@article{MTMT:33594496,
	title = {Synthesis and Antiproliferative Activity of Steroidal Diaryl Ethers},
	url = {https://m2.mtmt.hu/api/publication/33594496},
	author = {Kovács, Édua and Ali, Hazhmat and Minorics, Renáta and Traj, Péter and Resch, Vivien Erzsébet and Paragi, Gábor and Bruszel, Bella and Zupkó, István and Mernyák, Erzsébet},
	doi = {10.3390/molecules28031196},
	journal-iso = {MOLECULES},
	journal = {MOLECULES},
	volume = {28},
	unique-id = {33594496},
	issn = {1420-3049},
	abstract = {Novel 13α-estrone derivatives have been synthesized via direct arylation of the phenolic hydroxy function. Chan–Lam couplings of arylboronic acids with 13α-estrone as a nucleophilic partner were carried out under copper catalysis. The antiproliferative activities of the newly synthesized diaryl ethers against a panel of human cancer cell lines (A2780, MCF-7, MDA-MB 231, HeLa, SiHa) were investigated by means of MTT assays. The quinoline derivative displayed substantial antiproliferative activity against MCF-7 and HeLa cell lines with low micromolar IC50 values. Disturbance of tubulin polymerization has been confirmed by microplate-based photometric assay. Computational calculations reveal significant interactions of the quinoline derivative with the taxoid binding site of tubulin.},
	year = {2023},
	eissn = {1420-3049},
	orcid-numbers = {Minorics, Renáta/0000-0001-9685-813X; Resch, Vivien Erzsébet/0000-0003-0044-5731; Paragi, Gábor/0000-0001-5408-1748; Zupkó, István/0000-0003-3243-5300; Mernyák, Erzsébet/0000-0003-4494-1817}
}

@article{MTMT:33394853,
	title = {Inhibitor of Glucosinolate Sulfatases as a Potential Friendly Insecticide to Control Plutella xylostella},
	url = {https://m2.mtmt.hu/api/publication/33394853},
	author = {Li, Dehong and Wen, Yingjie and Ou, Ziyue and Yu, Ye and Zhao, Chen and Lin, Fei and Xu, Hanhong},
	doi = {10.1021/acs.jafc.2c04542},
	journal-iso = {J AGR FOOD CHEM},
	journal = {JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY},
	volume = {70},
	unique-id = {33394853},
	issn = {0021-8561},
	abstract = {The glucosinolate-myrosinase system is a two-component defense system characteristic of cruciferous plants. To evade the glucosinolate-myrosinase system, the crucifer specialist insect, Plutella xylostella, promptly desulfates the glucosinolates into harmless compounds by glucosinolate sulfatases (GSSs) in the gut. In this study, we identified an effective inhibitor of GSSs by virtual screening, molecular docking analysis, and in vitro enzyme inhibition assay. The combined effect of the GSS inhibitor with the plant glucosinolate-myrosinase system was assessed by the bioassay of P. xylostella. We show that irosustat is a GSS inhibitor and the inhibition of GSSs impairs the ability of P. xylostella to detoxify the glucosinolate-myrosinase system, leading to the systematic accumulation of toxic isothiocyanates in larvae, thereby severely affecting feeding, growth, survival, and reproduction of P. xylostella. While fed on the Arabidopsis mutants deficient in myrosinase or glucosinolates, irosustat had no significant negative effect on P. xylostella. These findings reveal that the GSS inhibitor is a novel friendly insecticide to control P. xylostella utilizing the plant glucosinolate-myrosinase system and promote the development of insecticide-plant chemical defense combination strategies.},
	keywords = {INHIBITOR; detoxification; sulfatase; glucosinolates; Plutella xylostella},
	year = {2022},
	eissn = {1520-5118},
	pages = {13528-13537},
	orcid-numbers = {Zhao, Chen/0000-0002-8042-7025}
}

