@article{MTMT:34720633,
	title = {Novel-Type GABA B PAMs: Structure–Activity Relationship in Light of the Protein Structure},
	url = {https://m2.mtmt.hu/api/publication/34720633},
	author = {Krámos, Balázs and Hadady, Zsuzsa and Makó, Attila and Szántó, Gábor and Felföldi, Nóra and Magdó, Ildikó and Bobok, Amrita Ágnes and Bata, Imre and Román, Viktor and Visegrády, András and Keserű, György Miklós and Greiner, István and Éles, János},
	doi = {10.1021/acsmedchemlett.3c00560},
	journal-iso = {ACS MED CHEM LETT},
	journal = {ACS MEDICINAL CHEMISTRY LETTERS},
	unique-id = {34720633},
	issn = {1948-5875},
	year = {2024},
	orcid-numbers = {Krámos, Balázs/0000-0002-6387-7382; Greiner, István/0000-0002-5336-2828; Éles, János/0000-0001-9185-1123}
}

@article{MTMT:34718013,
	title = {Boronic acid inhibitors of penicillin-binding protein 1b: serine and lysine labelling agents},
	url = {https://m2.mtmt.hu/api/publication/34718013},
	author = {Kollár, Levente and Grabrijan, Katarina and Hrast Rambaher, Martina and Bozovičar, Krištof and Imre, Tímea and Ferenczy, György and Gobec, Stanislav and Keserű, György Miklós},
	doi = {10.1080/14756366.2024.2305833},
	journal-iso = {J ENZYM INHIB MED CH},
	journal = {JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY},
	volume = {39},
	unique-id = {34718013},
	issn = {1475-6366},
	year = {2024},
	eissn = {1475-6374},
	orcid-numbers = {Ferenczy, György/0000-0002-5771-4616}
}

@{MTMT:34535308,
	title = {Free Energy Calculations in Covalent Drug Design},
	url = {https://m2.mtmt.hu/api/publication/34535308},
	author = {Mihalovits, Levente Márk and Ferenczy, György and Keserű, György Miklós},
	booktitle = {Computational Drug Discovery},
	doi = {10.1002/9783527840748.ch23},
	unique-id = {34535308},
	year = {2024},
	pages = {561-578},
	orcid-numbers = {Mihalovits, Levente Márk/0000-0003-1022-3294; Ferenczy, György/0000-0002-5771-4616}
}

@article{MTMT:34492242,
	title = {On-DNA Synthesis of Multisubstituted Indoles},
	url = {https://m2.mtmt.hu/api/publication/34492242},
	author = {Németh, András György and Kollár, Levente and Németh, K. and Schlosser, Gitta (Vácziné) and Minus, Annamária and Keserű, György Miklós},
	doi = {10.1021/acs.orglett.3c03602},
	journal-iso = {ORG LETT},
	journal = {ORGANIC LETTERS},
	volume = {26},
	unique-id = {34492242},
	issn = {1523-7060},
	abstract = {The increasing role of the DNA-encoded library technology in early phase drug discovery represents a significant demand for DNA-compatible synthetic methods for therapeutically relevant heterocycles. Herein, we report the first on-DNA synthesis of multisubstituted indoles via a cascade reaction of Sonogashira coupling and intramolecular ring closure. Further functionalization by Suzuki coupling at the third position exploits a diverse chemical space. The high fidelity of the method also enabled the construction of an indole-based mock library. © 2023 The Authors. Published by American Chemical Society.},
	year = {2024},
	eissn = {1523-7052},
	pages = {2517-2522},
	orcid-numbers = {Schlosser, Gitta (Vácziné)/0000-0002-7637-7133; Minus, Annamária/0009-0003-4199-3942}
}

