@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: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: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:32869275,
	title = {Maximizing the integration of virtual and experimental screening in hit discovery},
	url = {https://m2.mtmt.hu/api/publication/32869275},
	author = {Bajusz, Dávid and Keserű, György Miklós},
	doi = {10.1080/17460441.2022.2085685},
	journal-iso = {EXPERT OPIN DRUG DIS},
	journal = {EXPERT OPINION ON DRUG DISCOVERY},
	volume = {17},
	unique-id = {32869275},
	issn = {1746-0441},
	year = {2022},
	eissn = {1746-045X},
	pages = {629-640},
	orcid-numbers = {Bajusz, Dávid/0000-0003-4277-9481}
}

@article{MTMT:33119096,
	title = {Semisynthetic teicoplanin derivatives with dual antimicrobial activity against SARS-CoV-2 and multiresistant bacteria},
	url = {https://m2.mtmt.hu/api/publication/33119096},
	author = {Bakai-Bereczki, Ilona and Vimberg, Vladimir and Lőrincz, Eszter Boglárka and Papp, Henrietta and Nagy, Lajos and Kéki, Sándor and Batta, Gyula and Mitrović, Ana and Kos, Janko and Zsigmond, Áron and Hajdú, István and Lőrincz, Zsolt and Bajusz, Dávid and Petri, László and Hodek, Jan and Jakab, Ferenc and Keserű, György Miklós and Weber, Jan and Naesens, Lieve and Herczegh, Pál and Borbás, Anikó},
	doi = {10.1038/s41598-022-20182-y},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {12},
	unique-id = {33119096},
	issn = {2045-2322},
	abstract = {Patients infected with SARS-CoV-2 risk co-infection with Gram-positive bacteria, which severely affects their prognosis. Antimicrobial drugs with dual antiviral and antibacterial activity would be very useful in this setting. Although glycopeptide antibiotics are well-known as strong antibacterial drugs, some of them are also active against RNA viruses like SARS-CoV-2. It has been shown that the antiviral and antibacterial efficacy can be enhanced by synthetic modifications. We here report the synthesis and biological evaluation of seven derivatives of teicoplanin bearing hydrophobic or superbasic side chain. All but one teicoplanin derivatives were effective in inhibiting SARS-CoV-2 replication in VeroE6 cells. One lipophilic and three perfluoroalkyl conjugates showed activity against SARS-CoV-2 in human Calu-3 cells and against HCoV-229E, an endemic human coronavirus, in HEL cells. Pseudovirus entry and enzyme inhibition assays established that the teicoplanin derivatives efficiently prevent the cathepsin-mediated endosomal entry of SARS-CoV-2, with some compounds inhibiting also the TMPRSS2-mediated surface entry route. The teicoplanin derivatives showed good to excellent activity against Gram-positive bacteria resistant to all approved glycopeptide antibiotics, due to their ability to dually bind to the bacterial membrane and cell-wall. To conclude, we identified three perfluoralkyl and one monoguanidine analog of teicoplanin as dual inhibitors of Gram-positive bacteria and SARS-CoV-2.},
	year = {2022},
	eissn = {2045-2322},
	orcid-numbers = {Bakai-Bereczki, Ilona/0000-0003-4601-7257; Papp, Henrietta/0000-0003-3887-5657; Batta, Gyula/0000-0002-0442-1828; Bajusz, Dávid/0000-0003-4277-9481; Weber, Jan/0000-0002-2799-7352; Borbás, Anikó/0000-0001-8462-4547}
}