@article{MTMT:33394856,
	title = {Dual Targeting of Steroid Sulfatase and 17 beta-Hydroxysteroid Dehydrogenase Type 1 by a Novel Drug-Prodrug Approach: A Potential Therapeutic Option for the Treatment of Endometriosis},
	url = {https://m2.mtmt.hu/api/publication/33394856},
	author = {Mohamed, Abdelrahman and Salah, Mohamed and Tahoun, Mariam and Hawner, Manuel and Abdelsamie, Ahmed S. and Frotscher, Martin},
	doi = {10.1021/acs.jmedchem.2c00589},
	journal-iso = {J MED CHEM},
	journal = {JOURNAL OF MEDICINAL CHEMISTRY},
	unique-id = {33394856},
	issn = {0022-2623},
	abstract = {A novel approach for the dual inhibition of steroid sulfatase (STS) and 17 beta-hydroxysteroid dehydrogenase type 1(17 beta HSD1) by a single drug was explored, starting from in-house 17 beta HSD1 inhibitors via masking their phenolic OH group with a sulfamate ester. The sulfamates were intentionally designed as drugs for the inhibition of STS and, at the same time, prodrugs for 17 beta-HSD1 inhibition ("drug-prodrug approach"). The most promising sulfamates 13, 16, 18-20, 22-24, 36, and 37 showed nanomolar IC50 values for STS inhibition in a cellular assay and their corresponding phenols displayed potent 17 beta-HSD1 inhibition in cell-free and cellular assays, high selectivity over 17 beta-HSD2, reasonable metabolic stability, and low estrogen receptor alpha affinity. A close relationship was found between the liberation of the phenolic compound by sulfamate hydrolysis and 17 beta-HSD1 inactivation. These results showed that the envisaged drug-prodrug concept was successfully implemented. The novel compounds constitute a promising class of therapeutics for the treatment of endometriosis and other estrogen-dependent diseases.},
	year = {2022},
	eissn = {1520-4804},
	orcid-numbers = {Salah, Mohamed/0000-0002-9535-6741; Tahoun, Mariam/0000-0001-8787-0399}
}

@article{MTMT:32034458,
	title = {Steroid sulfatase inhibitors: the current landscape},
	url = {https://m2.mtmt.hu/api/publication/32034458},
	author = {Anbar, H.S. and Isa, Z. and Elounais, J.J. and Jameel, M.A. and Zib, J.H. and Samer, A.M. and Jawad, A.F. and El-Gamal, M.I.},
	doi = {10.1080/13543776.2021.1910237},
	journal-iso = {EXPERT OPIN THER PAT},
	journal = {EXPERT OPINION ON THERAPEUTIC PATENTS},
	volume = {31},
	unique-id = {32034458},
	issn = {1354-3776},
	abstract = {Introduction: Steroid sulfatase (STS) enzyme is responsible for transforming the inactive sulfate metabolites of steroid sex hormones into the active free steroids. Both the deficiency and the over-expression of STS are associated with the pathophysiology of certain diseases. This article provides the readership with a comprehensive review about STS enzyme and its recently reported inhibitors. Areas covered: In the present article, we reviewed the structure, location, and substrates of STS enzyme, physiological functions of STS, and disease states related to over-expression or deficiency of STS enzyme. STS inhibitors reported during the last five years (2016-present) have been reviewed as well. Expert opinion: Irosustat is the most successful STS inhibitor drug candidate so far. It is currently under investigation in clinical trials for treatment of estrogen-dependent breast cancer. Non-steroidal sulfamate is the most favorable scaffold for STS inhibitor design. They can be beneficial for the treatment of hormone-dependent cancers and neurodegenerative disorders without significant estrogenic side effects. Moreover, dual-acting molecules (inhibitors of STS + another synergistic mechanism) can be therapeutically efficient. © 2021 Informa UK Limited, trading as Taylor & Francis Group.},
	keywords = {steroid sulfatase; STS inhibitors; Hormone-dependent cancer; STS enzyme},
	year = {2021},
	eissn = {1744-7674},
	pages = {453-472}
}

@article{MTMT:32009571,
	title = {Design, synthesis and biological evaluation of novel estrone phosphonates as high affinity organic anion-transporting polypeptide 2B1 (OATP2B1) inhibitors},
	url = {https://m2.mtmt.hu/api/publication/32009571},
	author = {Jójárt, Rebeka and Laczkó-Rigó, Réka and Klement, Máté and Kőhl, Gabriella and Kecskeméti, Gábor and Laczka, Csilla and Mernyák, Erzsébet},
	doi = {10.1016/j.bioorg.2021.104914},
	journal-iso = {BIOORG CHEM},
	journal = {BIOORGANIC CHEMISTRY},
	volume = {112},
	unique-id = {32009571},
	issn = {0045-2068},
	year = {2021},
	eissn = {1090-2120},
	orcid-numbers = {Kecskeméti, Gábor/0000-0002-5584-6869; Mernyák, Erzsébet/0000-0003-4494-1817}
}