@article{MTMT:34445373,
	title = {Electrophilic MiniFrags Revealed Unprecedented Binding Sites for Covalent HDAC8 Inhibitors},
	url = {https://m2.mtmt.hu/api/publication/34445373},
	author = {Keeley, Aaron Brian and Kopranovic, Aleksandra and Di Lorenzo, Vincenzo and Ábrányi-Balogh, Péter and Jänsch, Niklas and Lai, Linh N. and Petri, László and Orgován, Zoltán and Pölöske, Daniel and Orlova, Anna and Németh, András György and Desczyk, Charlotte and Imre, Timea and Bajusz, Dávid and Moriggl, Richard and Meyer-Almes, Franz-Josef and Keserű, György Miklós},
	doi = {10.1021/acs.jmedchem.3c01779},
	journal-iso = {J MED CHEM},
	journal = {JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {67},
	unique-id = {34445373},
	issn = {0022-2623},
	abstract = {Screening of ultra-low-molecular weight ligands (MiniFrags) successfully identified viable chemical starting points for a variety of drug targets. Here we report the electrophilic analogues of MiniFrags that allow the mapping of potential binding sites for covalent inhibitors by biochemical screening and mass spectrometry. Small electrophilic heterocycles and their N-quaternized analogues were first characterized in the glutathione assay to analyze their electrophilic reactivity. Next, the library was used for systematic mapping of potential covalent binding sites available in human histone deacetylase 8 (HDAC8). The covalent labeling of HDAC8 cysteines has been proven by tandem mass spectrometry measurements, and the observations were explained by mutating HDAC8 cysteines. As a result, screening of electrophilic MiniFrags identified three potential binding sites suitable for the development of allosteric covalent HDAC8 inhibitors. One of the hit fragments was merged with a known HDAC8 inhibitor fragment using different linkers, and the linker length was optimized to result in a lead-like covalent inhibitor. © 2023 The Authors. Published by American Chemical Society},
	year = {2024},
	eissn = {1520-4804},
	pages = {572-585},
	orcid-numbers = {Di Lorenzo, Vincenzo/0000-0002-3140-3561; Bajusz, Dávid/0000-0003-4277-9481; Meyer-Almes, Franz-Josef/0000-0002-1001-3249}
}

@article{MTMT:34405999,
	title = {GproteinDb in 2024: new G protein-GPCR couplings, AlphaFold2-multimer models and interface interactions},
	url = {https://m2.mtmt.hu/api/publication/34405999},
	author = {Pándy-Szekeres, Gáspár and Taracena Herrera, Luis P and Caroli, Jimmy and Kermani, Ali A and Kulkarni, Yashraj and Keserű, György Miklós and Gloriam, David E},
	doi = {10.1093/nar/gkad1089},
	journal-iso = {NUCLEIC ACIDS RES},
	journal = {NUCLEIC ACIDS RESEARCH},
	volume = {52},
	unique-id = {34405999},
	issn = {0305-1048},
	abstract = {G proteins are the major signal proteins of ∼800 receptors for medicines, hormones, neurotransmitters, tastants and odorants. GproteinDb offers integrated genomic, structural, and pharmacological data and tools for analysis, visualization and experiment design. Here, we present the first major update of GproteinDb greatly expanding its coupling data and structural templates, adding AlphaFold2 structure models of GPCR–G protein complexes and advancing the interactive analysis tools for their interfaces underlying coupling selectivity. We present insights on coupling agreement across datasets and parameters, including constitutive activity, agonist-induced activity and kinetics. GproteinDb is accessible at https://gproteindb.org.},
	year = {2024},
	eissn = {1362-4962},
	pages = {D466-D475},
	orcid-numbers = {Gloriam, David E/0000-0002-4299-7561}
}

@article{MTMT:34223252,
	title = {Molecular Mechanism of Labelling Functional Cysteines by Heterocyclic Thiones},
	url = {https://m2.mtmt.hu/api/publication/34223252},
	author = {Mihalovits, Levente Márk and Kollár, Levente and Bajusz, Dávid and Knez, Damijan and Bozovičar, Krištof and Imre, Timea and Ferenczy, György and Gobec, Stanislav and Keserű, György Miklós},
	doi = {10.1002/cphc.202300596},
	journal-iso = {CHEMPHYSCHEM},
	journal = {CHEMPHYSCHEM: A EUROPEAN JOURNAL OF CHEMICAL PHYSICS AND PHYSICAL CHEMISTRY},
	volume = {25},
	unique-id = {34223252},
	issn = {1439-4235},
	abstract = {Heterocyclic thiones have recently been identified as reversible covalent warheads, consistent with their mild electrophilic nature. Little is known so far about their mechanism of action in labelling nucleophilic sidechains, especially cysteines. The vast number of tractable cysteines promotes a wide range of target proteins to examine; however, our focus was put on functional cysteines. We chose the main protease of SARS‐CoV‐2 harboring Cys145 at the active site that is a structurally characterized and clinically validated target of covalent inhibitors. We screened an in‐house, cysteine‐targeting covalent inhibitor library which resulted in several covalent fragment hits with benzoxazole, benzothiazole and benzimidazole cores. Thione derivatives and Michael acceptors were selected for further investigations with the objective of exploring the mechanism of inhibition of the thiones and using the thoroughly characterized Michael acceptors for benchmarking our studies. Classical and hybrid quantum mechanical/molecular mechanical (QM/MM) molecular dynamics simulations were carried out that revealed a new mechanism of covalent cysteine labelling by thione derivatives, which was supported by QM and free energy calculations and by a wide range of experimental results. Our study shows that the molecular recognition step plays a crucial role in the overall binding of both sets of molecules.},
	year = {2024},
	eissn = {1439-7641},
	orcid-numbers = {Mihalovits, Levente Márk/0000-0003-1022-3294; Bajusz, Dávid/0000-0003-4277-9481; Ferenczy, György/0000-0002-5771-4616}
}

