@article{MTMT:3344151,
	title = {Discovery of isatin and 1H-indazol-3-ol derivatives as d-amino acid oxidase (DAAO) inhibitors},
	url = {https://m2.mtmt.hu/api/publication/3344151},
	author = {Szilágyi, Bence and Kovacs, P and Ferenczy, György and Rácz, Anita and Németh, Krisztina and Benéné Visy, Júlia and Szabó, Pál Tamás and Ilas, J and Balogh, György Tibor and Monostory, Katalin and Vincze, István and Tábi, Tamás and Szökő, Éva and Keserű, György Miklós},
	doi = {10.1016/j.bmc.2018.02.004},
	journal-iso = {BIOORGAN MED CHEM},
	journal = {BIOORGANIC & MEDICINAL CHEMISTRY},
	volume = {26},
	unique-id = {3344151},
	issn = {0968-0896},
	abstract = {d-Amino acid oxidase (DAAO) is a potential target in the treatment of schizophrenia as its inhibition increases brain d-serine level and thus contributes to NMDA receptor activation. Inhibitors of DAAO were sought testing [6+5] type heterocycles and identified isatin derivatives as micromolar DAAO inhibitors. A pharmacophore and structure-activity relationship analysis of isatins and reported DAAO inhibitors led us to investigate 1H-indazol-3-ol derivatives and nanomolar inhibitors were identified. The series was further characterized by pKa and isothermal titration calorimetry measurements. Representative compounds exhibited beneficial properties in in vitro metabolic stability and PAMPA assays. 6-fluoro-1H-indazol-3-ol (37) significantly increased plasma d-serine level in an in vivo study on mice. These results show that the 1H-indazol-3-ol series represents a novel class of DAAO inhibitors with the potential to develop drug candidates.},
	year = {2018},
	eissn = {1464-3391},
	pages = {1579-1587},
	orcid-numbers = {Ferenczy, György/0000-0002-5771-4616; Szabó, Pál Tamás/0000-0003-2260-4641; Balogh, György Tibor/0000-0003-3347-1880; Vincze, István/0000-0002-6843-7159; Tábi, Tamás/0000-0001-5343-0205; Szökő, Éva/0000-0003-1464-6403}
}

@article{MTMT:2904364,
	title = {Synthesis and serum protein binding of novel ring-substituted harmine derivatives},
	url = {https://m2.mtmt.hu/api/publication/2904364},
	author = {Domonkos, Celesztina Diána and Zsila, Ferenc and Fitos, Ilona and Benéné Visy, Júlia and Kassai, Rudolf and Bálint, Balázs Károly and Kotschy, András},
	doi = {10.1039/C5RA06426K},
	journal-iso = {RSC ADV},
	journal = {RSC ADVANCES},
	volume = {5},
	unique-id = {2904364},
	issn = {2046-2069},
	abstract = {A series of new derivatives of the natural β-carboline alkaloid harmine, introducing hydrophobic substituents into positions 7 and 9 were synthetized as potential anticancer agents. Their binding affinities for human serum albumin (HSA) and α1-acid glycoprotein (AAG) were investigated by affinity chromatography combined with fluorescence, circular dichroism (CD) and UV absorption spectroscopy. The weak binding of harmine to both proteins (Ka ~ 3 × 104 M-1) was highly increased by aromatic substitutions (Ka ~ 105-106 M-1). Derivatives having a substituted benzyl group in the N9-position of the β-carboline nucleus showed about tenfold and hundredfold affinity enhancement for HSA and AAG, respectively. Such a strong plasma protein interaction would be of pharmacokinetic relevance for these potential drug candidates. Induced CD spectra indicated the variant selective, dimeric binding of the 7-pyridylethoxy derivative to AAG. Absorbance and fluorescence spectra refer to the binding preference of the neutral form of the studied β-carbolines for both proteins.},
	year = {2015},
	eissn = {2046-2069},
	pages = {53809-53818}
}

@article{MTMT:2826747,
	title = {The Janus facet of nanomaterials},
	url = {https://m2.mtmt.hu/api/publication/2826747},
	author = {Kardos, Julianna and Jemnitz, Katalin and Jablonkai, István and Bóta, Attila and Varga, Zoltán and Benéné Visy, Júlia and Héja, László},
	doi = {10.1155/2015/317184},
	journal-iso = {BIOMED RES INT},
	journal = {BIOMED RESEARCH INTERNATIONAL},
	volume = {2015},
	unique-id = {2826747},
	issn = {2314-6133},
	year = {2015},
	eissn = {2314-6141},
	orcid-numbers = {Varga, Zoltán/0000-0002-5741-2669}
}

@article{MTMT:2792054,
	title = {Cationic permethylated 6-monoamino-6-monodeoxy-beta-cyclodextrin as chiral selector of dansylated amino acids in capillary electrophoresis},
	url = {https://m2.mtmt.hu/api/publication/2792054},
	author = {Németh, Krisztina and Domonkos, Celesztina Diána and Virág, Sarnyai and Szemán, Julianna and László, Jicsinszky and Szente, Lajos and Benéné Visy, Júlia},
	doi = {10.1016/j.jpba.2014.06.028},
	journal-iso = {J PHARMACEUT BIOMED ANAL},
	journal = {JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS},
	volume = {99},
	unique-id = {2792054},
	issn = {0731-7085},
	year = {2014},
	eissn = {1873-264X},
	pages = {16-21}
}

