TY - JOUR AU - Keeley, Aaron Brian AU - Kopranovic, Aleksandra AU - Di Lorenzo, Vincenzo AU - Ábrányi-Balogh, Péter AU - Jänsch, Niklas AU - Lai, Linh N. AU - Petri, László AU - Orgován, Zoltán AU - Pölöske, Daniel AU - Orlova, Anna AU - Németh, András György AU - Desczyk, Charlotte AU - Imre, Timea AU - Bajusz, Dávid AU - Moriggl, Richard AU - Meyer-Almes, Franz-Josef AU - Keserű, György Miklós TI - Electrophilic MiniFrags Revealed Unprecedented Binding Sites for Covalent HDAC8 Inhibitors JF - JOURNAL OF MEDICINAL CHEMISTRY J2 - J MED CHEM VL - 67 PY - 2024 IS - 1 SP - 572 EP - 585 PG - 14 SN - 0022-2623 DO - 10.1021/acs.jmedchem.3c01779 UR - https://m2.mtmt.hu/api/publication/34445373 ID - 34445373 N1 - Medicinal Chemistry Research Group, Research Centre for Natural Sciences, Magyar tudósok krt 2, Budapest, H-1117, Hungary Department of Organic Chemistry and Technology, Faculty of Chemical Technology and Biotechnology, Budapest University of Technology and Economics, Müegyetem rkp. 3., Budapest, H-1111, Hungary National Laboratory for Drug Research and Development, Budapest, H-1117, Hungary Department of Chemical Engineering and Biotechnology, University of Applied Sciences Darmstadt, Haardtring 100, Darmstadt, 64295, Germany Institute of Animal Breeding and Genetics, University of Veterinary Medicine, Vienna, 1210, Austria MS Metabolomics Research Group, Research Centre for Natural Sciences, Magyar tudósok krt 2, Budapest, H-1117, Hungary Export Date: 14 March 2024 CODEN: JMCMA Correspondence Address: Meyer-Almes, F.-J.; Department of Chemical Engineering and Biotechnology, Haardtring 100, Germany; email: franz-josef.meyer-almes@h-da.de Correspondence Address: Keserü, G.M.; Medicinal Chemistry Research Group, Magyar tudósok krt 2, Hungary; email: keseru.gyorgy@ttk.hu AB - 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 LA - English DB - MTMT ER - TY - JOUR AU - Mihalovits, Levente Márk AU - Kollár, Levente AU - Bajusz, Dávid AU - Knez, Damijan AU - Bozovičar, Krištof AU - Imre, Timea AU - Ferenczy, György AU - Gobec, Stanislav AU - Keserű, György Miklós TI - Molecular Mechanism of Labelling Functional Cysteines by Heterocyclic Thiones JF - CHEMPHYSCHEM: A EUROPEAN JOURNAL OF CHEMICAL PHYSICS AND PHYSICAL CHEMISTRY J2 - CHEMPHYSCHEM VL - 25 PY - 2024 IS - 1 SN - 1439-4235 DO - 10.1002/cphc.202300596 UR - https://m2.mtmt.hu/api/publication/34223252 ID - 34223252 N1 - Medicinal Chemistry Research Group, HUN-REN Research Centre for Natural Sciences, Magyar tudósok krt. 2, Budapest, 1117, Hungary Department of Organic Chemistry and Technology, Faculty of Chemical Technology and Biotechnology, Budapest University of Technology and Economics, Műegyetem rkp. 3., Budapest, 1111, Hungary Department of Medicinal Chemistry, Faculty of Pharmacy, University of Ljubljana, Aškerčeva cesta 7, Ljubljana, 1000, Slovenia Department of Pharmaceutical Biology, Faculty of Pharmacy, University of Ljubljana, Aškerčeva cesta 7, Ljubljana, 1000, Slovenia MS Metabolomics Research Group, HUN-REN Research Centre for Natural Sciences, Magyar tudósok krt. 2, Budapest, 1117, Hungary Export Date: 24 November 2023 CODEN: CPCHF Correspondence Address: Bajusz, D.; Medicinal Chemistry Research Group, Magyar tudósok krt. 2, Hungary; email: bajusz.david@ttk.hu Correspondence Address: Keserű, G.M.; Medicinal Chemistry Research Group, Magyar tudósok krt. 2, Hungary; email: keseru.gyorgy@ttk.hu AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Bajusz, Dávid AU - Pándy-Szekeres, Gáspár AU - Takács, Ágnes AU - de