@article{MTMT:35781560,
	title = {Target agnostic photoaffinity labelling by sulfonylhydrazones},
	url = {https://m2.mtmt.hu/api/publication/35781560},
	author = {Garami, Kristóf Noel and Péczka, Nikolett and Petri, László and Imre, Tímea and Langó, Tamás and Szabó, Zoltán and Orgován, Zoltán and Szabó, Pál Tamás and Keserű, György Miklós and Ábrányi-Balogh, Péter},
	doi = {10.1002/anie.202408701},
	journal-iso = {ANGEW CHEM INT EDIT},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	volume = {64},
	unique-id = {35781560},
	issn = {1433-7851},
	abstract = {Photoaffinity labeling is a widely used methodology for interrogating small molecule-protein interactions. However, these applications are limited by the few photo-crosslinkers that typically modify the affinity and the binding mode of the original ligand. Here, we report the development of new target agnostic photoaffinity warheads, sulfohydrazones that form a reactive carbene upon UV irradiation. Careful optimization of the reaction conditions allowed us to effectively label five different amino acid residues in proteins. Our approach turned biologically relevant hydrazones and sulfohydrazones to intrinsically irreversible covalent binders without structural modifications by photoactivation as demonstrated on monoamine oxidase A (MAO-A) enzyme and STAT5b (Signal transducer and activator of transcription 5b) transcription factor. Sulfohydrazones are readily accessible by transforming the corresponding carbonyl group of a ligand or a suitable tag that extends the application domain of the method for any ligands exemplified by conditional labelling of the acetylcholine esterase enzyme and the oncogenic mutant of GTP-ase KRasG12D. © 2025 The Author(s). Angewandte Chemie International Edition published by Wiley-VCH GmbH.},
	keywords = {LIGANDS; IRRADIATION; BINDING MODES; Crosslinking; protein interaction; Small molecules; photoaffinity labeling; KRAS; STAT; Acetylcholine esterase; photoaffinity; sulfohydrazone; Kra; Photo-crosslinker; Sulfohydrazone},
	year = {2025},
	eissn = {1521-3773},
	orcid-numbers = {Petri, László/0000-0001-9881-5096; Szabó, Zoltán/0000-0001-8278-8038; Szabó, Pál Tamás/0000-0003-2260-4641}
}