@article{MTMT:32476090,
	title = {Consensus Virtual Screening Identified [1,2,4]Triazolo[1,5-b]isoquinolines As MELK Inhibitor Chemotypes},
	url = {https://m2.mtmt.hu/api/publication/32476090},
	author = {Rácz, Anita and Palkó, Roberta and Csányi, Dorottya and Riedl, Zsuzsanna and Bajusz, Dávid and Keserű, György Miklós},
	doi = {10.1002/cmdc.202100569},
	journal-iso = {CHEMMEDCHEM},
	journal = {CHEMMEDCHEM},
	volume = {17},
	unique-id = {32476090},
	issn = {1860-7179},
	abstract = {Maternal Embryonic Leucine-zipper Kinase (MELK) is a current oncotarget involved in a diverse range of human cancers, with the usage of MELK inhibitors being explored clinically. Here, we aimed to discover new MELK inhibitor chemotypes from our in-house compound library with a consensus-based virtual screening workflow, employing three screening concepts. After careful retrospective validation, prospective screening and in vitro enzyme inhibition testing revealed a series of [1,2,4]triazolo[1,5-b]isoquinolines as a new structural class of MELK inhibitors, with the lead compound of the series exhibiting a sub-micromolar inhibitory activity. The structure-activity relationship of the series was explored by testing further analogs based on a structure-guided selection process. Importantly, the present work marks the first disclosure of the synthesis and bioactivity of this class of compounds. © 2021 The Authors. ChemMedChem published by Wiley-VCH GmbH},
	keywords = {KINASE; ISOQUINOLINE; Docking; Virtual screening; MELK inhibitor},
	year = {2022},
	eissn = {1860-7187},
	orcid-numbers = {Bajusz, Dávid/0000-0003-4277-9481}
}

@article{MTMT:32992489,
	title = {Molecular Dynamics Simulations and Diversity Selection by Extended Continuous Similarity Indices},
	url = {https://m2.mtmt.hu/api/publication/32992489},
	author = {Rácz, Anita and Mihalovits, Levente Márk and Bajusz, Dávid and Héberger, Károly and Miranda-Quintana, Ramón Alain},
	doi = {10.1021/acs.jcim.2c00433},
	journal-iso = {J CHEM INF MODEL},
	journal = {JOURNAL OF CHEMICAL INFORMATION AND MODELING},
	volume = {62},
	unique-id = {32992489},
	issn = {1549-9596},
	year = {2022},
	eissn = {1549-960X},
	pages = {3415-3425},
	orcid-numbers = {Mihalovits, Levente Márk/0000-0003-1022-3294; Bajusz, Dávid/0000-0003-4277-9481; Miranda-Quintana, Ramón Alain/0000-0003-2121-4449}
}

@article{MTMT:32741735,
	title = {Extended continuous similarity indices: theory and application for QSAR descriptor selection},
	url = {https://m2.mtmt.hu/api/publication/32741735},
	author = {Rácz, Anita and Dunn, Timothy B. and Bajusz, Dávid and Kim, Taewon D. and Miranda-Quintana, Ramón Alain and Héberger, Károly},
	doi = {10.1007/s10822-022-00444-7},
	journal-iso = {J COMPUT AID MOL DES},
	journal = {JOURNAL OF COMPUTER-AIDED MOLECULAR DESIGN},
	volume = {36},
	unique-id = {32741735},
	issn = {0920-654X},
	year = {2022},
	eissn = {1573-4951},
	pages = {157-173},
	orcid-numbers = {Bajusz, Dávid/0000-0003-4277-9481; Miranda-Quintana, Ramón Alain/0000-0003-2121-4449}
}

@article{MTMT:32561462,
	title = {Designed Peptide Inhibitors of STEP Phosphatase–GluA2 AMPA Receptor Interaction Enhance the Cognitive Performance in Rats},
	url = {https://m2.mtmt.hu/api/publication/32561462},
	author = {Szedlacsek, Horea Stefan and Bajusz, Dávid and Badea, Rodica Aura and Pop, Andreea and Bică, Constantin Cătălin and Ravasz, Lilla and Mittli, Dániel Árpád and Mátyás, Dominik and Necula-Petrăreanu, Georgiana and Munteanu, Cristian V. A. and Papp, Ildikó and Juhász, Gábor and Hritcu, Lucian and Keserű, György Miklós and Szedlacsek, Stefan Eugen},
	doi = {10.1021/acs.jmedchem.1c01303},
	journal-iso = {J MED CHEM},
	journal = {JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {65},
	unique-id = {32561462},
	issn = {0022-2623},
	year = {2022},
	eissn = {1520-4804},
	pages = {217-233},
	orcid-numbers = {Bajusz, Dávid/0000-0003-4277-9481; Szedlacsek, Stefan Eugen/0000-0002-3416-5036}
}