@article{MTMT:31645359,
	title = {Synthesis and evaluation of anticancer activities of 2- or 4-substituted 3-(N-benzyltriazolylmethyl)-13α-oestrone derivatives},
	url = {https://m2.mtmt.hu/api/publication/31645359},
	author = {Jójárt, Rebeka and Senobar Tahaei, Seyyed Ashkan and Trungel-Nagy, Péter and Kele, Zoltán and Minorics, Renáta and Paragi, Gábor and Zupkó, István and Mernyák, Erzsébet},
	doi = {10.1080/14756366.2020.1838500},
	journal-iso = {J ENZYM INHIB MED CH},
	journal = {JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY},
	volume = {36},
	unique-id = {31645359},
	issn = {1475-6366},
	year = {2021},
	eissn = {1475-6374},
	pages = {58-67},
	orcid-numbers = {Kele, Zoltán/0000-0002-4401-0302; Minorics, Renáta/0000-0001-9685-813X; Paragi, Gábor/0000-0001-5408-1748; Zupkó, István/0000-0003-3243-5300; Mernyák, Erzsébet/0000-0003-4494-1817}
}

@article{MTMT:32178981,
	title = {Selective antiproliferative effect of C-2 halogenated 13α-estrones on cells expressing Organic anion-transporting polypeptide 2B1 (OATP2B1)},
	url = {https://m2.mtmt.hu/api/publication/32178981},
	author = {Laczkó-Rigó, Réka and Bakos, Éva and Jójárt, Rebeka and Tömböly, Csaba and Mernyák, Erzsébet and Laczka, Csilla},
	doi = {10.1016/j.taap.2021.115704},
	journal-iso = {TOXICOL APPL PHARM},
	journal = {TOXICOLOGY AND APPLIED PHARMACOLOGY},
	volume = {429},
	unique-id = {32178981},
	issn = {0041-008X},
	abstract = {Organic anion-transporting polypeptide 2B1 (OATP2B1) is a multispecific transporter mediating the cellular uptake of steroids and numerous drugs. OATP2B1 is abundantly expressed in the intestine and is also present in various tumors. Increased steroid hormone uptake by OATP2B1 has been suggested to promote progression of hormone dependent tumors. 13 alpha-estrones are effective inhibitors of endogenous estrogen formation and are potential candidates to inhibit proliferation of hormone dependent cancers. Recently, we have identified a variety of 13 alpha/beta-estrone-based inhibitors of OATP2B1. However, the nature of this interaction, whether these inhibitors are potential transported substrates of OATP2B1 and hence may be enriched in OATP2B1overexpressing cells, has not yet been investigated. In the current study we explored the antiproliferative effect of the most effective OATP2B1 inhibitor 13 alpha/beta-estrones in control and OATP2B1-overexpressing A431 carcinoma cells. We found an increased antiproliferative effect of 3-O-benzyl 13 alpha/beta-estrones in both mock transfected and OATP2B1-overexpressing cells. However, C-2 halogenated 13 alpha-estrones had a selective OATP2B1-mediated cell growth inhibitory effect. In order to demonstrate that increased sensitization can be attributed to OATP2B1-mediated cellular uptake, tritium labeled 2-bromo-13 alpha-estrone was synthesized for direct transport measurements. These experiments revealed increased accumulation of [H-3]2-bromo-13 alpha-estrone due to OATP2B1 function. Our results indicate that C-2 halogenated 13 alpha-estrones are good candidates in the design of anti-cancer drugs targeting OATP2B1.},
	year = {2021},
	eissn = {1096-0333},
	orcid-numbers = {Mernyák, Erzsébet/0000-0003-4494-1817}
}

@article{MTMT:32161034,
	title = {Microwave-assisted Phospha-Michael addition reactions in the 13alpha-oestrone series and in vitro antiproliferative properties},
	url = {https://m2.mtmt.hu/api/publication/32161034},
	author = {Mernyák, Erzsébet and Bartha, Sándor and Kóczán , Lili and Jójárt, Rebeka and Resch, Vivien Erzsébet and Paragi, Gábor and Vágvölgyi, Máté and Hunyadi, Attila and Bruszel, Bella and Zupkó, István and Minorics, Renáta},
	doi = {10.1080/14756366.2021.1963241},
	journal-iso = {J ENZYM INHIB MED CH},
	journal = {JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY},
	volume = {36},
	unique-id = {32161034},
	issn = {1475-6366},
	year = {2021},
	eissn = {1475-6374},
	pages = {1931-1937},
	orcid-numbers = {Mernyák, Erzsébet/0000-0003-4494-1817; Resch, Vivien Erzsébet/0000-0003-0044-5731; Paragi, Gábor/0000-0001-5408-1748; Vágvölgyi, Máté/0000-0002-2233-9422; Hunyadi, Attila/0000-0003-0074-3472; Zupkó, István/0000-0003-3243-5300; Minorics, Renáta/0000-0001-9685-813X}
}

