@{MTMT:2595161,
	title = {Evodiamin szérumfehérje kötődésének vizsgálata},
	url = {https://m2.mtmt.hu/api/publication/2595161},
	author = {Domonkos, Celesztina Diána and Zsila, F and Fitos, Ilona and Benéné Visy, Júlia},
	booktitle = {Vegyészkonferencia 2013},
	unique-id = {2595161},
	year = {2013}
}

@{MTMT:2594314,
	title = {Stereoselective analysis of amino acids and endomorphin analogue tetrapeptides by CE},
	url = {https://m2.mtmt.hu/api/publication/2594314},
	author = {Németh, K and Domonkos, Celesztina Diána and Szemán, Julianna and Mallareddy, J R and Sarnyai, V and Tóth, G and Jicsinszky, L and Szente, Lajos and Péter, Antal and Benéné Visy, Júlia},
	booktitle = {CECE 2013 10th International Interdisciplinary Meeting on Bioanalysis},
	unique-id = {2594314},
	year = {2013},
	pages = {80-80}
}

@article{MTMT:2446448,
	title = {Fatty acid modulated human serum albumin binding of the β-carboline alkaloids norharmane and harmane},
	url = {https://m2.mtmt.hu/api/publication/2446448},
	author = {Domonkos, Celesztina Diána and Fitos, Ilona and Benéné Visy, Júlia and Zsila, Ferenc},
	doi = {10.1021/mp400531n},
	journal-iso = {MOL PHARM},
	journal = {MOLECULAR PHARMACEUTICS},
	volume = {10},
	unique-id = {2446448},
	issn = {1543-8384},
	abstract = {Harmane and norharmane are representative members of the large group of natural β-carboline alkaloids featured with diverse pharmacological activities. In blood, these agents are transported by human serum albumin (HSA) which has a profound impact on the pharmacokinetic and pharmacodynamic properties of many therapeutic drugs and xenobiotics. By combination of various spectroscopic methods, the present contribution is aimed to elucidate how non-esterified fatty acids (FAs), the primary endogenous ligands of HSA, affect the binding properties of harmane and norharmane. Analysis of induced circular dichroism (CD) and fluorescence spectroscopic data indicates the inclusion of the neutral form of both molecules into the binding pocket of subdomain IIIA, which hosts two FA binding sites, too. The induced CD and UV absorption spectra of harmane and norharmane exhibit peculiar changes upon addition of FAs suggesting the formation of ternary complexes in which the lipid ligands significantly alter the binding mode of the alkaloids via cooperative allosteric mechanism. To our knowledge, it is the first instance of the demonstration of drug-FA co-binding at site IIIA. In line with these results, molecular docking calculations showed two distinct binding positions of norharmane within subdomain IIIA. The profound increase in the affinity constants of β-carbolines estimated in the presence of FAs predicts that the unbound, pharmacologically active serum fraction of these compounds strongly depends on the actual lipid binding profile of HSA.},
	year = {2013},
	eissn = {1543-8392},
	pages = {4706-4716}
}

@article{MTMT:2391104,
	title = {Circular dichroism spectroscopic detection of ligand binding induced subdomain IB specific structural adjustment of human serum albumin},
	url = {https://m2.mtmt.hu/api/publication/2391104},
	author = {Zsila, Ferenc},
	doi = {10.1021/jp4067108},
	journal-iso = {J PHYS CHEM B},
	journal = {JOURNAL OF PHYSICAL CHEMISTRY B},
	volume = {117},
	unique-id = {2391104},
	issn = {1520-6106},
	abstract = {This work demonstrates for the first time that binding of various compounds within subdomain IB of human serum albumin (HSA) provokes characteristic changes in the near-UV circular dichroism (CD) spectrum of the protein. It can be inferred from the spectroscopic features of difference ellipticity signals and from CD displacement experiments that tyrosine residues located in subdomain IB are the source of the observed spectral alterations. It is proposed that inclusion of some ligand molecules (bile acids, dehydroepiandrosterone sulfate, steroidal terpenes, fatty acids, ibuprofen, and gemfibrozil) into the pocket of subdomain IB disrupts the Tyr138?Tyr161 interhelical π?π stacking interaction, which is reflected in the CD spectrum. This phenomenon can be utilized for the CD detection of subdomain IB specific binding of endo- as well as exogenous agents and to study the drug binding associated local conformational adaptation of the HSA molecule.},
	year = {2013},
	eissn = {1520-5207},
	pages = {10798-10806}
}