@article{MTMT:33129525,
	title = {Conservation of Allosteric Ligand Binding Sites in G-Protein Coupled Receptors},
	url = {https://m2.mtmt.hu/api/publication/33129525},
	author = {Wakefield, Amanda E. and Bajusz, Dávid and Kozakov, Dima and Keserű, György Miklós and Vajda, Sandor},
	doi = {10.1021/acs.jcim.2c00209},
	journal-iso = {J CHEM INF MODEL},
	journal = {JOURNAL OF CHEMICAL INFORMATION AND MODELING},
	volume = {62},
	unique-id = {33129525},
	issn = {1549-9596},
	year = {2022},
	eissn = {1549-960X},
	pages = {4937-4954},
	orcid-numbers = {Wakefield, Amanda E./0000-0001-7962-2686; Bajusz, Dávid/0000-0003-4277-9481; Kozakov, Dima/0000-0003-0464-4500; Vajda, Sandor/0000-0003-1540-8220}
}

@article{MTMT:32216560,
	title = {Discovery of a Non-Nucleoside SETD2 Methyltransferase Inhibitor against Acute Myeloid Leukemia},
	url = {https://m2.mtmt.hu/api/publication/32216560},
	author = {Bajusz, Dávid and Bognár, Zsolt and Ebner, Jessica and Grebien, Florian and Keserű, György Miklós},
	doi = {10.3390/ijms221810055},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {22},
	unique-id = {32216560},
	issn = {1661-6596},
	year = {2021},
	eissn = {1422-0067},
	orcid-numbers = {Bajusz, Dávid/0000-0003-4277-9481; Bognár, Zsolt/0000-0002-6839-8460; Ebner, Jessica/0000-0002-4606-6051; Grebien, Florian/0000-0003-4289-2281}
}

@article{MTMT:32173932,
	title = {Gyógyszertervezés számítógéppel - Hogyan tervezhetünk új hatóanyagokat?},
	url = {https://m2.mtmt.hu/api/publication/32173932},
	author = {Bajusz, Dávid},
	journal-iso = {ÉLET ÉS TUDOMÁNY},
	journal = {ÉLET ÉS TUDOMÁNY},
	volume = {76},
	unique-id = {32173932},
	issn = {0013-6077},
	year = {2021},
	pages = {1097-1099},
	orcid-numbers = {Bajusz, Dávid/0000-0003-4277-9481}
}

@article{MTMT:32089303,
	title = {Extended many-item similarity indices for sets of nucleotide and protein sequences},
	url = {https://m2.mtmt.hu/api/publication/32089303},
	author = {Bajusz, Dávid and Miranda-Quintana, Ramón Alain and Rácz, Anita and Héberger, Károly},
	doi = {10.1016/j.csbj.2021.06.021},
	journal-iso = {CSBJ},
	journal = {COMPUTATIONAL AND STRUCTURAL BIOTECHNOLOGY JOURNAL},
	volume = {19},
	unique-id = {32089303},
	issn = {2001-0370},
	year = {2021},
	eissn = {2001-0370},
	pages = {3628-3639},
	orcid-numbers = {Bajusz, Dávid/0000-0003-4277-9481}
}

