@article{MTMT:34766036,
	title = {Effects of Chrysin and Chrysin-7-sulfate on Ochratoxin A-Albumin Interactions and on the Plasma and Kidney Levels of the Mycotoxin in Rats},
	url = {https://m2.mtmt.hu/api/publication/34766036},
	author = {Poór, Miklós and Dombi, Ágnes and Fliszár-Nyúl, Eszter and Pedroni, Lorenzo and Dellafiora, Luca},
	doi = {10.1021/acsomega.4c01738},
	journal-iso = {ACS OMEGA},
	journal = {ACS OMEGA},
	volume = {9},
	unique-id = {34766036},
	issn = {2470-1343},
	year = {2024},
	eissn = {2470-1343},
	pages = {17655-17666},
	orcid-numbers = {Fliszár-Nyúl, Eszter/0000-0003-0923-0059; Dellafiora, Luca/0000-0002-1901-3317}
}

@article{MTMT:33633568,
	title = {Impacts of β-cyclodextrin bead polymer (BBP) treatment on the quality of red and white wines: Color, polyphenol content, and electronic tongue analysis},
	url = {https://m2.mtmt.hu/api/publication/33633568},
	author = {Fliszár-Nyúl, Eszter and Zinia Zaukuu, John-Lewis and Szente, Lajos and Kovács, Zoltán and Poór, Miklós},
	doi = {10.1016/j.lwt.2023.114567},
	journal-iso = {LWT-FOOD SCI TECHNOL},
	journal = {LWT-FOOD SCIENCE AND TECHNOLOGY},
	volume = {176},
	unique-id = {33633568},
	issn = {0023-6438},
	year = {2023},
	eissn = {1096-1127},
	orcid-numbers = {Fliszár-Nyúl, Eszter/0000-0003-0923-0059}
}

@article{MTMT:33547988,
	title = {Interactions of Mycotoxin Alternariol with Cytochrome P450 Enzymes and OATP Transporters},
	url = {https://m2.mtmt.hu/api/publication/33547988},
	author = {Fliszár-Nyúl, Eszter and Ungvári, Orsolya and Dombi, Ágnes and Laczka, Csilla and Poór, Miklós},
	doi = {10.3390/metabo13010045},
	journal-iso = {METABOLITES},
	journal = {METABOLITES},
	volume = {13},
	unique-id = {33547988},
	issn = {2218-1989},
	abstract = {Alternariol (AOH) is an emerging mycotoxin produced by Alternaria strains. The acute toxicity of the mycotoxin is low; however, chronic exposure to AOH may result in the development of endocrine disruptor and/or carcinogenic effects. The toxicokinetic properties of AOH have barely been characterized. Therefore, in this study, we aimed to investigate its interactions with CYP (1A2, 2C9, 2C19, 2D6, and 3A4) enzymes and OATP (1A2, 1B1, 1B3, and 2B1) transporters employing in vitro enzyme assays and OATP overexpressing cells, respectively. Our results demonstrated that AOH is a strong inhibitor of CYP1A2 (IC50 = 0.15 μM) and CYP2C9 (IC50 = 7.4 μM). Based on the AOH depletion assays in the presence of CYP enzymes, CYP1A2 is mainly involved, while CYP2C19 is moderately involved in the CYP-catalyzed biotransformation of the mycotoxin. AOH proved to be a strong inhibitor of each OATP transporter examined (IC50 = 1.9 to 5.4 μM). In addition, both direct and indirect assays suggest the involvement of OATP1B1 in the cellular uptake of the mycotoxin. These findings promote the deeper understanding of certain toxicokinetic interactions of AOH.},
	year = {2023},
	eissn = {2218-1989},
	orcid-numbers = {Fliszár-Nyúl, Eszter/0000-0003-0923-0059; Poór, Miklós/0000-0003-1425-7459}
}

