@article{MTMT:33641738,
	title = {Synergistic effect of carbon nanotubes and carbon black as nanofillers of silicone rubber pressure sensors},
	url = {https://m2.mtmt.hu/api/publication/33641738},
	author = {Al-Mandalawi, Mohammed and Kuzsella, László and Viskolcz, Béla and Szabóné Kollár, Mariann and Fiser, Béla and Vanyorek, László},
	doi = {10.1016/j.arabjc.2023.104594},
	journal-iso = {ARAB J CHEM},
	journal = {ARABIAN JOURNAL OF CHEMISTRY},
	volume = {16},
	unique-id = {33641738},
	issn = {1878-5352},
	year = {2023},
	eissn = {1878-5379},
	orcid-numbers = {Fiser, Béla/0000-0003-0603-4626}
}

@article{MTMT:31898520,
	title = {Crystal structures of zinc(II) complexes with β-hydroxypyridinecarboxylate ligands: examples of structure-directing effects used in inorganic crystal engineering},
	url = {https://m2.mtmt.hu/api/publication/31898520},
	author = {May, Nóra Veronika and Nys, Kevin and Ching, H. Y. Vincent and Nagyné Bereczki, Laura and Holczbauer, Tamás and Di Marco, Valerio B. and Bombicz, Petra},
	doi = {10.1107/S2052520621000299},
	journal-iso = {ACTA CRYSTALLOGR B},
	journal = {ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE CRYSTAL ENGINEERING AND MATERIALS},
	volume = {77},
	unique-id = {31898520},
	issn = {2052-5192},
	year = {2021},
	eissn = {2052-5206},
	pages = {193-204},
	orcid-numbers = {May, Nóra Veronika/0000-0003-4770-4681; Di Marco, Valerio B./0000-0001-6108-746X; Bombicz, Petra/0000-0002-5509-1515}
}

@article{MTMT:31295386,
	title = {Nuclear Quantum Effects from the Analysis of Smoothed Trajectories: Pilot Study for Water},
	url = {https://m2.mtmt.hu/api/publication/31295386},
	author = {Berta, Dénes and Ferenc, Dávid and Bakó, Imre and Madarász, Ádám},
	doi = {10.1021/acs.jctc.9b00703},
	journal-iso = {J CHEM THEORY COMPUT},
	journal = {JOURNAL OF CHEMICAL THEORY AND COMPUTATION},
	volume = {16},
	unique-id = {31295386},
	issn = {1549-9618},
	year = {2020},
	eissn = {1549-9626},
	pages = {3316-3334},
	orcid-numbers = {Berta, Dénes/0000-0002-8299-3784; Ferenc, Dávid/0000-0002-5193-540X}
}

@{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}
}

@article{MTMT:2103369,
	title = {Fragmentation characteristics of glycopeptides},
	url = {https://m2.mtmt.hu/api/publication/2103369},
	author = {Vékey, Károly and Ozohanics, Olivér and Tóth, Eszter and Anita, Jekő and Rokobné Révész, Ágnes and Krenyácz, Judit and Drahos, László},
	doi = {10.1016/j.ijms.2012.08.031},
	journal-iso = {INT J MASS SPECTROM},
	journal = {INTERNATIONAL JOURNAL OF MASS SPECTROMETRY},
	volume = {345},
	unique-id = {2103369},
	issn = {1387-3806},
	year = {2013},
	eissn = {1873-2798},
	pages = {71-79},
	orcid-numbers = {Ozohanics, Olivér/0000-0002-2705-9921; Rokobné Révész, Ágnes/0000-0002-6221-1239; Drahos, László/0000-0001-9589-6652}
}

@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}
}