@article{MTMT:32044302,
	title = {Exploring protein hotspots by optimized fragment pharmacophores},
	url = {https://m2.mtmt.hu/api/publication/32044302},
	author = {Bajusz, Dávid and Wade, Warren S. and Satała, Grzegorz and Bojarski, Andrzej J. and Ilaš, Janez and Ebner, Jessica and Grebien, Florian and Papp, Henrietta and Jakab, Ferenc and Douangamath, Alice and Fearon, Daren and von Delft, Frank and Schuller, Marion and Ahel, Ivan and Wakefield, Amanda and Vajda, Sándor and Gerencsér, János and Pallai, Péter and Keserű, György Miklós},
	doi = {10.1038/s41467-021-23443-y},
	journal-iso = {NAT COMMUN},
	journal = {NATURE COMMUNICATIONS},
	volume = {12},
	unique-id = {32044302},
	issn = {2041-1723},
	year = {2021},
	eissn = {2041-1723},
	orcid-numbers = {Bajusz, Dávid/0000-0003-4277-9481; Ilaš, Janez/0000-0002-0124-0474; Grebien, Florian/0000-0003-4289-2281; Papp, Henrietta/0000-0003-3887-5657; Douangamath, Alice/0000-0002-9196-8644; Fearon, Daren/0000-0003-3529-7863; von Delft, Frank/0000-0003-0378-0017; Gerencsér, János/0000-0002-1928-0650}
}

@article{MTMT:32473976,
	title = {Natural Apocarotenoids and Their Synthetic Glycopeptide Conjugates Inhibit SARS-CoV-2 Replication},
	url = {https://m2.mtmt.hu/api/publication/32473976},
	author = {Bakai-Bereczki, Ilona and Papp, Henrietta and Kuczmog, Anett and Madai, Mónika and Nagy, Veronika and Agócs, Attila and Batta, Gyula and Milánkovits, Márton and Ostorházi, Eszter and Mitrović, Ana and Kos, Janko and Zsigmond, Áron and Hajdú, István and Lőrincz, Zsolt and Bajusz, Dávid and Keserű, György Miklós and Hodek, Jan and Weber, Jan and Jakab, Ferenc and Herczegh, Pál and Borbás, Anikó},
	doi = {10.3390/ph14111111},
	journal-iso = {PHARMACEUTICALS-BASE},
	journal = {PHARMACEUTICALS},
	volume = {14},
	unique-id = {32473976},
	abstract = {The protracted global COVID-19 pandemic urges the development of new drugs against the causative agent SARS-CoV-2. The clinically used glycopeptide antibiotic, teicoplanin, emerged as a potential antiviral, and its efficacy was improved with lipophilic modifications. This prompted us to prepare new lipophilic apocarotenoid conjugates of teicoplanin, its pseudoaglycone and the related ristocetin aglycone. Their antiviral effect was tested against SARS-CoV-2 in Vero E6 cells, using a cell viability assay and quantitative PCR of the viral RNA, confirming their micromolar inhibitory activity against viral replication. Interestingly, two of the parent apocarotenoids, bixin and ?-apo-8'carotenoic acid, exerted remarkable anti-SARS-CoV-2 activity. Mechanistic studies involved cathepsin L and B, as well as the main protease 3CLPro, and the results were rationalized by computational studies. Glycopeptide conjugates show dual inhibitory action, while apocarotenoids have mostly cathepsin B and L affinity. Since teicoplanin is a marketed antibiotic and the natural bixin is an approved, cheap and widely used red colorant food additive, these readily available compounds and their conjugates as potential antivirals are worthy of further exploration.},
	keywords = {antiviral activity; Ristocetin; antibacterial activity; teicoplanin; bixin; crocetin; SARS-CoV-2; β-apocarotenoic acid},
	year = {2021},
	eissn = {1424-8247},
	orcid-numbers = {Bakai-Bereczki, Ilona/0000-0003-4601-7257; Papp, Henrietta/0000-0003-3887-5657; Kuczmog, Anett/0000-0002-5680-4951; Nagy, Veronika/0000-0002-9019-7980; Batta, Gyula/0000-0002-0442-1828; Ostorházi, Eszter/0000-0002-9459-7316; Mitrović, Ana/0000-0002-6996-4831; Hajdú, István/0000-0003-2312-0833; Bajusz, Dávid/0000-0003-4277-9481; Borbás, Anikó/0000-0001-8462-4547}
}