@article{MTMT:35427664,
	title = {Target‐templated Construction of Functional Proteomimetics Using Photo‐foldamer Libraries},
	url = {https://m2.mtmt.hu/api/publication/35427664},
	author = {Wéber, Edit and Ábrányi-Balogh, Péter and Martinek, Tamas A. and Nagymihály, Bence and Karancsiné Menyhárd, Dóra and Péczka, Nikolett and Gadanecz, Márton and Schlosser, Gitta (Vácziné) and Orgován, Zoltán and Bogár, Ferenc and Bajusz, Dávid and Kecskeméti, Gábor and Szabó, Zoltán and Bartus, Éva and Tököli, Attila and Tóth, Gábor K. and Szalai, Tibor Viktor and Takács, Tamás and de Araujo, Elvin and Buday, László and Perczel, András and Keserű, György Miklós},
	doi = {10.1002/ange.202410435},
	journal-iso = {ANGEW CHEM},
	journal = {ANGEWANDTE CHEMIE},
	volume = {137},
	unique-id = {35427664},
	issn = {0044-8249},
	abstract = {Current methods for proteomimetic engineering rely on structure‐based design. Here we describe a design strategy that allows the construction of proteomimetics against challenging targets without a priori characterization of the target surface. Our approach relies on (i) a 100‐membered photoreactive foldamer library, the members of which act as local surface mimetics, and (ii) the subsequent affinity maturation of the primary hits using systems chemistry. Two surface‐oriented proteinogenic side chains drove the interactions between the short helical foldamer fragments and the proteins. Diazirine‐based photo‐crosslinking was applied to sensitively detected and localize binding even to shallow and dynamic patches on representatively difficult targets. Photo‐foldamers identified functionally relevant protein interfaces, allosteric and previously unexplored targetable regions on the surface of STAT3 and an oncogenic K‐Ras variant. Target‐templated dynamic linking of foldamer hits resulted in two orders of magnitude affinity improvement in a single step. The dimeric K‐Ras ligand mimicked protein‐like catalytic functions. The photo‐foldamer approach thus enables the highly efficient mapping of protein‐protein interaction sites and provides a viable starting point for proteomimetic ligand development without a priori structural hypotheses.},
	year = {2025},
	eissn = {1521-3757},
	orcid-numbers = {Karancsiné Menyhárd, Dóra/0000-0002-0095-5531; Gadanecz, Márton/0009-0009-8076-7597; Schlosser, Gitta (Vácziné)/0000-0002-7637-7133; Bajusz, Dávid/0000-0003-4277-9481; Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:35160281,
	title = {Mapping protein binding sites by photoreactive fragment pharmacophores},
	url = {https://m2.mtmt.hu/api/publication/35160281},
	author = {Ábrányi-Balogh, Péter and Bajusz, Dávid and Orgován, Zoltán and Keeley, Aaron Brian and Petri, László and Péczka, Nikolett and Szalai, Tibor Viktor and Pálfy, Gyula and Gadanecz, Márton and Grant, Emma K. and Imre, Tímea and Takács, Tamás and Randelovic, Ivan and Baranyi, Marcell and Marton, András Dénes and Schlosser, Gitta (Vácziné) and Ashraf, Qirat F. and de Araujo, Elvin D. and Karancsi, Tamás and Buday, László and Tóvári, József and Perczel, András and Bush, Jacob T. and Keserű, György Miklós},
	doi = {10.1038/s42004-024-01252-w},
	journal-iso = {COMMUN CHEM},
	journal = {COMMUNICATIONS CHEMISTRY},
	volume = {7},
	unique-id = {35160281},
	issn = {2399-3669},
	abstract = {Fragment screening is a popular strategy of generating viable chemical starting points especially for challenging targets. Although fragments provide a better coverage of chemical space and they have typically higher chance of binding, their weak affinity necessitates highly sensitive biophysical assays. Here, we introduce a screening concept that combines evolutionary optimized fragment pharmacophores with the use of a photoaffinity handle that enables high hit rates by LC-MS-based detection. The sensitivity of our screening protocol was further improved by a target-conjugated photocatalyst. We have designed, synthesized, and screened 100 diazirine-tagged fragments against three benchmark and three therapeutically relevant protein targets of different tractability. Our therapeutic targets included a conventional enzyme, the first bromodomain of BRD4, a protein-protein interaction represented by the oncogenic KRas G12D protein, and the yet unliganded N -terminal domain of the STAT5B transcription factor. We have discovered several fragment hits against all three targets and identified their binding sites via enzymatic digestion, structural studies and modeling. Our results revealed that this protocol outperforms screening traditional fully functionalized and photoaffinity fragments in better exploration of the available binding sites and higher hit rates observed for even difficult targets.},
	year = {2024},
	eissn = {2399-3669},
	orcid-numbers = {Bajusz, Dávid/0000-0003-4277-9481; Petri, László/0000-0001-9881-5096; Pálfy, Gyula/0000-0003-1590-5331; Gadanecz, Márton/0009-0009-8076-7597; Grant, Emma K./0009-0005-5229-9125; Randelovic, Ivan/0000-0003-0161-0022; Marton, András Dénes/0009-0008-5683-5484; Schlosser, Gitta (Vácziné)/0000-0002-7637-7133; de Araujo, Elvin D./0000-0003-0716-2830; Tóvári, József/0000-0002-5543-3204; Perczel, András/0000-0003-1252-6416; Bush, Jacob T./0000-0001-7165-0092}
}

@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; Petri, László/0000-0001-9881-5096; Bajusz, Dávid/0000-0003-4277-9481; Meyer-Almes, Franz-Josef/0000-0002-1001-3249}
}