@article{MTMT:2735829,
	title = {Role of the conformational flexibility of evodiamine in its binding to protein hosts: a comparative spectroscopic and molecular modeling evaluation with rutaecarpine},
	url = {https://m2.mtmt.hu/api/publication/2735829},
	author = {Domonkos, Celesztina Diána and Fitos, Ilona and Benéné Visy, Júlia and Zsila, Ferenc},
	doi = {10.1039/C4CP02483D},
	journal-iso = {PHYS CHEM CHEM PHYS},
	journal = {PHYSICAL CHEMISTRY CHEMICAL PHYSICS},
	volume = {16},
	unique-id = {2735829},
	issn = {1463-9076},
	abstract = {Spectroscopic studies combined with computational analysis indicate the inherent conformational flexibility of the [small beta]-carbolin derivative evodiamine (EVD) featured with diverse pharmacological activities. Qualitative evaluation of the circular dichroism (CD) spectra of EVD enantiomers complemented with quantum chemical calculations reveals a chiral exciton signature that can be assigned to the folded, L-shaped conformation of the molecule. Changes of the exciton couplet measured in different solvents and the near-UV CD profile upon binding to human serum albumin (HSA) refer to the structural adaptability of EVD. The enantioselectivity of EVD-HSA interaction is demonstrated showing the binding preference of the (R)-enantiomer. Comparison of experimental and calculated CD spectra of various conformers of EVD as well as the results of molecular docking data suggest that the (R)-antipode is accomodated within the IIA subdomain of HSA in ridge-tile conformation. Rutaecarpine (RTC), the close congener of EVD, forms much tighter association complexes both with HSA and [small alpha]1-acid glycoprotein. In contrast to EVD, the nearly planar geometry of the indoloquinazoline ring system of RTC allows its stacked dimeric binding to the HSA.},
	year = {2014},
	eissn = {1463-9084},
	pages = {22632-22642}
}

@article{MTMT:2571740,
	title = {Intercalation of Bovine Serum Albumin Coated Gold Clusters Between Phospholipid Bilayers: Temperature-Dependent Behavior of Lipid-AuQC@BSA Assemblies with Red Emission and Superlattice Structure},
	url = {https://m2.mtmt.hu/api/publication/2571740},
	author = {Söptei, Balázs and Mihály, Judith and Benéné Visy, Júlia and Wacha, András Ferenc and Bóta, Attila},
	doi = {10.1021/jp4124138},
	journal-iso = {J PHYS CHEM B},
	journal = {JOURNAL OF PHYSICAL CHEMISTRY B},
	volume = {118},
	unique-id = {2571740},
	issn = {1520-6106},
	abstract = {A method has been developed to encapsulate bovine serum albumin (BSA)-coated gold quantum clusters (AuQC@BSA) in a multilamellar system of dipalmitoylphosphatidylcholine (DPPC).
		Results have shown that intercalation of AuQC@BSA particles into
		lipid bilayers occurs in the presence of CaCl2. Intense red photoluminescence emission was observed after encapsulation of the clusters. A well-defined structure was found with periodic distances drastically larger than that in the pure DPPC/water system. Although Ca2+ ions can change the dipole characteristics of the lipid bilayer surface, leading to unbinding between the bilayers of multilamellar DPPC/water system, the repulsion is shielded in the presence of
		AuQC@BSA particles. A coherent superlattice structure evolves due to mixed Ca2+-DPPC and Ca2+-AuQC@BSA interactions. Studies at different temperatures have suggested a correlation between
		the luminescence properties of the clusters and phase transition of the lipid layers. The temperature-dependent behavior assumes the connection between the coating and the lipid bilayer surface. Temperature-dependent features of lipid intercalated Au clusters provide new opportunities in their application.},
	year = {2014},
	eissn = {1520-5207},
	pages = {3887-3892},
	orcid-numbers = {Wacha, András Ferenc/0000-0002-9609-0893}
}

@article{MTMT:2482487,
	title = {Influence of acid-induced conformational variability on protein separation in reversed phase high performance liquid chromatography},
	url = {https://m2.mtmt.hu/api/publication/2482487},
	author = {Bobály, Balázs and Tóth, Eszter and Drahos, László and Zsila, Ferenc and Benéné Visy, Júlia and Fekete, Jenő and Vékey, Károly},
	doi = {10.1016/j.chroma.2013.12.022},
	journal-iso = {J CHROMATOGR A},
	journal = {JOURNAL OF CHROMATOGRAPHY A},
	volume = {1325},
	unique-id = {2482487},
	issn = {0021-9673},
	keywords = {Protein Conformation; RP-HPLC; Protein separation mechanism; TFA-protein adduct},
	year = {2014},
	eissn = {1873-3778},
	pages = {155-162},
	orcid-numbers = {Drahos, László/0000-0001-9589-6652}
}

@article{MTMT:2452779,
	title = {Development of novel chiral capillary electrophoresis methods for the serotonin receptor (5-HT2A) antagonist MDL 100,907 (volinanserin) and for its key intermediate compound},
	url = {https://m2.mtmt.hu/api/publication/2452779},
	author = {Németh, Krisztina and Palkó, Roberta and Kovács, Péter and Benéné Visy, Júlia},
	doi = {10.1016/j.jpba.2013.10.017},
	journal-iso = {J PHARMACEUT BIOMED ANAL},
	journal = {JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS},
	volume = {88},
	unique-id = {2452779},
	issn = {0731-7085},
	year = {2014},
	eissn = {1873-264X},
	pages = {579-583}
}

@{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}
}