@article{MTMT:3097533, title = {Comparative investigation of the in vitro inhibitory potencies of 13-epimeric estrones and D-secoestrones towards 17β-hydroxysteroid dehydrogenase type 1}, url = {https://m2.mtmt.hu/api/publication/3097533}, author = {Herman, Bianka Edina and Szabó, Johanna and Bacsa, Ildikó and Wölfling, János and Schneider, Gyula and Bálint, Mónika Enikő and Hetényi, Csaba and Mernyák, Erzsébet and Szécsi, Mihály}, doi = {10.1080/14756366.2016.1204610}, journal-iso = {J ENZYM INHIB MED CH}, journal = {JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY}, volume = {31}, unique-id = {3097533}, issn = {1475-6366}, abstract = {The inhibitory effects of 13-epimeric estrones, D-secooxime and D-secoalcohol estrone compounds on human placental 17β-hydroxysteroid dehydrogenase type 1 isozyme (17β-HSD1) were investigated. The transformation of estrone to 17β-estradiol was studied by an in vitro radiosubstrate incubation method. 13α-Estrone inhibited the enzyme activity effectively with an IC50 value of 1.2 μM, which indicates that enzyme affinity is similar to that of the natural estrone substrate. The 13β derivatives and the compounds bearing a 3-hydroxy group generally exerted stronger inhibition than the 13α and 3-ether counterparts. The 3-hydroxy-13β-D-secoalcohol and the 3-hydroxy-13α-D-secooxime displayed an outstanding cofactor dependence, i.e. more efficient inhibition in the presence of NADH than NADPH. The 3-hydroxy-13β-D-secooxime has an IC50 value of 0.070 μM and is one of the most effective 17β-HSD1 inhibitors reported to date in the literature. © 2016 Informa UK Limited, trading as Taylor & Francis Group.}, keywords = {NADPH; NADH; 13α-estrone; D-secoestrone; 17β-HSD1 inhibition}, year = {2016}, eissn = {1475-6374}, pages = {61-69}, orcid-numbers = {Bacsa, Ildikó/0000-0001-8277-631X; Wölfling, János/0000-0002-3037-309X; Mernyák, Erzsébet/0000-0003-4494-1817; Szécsi, Mihály/0000-0002-4272-1362} } @article{MTMT:2939481, title = {Synthesis and in vitro pharmacological evaluation of N-[(1-benzyl-1,2,3-triazol-4-yl)methyl]-carboxamides on d-secoestrone scaffolds}, url = {https://m2.mtmt.hu/api/publication/2939481}, author = {Szabó, Johanna and Bacsa, Ildikó and Wölfling, János and Schneider, Gyula and Zupkó, István and Varga, Mónika and Herman, Bianka Edina and Kalmár, László and Szécsi, Mihály and Mernyák, Erzsébet}, doi = {10.3109/14756366.2015.1050008}, journal-iso = {J ENZYM INHIB MED CH}, journal = {JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY}, volume = {31}, unique-id = {2939481}, issn = {1475-6366}, year = {2016}, eissn = {1475-6374}, pages = {574-579}, orcid-numbers = {Bacsa, Ildikó/0000-0001-8277-631X; Wölfling, János/0000-0002-3037-309X; Zupkó, István/0000-0003-3243-5300; Szécsi, Mihály/0000-0002-4272-1362; Mernyák, Erzsébet/0000-0003-4494-1817} } @article{MTMT:2994658, title = {Synthesis of A-ring halogenated 13alpha-estrone derivatives as potential 17beta-HSD1 inhibitors}, url = {https://m2.mtmt.hu/api/publication/2994658}, author = {Bacsa, Ildikó and Jójárt, Rebeka and Schneider, Gyula and Wölfling, János and Maróti, Péter and Herman, Bianka Edina and Szécsi, Mihály and Mernyák, Erzsébet}, doi = {10.1016/j.steroids.2015.10.008}, journal-iso = {STEROIDS}, journal = {STEROIDS}, volume = {104}, unique-id = {2994658}, issn = {0039-128X}, abstract = {13alpha-Estrone and its 3-methyl or benzyl ether were halogenated in ring A with N-bromo- or N-iodosuccinimide or 1,3-dibromo-5,5-dimethylhydantoin as electrophile triggers. The chemo- and regioselectivities of the reactions depended greatly on the nature of the substituent on C-3. Bromination of the ethers led to 2- and 4-regioisomers. Bis-halogenation occurred only in the case of the phenolic derivative. Iodination and bromination resulted in similar products, except that the 3-benzyl ether could not be iodinated under the applied conditions. The potential inhibitory action of the new halogenated 13alpha-estrones on human 17beta-hydroxysteroid dehydrogenase 1 activity was investigated via in vitro radiosubstrate incubation. Some compounds proved to be effective inhibitors, with IC50 values in the submicromolar range.}, year = {2015}, eissn = {1878-5867}, pages = {230-236}, orcid-numbers = {Bacsa, Ildikó/0000-0001-8277-631X; Wölfling, János/0000-0002-3037-309X; Szécsi, Mihály/0000-0002-4272-1362; Mernyák, Erzsébet/0000-0003-4494-1817} }