@article{MTMT:35134356,
	title = {Contribution of Noncovalent Recognition and Reactivity to the Optimization of Covalent Inhibitors : A Case Study on KRasG12C},
	url = {https://m2.mtmt.hu/api/publication/35134356},
	author = {Péczka, Nikolett and Randelovic, Ivan and Orgován, Zoltán and Csorba, Noémi and Egyed, Attila and Petri, László and Ábrányi-Balogh, Péter and Gadanecz, Márton and Perczel, András and Tóvári, József and Schlosser, Gitta (Vácziné) and Takács, Tamás and Mihalovits, Levente Márk and Ferenczy, György and Buday, László and Keserű, György Miklós},
	doi = {10.1021/acschembio.4c00217},
	journal-iso = {ACS CHEM BIOL},
	journal = {ACS CHEMICAL BIOLOGY},
	volume = {19},
	unique-id = {35134356},
	issn = {1554-8929},
	abstract = {Covalent drugs might bear electrophiles to chemically modify their targets and have the potential to target previously undruggable proteins with high potency. Covalent binding of drug-size molecules includes a noncovalent recognition provided by secondary interactions and a chemical reaction leading to covalent complex formation. Optimization of their covalent mechanism of action should involve both types of interactions. Noncovalent and covalent binding steps can be characterized by an equilibrium dissociation constant (KI) and a reaction rate constant (kinact), respectively, and they are affected by both the warhead and the scaffold of the ligand. The relative contribution of these two steps was investigated on a prototypic drug target KRASG12C, an oncogenic mutant of KRAS. We used a synthetically more accessible nonchiral core derived from ARS-1620 that was equipped with four different warheads and a previously described KRAS-specific basic side chain. Combining these structural changes, we have synthesized novel covalent KRASG12C inhibitors and tested their binding and biological effect on KRASG12C by various biophysical and biochemical assays. These data allowed us to dissect the effect of scaffold and warhead on the noncovalent and covalent binding event. Our results revealed that the atropisomeric core of ARS-1620 is not indispensable for KRASG12C inhibition, the basic side chain has little effect on either binding step, and warheads affect the covalent reactivity but not the noncovalent binding. This type of analysis helps identify structural determinants of efficient covalent inhibition and may find use in the design of covalent agents.},
	year = {2024},
	eissn = {1554-8937},
	pages = {1743-1756},
	orcid-numbers = {Randelovic, Ivan/0000-0003-0161-0022; Petri, László/0000-0001-9881-5096; Gadanecz, Márton/0009-0009-8076-7597; Perczel, András/0000-0003-1252-6416; Tóvári, József/0000-0002-5543-3204; Schlosser, Gitta (Vácziné)/0000-0002-7637-7133; Mihalovits, Levente Márk/0000-0003-1022-3294; Ferenczy, György/0000-0002-5771-4616; Buday, László/0000-0003-3518-5757}
}

@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 = {Petri, László/0000-0001-9881-5096; Randelovic, Ivan/0000-0003-0161-0022; Pálfy, Gyula/0000-0003-1590-5331; Perczel, András/0000-0003-1252-6416; Tóvári, József/0000-0002-5543-3204}
}

@mastersthesis{MTMT:34738155,
	title = {Computational investigation of the allosteric modulation of metabotropic glutamate receptor 5},
	url = {https://m2.mtmt.hu/api/publication/34738155},
	author = {Orgován, Zoltán},
	publisher = {Budapest University of Technology and Economics},
	unique-id = {34738155},
	year = {2023}
}

@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:32756662,
	title = {Electrophilic warheads in covalent drug discovery: an overview},
	url = {https://m2.mtmt.hu/api/publication/32756662},
	author = {Péczka, Nikolett and Orgován, Zoltán and Ábrányi-Balogh, Péter and Keserű, György Miklós},
	doi = {10.1080/17460441.2022.2034783},
	journal-iso = {EXPERT OPIN DRUG DIS},
	journal = {EXPERT OPINION ON DRUG DISCOVERY},
	volume = {17},
	unique-id = {32756662},
	issn = {1746-0441},
	year = {2022},
	eissn = {1746-045X},
	pages = {413-422}
}