@article{MTMT:31916683,
	title = {Transition metal-catalyzed A-ring C–H activations and C(sp2)–C(sp2) couplings in the 13α-estrone series and in vitro evaluation of antiproliferative properties},
	url = {https://m2.mtmt.hu/api/publication/31916683},
	author = {Traj, Péter and Ali, Hazhmat and Motzwickler-Németh, Anett and Dajcs, Sámuel Trisztán and Tömösi, Ferenc and Tea, Lanisnik-Rizner and Zupkó, István and Mernyák, Erzsébet},
	doi = {10.1080/14756366.2021.1900165},
	journal-iso = {J ENZYM INHIB MED CH},
	journal = {JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY},
	volume = {36},
	unique-id = {31916683},
	issn = {1475-6366},
	year = {2021},
	eissn = {1475-6374},
	pages = {895-902},
	orcid-numbers = {Tömösi, Ferenc/0000-0002-6657-5777; Zupkó, István/0000-0003-3243-5300; Mernyák, Erzsébet/0000-0003-4494-1817}
}

@article{MTMT:32096593,
	title = {Synthesis and evaluation of AKR1C inhibitory properties of A-ring halogenated oestrone derivatives},
	url = {https://m2.mtmt.hu/api/publication/32096593},
	author = {Sinreih, Maša and Jójárt, Rebeka and Kele, Zoltán and Büdefeld, Tomaž and Paragi, Gábor and Mernyák, Erzsébet and Rižner, Tea Lanišnik},
	doi = {10.1080/14756366.2021.1937142},
	journal-iso = {J ENZYM INHIB MED CH},
	journal = {JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY},
	volume = {36},
	unique-id = {32096593},
	issn = {1475-6366},
	year = {2021},
	eissn = {1475-6374},
	pages = {1500-1508},
	orcid-numbers = {Kele, Zoltán/0000-0002-4401-0302; Paragi, Gábor/0000-0001-5408-1748; Mernyák, Erzsébet/0000-0003-4494-1817}
}

@article{MTMT:32096686,
	title = {Data-Driven Ensemble Docking to Map Molecular Interactions of Steroid Analogs with Hepatic Organic Anion Transporting Polypeptides},
	url = {https://m2.mtmt.hu/api/publication/32096686},
	author = {Tuerkova, Alzbeta and Ungvári, Orsolya and Laczkó-Rigó, Réka and Mernyák, Erzsébet and Szakács, Gergely and Laczka, Csilla and Zdrazil, Barbara},
	doi = {10.1021/acs.jcim.1c00362},
	journal-iso = {J CHEM INF MODEL},
	journal = {JOURNAL OF CHEMICAL INFORMATION AND MODELING},
	volume = {61},
	unique-id = {32096686},
	issn = {1549-9596},
	year = {2021},
	eissn = {1549-960X},
	pages = {3109-3127},
	orcid-numbers = {Mernyák, Erzsébet/0000-0003-4494-1817; Zdrazil, Barbara/0000-0001-9395-1515}
}

@article{MTMT:31848935,
	title = {Effective anti-aromatase therapy to battle against estrogen-mediated breast cancer: Comparative SAR/QSAR assessment on steroidal aromatase inhibitors},
	url = {https://m2.mtmt.hu/api/publication/31848935},
	author = {Adhikari, Nilanjan and Baidya, Sandip Kumar and Jha, Tarun},
	doi = {10.1016/j.ejmech.2020.112845},
	journal-iso = {EUR J MED CHEM},
	journal = {EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {208},
	unique-id = {31848935},
	issn = {0223-5234},
	year = {2020},
	eissn = {1768-3254},
	orcid-numbers = {Baidya, Sandip Kumar/0000-0001-9362-3909; Jha, Tarun/0000-0002-9996-738X}
}