@article{MTMT:34205650,
	title = {Effective Synthesis, Development and Application of a Highly Fluorescent Cyanine Dye for Antibody Conjugation and Microscopy Imaging},
	url = {https://m2.mtmt.hu/api/publication/34205650},
	author = {Szepesi Kovács, Dénes and Kontra, Bence and Chiovini, Balázs and Müller, Dalma and Tóth, Estilla Zsófia and Ábrányi-Balogh, Péter and Wittner, Lucia and Várady, György and Turczel, Gábor and Farkas, Ödön and Owen, Michael Christopher and Katona, Gergely and Győrffy, Balázs and Keserű, György Miklós and Mucsi, Zoltán and Rózsa J., Balázs and Kovács, Ervin},
	doi = {10.1039/D3OB01471A},
	journal-iso = {ORG BIOMOL CHEM},
	journal = {ORGANIC & BIOMOLECULAR CHEMISTRY},
	volume = {21},
	unique-id = {34205650},
	issn = {1477-0520},
	abstract = {An asymmetric cyanine-type fluorescent dye was designed and synthesized via a versatile, multi-step process, aiming to conjugate with an Her2+ receptor specific antibody by an azide-alkyne click reaction. The aromaticity and the excitation and relaxation energetics of the fluorophore were characterized by computational methods. The synthesized dye exhibited excellent fluorescence properties for confocal microscopy, offering efficient applicability in in vitro imaging due to its merits such as a high molar absorption coefficient (36 816 M-1 cm-1), excellent brightness, optimal wavelength (627 nm), larger Stokes shift (26 nm) and appropriate photostability compared to cyanines. The conjugated cyanine-trastuzumab was constructed via an effective, metal-free, strain-promoted azide-alkyne click reaction leading to a regulated number of dyes being conjugated. This novel cyanine-labelled antibody was successfully applied for in vitro confocal imaging and flow cytometry of Her2+ tumor cells. An azido cyanine dye was synthesized and characterized by computational and experimental techniques and applied in tumor cell imaging.},
	keywords = {RECEPTOR; REAGENTS; FUTURE},
	year = {2023},
	eissn = {1477-0539},
	pages = {8829-8836},
	orcid-numbers = {Kontra, Bence/0000-0001-8293-3637; Wittner, Lucia/0000-0001-6800-0953; Várady, György/0000-0003-2012-9680; Farkas, Ödön/0000-0002-4217-0150; Katona, Gergely/0000-0002-4173-0355; Győrffy, Balázs/0000-0002-5772-3766; Mucsi, Zoltán/0000-0003-3224-8847; Kovács, Ervin/0000-0002-3939-6925}
}

@article{MTMT:34160949,
	title = {Covalent fragment approaches targeting non-cysteine residues},
	url = {https://m2.mtmt.hu/api/publication/34160949},
	author = {Csorba, Noémi and Ábrányi-Balogh, Péter and Keserű, György Miklós},
	doi = {10.1016/j.tips.2023.08.014},
	journal-iso = {TRENDS PHARMACOL SCI},
	journal = {TRENDS IN PHARMACOLOGICAL SCIENCES},
	volume = {44},
	unique-id = {34160949},
	issn = {0165-6147},
	year = {2023},
	eissn = {1873-3735},
	pages = {802-816}
}