@article{MTMT:33294693,
	title = {Interaction of luteolin, naringenin, and their sulfate and glucuronide conjugates with human serum albumin, cytochrome P450 (CYP2C9, CYP2C19, and CYP3A4) enzymes and organic anion transporting polypeptide (OATP1B1 and OATP2B1) transporters},
	url = {https://m2.mtmt.hu/api/publication/33294693},
	author = {Kaci, Hana and Bodnárová, Slávka and Fliszár-Nyúl, Eszter and Lemli, Beáta and Pelantová, Helena and Valentová, Kateřina and Bakos, Éva and Laczka, Csilla and Poór, Miklós},
	doi = {10.1016/j.biopha.2022.114078},
	journal-iso = {BIOMED PHARMACOTHER},
	journal = {BIOMEDICINE & PHARMACOTHERAPY},
	volume = {157},
	unique-id = {33294693},
	issn = {0753-3322},
	abstract = {Luteolin and naringenin are flavonoids found in various foods/beverages and present in certain dietary supplements. After a high intake of these flavonoids, their sulfate and glucuronide conjugates reach micromolar concentrations in the bloodstream. Some pharmacokinetic interactions of luteolin and naringenin have been investigated in previous studies; however, only limited data are available in regard to their metabolites. In this study, we aimed to investigate the interactions of the sulfate and glucuronic acid conjugates of luteolin and naringenin with human serum albumin, cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes, and organic anion transporting polypeptide (OATP1B1 and OATP2B1) transporters. Our main findings are as follows: (1) Sulfate conjugates formed more stable complexes with albumin than the parent flavonoids. (2) Luteolin and naringenin conjugates showed no or only weak inhibitory action on the CYP enzymes examined. (3) Certain conjugates of luteolin and naringenin are potent inhibitors of OATP1B1 and/or OATP2B1 enzymes. (4) Conjugated metabolites of luteolin and naringenin may play an important role in the pharmacokinetic interactions of these flavonoids.},
	year = {2023},
	eissn = {1950-6007},
	orcid-numbers = {Fliszár-Nyúl, Eszter/0000-0003-0923-0059; Lemli, Beáta/0000-0001-8903-1337}
}

@article{MTMT:33258382,
	title = {Testing Serum Albumins and Cyclodextrins as Potential Binders of the Mycotoxin Metabolites Alternariol-3-Sulfate, Alternariol-9-Monomethylether and Alternariol-9-Monomethylether-3-Sulfate},
	url = {https://m2.mtmt.hu/api/publication/33258382},
	author = {Lemli, Beáta and Vilmányi, Péter and Fliszár-Nyúl, Eszter and Zsidó, Balázs Zoltán and Hetényi, Csaba and Szente, Lajos and Poór, Miklós},
	doi = {10.3390/ijms232214353},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {23},
	unique-id = {33258382},
	issn = {1661-6596},
	abstract = {Alternaria mycotoxins, including alternariol (AOH), alternariol-9-monomethylether (AME), and their masked/modified derivatives (e.g., sulfates or glycosides), are common food contaminants. Their acute toxicity is relatively low, while chronic exposure can lead to the development of adverse health effects. Masked/modified metabolites can probably release the more toxic parent mycotoxin due to their enzymatic hydrolysis in the intestines. Previously, we demonstrated the complex formation of AOH with serum albumins and cyclodextrins; these interactions were successfully applied for the extraction of AOH from aqueous matrices (including beverages). Therefore, in this study, the interactions of AME, alternariol-3-sulfate (AS), and alternariol-9-monomethylether-3-sulfate (AMS) were investigated with albumins (human, bovine, porcine, and rat) and with cyclodextrins (sulfobutylether-β-cyclodextrin, sugammadex, and cyclodextrin bead polymers). Our major results/conclusions are the following: (1) The stability of mycotoxin–albumin complexes showed only minor species dependent variations. (2) AS and AMS formed highly stable complexes with albumins in a wide pH range, while AME–albumin interactions preferred alkaline conditions. (3) AME formed more stable complexes with the cyclodextrins examined than AS and AMS. (4) Beta-cyclodextrin bead polymer proved to be highly suitable for the extraction of AME, AS, and AMS from aqueous solution. (5) Albumins and cyclodextrins are promising binders of the mycotoxins tested.},
	year = {2022},
	eissn = {1422-0067},
	orcid-numbers = {Lemli, Beáta/0000-0001-8903-1337; Fliszár-Nyúl, Eszter/0000-0003-0923-0059}
}