@article{MTMT:31689996,
	title = {Delta(9,11)-Estrone derivatives as potential antiproliferative agents: synthesis, in vitro biological evaluation and docking studies},
	url = {https://m2.mtmt.hu/api/publication/31689996},
	author = {Canario, Catarina and Matias, Mariana and de Brito, Vanessa and Santos, Adriana O. and Falcao, Amilcar and Silvestre, Samuel and Alves, Gilberto},
	doi = {10.5802/crchim.17},
	journal-iso = {CR CHIM},
	journal = {COMPTES RENDUS CHIMIE},
	volume = {23},
	unique-id = {31689996},
	issn = {1631-0748},
	abstract = {A series of Delta(9,11)-estrone derivatives with A- and D-ring modifications has been synthesized and evaluated as antiproliferative agents. The cytotoxicity was assessed in six cell lines (MCF-7, T47-D, LNCaP, llepaRG, Caco-2 and NUM.) by the 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide assay, and a cell cycle distribution analysis was performed by flow cytometry. Some compounds exhibited relevant cytotoxicity, particularly Delta(9,11)-estrone, which was the most active against llepaRG cells (IC50 = 6.67 mu M). Besides the relevance of the double bond in the C-ring, the presence of a 16E-benzylidene group increased the antiproliferative effect on MCF-7 and T47-D cells. Moreover, the introduction of iodine in positions 2 and 4 of estrone seemed to induce a selective cytotoxicity for I lepaRG cells. Flow cytometry experiments evidenced a 34% reduction of HepaRG cell viability after treatment with Delta(9,11)-estrone and a cell cycle arrest at the G(0)/G(1) phase. Estrogenic activity was also observed for this compound at 0.1 mu M in T47-D cells, and molecular docking studies estimated a marked interaction between this compound and the estrogen receptor alpha.},
	keywords = {Flow Cytometry; ESTRONE; Docking; ANTIPROLIFERATIVE ACTIVITY; Delta(9,11)-estrone derivatives},
	year = {2020},
	eissn = {1878-1543},
	pages = {201-217}
}

@article{MTMT:31501725,
	title = {Recent progress in the development of steroid sulphatase inhibitors - examples of the novel and most promising compounds from the last decade},
	url = {https://m2.mtmt.hu/api/publication/31501725},
	author = {Dasko, Mateusz and Demkowicz, Sebastian and Biernacki, Karol and Ciupak, Olga and Kozak, Witold and Maslyk, Maciej and Rachon, Janusz},
	doi = {10.1080/14756366.2020.1758692},
	journal-iso = {J ENZYM INHIB MED CH},
	journal = {JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY},
	volume = {35},
	unique-id = {31501725},
	issn = {1475-6366},
	abstract = {The purpose of this review article is to provide an overview of recent achievements in the synthesis of novel steroid sulphatase (STS) inhibitors. STS is a crucial enzyme in the biosynthesis of active hormones (including oestrogens and androgens) and, therefore, represents an extremely attractive molecular target for the development of hormone-dependent cancer therapies. The inhibition of STS may effectively reduce the availability of active hormones for cancer cells, causing a positive therapeutic effect. Herein, we report examples of novel STS inhibitors based on steroidal and nonsteroidal cores that contain various functional groups (e.g. sulphamate and phosphorus moieties) and halogen atoms, which may potentially be used in therapies for hormone-dependent cancers. The presented work also includes examples of multitargeting agents with STS inhibitory activities. Furthermore, the fundamental discoveries in the development of the most promising drug candidates exhibiting STS inhibitory activities are highlighted.},
	keywords = {STEROIDS; Multitargeting agents; Steroid sulphatase; STS inhibitors},
	year = {2020},
	eissn = {1475-6374},
	pages = {1163-1184},
	orcid-numbers = {Dasko, Mateusz/0000-0002-3367-6491; Demkowicz, Sebastian/0000-0002-4252-4297; Biernacki, Karol/0000-0003-3036-8693; Ciupak, Olga/0000-0003-0083-9634; Kozak, Witold/0000-0003-3253-5555}
}

@article{MTMT:31365295,
	title = {Steroidal ferrocenes as potential enzyme inhibitors of the estrogen biosynthesis},
	url = {https://m2.mtmt.hu/api/publication/31365295},
	author = {Herman, Bianka Edina and Gardi, János and Julesz, János and Tömböly, Csaba and Szánti-Pintér, Eszter and Fehér, Klaudia and Skodáné Földes, Rita and Szécsi, Mihály},
	doi = {10.1007/s42977-020-00023-7},
	journal-iso = {BIOL FUTURA},
	journal = {BIOLOGIA FUTURA},
	volume = {71},
	unique-id = {31365295},
	issn = {2676-8615},
	year = {2020},
	eissn = {2676-8607},
	pages = {249-264},
	orcid-numbers = {Szánti-Pintér, Eszter/0000-0001-8263-9884; Skodáné Földes, Rita/0000-0002-9810-1509; Szécsi, Mihály/0000-0002-4272-1362}
}