@article{MTMT:34015800,
	title = {Synthesis and Application of Two-Photon Active Fluorescent Rhodol Dyes for Antibody Conjugation and In Vitro Cell Imaging},
	url = {https://m2.mtmt.hu/api/publication/34015800},
	author = {Szepesi Kovács, Dénes and Chiovini, Balázs and Müller, Dalma and Tóth, Estilla Zsófia and Fülöp, Anna and Ábrányi-Balogh, Péter and Wittner, Lucia and Várady, György and Farkas, Ödön and Turczel, Gábor and Katona, Gergely and Győrffy, Balázs and Keserű, György Miklós and Mucsi, Zoltán and Rózsa J., Balázs and Kovács, Ervin},
	doi = {10.1021/acsomega.3c01796},
	journal-iso = {ACS OMEGA},
	journal = {ACS OMEGA},
	volume = {8},
	unique-id = {34015800},
	issn = {2470-1343},
	year = {2023},
	eissn = {2470-1343},
	pages = {22836-22843},
	orcid-numbers = {Wittner, Lucia/0000-0001-6800-0953; Várady, György/0000-0003-2012-9680; Farkas, Ödön/0000-0002-4217-0150; Katona, Gergely/0000-0002-4173-0355; Győrffy, Balázs/0000-0002-5772-3766; Mucsi, Zoltán/0000-0003-3224-8847; Kovács, Ervin/0000-0002-3939-6925}
}

@article{MTMT:33845452,
	title = {SH2db, an information system for the SH2 domain},
	url = {https://m2.mtmt.hu/api/publication/33845452},
	author = {Bajusz, Dávid and Pándy-Szekeres, Gáspár and Takács, Ágnes and de Araujo, Elvin D and Keserű, György Miklós},
	doi = {10.1093/nar/gkad420},
	journal-iso = {NUCLEIC ACIDS RES},
	journal = {NUCLEIC ACIDS RESEARCH},
	volume = {51},
	unique-id = {33845452},
	issn = {0305-1048},
	abstract = {SH2 domains are key mediators of phosphotyrosine-based signalling, and therapeutic targets for diverse, mostly oncological, disease indications. They have a highly conserved structure with a central beta sheet that divides the binding surface of the protein into two main pockets, responsible for phosphotyrosine binding (pY pocket) and substrate specificity (pY + 3 pocket). In recent years, structural databases have proven to be invaluable resources for the drug discovery community, as they contain highly relevant and up-to-date information on important protein classes. Here, we present SH2db, a comprehensive structural database and webserver for SH2 domain structures. To organize these protein structures efficiently, we introduce (i) a generic residue numbering scheme to enhance the comparability of different SH2 domains, (ii) a structure-based multiple sequence alignment of all 120 human wild-type SH2 domain sequences and their PDB and AlphaFold structures. The aligned sequences and structures can be searched, browsed and downloaded from the online interface of SH2db (http://sh2db.ttk.hu), with functions to conveniently prepare multiple structures into a Pymol session, and to export simple charts on the contents of the database. Our hope is that SH2db can assist researchers in their day-to-day work by becoming a one-stop shop for SH2 domain related research.},
	year = {2023},
	eissn = {1362-4962},
	pages = {W542-W552},
	orcid-numbers = {Bajusz, Dávid/0000-0003-4277-9481}
}