@article{MTMT:31698584,
	title = {Allosteric Molecular Switches in Metabotropic Glutamate Receptors},
	url = {https://m2.mtmt.hu/api/publication/31698584},
	author = {Orgován, Zoltán and Ferenczy, György and Keserű, György Miklós},
	doi = {10.1002/cmdc.202000444},
	journal-iso = {CHEMMEDCHEM},
	journal = {CHEMMEDCHEM},
	volume = {16},
	unique-id = {31698584},
	issn = {1860-7179},
	abstract = {Metabotropic glutamate receptors (mGlu) are class C G protein-coupled receptors of eight subtypes that are omnipresently expressed in the central nervous system. mGlus have relevance in several psychiatric and neurological disorders, therefore they raise considerable interest as drug targets. Allosteric modulators of mGlus offer advantages over orthosteric ligands owing to their increased potential to achieve subtype selectivity, and this has prompted discovery programs that have produced a large number of reported allosteric mGlu ligands. However, the optimization of allosteric ligands into drug candidates has proved to be challenging owing to induced-fit effects, flat or steep structure-activity relationships and unexpected changes in theirpharmacology. Subtle structural changes identified as molecular switches might modulate the functional activity of allosteric ligands. Here we review these switches discovered in the metabotropic glutamate receptor family..},
	keywords = {METABOTROPIC GLUTAMATE RECEPTORS; Allosteric modulation; MOLECULAR SWITCHES; GPCRs; water networks},
	year = {2021},
	eissn = {1860-7187},
	pages = {81-93},
	orcid-numbers = {Ferenczy, György/0000-0002-5771-4616}
}

@article{MTMT:30834454,
	title = {Allosteric activation of metabotropic glutamate receptor 5},
	url = {https://m2.mtmt.hu/api/publication/30834454},
	author = {Jójárt, Balázs and Orgován, Zoltán and Márki, Árpád and Pándy-Szekeres, Gáspár and Ferenczy, György and Keserű, György Miklós},
	doi = {10.1080/07391102.2019.1638302},
	journal-iso = {J BIOMOL STRUCT DYN},
	journal = {JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS},
	volume = {38},
	unique-id = {30834454},
	issn = {0739-1102},
	year = {2020},
	eissn = {1538-0254},
	pages = {2624-2632},
	orcid-numbers = {Márki, Árpád/0000-0002-6056-8891; Ferenczy, György/0000-0002-5771-4616}
}

@article{MTMT:31605838,
	title = {Structural impact of GTP binding on downstream KRAS signaling},
	url = {https://m2.mtmt.hu/api/publication/31605838},
	author = {Karancsiné Menyhárd, Dóra and Pálfy, Gyula and Orgován, Zoltán and Vida, István and Keserű, György Miklós and Perczel, András},
	doi = {10.1039/d0sc03441j},
	journal-iso = {CHEM SCI},
	journal = {CHEMICAL SCIENCE},
	volume = {11},
	unique-id = {31605838},
	issn = {2041-6520},
	abstract = {Oncogenic RAS proteins, involved in similar to 30% of human tumors, are molecular switches of various signal transduction pathways. Here we apply a new protocol for the NMR study of KRAS in its (inactive) GDP- and (activated) GTP-bound form, allowing a comprehensive analysis of the backbone dynamics of its WT-, G12C- and G12D variants. We found that Tyr32 shows opposite mobility with respect to the backbone of its surroundings: it is more flexible in the GDP-bound form while more rigid in GTP-complexes (especially in WT- and G12D-GTP). Using the G12C/Y32F double mutant, we showed that the presence of the hydroxyl group of Tyr32 has a marked effect on the G12C-KRAS-GTP system as well. Molecular dynamics simulations indicate that Tyr32 is linked to the gamma-phosphate of GTP in the activated states - an arrangement shown, using QM/MM calculations, to support catalysis. Anchoring Tyr32 to the gamma-phosphate contributes to the capture of the catalytic waters participating in the intrinsic hydrolysis of GTP and supports a simultaneous triple proton transfer step (catalytic water -> assisting water -> Tyr32 -> O1G of the gamma-phosphate) leading to straightforward product formation. The coupled flip of negatively charged residues of switch I toward the inside of the effector binding pocket potentiates ligand recognition, while positioning of Thr35 to enter the coordination sphere of the Mg(2+)widens the pocket. Position 12 mutations do not disturb the capture of Tyr32 by the gamma-phosphate, but (partially) displace Gln61, which opens up the catalytic pocket and destabilizes catalytic water molecules thus impairing intrinsic hydrolysis.},
	keywords = {ACTIVATION; MODEL-FREE APPROACH; HYDROLYSIS; RAS; MAGNETIC-RESONANCE RELAXATION; BACKBONE DYNAMICS; HOT-SPOTS; conformational ensembles; MOLECULAR SWITCH},
	year = {2020},
	eissn = {2041-6539},
	pages = {9272-9289},
	orcid-numbers = {Karancsiné Menyhárd, Dóra/0000-0002-0095-5531; Pálfy, Gyula/0000-0003-1590-5331; Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:31473660,
	title = {Small molecule inhibitors of RAS proteins with oncogenic mutations},
	url = {https://m2.mtmt.hu/api/publication/31473660},
	author = {Orgován, Zoltán and Keserű, György Miklós},
	doi = {10.1007/s10555-020-09911-9},
	journal-iso = {CANCER METAST REV},
	journal = {CANCER AND METASTASIS REVIEWS},
	volume = {39},
	unique-id = {31473660},
	issn = {0167-7659},
	abstract = {RAS proteins control a number of essential cellular processes as molecular switches in the human body. Presumably due to their important signalling role, RAS proteins are among the most frequently mutated oncogenes in human cancers. Hence, numerous efforts were done to develop appropriate therapies for RAS-mutant cancers in the last three decades. This review aimed to collect all of the reported small molecules that affect RAS signalling. These molecules can be divided in four main branches. First, we address approaches blocking RAS membrane association. Second, we focus on the stabilization efforts of non-productive RAS complexes. Third, we examine the approach to block RAS downstream signalling through disturbance of RAS-effector complex formation. Finally, we discuss direct inhibition; particularly the most recently reported covalent inhibitors, which are already advanced to human clinical trials. © 2020, The Author(s).},
	keywords = {ras Proteins; GTPASES; Oncogenic mutations; Small molecular inhibitors},
	year = {2020},
	eissn = {1573-7233},
	pages = {1107-1126}
}