@article{MTMT:31606817,
	title = {Pd-Catalyzed Suzuki–Miyaura couplings and evaluation of 13α-estrone derivatives as potential anticancer agents},
	url = {https://m2.mtmt.hu/api/publication/31606817},
	author = {Jójárt, Rebeka and Ali, Hazhmat and Horváth, Gergely and Kele, Zoltán and Zupkó, István and Mernyák, Erzsébet},
	doi = {10.1016/j.steroids.2020.108731},
	journal-iso = {STEROIDS},
	journal = {STEROIDS},
	volume = {164},
	unique-id = {31606817},
	issn = {0039-128X},
	year = {2020},
	eissn = {1878-5867},
	orcid-numbers = {Kele, Zoltán/0000-0002-4401-0302; Zupkó, István/0000-0003-3243-5300; Mernyák, Erzsébet/0000-0003-4494-1817}
}

@article{MTMT:31453011,
	title = {Aromatase inhibitors: Role in postmenopausal breast cancer},
	url = {https://m2.mtmt.hu/api/publication/31453011},
	author = {Kharb, Rajeev and Haider, Kashif and Neha, Kumari and Yar, Mohammad S.},
	doi = {10.1002/ardp.202000081},
	journal-iso = {ARCH PHARM},
	journal = {ARCHIV DER PHARMAZIE},
	volume = {353},
	unique-id = {31453011},
	issn = {0365-6233},
	abstract = {Postmenopausal women are at high risk of developing breast cancer due to estrogen production in peripheral tissues of the body other than ovaries. Aromatase is present in breast tissue, leading to local estrogen production which can be inhibited by a variety of steroidal and nonsteroidal aromatase inhibitors. There are many aromatase inhibitors available in clinical practice like exemestane, formestane, anastrozole, letrozole, fadrozole, vorozole, and so forth, but the major challenge in anti-breast cancer therapy is the toxicity associated with aromatase inhibitors, especially the steroidal class of drugs. It is, therefore, urgently required to develop novel anticancer drugs having better safety and efficacy for the treatment of breast cancer. This study highlights the aromatase inhibitors reported in the current literature as well as the recent advances in the management of breast cancer.},
	keywords = {breast cancer; Aromatase inhibitors; Postmenopausal; heterocyclic motifs},
	year = {2020},
	eissn = {1521-4184}
}

@article{MTMT:31240434,
	title = {Structural dissection of 13-epiestrones based on the interaction with human Organic anion-transporting polypeptide, OATP2B1.},
	url = {https://m2.mtmt.hu/api/publication/31240434},
	author = {Laczkó-Rigó, Réka and Jójárt, Rebeka and Mernyák, Erzsébet and Bakos, Éva and Tuerkova, Alzbeta and Zdrazil, Barbara and Laczka, Csilla},
	doi = {10.1016/j.jsbmb.2020.105652},
	journal-iso = {J STEROID BIOCHEM MOL BIOL},
	journal = {JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY},
	volume = {200},
	unique-id = {31240434},
	issn = {0960-0760},
	abstract = {Human OATP2B1 encoded by the SLCO2B1 gene is a multispecific transporter mediating the cellular uptake of large, organic molecules, including hormones, prostaglandins and bile acids. OATP2B1 is ubiquitously expressed in the human body, with highest expression levels in pharmacologically relevant barriers, like enterocytes, hepatocytes and endothelial cells of the blood-brain-barrier. In addition to its endogenous substrates, OATP2B1 also recognizes clinically applied drugs, such as statins, antivirals, antihistamines and chemotherapeutic agents and influences their pharmacokinetics. On the other hand, OATP2B1 is also overexpressed in various tumors. Considering that elevated hormone uptake by OATP2B1 results in increased cell proliferation of hormone dependent tumors (e.g. breast or prostate), inhibition of OATP2B1 can be a good strategy to inhibit the growth of these tumors. 13-epiestrones represent a potential novel strategy in the treatment of hormone dependent cancers by the suppression of local estrogen production due to the inhibition of the key enzyme of estrone metabolism, 17ß-hydroxysteroid-dehydrogenase type 1 (HSD17ß1). Recently, we have demonstrated that various phosphonated 13-epiestrones are dual inhibitors also suppressing OATP2B1 function. In order to gain better insights into the molecular determinants of OATP2B1 13-epiestrone interaction we investigated the effect of C-2 and C-4 halogen or phenylalkynyl modified epiestrones on OATP2B1 transport function. Potent inhibitors (with EC50 values in the low micromolar range) as well as non-inhibitors of OATP2B1 function were identified. Based on the structure-activity relationship (SAR) of the various 13-epiestrone derivatives we could define structural elements important for OATP2B1 inhibition. Our results may help to understand the drug/inhibitor interaction profile of OATP2B1, and also may be a useful strategy to block steroid hormone entry into tumors.},
	keywords = {INHIBITOR; SAR; Organic anion-transporting polypeptide; 13-epiestrones},
	year = {2020},
	eissn = {1879-1220},
	orcid-numbers = {Mernyák, Erzsébet/0000-0003-4494-1817}
}

