY | ENDOCRINOLOGY & METABOLISM | TYPE-1 | INSIGHTS | Fungal Proteins - chemistry | Molecular Conformation | Phytoestrogens - chemistry | Crystallography, X-Ray | Holoenzymes - chemistry | Fungal Proteins - antagonists & inhibitors | Structure-Activity Relationship | Holoenzymes - metabolism | Genistein - metabolism | Databases, Protein | Enzyme Inhibitors - chemistry | Kaempferols - metabolism | Binding Sites | Recombinant Proteins - metabolism | Biocatalysis | Enzyme Inhibitors - metabolism | Hydroxylation | Kaempferols - chemistry | 17-Hydroxysteroid Dehydrogenases - antagonists & inhibitors | Models, Molecular | Recombinant Proteins - chemistry | Genistein - chemistry | Ascomycota - enzymology | Fungal Proteins - genetics | 17-Hydroxysteroid Dehydrogenases - genetics | Flavonoids - metabolism | Phytoestrogens - metabolism | Protein Conformation | Holoenzymes - genetics | 17-Hydroxysteroid Dehydrogenases - chemistry | 17-Hydroxysteroid Dehydrogenases - metabolism | Dietary Supplements | Flavonoids - chemistry | Fungal Proteins - metabolism
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14. Full Text Sirtuin 4 Regulates Lipopolysaccharide Mediated Leydig Cell Dysfunction
by Ramatchandirin, Balamurugan and Sadasivam, Mohanraj and Kannan, Arun and Prahalathan, Chidambaram
Journal of Cellular Biochemistry, ISSN 0730-2312, 04/2016, Volume 117, Issue 4, pp. 904 - 916
ABSTRACT Bacterial lipopolysaccharide (LPS) is the most important contributing factor in pathogenesis of bacterial infection in male accessory glands; and it... 
LEYDIG CELLS | SIRT4 | STEROIDOGENESIS | APOPTOSIS | LPS | SIGNALING PATHWAYS | OXIDATIVE STRESS | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | MITOCHONDRIA | RECEPTOR | SUPPRESSION | CELL BIOLOGY | EXPRESSION | Leydig Cells - cytology | Apoptosis - drug effects | Glutathione - metabolism | JNK Mitogen-Activated Protein Kinases - metabolism | Male | Leydig Cells - drug effects | Lipopolysaccharides - antagonists & inhibitors | Stilbenes - pharmacology | Membrane Potential, Mitochondrial - drug effects | RNA, Messenger - metabolism | 3-Hydroxysteroid Dehydrogenases - antagonists & inhibitors | Glutathione - agonists | Leydig Cells - metabolism | 3-Hydroxysteroid Dehydrogenases - metabolism | JNK Mitogen-Activated Protein Kinases - genetics | Sirtuins - genetics | Cell Line | Cell Survival - drug effects | Signal Transduction | 17-Hydroxysteroid Dehydrogenases - antagonists & inhibitors | RNA, Messenger - genetics | Gene Expression Regulation | Rats | Glutathione - antagonists & inhibitors | Antioxidants - pharmacology | Mitochondria - drug effects | Animals | 17-Hydroxysteroid Dehydrogenases - genetics | Lipopolysaccharides - pharmacology | 3-Hydroxysteroid Dehydrogenases - genetics | 17-Hydroxysteroid Dehydrogenases - metabolism | Sirtuins - metabolism | Bacterial infections | RNA | Mitogens | Resveratrol
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