@article{MTMT:33802561,
	title = {Allosteric regulation and crystallographic fragment screening of SARS-CoV-2 NSP15 endoribonuclease},
	url = {https://m2.mtmt.hu/api/publication/33802561},
	author = {Godoy, Andre Schutzer and Nakamura, Aline Minalli and Douangamath, Alice and Song, Yun and Noske, Gabriela Dias and Gawriljuk, Victor Oliveira and Fernandes, Rafaela Sachetto and Pereira, Humberto D Muniz and Oliveira, Ketllyn Irene Zagato and Fearon, Daren and Dias, Alexandre and Krojer, Tobias and Fairhead, Michael and Powell, Alisa and Dunnet, Louise and Brandao-Neto, Jose and Skyner, Rachael and Chalk, Rod and Bajusz, Dávid and Bege, Miklós and Borbás, Anikó and Keserű, György Miklós and von Delft, Frank and Oliva, Glaucius},
	doi = {10.1093/nar/gkad314},
	journal-iso = {NUCLEIC ACIDS RES},
	journal = {NUCLEIC ACIDS RESEARCH},
	volume = {51},
	unique-id = {33802561},
	issn = {0305-1048},
	abstract = {Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of coronavirus disease 2019 (COVID-19). The NSP15 endoribonuclease enzyme, known as NendoU, is highly conserved and plays a critical role in the ability of the virus to evade the immune system. NendoU is a promising target for the development of new antiviral drugs. However, the complexity of the enzyme's structure and kinetics, along with the broad range of recognition sequences and lack of structural complexes, hampers the development of inhibitors. Here, we performed enzymatic characterization of NendoU in its monomeric and hexameric form, showing that hexamers are allosteric enzymes with a positive cooperative index, and with no influence of manganese on enzymatic activity. Through combining cryo-electron microscopy at different pHs, X-ray crystallography and biochemical and structural analysis, we showed that NendoU can shift between open and closed forms, which probably correspond to active and inactive states, respectively. We also explored the possibility of NendoU assembling into larger supramolecular structures and proposed a mechanism for allosteric regulation. In addition, we conducted a large fragment screening campaign against NendoU and identified several new allosteric sites that could be targeted for the development of new inhibitors. Overall, our findings provide insights into the complex structure and function of NendoU and offer new opportunities for the development of inhibitors.},
	year = {2023},
	eissn = {1362-4962},
	pages = {5255-5270},
	orcid-numbers = {Godoy, Andre Schutzer/0000-0002-0613-9164; Bajusz, Dávid/0000-0003-4277-9481; Borbás, Anikó/0000-0001-8462-4547; von Delft, Frank/0000-0003-0378-0017}
}

@article{MTMT:33729477,
	title = {Activation-Free Sulfonyl Fluoride Probes for Fragment Screening},
	url = {https://m2.mtmt.hu/api/publication/33729477},
	author = {Petri, László and Ábrányi-Balogh, Péter and Csorba, Noémi and Keeley, Aaron Brian and Simon, József and Randelovic, Ivan and Tóvári, József and Schlosser, Gitta (Vácziné) and Szabó, Dániel and Drahos, László and Keserű, György Miklós},
	doi = {10.3390/molecules28073042},
	journal-iso = {MOLECULES},
	journal = {MOLECULES},
	volume = {28},
	unique-id = {33729477},
	issn = {1420-3049},
	abstract = {SuFEx chemistry is based on the unique reactivity of the sulfonyl fluoride group with a range of nucleophiles. Accordingly, sulfonyl fluorides label multiple nucleophilic amino acid residues, making these reagents popular in both chemical biology and medicinal chemistry applications. The reactivity of sulfonyl fluorides nominates this warhead chemotype as a candidate for an external, activation-free general labelling tag. Here, we report the synthesis and characterization of a small sulfonyl fluoride library that yielded the 3-carboxybenzenesulfonyl fluoride warhead for tagging tractable targets at nucleophilic residues. Based on these results, we propose that coupling diverse fragments to this warhead would result in a library of sulfonyl fluoride bits (SuFBits), available for screening against protein targets. SuFBits will label the target if it binds to the core fragment, which facilitates the identification of weak fragments by mass spectrometry.},
	keywords = {fragment screening; chemical probe; Electrophilic warhead; Sulfonyl fluoride; Targeted covalent inhibitor; covalent fragment},
	year = {2023},
	eissn = {1420-3049},
	orcid-numbers = {Randelovic, Ivan/0000-0003-0161-0022; Tóvári, József/0000-0002-5543-3204; Schlosser, Gitta (Vácziné)/0000-0002-7637-7133; Szabó, Dániel/0000-0003-3375-395X; Drahos, László/0000-0001-9589-6652}
}