@article{MTMT:2229453,
	title = {Subdomain IB is the third major drug binding region of human serum albumin: Toward the three-sites model.},
	url = {https://m2.mtmt.hu/api/publication/2229453},
	author = {Zsila, Ferenc},
	doi = {10.1021/mp400027q},
	journal-iso = {MOL PHARM},
	journal = {MOLECULAR PHARMACEUTICS},
	volume = {10},
	unique-id = {2229453},
	issn = {1543-8384},
	abstract = {According to the conventional view, noncovalent association of small molecules with human serum albumin (HSA) occurs principally at the so-called Sudlow’s sites located in subdomain IIA and IIIA. By employing a circular dichroism (CD) spectroscopic approach, it is shown that biliverdin is the specific CD label of an additional drug binding area in subdomain IB. CD competition experiments disclosed the entrapment of a diverse assortment of acidic, neutral, and basic molecules within subdomain IB including anticancer agents (camptothecin, doxorubicin, daunorubicin, teniposide, suramin, tyrosine kinase inhibitors), anticoagulants (dicoumarol), various steroids (bile acids, carbenoxolone), nonsteroidal antiinflammatory drugs, natural substances (aristolochic acid, glycyrrhetinic acid), and synthetic dyes (methyl orange, azocarmine B). These finding imply that subdomain IB can be considered as the third major drug binding region of HSA featured with promiscuous ligand recognition ability. Additionally, subdomain IB is allosterically coupled with the Sudlow’s sites, the ligand binding of which is shown to alter the HSA binding mode and affinity of biliverdin and hemin. Brief case studies are presented to illustrate how the evaluation of spectral changes of tetrapyrrole CD probes gains new insight into the HSA binding properties of endogenous as well as pharmaceutical compounds.},
	year = {2013},
	eissn = {1543-8392},
	pages = {1668-1682}
}

@CONFERENCE{MTMT:2595138,
	title = {β-Karbolin származékok szérumfehérje kötődésének vizsgálata. Serum Protein Binding Study of Β-Carboline Derivatives},
	url = {https://m2.mtmt.hu/api/publication/2595138},
	author = {Domonkos, Celesztina Diána and Fitos, Ilona and Zsila, F and Németh, Krisztina and Benéné Visy, Júlia},
	booktitle = {XVIII. Nemzetközi Vegyészkonferencia},
	unique-id = {2595138},
	year = {2012},
	pages = {n-nn}
}

@inproceedings{MTMT:2595114,
	title = {β-Karbolin származékok szérumfehérje kötődésének vizsgálata},
	url = {https://m2.mtmt.hu/api/publication/2595114},
	author = {Domonkos, Celesztina Diána and Fitos, Ilona and Zsila, F and Németh, Krisztina and Benéné Visy, Júlia},
	booktitle = {Kálmán Erika Doktori Konferencia 2012},
	unique-id = {2595114},
	year = {2012},
	pages = {22-23}
}

@{MTMT:2594308,
	title = {SERUM PROTEIN BINDING STUDY OF β -CARBOLINE DERIVATIVES},
	url = {https://m2.mtmt.hu/api/publication/2594308},
	author = {Domonkos, Celesztina Diána and Fitos, Ilona and Zsila, F and Németh, K and Benéné Visy, Júlia},
	booktitle = {Kálmán Erika Doktori Konferencia 2012},
	unique-id = {2594308},
	year = {2012},
	pages = {23-23}
}

@CONFERENCE{MTMT:2521076,
	title = {Valproát és metabolitjai vérszintjének meghatározása LC-MS/MS technikával},
	url = {https://m2.mtmt.hu/api/publication/2521076},
	author = {Magda, Balázs and Tóth, Katalin and Temesvári, Manna and Monostory, Katalin and Szabó, Pál Tamás},
	booktitle = {TOX'2012 Tudományos Konferencia, Magyar toxikológusok társasága},
	unique-id = {2521076},
	year = {2012},
	orcid-numbers = {Szabó, Pál Tamás/0000-0003-2260-4641}
}

@article{MTMT:2067021,
	title = {Comparison of separation performances of novel β-cyclodextrin-based chiral stationary phases in high-performance liquid chromatographic enantioseparation},
	url = {https://m2.mtmt.hu/api/publication/2067021},
	author = {Varga, G and Fodor, G and Ilisz, István and Szemán, Julianna and Benéné Visy, Júlia and Szente, Lajos and Péter, Antal},
	doi = {10.1016/j.jpba.2012.05.023},
	journal-iso = {J PHARMACEUT BIOMED ANAL},
	journal = {JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS},
	volume = {70},
	unique-id = {2067021},
	issn = {0731-7085},
	abstract = {Three β-cyclodextrin-based chiral stationary phases were developed applying novel bonding chemistry. The separation performances of β-cyclodextrin, (R,S)-2-hydroxypropyl-β-cyclodextrin, and permethyl-β-cyclodextrin-based CSPs were compared in the resolution of structurally divergent analytes, such as coumarins, dansyl amino acids, and propionic acid derivatives. Separations were carried out in reversed phase mode applying 0.1% triethylammonium phosphate (pH 3.5)/MeOH mobile phase systems in different compositions. Of the three novel CSPs the permethyl-β-cyclodextrin bonded phase proved to be the most effective one for the enantioseparation of investigated analytes. © 2012.},
	keywords = {CHIRAL SEPARATION; column liquid chromatography; Cyclodextrin-based chiral stationary phase},
	year = {2012},
	eissn = {1873-264X},
	pages = {71-76},
	orcid-numbers = {Ilisz, István/0000-0001-8282-457X}
}