@article{MTMT:33092073,
	title = {Analysis and Comparison of Rapid Methods for the Determination of Ochratoxin A Levels in Organs and Body Fluids Obtained from Exposed Mice},
	url = {https://m2.mtmt.hu/api/publication/33092073},
	author = {Szőke, Zsuzsanna and Babarczi, Bianka and Mézes, Miklós and Lakatos, István and Poór, Miklós and Fliszár-Nyúl, Eszter and Oldal, Miklós and Czéh, Árpád and Bodó, Kornélia and Nagyéri, György and Ferenczi, Szilamér},
	doi = {10.3390/toxins14090634},
	journal-iso = {TOXINS},
	journal = {TOXINS},
	volume = {14},
	unique-id = {33092073},
	issn = {2072-6651},
	abstract = {Mycotoxins are bioaccumulative contaminants impacting animals and humans. The simultaneous detection of frequent active exposures and accumulated mycotoxin level (s) in exposed organisms would be the most ideal to enable appropriate actions. However, few methods are available for the purpose, and there is a demand for dedicated, sensitive, reliable, and practical assays. To demonstrate the issue, mice were exposed to a relevant agent Ochratoxin A (OTA), and accumulated OTA was measured by fine-tuned commercial assays. Quantitative high-performance liquid chromatography with fluorescence detection, enzyme-linked immunosorbent assay, and flow cytometry assays have been developed/modified using reagents available as commercial products when appropriate. Assays were performed on excised samples, and results were compared. Accumulated OTA could be detected and quantified; positive correlations (between applied doses of exposure and accumulated OTA levels and the results from assays) were found. Dedicated assays could be developed, which provided comparable results. The presence and accumulation of OTA following even a short exposure could be quantitatively detected. The assays performed similarly, but HPLC had the greatest sensitivity. Blood contained higher levels of OTA than liver and kidney. We demonstrate that specific but flexible and practical assays should be used for specific/local purposes, to measure the exposure itself and accumulation in blood or organs.},
	keywords = {exposure; ACCUMULATION; Flow Cytometry; ELISA; OCHRATOXIN-A; MYCOTOXINS; ochratoxin A; Analytical methods; HPLC–FLD},
	year = {2022},
	eissn = {2072-6651},
	orcid-numbers = {Poór, Miklós/0000-0003-1425-7459; Fliszár-Nyúl, Eszter/0000-0003-0923-0059}
}

@article{MTMT:33088493,
	title = {Testing the Protective Effects of Sulfobutylether-Βeta-Cyclodextrin (SBECD) and Sugammadex against Chlorpromazine-Induced Acute Toxicity in SH-SY5Y Cell Line and in NMRI Mice},
	url = {https://m2.mtmt.hu/api/publication/33088493},
	author = {Fliszár-Nyúl, Eszter and Jakabfi-Csepregi, Rita and Benkovics, Gábor and Szente, Lajos and Poór, Miklós},
	doi = {10.3390/pharmaceutics14091888},
	journal-iso = {PHARMACEUTICS},
	journal = {PHARMACEUTICS},
	volume = {14},
	unique-id = {33088493},
	issn = {1999-4923},
	abstract = {Chlorpromazine (CPZ) is an antipsychotic drug which can cause several adverse effects and drug poisoning. Recent studies demonstrated that CPZ forms highly stable complexes with certain cyclodextrins (CDs) such as sulfobutylether-β-CD (SBECD) and sugammadex (SGD). Since there is no available antidote in CPZ intoxication, and considering the good tolerability of these CDs even if when administered parenterally, we aimed to investigate the protective effects of SBECD and SGD against CPZ-induced acute toxicity employing in vitro (SH-SY5Y neuroblastoma cells) and in vivo (zebrafish embryo) models. Our major findings and conclusions are the following: (1) both SBECD and SGD strongly relieved the cytotoxic effects of CPZ in SH-SY5Y cells. (2) SGD co-treatment did not affect or increase the CPZ-induced 24 h mortality in NMRI mice, while SBECD caused a protective effect in a dose-dependent fashion. (3) The binding constants of ligand–CD complexes and/or the in vitro protective effects of CDs can help to estimate the in vivo suitability of CDs as antidotes; however, some other factors can overwrite these predictions.},
	year = {2022},
	eissn = {1999-4923},
	orcid-numbers = {Fliszár-Nyúl, Eszter/0000-0003-0923-0059}
}