@article{MTMT:33647485,
	title = {Covalent fragment mapping of KRasG12C revealed novel chemotypes with in vivo potency},
	url = {https://m2.mtmt.hu/api/publication/33647485},
	author = {Orgován, Zoltán and Péczka, Nikolett and Petri, László and Ábrányi-Balogh, Péter and Randelovic, Ivan and Tóth, Szilárd and Szakács, Gergely and Nyíri, Kinga and Vértessy, Beáta (Grolmuszné) and Pálfy, Gyula and Vida, István and Perczel, András and Tóvári, József and Keserű, György Miklós},
	doi = {10.1016/j.ejmech.2023.115212},
	journal-iso = {EUR J MED CHEM},
	journal = {EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {250},
	unique-id = {33647485},
	issn = {0223-5234},
	abstract = {G12C mutant KRas is considered druggable by allele-specific covalent inhibitors due to the nucleophilic character of the oncogenic mutant cysteine at position 12. Discovery of these inhibitors requires the optimization of both covalent and noncovalent interactions. Here, we report covalent fragment screening of our electrophilic fragment library of diverse non-covalent scaffolds equipped with 40 different electrophilic functionalities to identify fragments as suitable starting points targeting Cys12. Screening the library against KRasG12C using Ellman's free thiol assay, followed by protein NMR and cell viability assays, resulted in two potential inhibitor chemotypes. Characterization of these scaffolds in in vitro cellular- and in vivo xenograft models revealed them as promising starting points for covalent drug discovery programs.},
	year = {2023},
	eissn = {1768-3254},
	orcid-numbers = {Randelovic, Ivan/0000-0003-0161-0022; Pálfy, Gyula/0000-0003-1590-5331; Perczel, András/0000-0003-1252-6416; Tóvári, József/0000-0002-5543-3204}
}

@article{MTMT:33421768,
	title = {GPCRdb in 2023: state-specific structure models using AlphaFold2 and new ligand resources},
	url = {https://m2.mtmt.hu/api/publication/33421768},
	author = {Pándy-Szekeres, Gáspár and Caroli, Jimmy and Mamyrbekov, Alibek and Kermani, Ali A. and Keserű, György Miklós and Kooistra, Albert J. and Gloriam, David E.},
	doi = {10.1093/nar/gkac1013},
	journal-iso = {NUCLEIC ACIDS RES},
	journal = {NUCLEIC ACIDS RESEARCH},
	volume = {51},
	unique-id = {33421768},
	issn = {0305-1048},
	abstract = {G protein-coupled receptors (GPCRs) are physiologically abundant signaling hubs routing hundreds of extracellular signal substances and drugs into intracellular pathways. The GPCR database, GPCRdb supports > 5000 interdisciplinary researchers every month with reference data, analysis, visualization, experiment design and dissemination. Here, we present our fifth major GPCRdb release setting out with an overview of the many resources for receptor sequences, structures, and ligands. This includes recently published additions of class D generic residue numbers, a comparative structure analysis tool to identify functional determinants, trees clustering GPCR structures by 3D conformation, and mutations stabilizing inactive/active states. We provide new state-specific structure models of all human non-olfactory GPCRs built using AlphaFold2-MultiState. We also provide a new resource of endogenous ligands along with a larger number of surrogate ligands with bioactivity, vendor, and physiochemical descriptor data. The one-stop-shop ligand resources integrate ligands/data from the ChEMBL, Guide to Pharmacology, PDSP Ki and PubChem database. The GPCRdb is available athttps://gpcrdb.org.},
	year = {2023},
	eissn = {1362-4962},
	pages = {D395-D402}
}

@article{MTMT:33283298,
	title = {Safe and Efficient Continuous-Flow Synthesis and Batchwise Hydrolysis of Ethyl 5-Acetyl-1H-pyrazole-3-carboxylate: A Key Synthon of Darolutamide},
	url = {https://m2.mtmt.hu/api/publication/33283298},
	author = {Szilágyi, Bence and Egyed, Attila and Mándity, István and Nagy, Tamás and Kátainé Fadgyas, Katalin and Volk, Balázs and Keserű György, M.},
	doi = {10.1055/s-0042-1751389},
	journal-iso = {SYNTHESIS-STUTTGART},
	journal = {SYNTHESIS-STUTTGART},
	volume = {55},
	unique-id = {33283298},
	issn = {0039-7881},
	year = {2023},
	eissn = {1437-210X},
	pages = {959-966},
	orcid-numbers = {Mándity, István/0000-0003-2865-6143; Volk, Balázs/0000-0002-2019-1874}
}

@article{MTMT:33543903,
	title = {A kovalens enziminhibíció számításos kémiai jellemzése},
	url = {https://m2.mtmt.hu/api/publication/33543903},
	author = {Mihalovits, Levente Márk and Ferenczy, György and Keserű, György Miklós},
	doi = {10.24100/MKF.2022.03-4.150},
	journal-iso = {MAGY KÉM FOLY KÉM KÖZL},
	journal = {MAGYAR KÉMIAI FOLYÓIRAT - KÉMIAI KÖZLEMÉNYEK (1997-)},
	volume = {128},
	unique-id = {33543903},
	issn = {1418-9933},
	year = {2022},
	eissn = {1418-8600},
	pages = {150-156},
	orcid-numbers = {Mihalovits, Levente Márk/0000-0003-1022-3294; Ferenczy, György/0000-0002-5771-4616}
}

