@article{MTMT:34567562,
	title = {Saturation Transfer Difference NMR and Molecular Docking Interaction Study of Aralkyl-Thiodigalactosides as Potential Inhibitors of the Human-Galectin-3 Protein},
	url = {https://m2.mtmt.hu/api/publication/34567562},
	author = {Hőgye, Fanni and Farkas, László Bence and Balogh, Álex Kálmán and Szilágyi, László and Alnukari, Samar and Bajza, István and Borbás, Anikó and Fehér, Krisztina and Tóthné Illyés, Tünde Zita and Timári, István},
	doi = {10.3390/ijms25031742},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {25},
	unique-id = {34567562},
	issn = {1661-6596},
	abstract = {Human Galectin-3 (hGal-3) is a protein that selectively binds to β-galactosides and holds diverse roles in both normal and pathological circumstances. Therefore, targeting hGal-3 has become a vibrant area of research in the pharmaceutical chemistry. As a step towards the development of novel hGal-3 inhibitors, we synthesized and investigated derivatives of thiodigalactoside (TDG) modified with different aromatic substituents. Specifically, we describe a high-yielding synthetic route of thiodigalactoside (TDG); an optimized procedure for the synthesis of the novel 3,3′-di-O-(quinoline-2-yl)methyl)-TDG and three other known, symmetric 3,3′-di-O-TDG derivatives ((naphthalene-2yl)methyl, benzyl, (7-methoxy-2H-1-benzopyran-2-on-4-yl)methyl). In the present study, using competition Saturation Transfer Difference (STD) NMR spectroscopy, we determined the dissociation constant (Kd) of the former three TDG derivatives produced to characterize the strength of the interaction with the target protein (hGal-3). Based on the Kd values determined, the (naphthalen-2-yl)methyl, the (quinolin-2-yl)methyl and the benzyl derivatives bind to hGal-3 94, 30 and 24 times more strongly than TDG. Then, we studied the binding modes of the derivatives in silico by molecular docking calculations. Docking poses similar to the canonical binding modes of well-known hGal-3 inhibitors have been found. However, additional binding forces, cation–π interactions between the arginine residues in the binding pocket of the protein and the aromatic groups of the ligands, have been established as significant features. Our results offer a molecular-level understanding of the varying affinities observed among the synthesized thiodigalactoside derivatives, which can be a key aspect in the future development of more effective ligands of hGal-3.},
	keywords = {lectin; NMR spectroscopy; Galectin-3; Molecular docking; STD NMR; thiodigalactosides},
	year = {2024},
	eissn = {1422-0067},
	orcid-numbers = {Borbás, Anikó/0000-0001-8462-4547}
}

@misc{MTMT:34159529,
	title = {Characterization of copolymers using gel permeation chromatography and neural networks, Young Researchers' International Conference on Chemistry and Chemical Engineering},
	url = {https://m2.mtmt.hu/api/publication/34159529},
	author = {Máté, BENEDEK and Nagy, Tibor and Róth, Gergő and Kuki, Ákos and Timári, István and Zsuga, Miklós and Kéki, Sándor},
	unique-id = {34159529},
	year = {2023},
	orcid-numbers = {Nagy, Tibor/0000-0001-8568-914X}
}

@article{MTMT:34110916,
	title = {Enhanced Copolymer Characterization for Polyethers Using Gel Permeation Chromatography Combined with Artificial Neural Networks},
	url = {https://m2.mtmt.hu/api/publication/34110916},
	author = {Nagy, Tibor and Róth, Gergő and Benedek, Máté and Kuki, Ákos and Timári, István and Zsuga, Miklós and Kéki, Sándor},
	doi = {10.1021/acs.analchem.2c02913},
	journal-iso = {ANAL CHEM},
	journal = {ANALYTICAL CHEMISTRY},
	volume = {95},
	unique-id = {34110916},
	issn = {0003-2700},
	abstract = {Gel permeation chromatography (GPC) is a generally applied method for the mass analysis of various polymers and copolymers, but it inherently fails to provide additional important information such as the composition of copolymers. However, we will show that GPC measurements using different solvents can yield not just the correct molecular weight but the composition of the copolymer. Accordingly, artificial neural networks (ANNs) have been developed to process the data of GPC measurements and determine the molecular weight and the chemical composition of the copolymers. The target values of the ANNs were obtained by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) and nuclear magnetic resonance (NMR) spectroscopy. Our GPC-ANN method is demonstrated by the analysis of various poloxamers, i.e., poly(ethylene oxide) (PEO)-poly(propylene oxide) (PPO) block copolymers. Two ANNs were constructed. The first one (ANN_1) works in a wider mass range (from 900 to 12,500 dalton), while the second one (ANN_2) produces more output values. ANN_2 can thus predict seven characteristic copolymer parameters, namely, two average molecular weights, the average weight fraction of the EO unit, and four average numbers of the repeat units. The correlation between the experimentally obtained outputs and the predicted ones is high (r > 0.98). The accuracy of the ANNs is very convincing, and both ANNs predict the number-average molecular weight (M-n) with an accuracy below 5%. Furthermore, this work is the first step for creating an open database and applications extending the use of the GPC-ANN method for the analysis of copolymers.},
	year = {2023},
	eissn = {1520-6882},
	pages = {10504-10511},
	orcid-numbers = {Nagy, Tibor/0000-0001-8568-914X}
}