@article{MTMT:30928052,
	title = {Discovery of dihydropyrazino-benzimidazole derivatives as metabotropic glutamate receptor-2 (mGluR2) positive allosteric modulators (PAMs)},
	url = {https://m2.mtmt.hu/api/publication/30928052},
	author = {Szabó, György and Kolok, Sándor and Orgován, Zoltán and Vastag, Monika and Béni, Zoltán and Kóti, János and Sághy, Katalin and Lévay, György István and Greiner, István and Keserű, György Miklós},
	doi = {10.1016/j.ejmech.2019.111881},
	journal-iso = {EUR J MED CHEM},
	journal = {EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {186},
	unique-id = {30928052},
	issn = {0223-5234},
	year = {2020},
	eissn = {1768-3254},
	orcid-numbers = {Szabó, György/0000-0002-9255-4486; Béni, Zoltán/0000-0002-1275-4155; Keserű, György Miklós/0000-0003-1039-7809}
}

@article{MTMT:30334026,
	title = {Structure-Based Optimization Strategies for G Protein-Coupled Receptor (GPCR) Allosteric Modulators: A Case Study from Analyses of New Metabotropic Glutamate Receptor 5 (mGlu 5 ) X-ray Structures},
	url = {https://m2.mtmt.hu/api/publication/30334026},
	author = {Christopher, John A. and Orgován, Zoltán and Congreve, Miles and Doré, Andrew S. and Errey, James C. and Marshall, Fiona H. and Mason, Jonathan S. and Okrasa, Krzysztof and Rucktooa, Prakash and Serrano-Vega, Maria J. and Ferenczy, György and Keserű, György Miklós},
	doi = {10.1021/acs.jmedchem.7b01722},
	journal-iso = {J MED CHEM},
	journal = {JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {62},
	unique-id = {30334026},
	issn = {0022-2623},
	year = {2019},
	eissn = {1520-4804},
	pages = {207-222},
	orcid-numbers = {Ferenczy, György/0000-0002-5771-4616}
}

@article{MTMT:31038395,
	title = {Allélspecifikus inhibitorok nyomában: a RASopátia konzorcium célpontjában a KRAS fehérje onkogén mutációi},
	url = {https://m2.mtmt.hu/api/publication/31038395},
	author = {Nyíri, Kinga and Koppány, Gergely and Pálfy, Gyula and Vida, István and Tóth, Szilárd and Orgován, Zoltán and Randelovic, Ivan and Baranyi, Marcell and Molnár, Eszter and Keserű, György Miklós and Tóvári, József and Perczel, András and Vértessy, Beáta (Grolmuszné) and Tímár, József},
	journal-iso = {MAGYAR ONKOLÓGIA},
	journal = {MAGYAR ONKOLÓGIA},
	volume = {63},
	unique-id = {31038395},
	issn = {0025-0244},
	year = {2019},
	eissn = {2060-0399},
	pages = {310-323},
	orcid-numbers = {Pálfy, Gyula/0000-0003-1590-5331; Randelovic, Ivan/0000-0003-0161-0022; Molnár, Eszter/0000-0002-4745-2018; Tóvári, József/0000-0002-5543-3204; Tímár, József/0000-0001-9183-0859}
}