@article{MTMT:33543663,
	title = {Sejtosztódásgátló hatású vindolin- és flavonoidszármazékok előállítása},
	url = {https://m2.mtmt.hu/api/publication/33543663},
	author = {Mayer, Szabolcs and Nagy, Nóra and Keglevich, Péter and Ábrányi-Balogh, Péter and Hazai, László},
	doi = {10.24100/MKF.2022.03-4.137},
	journal-iso = {MAGY KÉM FOLY KÉM KÖZL},
	journal = {MAGYAR KÉMIAI FOLYÓIRAT - KÉMIAI KÖZLEMÉNYEK (1997-)},
	volume = {128},
	unique-id = {33543663},
	issn = {1418-9933},
	year = {2022},
	eissn = {1418-8600},
	pages = {137-142}
}

@article{MTMT:33307131,
	title = {A carbapenem antibiotic inhibiting a mammalian serine protease: structure of the acylaminoacyl peptidase–meropenem complex},
	url = {https://m2.mtmt.hu/api/publication/33307131},
	author = {Kiss-Szemán, Anna Júlia and Takács, Luca and Orgován, Zoltán and Stráner, Pál and Jákli, Imre and Schlosser, Gitta (Vácziné) and Masiulis, Simonas and Harmat, Veronika and Karancsiné Menyhárd, Dóra and Perczel, András},
	doi = {10.1039/D2SC05520A},
	journal-iso = {CHEM SCI},
	journal = {CHEMICAL SCIENCE},
	volume = {13},
	unique-id = {33307131},
	issn = {2041-6520},
	abstract = {The structure of porcine AAP (pAAP) in a covalently bound complex with meropenem was determined by cryo-EM to 2.1 Å resolution, showing the mammalian serine-protease inhibited by a carbapenem antibiotic.},
	year = {2022},
	eissn = {2041-6539},
	pages = {14264-14276},
	orcid-numbers = {Kiss-Szemán, Anna Júlia/0000-0002-3039-0324; Takács, Luca/0000-0002-4864-8872; Stráner, Pál/0000-0003-2240-8501; Schlosser, Gitta (Vácziné)/0000-0002-7637-7133; Harmat, Veronika/0000-0002-1866-9904; Karancsiné Menyhárd, Dóra/0000-0002-0095-5531; Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:33298396,
	title = {Next-Generation Heterocyclic Electrophiles as Small-Molecule Covalent MurA Inhibitors},
	url = {https://m2.mtmt.hu/api/publication/33298396},
	author = {Ábrányi-Balogh, Péter and Keeley, Aaron and Ferenczy, György and Petri, László and Imre, Timea and Grabrijan, Katarina and Hrast, Martina and Knez, Damijan and Ilaš, Janez and Gobec, Stanislav and Keserű, György Miklós},
	doi = {10.3390/ph15121484},
	journal-iso = {PHARMACEUTICALS-BASE},
	journal = {PHARMACEUTICALS},
	volume = {15},
	unique-id = {33298396},
	abstract = {Heterocyclic electrophiles as small covalent fragments showed promising inhibitory activity on the antibacterial target MurA (UDP-N-acetylglucosamine 1-carboxyvinyltransferase, EC:2.5.1.7). Here, we report the second generation of heterocyclic electrophiles: the quaternized analogue of the heterocyclic covalent fragment library with improved reactivity and MurA inhibitory potency. Quantum chemical reaction barrier calculations, GSH (L-glutathione) reactivity assay, and thrombin counter screen were also used to demonstrate and explain the improved reactivity and selectivity of the N-methylated heterocycles and to compare the two generations of heterocyclic electrophiles.},
	year = {2022},
	eissn = {1424-8247},
	orcid-numbers = {Ferenczy, György/0000-0002-5771-4616; Hrast, Martina/0000-0003-0488-2445; Knez, Damijan/0000-0001-9917-1384; Ilaš, Janez/0000-0002-0124-0474; Gobec, Stanislav/0000-0002-9678-3083}
}