@article{MTMT:33699950,
	title = {Phosphorylated Peptide Derived from the Myosin Phosphatase Target Subunit Is a Novel Inhibitor of Protein Phosphatase-1},
	url = {https://m2.mtmt.hu/api/publication/33699950},
	author = {Kónya, Zoltán and Tamás, István and Bécsi, Bálint and Lontay, Beáta and Hadháziné Raics, Mária and Timári, István and E Kövér, Katalin and Erdődi, Ferenc},
	doi = {10.3390/ijms24054789},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {33699950},
	issn = {1661-6596},
	abstract = {Identification of specific protein phosphatase-1 (PP1) inhibitors is of special importance regarding the study of its cellular functions and may have therapeutic values in diseases coupled to signaling processes. In this study, we prove that a phosphorylated peptide of the inhibitory region of myosin phosphatase (MP) target subunit (MYPT1), R690QSRRS(pT696)QGVTL701 (P-Thr696-MYPT1690−701), interacts with and inhibits the PP1 catalytic subunit (PP1c, IC50 = 3.84 µM) and the MP holoenzyme (Flag-MYPT1-PP1c, IC50 = 3.84 µM). Saturation transfer difference NMR measurements established binding of hydrophobic and basic regions of P-Thr696-MYPT1690−701 to PP1c, suggesting interactions with the hydrophobic and acidic substrate binding grooves. P-Thr696-MYPT1690−701 was dephosphorylated by PP1c slowly (t1/2 = 81.6–87.9 min), which was further impeded (t1/2 = 103 min) in the presence of the phosphorylated 20 kDa myosin light chain (P-MLC20). In contrast, P-Thr696-MYPT1690−701 (10–500 µM) slowed down the dephosphorylation of P-MLC20 (t1/2 = 1.69 min) significantly (t1/2 = 2.49–10.06 min). These data are compatible with an unfair competition mechanism between the inhibitory phosphopeptide and the phosphosubstrate. Docking simulations of the PP1c-P-MYPT1690−701 complexes with phosphothreonine (PP1c-P-Thr696-MYPT1690−701) or phosphoserine (PP1c-P-Ser696-MYPT1690−701) suggested their distinct poses on the surface of PP1c. In addition, the arrangements and distances of the surrounding coordinating residues of PP1c around the phosphothreonine or phosphoserine at the active site were distinct, which may account for their different hydrolysis rate. It is presumed that P-Thr696-MYPT1690−701 binds tightly at the active center but the phosphoester hydrolysis is less preferable compared to P-Ser696-MYPT1690−701 or phosphoserine substrates. Moreover, the inhibitory phosphopeptide may serve as a template to synthesize cell permeable PP1-specific peptide inhibitors.},
	keywords = {Molecular docking; saturation transfer difference NMR; protein phosphatase-1 (PP1); myosin phosphatase (MP); myosin phosphatase target subunit-1 (MYPT1); MYPT1 inhibitory peptide (P-Thr696-MYPT1690-701)},
	year = {2023},
	eissn = {1422-0067},
	orcid-numbers = {Timári, István/0000-0003-0504-6967}
}