@article{MTMT:32030041,
	title = {Discrimination Ability of Assessors in Check-All-That-Apply Tests: Method and Product Development},
	url = {https://m2.mtmt.hu/api/publication/32030041},
	author = {Gere, Attila and Bajusz, Dávid and Biró, Barbara and Rácz, Anita},
	doi = {10.3390/foods10051123},
	journal-iso = {FOODS},
	journal = {FOODS},
	volume = {10},
	unique-id = {32030041},
	issn = {2304-8158},
	year = {2021},
	eissn = {2304-8158},
	orcid-numbers = {Gere, Attila/0000-0003-3075-1561; Bajusz, Dávid/0000-0003-4277-9481}
}

@article{MTMT:31664103,
	title = {Multicriteria decision making for evergreen problems in food science by sum of ranking differences},
	url = {https://m2.mtmt.hu/api/publication/31664103},
	author = {Gere, Attila and Rácz, Anita and Bajusz, Dávid and Héberger, Károly},
	doi = {10.1016/j.foodchem.2020.128617},
	journal-iso = {FOOD CHEM},
	journal = {FOOD CHEMISTRY},
	volume = {344},
	unique-id = {31664103},
	issn = {0308-8146},
	year = {2021},
	eissn = {1873-7072},
	orcid-numbers = {Gere, Attila/0000-0003-3075-1561; Bajusz, Dávid/0000-0003-4277-9481}
}

@article{MTMT:31836393,
	title = {Effect of An 84-bp Deletion of the Receptor-Binding Domain on the ACE2 Binding Affinity of the SARS-CoV-2 Spike Protein: An In Silico Analysis},
	url = {https://m2.mtmt.hu/api/publication/31836393},
	author = {Kemenesi, Gábor and Tóth, Gábor Endre and Bajusz, Dávid and Keserű, György Miklós and Terhes, Gabriella and Burián, Katalin and Zeghbib, Safia and Somogyi, Balázs Antal and Jakab, Ferenc},
	doi = {10.3390/genes12020194},
	journal-iso = {GENES-BASEL},
	journal = {GENES},
	volume = {12},
	unique-id = {31836393},
	issn = {2073-4425},
	year = {2021},
	eissn = {2073-4425},
	orcid-numbers = {Kemenesi, Gábor/0000-0001-9775-3065; Tóth, Gábor Endre/0000-0002-7201-9646; Bajusz, Dávid/0000-0003-4277-9481; Terhes, Gabriella/0000-0002-7301-9672; Burián, Katalin/0000-0003-1300-2374}
}

@article{MTMT:31984014,
	title = {Discovery of selective fragment-sized immunoproteasome inhibitors},
	url = {https://m2.mtmt.hu/api/publication/31984014},
	author = {Kollár, Levente and Gobec, Martina and Szilágyi, Bence and Proj, Matic and Knez, Damijan and Ábrányi-Balogh, Péter and Petri, László and Imre, Timea and Bajusz, Dávid and Ferenczy, György and Gobec, Stanislav and Keserű, György Miklós and Sosič, Izidor},
	doi = {10.1016/j.ejmech.2021.113455},
	journal-iso = {EUR J MED CHEM},
	journal = {EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {219},
	unique-id = {31984014},
	issn = {0223-5234},
	year = {2021},
	eissn = {1768-3254},
	orcid-numbers = {Bajusz, Dávid/0000-0003-4277-9481; Ferenczy, György/0000-0002-5771-4616; Gobec, Stanislav/0000-0002-9678-3083}
}