@article{MTMT:31692545,
	title = {Decarboxylative Bromination of Heteroarenes: Initial Mechanistic Insights},
	url = {https://m2.mtmt.hu/api/publication/31692545},
	author = {Patel, Pritesh R. and Henderson, Scott H. and Roe, Mark S. and Honey, Mark A.},
	doi = {10.1055/s-0040-1707901},
	journal-iso = {SYNLETT},
	journal = {SYNLETT},
	volume = {31},
	unique-id = {31692545},
	issn = {0936-5214},
	abstract = {After an initial report from our laboratory describing metal-free decarboxylative halogenation of various azaheteroarenes, we set out to investigate the possible mechanism by which this chemistry occurs. Evidence from this mechanistic investigation suggests that this chemistry occurs via a radical pathway, with(1)H NMR studies suggesting that the acidic substrates activate NBS.},
	keywords = {reaction mechanism; Halogenation; decarboxylation; bromosuccinimide; azahetarenes},
	year = {2020},
	eissn = {1437-2096},
	pages = {1603-1607}
}

@article{MTMT:31575515,
	title = {Estrogen Receptor alpha (ER alpha)-targeting Compounds and Derivatives: Recent Advances in Structural Modification and Bioactivity},
	url = {https://m2.mtmt.hu/api/publication/31575515},
	author = {Guo, Wei-Yun and Zeng, Shang-Ming-Zhu and Deora, Girdhar Singh and Li, Qing-Shan and Ruan, Ban-Feng},
	doi = {10.2174/1568026619666190619142504},
	journal-iso = {CURR TOP MED CHEM},
	journal = {CURRENT TOPICS IN MEDICINAL CHEMISTRY},
	volume = {19},
	unique-id = {31575515},
	issn = {1568-0266},
	abstract = {Breast cancer is the most common cancer suffered by female, and the second highest cause of cancer-related death among women worldwide. At present, hormone therapy is still the main treatment route and can be divided into three main categories: selective estrogen receptor modulators (SERMs), selective estrogen receptor downregulators (SERDs), and aromatase inhibitors (AIs). However, breast cancer is difficult to cure even after several rounds of anti-estrogen therapy and most drugs have serious side-effects. Here, we review the literature published over the past five years regarding the isolation and synthesis of analogs and their derivatives.},
	keywords = {DERIVATIVES; ANALOGS; Estrogen Receptor alpha; structure-activity relationship; breast cancer; BIOACTIVITY},
	year = {2019},
	eissn = {1873-4294},
	pages = {1318-1337},
	orcid-numbers = {Deora, Girdhar Singh/0000-0001-9857-101X}
}

@article{MTMT:30672179,
	title = {Synthesis, Biological Evaluation and Docking Studies of 13-Epimeric 10-fluoro- and 10-Chloroestra-1,4-dien-3-ones as Potential Aromatase Inhibitors},
	url = {https://m2.mtmt.hu/api/publication/30672179},
	author = {Jójárt, Rebeka and Traj, Péter and Kovács, Édua and Horváth, Ágnes and Schneider, Gyula and Szécsi, Mihály and Pál, Attila and Paragi, Gábor and Mernyák, Erzsébet},
	doi = {10.3390/molecules24091783},
	journal-iso = {MOLECULES},
	journal = {MOLECULES},
	volume = {24},
	unique-id = {30672179},
	issn = {1420-3049},
	year = {2019},
	eissn = {1420-3049},
	orcid-numbers = {Szécsi, Mihály/0000-0002-4272-1362; Paragi, Gábor/0000-0001-5408-1748; Mernyák, Erzsébet/0000-0003-4494-1817}
}