@{MTMT:34413868,
	title = {Catalyst-free coupling reactions of anhydro-aldose tosylhydrazones with 1H-1,2,3-triazoles and 5-benzyl-2H-tetrazoles: synthesis of C-(β-D-glycopyranosyl)methyl-triazoles and -tetrazoles},
	url = {https://m2.mtmt.hu/api/publication/34413868},
	author = {Szakács, Bence and Kaszás, Tímea and Juhászné Tóth, Éva and Cservenyák, Ivett and Kovács, Tamara and Timári, István and Juhász, László and Somsák, László and Vágvölgyiné Tóth, Marietta},
	booktitle = {Debrecen Colloquium on Carbohydrates 2020 in 2022: Rezső Bognár Memorial Conference on Glycomimetics},
	unique-id = {34413868},
	year = {2022},
	pages = {43. oldal, OL-9},
	orcid-numbers = {Szakács, Bence/0000-0002-9157-3028; Juhász, László/0000-0002-7462-7944; Somsák, László/0000-0002-9103-9845}
}

@misc{MTMT:34413789,
	title = {Catalyst-free coupling reactions of anhydro-aldose and aromatic tosylhydrazones with tetrazoles and triazoles},
	url = {https://m2.mtmt.hu/api/publication/34413789},
	author = {Kaszás, Tímea and Szakács, Bence and Juhászné Tóth, Éva and Cservenyák, Ivett and Kovács, Tamara and Timári, István and Nilsson, Ulf J. and Juhász, László and Somsák, László and Vágvölgyiné Tóth, Marietta},
	unique-id = {34413789},
	year = {2022},
	orcid-numbers = {Szakács, Bence/0000-0002-9157-3028; Juhász, László/0000-0002-7462-7944; Somsák, László/0000-0002-9103-9845}
}

@misc{MTMT:34413585,
	title = {Catalyst-free coupling reactions for the synthesis of C-(β-D-glycopyranosyl)methyl-triazoles, -tetrazoles and alkyl/aryl substituted tetrazoles},
	url = {https://m2.mtmt.hu/api/publication/34413585},
	author = {Kaszás, Tímea and Szakács, Bence and Juhászné Tóth, Éva and Cservenyák, Ivett and Kovács, Tamara and Timári, István and Juhász, László and Somsák, László and Vágvölgyiné Tóth, Marietta},
	unique-id = {34413585},
	year = {2022},
	orcid-numbers = {Szakács, Bence/0000-0002-9157-3028; Juhász, László/0000-0002-7462-7944; Somsák, László/0000-0002-9103-9845}
}

@{MTMT:34413543,
	title = {N-Tozilhidrazonok fémmentes kapcsolása 1,2,3-triazolokkal},
	url = {https://m2.mtmt.hu/api/publication/34413543},
	author = {Szakács, Bence and Juhászné Tóth, Éva and Cservenyák, Ivett and Kaszás, Tímea and Timári, István and Somsák, László and Vágvölgyiné Tóth, Marietta},
	booktitle = {Vegyészkonferencia 2022},
	unique-id = {34413543},
	year = {2022},
	pages = {65. oldal, O-39},
	orcid-numbers = {Szakács, Bence/0000-0002-9157-3028; Somsák, László/0000-0002-9103-9845}
}

@misc{MTMT:34413487,
	title = {Anhidro-aldóz tozilhidrazonok kapcsolási reakciói 4-aril-1H-1,2,3-triazolokkal},
	url = {https://m2.mtmt.hu/api/publication/34413487},
	author = {Szakács, Bence and Kaszás, Tímea and Cservenyák, Ivett and Juhászné Tóth, Éva and Timári, István and Somsák, László and Vágvölgyiné Tóth, Marietta},
	unique-id = {34413487},
	year = {2022},
	orcid-numbers = {Szakács, Bence/0000-0002-9157-3028; Somsák, László/0000-0002-9103-9845}
}

@misc{MTMT:34160640,
	title = {The Polydispersity Ratio and its Implementation for the Interpretation of Pluronics, XXIV. International Mass Spectrometry Conference. Maastricht},
	url = {https://m2.mtmt.hu/api/publication/34160640},
	author = {Róth, Gergő and Nagy, Tibor and Kuki, Ákos and Hashimov, Mahir and Zsófia, Vonza and Timári, István and Zsuga, Miklós and Kéki, Sándor},
	unique-id = {34160640},
	year = {2022},
	orcid-numbers = {Nagy, Tibor/0000-0001-8568-914X; Hashimov, Mahir/0000-0003-1713-4366}
}