@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}
}

@mastersthesis{MTMT:36163688,
	title = {Identification of covalent inhibitors against oncogenic protein targets},
	url = {https://m2.mtmt.hu/api/publication/36163688},
	author = {Péczka, Nikolett},
	publisher = {Budapest University of Technology and Economics},
	unique-id = {36163688},
	year = {2025}
}

@article{MTMT:36001331,
	title = {Size-Dependent Target Engagement of Covalent Probes},
	url = {https://m2.mtmt.hu/api/publication/36001331},
	author = {Petri, László and Gabizon, Ronen and Ferenczy, György and Péczka, Nikolett and Egyed, Attila and Ábrányi-Balogh, Péter and Takács, Tamás and Keserű, György Miklós},
	doi = {10.1021/acs.jmedchem.5c00017},
	journal-iso = {J MED CHEM},
	journal = {JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {68},
	unique-id = {36001331},
	issn = {0022-2623},
	abstract = {Labeling proteins with covalent ligands is finding increasing use in proteomics applications, including identifying nucleophilic residues amenable for labeling and in the development of targeted covalent inhibitors (TCIs). Labeling efficiency is measured by the covalent occupancy of the target or by biochemical activity. Here, we investigate how these observed quantities relate to the intrinsic parameters of complex formation, namely, noncovalent affinity and covalent reactivity, and to experimental conditions, including incubation time and ligand concentration. It is shown that target engagement is beneficially driven by noncovalent recognition for lead-like compounds, which are appropriate starting points for targeted covalent inhibitors owing to their easily detectable occupancy and fixed binding mode, facilitating optimization. In contrast, labeling by fragment-sized compounds is inevitably reactivity-driven as their small size limits noncovalent affinity. They are well-suited for exploring ligandable nucleophilic residues, while small fragments are less appropriate starting points for TCI development.},
	year = {2025},
	eissn = {1520-4804},
	pages = {6616-6632},
	orcid-numbers = {Petri, László/0000-0001-9881-5096; Gabizon, Ronen/0000-0002-3626-5073; Ferenczy, György/0000-0002-5771-4616}
}

@article{MTMT:36122949,
	title = {Allosteric Covalent Inhibitors of the STAT3 Transcription Factor from Virtual Screening},
	url = {https://m2.mtmt.hu/api/publication/36122949},
	author = {Szalai, Tibor Viktor and Di Lorenzo, Vincenzo and Péczka, Nikolett and Mihalovits, Levente Márk and Petri, László and Ashraf, Qirat F. and de Araujo, Elvin D. and Honti, Viktor and Bajusz, Dávid and Keserű, György Miklós},
	doi = {10.1021/acsmedchemlett.4c00622},
	journal-iso = {ACS MED CHEM LETT},
	journal = {ACS MEDICINAL CHEMISTRY LETTERS},
	volume = {16},
	unique-id = {36122949},
	issn = {1948-5875},
	abstract = {The STAT family of transcription factors are important signaling hubs, with several of them, particularly STAT3, being emerging oncotargets already investigated in clinical trials. The modular structure of STAT3 nominates several of its protein domains as possible drug targets, but their exploitation with potential small-molecule inhibitors has been unevenly distributed so far, with past efforts highly favoring the conserved SH2 domain. Here, we have targeted a sparsely studied binding site at the junction of the coiled-coil and DNA-binding domains and discovered several new lead-like covalent inhibitors by virtual screening. The most favorable hit compound has been explored via structure-guided hit expansion and optimized into a low micromolar inhibitor. This compound can serve as a chemical biology tool against this site in future exploratory studies or form the basis of a more advanced stage of lead optimization. © 2025 The Authors. Published by American Chemical Society.},
	year = {2025},
	pages = {991-997},
	orcid-numbers = {Mihalovits, Levente Márk/0000-0003-1022-3294; Petri, László/0000-0001-9881-5096; Bajusz, Dávid/0000-0003-4277-9481}
}

@article{MTMT:36228040,
	title = {Ultrahigh-Throughput Virtual Screening Strategies against PPI Targets: A Case Study of STAT Inhibitors},
	url = {https://m2.mtmt.hu/api/publication/36228040},
	author = {Szalai, Tibor Viktor and Péczka, Nikolett and Sipos-Szabó, Levente and Petri, László and Bajusz, Dávid and Keserű, György Miklós},
	doi = {10.1021/acs.jcim.5c00907},
	journal-iso = {J CHEM INF MODEL},
	journal = {JOURNAL OF CHEMICAL INFORMATION AND MODELING},
	volume = {65},
	unique-id = {36228040},
	issn = {1549-9596},
	abstract = {In recent years, virtual screening of ultralarge (108+) libraries of synthetically accessible compounds (uHTVS) became a popular approach in hit identification. With AI-assisted virtual screening workflows, such as Deep Docking, these protocols might be feasible even without supercomputers. Yet, these methodologies have their own conceptual limitations, including the fact that physics-based docking is replaced by a cheaper deep learning (DL) step for the vast majority of compounds. In turn, the performance of this DL step will highly depend on the performance of the underlying docking model that is used to evaluate parts of the whole data set to train the DL architecture itself. Here, we evaluated the performance of the popular Deep Docking workflow on compound libraries of different sizes, against benchmark cases of classic brute-force docking approaches conducted on smaller libraries. We were especially interested in more difficult, protein-protein interaction-type oncotargets where the reliability of the underlying docking model is harder to assess. Specifically, our virtual screens have resulted in several new inhibitors of two oncogenic transcription factors, STAT3 and STAT5b. For STAT5b, in particular, we disclose the first application of virtual screening against its N-terminal domain, whose importance was recognized more recently. While the AI-based uHTVS is computationally more demanding, it can achieve exceptionally good hit rates (50.0% for STAT3). Deep Docking can also work well with a compound library containing only several million (instead of several billion) compounds, achieving a 42.9% hit rate against the SH2 domain of STAT5b, while presenting a highly economic workflow with just under 120,000 compounds actually docked. © 2025 The Authors. Published by American Chemical Society.},
	year = {2025},
	eissn = {1549-960X},
	pages = {7734-7748},
	orcid-numbers = {Petri, László/0000-0001-9881-5096; Bajusz, Dávid/0000-0003-4277-9481}
}