@article{MTMT:30555885,
	title = {Preparation of two steroid derivatives and its theoretical interaction with a 17 beta-hydroxysteroid dehydrogenase type 1},
	url = {https://m2.mtmt.hu/api/publication/30555885},
	author = {Lauro, Figueroa-Valverde and Abelardo, Camacho-Luis and Francisco, Diaz-Cedillo and Marcela, Rosas-Nexticapa and Virginia, Mateu-Armand and Patricia, Hernandez-Vasquez and Eduardo, Pool-Gomez and Maria, Lopez-Ramos and Lenin, Hau-Heredia and Tomas Joel, Lopez-Gutierrez and Bety, Sarabia-Alcocer and Alondra, Alfonso-Jimenez and Jhair, Cabrera-Tuz},
	doi = {10.33263/BRIAC91.800805},
	journal-iso = {BIOINTERF RES APPL CHEM},
	journal = {BIOINTERFACE RESEARCH IN APPLIED CHEMISTRY},
	volume = {9},
	unique-id = {30555885},
	issn = {2069-5837},
	abstract = {The aim of this study was synthesizing two steroid derivatives to evaluate their theoretical interact with a 17 beta-hydroxysteroid dehydrogenase type 1. The first stage was achieved by the preparation of a steroid-imino analog (compound 2) using a reaction of imination and ii) etherification. Then, the theoretical interact of two steroid analogs with 17 beta-hydroxysteroid dehydrogenase type 1 (IIOL) was evaluated using fisetin and methyl paraben as controls in a docking model. The results suggest that steroid derivatives could interact via a different type of aminoacid residues of IIOL protein surface. However, the compound 2 showed a constant of inhibition lower compared with fisetin, methyl paraben and compound 3. All these data indicate that steroid derivative could act as 17 beta-hydroxysteroid dehydrogenase type 1 inhibitor.},
	keywords = {Docking; fisetin; paraben; 17 beta-hydroxysteroid hydrogenase},
	year = {2019},
	pages = {3800-3805}
}

@article{MTMT:30331520,
	title = {Pd-Catalyzed microwave-assisted synthesis of phosphonated 13α-estrones as potential OATP2B1, 17β-HSD1 and/or STS inhibitors},
	url = {https://m2.mtmt.hu/api/publication/30331520},
	author = {Jójárt, Rebeka and Pécsy, S. and Keglevich, György and Szécsi, Mihály and Laczkó-Rigó, Réka and Laczka, Csilla and Kecskeméti, Gábor and Mernyák, Erzsébet},
	doi = {10.3762/bjoc.14.262},
	journal-iso = {BEILSTEIN J ORG CHEM},
	journal = {BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY},
	volume = {14},
	unique-id = {30331520},
	issn = {1860-5397},
	abstract = {Novel 2- or 4-phosphonated 13 alpha-estrone derivatives were synthesized via the Hirao reaction. Bromo regioisomers (2- or 4-) of 13 alpha-estrone and its 3-benzyl or 3-methyl ether were reacted with diethyl phosphite or diphenylphosphine oxide using Pd(PPh3)(4) as catalyst under microwave irradiation. The influence of the new compounds on the transport function of the organic anion transporting polypeptide OATP2B1 was investigated by measuring Cascade Blue uptake. Derivatives bearing a 3-benzyl ether function displayed substantial submicromolar OATP2B1 inhibitory activity. The inhibitory effects of the compounds on human placental steroid sulfatase (STS) and 17 beta-hydroxysteroid dehydrogenase type 1 isozyme (17 beta-HSD1) were investigated by in vitro radiosub-strate incubation methods. None of the test compounds inhibited the STS markedly. The structure-activity relationship evaluation revealed that 2-substituted 3-hydroxy derivatives are able to inhibit the 17 beta-HSD1 enzyme with submicromolar IC50 values. Dual OATP2B1 and 17 beta-HSD1 inhibitors have been identified.},
	keywords = {ENZYME; CATALYSIS; STS; Hirao reaction; OATP2B1; 13 alpha-estrone; 17 beta-HSD1 inhibition},
	year = {2018},
	eissn = {1860-5397},
	pages = {2838-2845},
	orcid-numbers = {Szécsi, Mihály/0000-0002-4272-1362; Kecskeméti, Gábor/0000-0002-5584-6869; Mernyák, Erzsébet/0000-0003-4494-1817}
}