@article{MTMT:30834424,
	title = {The role of water and protein flexibility in the structure-based virtual screening of allosteric GPCR modulators: an mGlu5 receptor case study},
	url = {https://m2.mtmt.hu/api/publication/30834424},
	author = {Orgován, Zoltán and Ferenczy, György and Keserű, György Miklós},
	doi = {10.1007/s10822-019-00224-w},
	journal-iso = {J COMPUT AID MOL DES},
	journal = {JOURNAL OF COMPUTER-AIDED MOLECULAR DESIGN},
	volume = {33},
	unique-id = {30834424},
	issn = {0920-654X},
	year = {2019},
	eissn = {1573-4951},
	pages = {787-797},
	orcid-numbers = {Ferenczy, György/0000-0002-5771-4616}
}

@article{MTMT:30834430,
	title = {Fragment-Based Approaches for Allosteric Metabotropic Glutamate Receptor (mGluR) Modulators},
	url = {https://m2.mtmt.hu/api/publication/30834430},
	author = {Orgován, Zoltán and Ferenczy, György and Keserű, György Miklós},
	doi = {10.2174/1568026619666190808150039},
	journal-iso = {CURR TOP MED CHEM},
	journal = {CURRENT TOPICS IN MEDICINAL CHEMISTRY},
	volume = {19},
	unique-id = {30834430},
	issn = {1568-0266},
	year = {2019},
	eissn = {1873-4294},
	pages = {1768-1781},
	orcid-numbers = {Ferenczy, György/0000-0002-5771-4616}
}

@article{MTMT:3333356,
	title = {Validation of tautomeric and protomeric binding modes by free energy calculations. A case study for the structure based optimization of d-amino acid oxidase inhibitors},
	url = {https://m2.mtmt.hu/api/publication/3333356},
	author = {Orgován, Zoltán and Ferenczy, György and Steinbrecher, Thomas and Szilágyi, Bence and Bajusz, Dávid and Keserű, György Miklós},
	doi = {10.1007/s10822-018-0097-y},
	journal-iso = {J COMPUT AID MOL DES},
	journal = {JOURNAL OF COMPUTER-AIDED MOLECULAR DESIGN},
	volume = {32},
	unique-id = {3333356},
	issn = {0920-654X},
	year = {2018},
	eissn = {1573-4951},
	pages = {331-345},
	orcid-numbers = {Ferenczy, György/0000-0002-5771-4616; Bajusz, Dávid/0000-0003-4277-9481}
}

@article{MTMT:3291825,
	title = {Discovery and Preclinical Characterization of 3-((4-(4-Chlorophenyl)-7-fluoroquinoline-3-yl)sulfonyl)benzonitrile, a Novel Non-acetylenic Metabotropic Glutamate Receptor 5 (mGluR5) Negative Allosteric Modulator for Psychiatric Indications},
	url = {https://m2.mtmt.hu/api/publication/3291825},
	author = {Galambos, J and Bielik, A and Krasavin, M and Orgován, Zoltán and Domány, G and Nógrádi, K and Wágner, G and Balogh, György Tibor and Béni, Zoltán and Kóti, János and Szakács, Zoltán and Bobok, A and Kolok, S and Mikó-Bakk, ML and Vastag, Monika and Sághy, K and Laszy, J and Halász, AS and Balázs, O and Gál, K and Greiner, István and Szombathelyi, Zsolt and Keserű, György Miklós},
	doi = {10.1021/acs.jmedchem.6b01858},
	journal-iso = {J MED CHEM},
	journal = {JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {60},
	unique-id = {3291825},
	issn = {0022-2623},
	year = {2017},
	eissn = {1520-4804},
	pages = {2470-2484},
	orcid-numbers = {Balogh, György Tibor/0000-0003-3347-1880; Béni, Zoltán/0000-0002-1275-4155}
}