@article{MTMT:33069606,
	title = {Testing the protective effects of cyclodextrins vs. alternariol-induced acute toxicity in HeLa cells and in zebrafish embryos},
	url = {https://m2.mtmt.hu/api/publication/33069606},
	author = {Fliszár-Nyúl, Eszter and Bock, Illés and Jakabfi-Csepregi, Rita and Szente, Lajos and Szabó, István and Csenki, Zsolt Imre and Poór, Miklós},
	doi = {10.1016/j.etap.2022.103965},
	journal-iso = {ENVIRON TOXICOL PHAR},
	journal = {ENVIRONMENTAL TOXICOLOGY AND PHARMACOLOGY},
	volume = {95},
	unique-id = {33069606},
	issn = {1382-6689},
	year = {2022},
	eissn = {1872-7077},
	orcid-numbers = {Fliszár-Nyúl, Eszter/0000-0003-0923-0059; Szabó, István/0000-0002-3954-799X}
}

@article{MTMT:33050125,
	title = {Interaction of the Emerging Mycotoxins Beauvericin, Cyclopiazonic Acid, and Sterigmatocystin with Human Serum Albumin},
	url = {https://m2.mtmt.hu/api/publication/33050125},
	author = {Fliszár-Nyúl, Eszter and Faisal, Anna Zelma and Skaper, Renáta and Lemli, Beáta and Bayartsetseg, Bayarsaikhan and Hetényi, Csaba and Gömbös, Patrik and Szabó, András and Poór, Miklós},
	doi = {10.3390/biom12081106},
	journal-iso = {BIOMOLECULES},
	journal = {BIOMOLECULES},
	volume = {12},
	unique-id = {33050125},
	issn = {2218-273X},
	abstract = {Beauvericin (BEA), cyclopiazonic acid (CPA), and sterigmatocystin (STC) are emerging mycotoxins. They appear as contaminants in food and animal feed, leading to economic losses and health risks. Human serum albumin (HSA) forms stable complexes with certain mycotoxins, including ochratoxins, alternariol, citrinin, and zearalenone. HSA binding can influence the toxicokinetics of xenobiotics, and albumin can also be considered and applied as a relatively cheap affinity protein. Therefore, we examined the potential interactions of BEA, CPA, and STC with HSA employing fluorescence spectroscopy, ultracentrifugation, ultrafiltration, and molecular modeling. Spectroscopic and ultracentrifugation studies demonstrated the formation of low-affinity BEA–HSA (Ka ≈ 103 L/mol) and moderately strong CPA–HSA and STC–HSA complexes (Ka ≈ 104 L/mol). In ultrafiltration experiments, CPA slightly displaced each site marker (warfarin, naproxen, and camptothecin) tested, while BEA and STC did not affect significantly the albumin binding of these drugs. Modeling studies suggest that CPA occupies Sudlow’s site I, while STC binds to the Heme site (FA1) on HSA. Considering the interactions of CPA with the site markers, the CPA–HSA interaction may have toxicological importance.},
	keywords = {human serum albumin; CYCLOPIAZONIC ACID; sterigmatocystin; albumin-ligand interaction; Beauvericin},
	year = {2022},
	eissn = {2218-273X},
	orcid-numbers = {Fliszár-Nyúl, Eszter/0000-0003-0923-0059; Lemli, Beáta/0000-0001-8903-1337; Szabó, András/0000-0002-5315-0024; Poór, Miklós/0000-0003-1425-7459}
}

@article{MTMT:32828207,
	title = {In vitro characterization of the furin inhibitor MI-1851: Albumin binding, interaction with cytochrome P450 enzymes and cytotoxicity},
	url = {https://m2.mtmt.hu/api/publication/32828207},
	author = {Pásztiné Gere, Erzsébet and Szentkirályi-Tóth, Anna and Szabó, Pál Tamás and Steinmetzer, Torsten and Fliszár-Nyúl, Eszter and Poór, Miklós},
	doi = {10.1016/j.biopha.2022.113124},
	journal-iso = {BIOMED PHARMACOTHER},
	journal = {BIOMEDICINE & PHARMACOTHERAPY},
	volume = {151},
	unique-id = {32828207},
	issn = {0753-3322},
	year = {2022},
	eissn = {1950-6007},
	orcid-numbers = {Szabó, Pál Tamás/0000-0003-2260-4641; Fliszár-Nyúl, Eszter/0000-0003-0923-0059}
}