@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 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 Martinek, Tamas A. 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:35431408,
	title = {Target‐templated Construction of Functional Proteomimetics Using Photo‐foldamer Libraries},
	url = {https://m2.mtmt.hu/api/publication/35431408},
	author = {Wéber, Edit and Ábrányi-Balogh, Péter 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 and Szalai, Tibor V. and Takács, Tamás and de Araujo, Elvin and Buday, László and Perczel, András and Martinek, Tamás and Keserű, György Miklós},
	doi = {10.1002/anie.202410435},
	journal-iso = {ANGEW CHEM INT EDIT},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	volume = {64},
	unique-id = {35431408},
	issn = {1433-7851},
	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.},
	keywords = {photoaffinity labeling; Protein-protein interaction; foldamer; fragment screening; protein design},
	year = {2025},
	eissn = {1521-3773},
	orcid-numbers = {Wéber, Edit/0000-0002-5904-0619; Karancsiné Menyhárd, Dóra/0000-0002-0095-5531; Gadanecz, Márton/0009-0009-8076-7597; Schlosser, Gitta (Vácziné)/0000-0002-7637-7133; Bogár, Ferenc/0000-0002-0611-1452; Bajusz, Dávid/0000-0003-4277-9481; Kecskeméti, Gábor/0000-0002-5584-6869; Szabó, Zoltán/0000-0001-8278-8038; Bartus, Éva/0000-0001-9976-6978; Tököli, Attila/0000-0001-8413-3182; Tóth, Gábor/0000-0002-3604-4385; Buday, László/0000-0003-3518-5757; Perczel, András/0000-0003-1252-6416; Martinek, Tamás/0000-0003-3168-8066}
}

@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: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}
}

@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:31291784,
	title = {Preparation of 2-phospholene oxides by the isomerization of 3-phospholene oxides},
	url = {https://m2.mtmt.hu/api/publication/31291784},
	author = {Bagi, Péter and Herbay, Réka Gizella and Péczka, Nikolett and Mucsi, Zoltán and Timári, István and Keglevich, György},
	doi = {10.3762/bjoc.16.75},
	journal-iso = {BEILSTEIN J ORG CHEM},
	journal = {BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY},
	volume = {16},
	unique-id = {31291784},
	issn = {1860-5397},
	abstract = {A series of 1-substituted-3-methyl-2-phospholene oxides was prepared from the corresponding 3-phospholene oxides by double bond rearrangement. The 2-phospholene oxides could be obtained by heating the 3-phospholene oxides in methanesulfonic acid, or via the formation of cyclic chlorophosphonium salts. Whereas mixtures of the 2- and 3-phospholene oxides formed, when the isomerization of 3-phospholene oxides was attempted under thermal conditions, or in the presence of a base. The mechanisms of the various double bond migration pathways were elucidated by quantum chemical calculations.},
	keywords = {ISOMERIZATION; Quantum chemistry; Chlorophosphonium salts; 2-phospholene oxides; 3-phospholene oxides},
	year = {2020},
	eissn = {1860-5397},
	pages = {818-832},
	orcid-numbers = {Bagi, Péter/0000-0002-9043-6435; Mucsi, Zoltán/0000-0003-3224-8847; Keglevich, György/0000-0002-5366-472X}
}

@article{MTMT:30385211,
	title = {Isomerization and application of phospholene oxides},
	url = {https://m2.mtmt.hu/api/publication/30385211},
	author = {Herbay, Réka Gizella and Péczka, Nikolett and Györke, Gábor and Bagi, Péter and Fogassy, Elemér and Keglevich, György},
	doi = {10.1080/10426507.2018.1553043},
	journal-iso = {PHOSPHOR SULFUR SIL REL ELEM},
	journal = {PHOSPHORUS SULFUR AND SILICON AND THE RELATED ELEMENTS},
	volume = {194},
	unique-id = {30385211},
	issn = {1042-6507},
	year = {2019},
	eissn = {1563-5325},
	pages = {610-613},
	orcid-numbers = {Györke, Gábor/0000-0002-5882-9837; Bagi, Péter/0000-0002-9043-6435}
}

@misc{MTMT:32112749,
	title = {P-Sztereogén centrumot tartalmazó foszfin-oxidok alkalmazása enantioszelektív katalitikus Wittig-reakcióban},
	url = {https://m2.mtmt.hu/api/publication/32112749},
	author = {Péczka, Nikolett},
	unique-id = {32112749},
	year = {2019}
}

@misc{MTMT:32112809,
	title = {Investigation of the isomerization of 1-substituted 3-methyl-3-phospholene oxides},
	url = {https://m2.mtmt.hu/api/publication/32112809},
	author = {Péczka, Nikolett},
	unique-id = {32112809},
	year = {2018}
}

@misc{MTMT:32112736,
	title = {1-Szubsztituált-3-metil-3-foszfolén-oxidok izomerizációjának vizsgálata},
	url = {https://m2.mtmt.hu/api/publication/32112736},
	author = {Péczka, Nikolett},
	unique-id = {32112736},
	year = {2017}
}