Araujo, Elvin D AU - Keserű, György Miklós TI - SH2db, an information system for the SH2 domain JF - NUCLEIC ACIDS RESEARCH J2 - NUCLEIC ACIDS RES VL - 51 PY - 2023 IS - W1 SP - W542 EP - W552 SN - 0305-1048 DO - 10.1093/nar/gkad420 UR - https://m2.mtmt.hu/api/publication/33845452 ID - 33845452 N1 - Funding Agency and Grant Number: MSCA ITN ALLODD [956314]; National Research Development and Innovation Office of Hungary [K135150, RRF-2.3.1-21-2022-00015]; Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences; New National Excellence Program of the Ministry for Innovation and Technology [UNKP-22-5]; MSCA [956314, K135150] Funding text: MSCA ITN ALLODD [956314 to G.M.K.]; National Research Development and Innovation Office of Hungary [K135150, PharmaLab (RRF-2.3.1-21-2022-00015)]; the work of D.B. was supported by the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences and the 'UNKP-22-5 New National Excellence Program of the Ministry for Innovation and Technology. FUNDING for open access charge: MSCA-funded project 'ALLODD' [956314] and NRDIO grant [K135150]. AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Godoy, Andre Schutzer AU - Nakamura, Aline Minalli AU - Douangamath, Alice AU - Song, Yun AU - Noske, Gabriela Dias AU - Gawriljuk, Victor Oliveira AU - Fernandes, Rafaela Sachetto AU - Pereira, Humberto D Muniz AU - Oliveira, Ketllyn Irene Zagato AU - Fearon, Daren AU - Dias, Alexandre AU - Krojer, Tobias AU - Fairhead, Michael AU - Powell, Alisa AU - Dunnet, Louise AU - Brandao-Neto, Jose AU - Skyner, Rachael AU - Chalk, Rod AU - Bajusz, Dávid AU - Bege, Miklós AU - Borbás, Anikó AU - Keserű, György Miklós AU - von Delft, Frank AU - Oliva, Glaucius TI - Allosteric regulation and crystallographic fragment screening of SARS-CoV-2 NSP15 endoribonuclease JF - NUCLEIC ACIDS RESEARCH J2 - NUCLEIC ACIDS RES VL - 51 PY - 2023 IS - 10 SP - 5255 EP - 5270 PG - 16 SN - 0305-1048 DO - 10.1093/nar/gkad314 UR - https://m2.mtmt.hu/api/publication/33802561 ID - 33802561 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Bajusz, Dávid AU - Keserű, György Miklós TI - Maximizing the integration of virtual and experimental screening in hit discovery JF - EXPERT OPINION ON DRUG DISCOVERY J2 - EXPERT OPIN DRUG DIS VL - 17 PY - 2022 IS - 6 SP - 629 EP - 640 PG - 12 SN - 1746-0441 DO - 10.1080/17460441.2022.2085685 UR - https://m2.mtmt.hu/api/publication/32869275 ID - 32869275 LA - English DB - MTMT ER - TY - JOUR AU - Bakai-Bereczki, Ilona AU - Vimberg, Vladimir AU - Lőrincz, Eszter Boglárka AU - Papp, Henrietta AU - Nagy, Lajos AU - Kéki, Sándor AU - Batta, Gyula AU - Mitrović, Ana AU - Kos, Janko AU - Zsigmond, Áron AU - Hajdú, István AU - Lőrincz, Zsolt AU - Bajusz, Dávid AU - Petri, László AU - Hodek, Jan AU - Jakab, Ferenc AU - Keserű, György Miklós AU - Weber, Jan AU - Naesens, Lieve AU - Herczegh, Pál AU - Borbás, Anikó TI - Semisynthetic teicoplanin derivatives with dual antimicrobial activity against SARS-CoV-2 and multiresistant bacteria JF - SCIENTIFIC REPORTS J2 - SCI REP VL - 12 PY - 2022 IS - 1 PG - 15 SN - 2045-2322 DO - 10.1038/s41598-022-20182-y UR - https://m2.mtmt.hu/api/publication/33119096 ID - 33119096 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Rácz, Anita AU - Palkó, Roberta AU - Csányi, Dorottya AU - Riedl, Zsuzsanna AU - Bajusz, Dávid AU - Keserű, György Miklós TI - Consensus Virtual Screening Identified [1,2,4]Triazolo[1,5-b]isoquinolines As MELK Inhibitor Chemotypes JF - CHEMMEDCHEM J2 - CHEMMEDCHEM VL - 17 PY - 2022 IS - 2 SN - 1860-7179 DO - 10.1002/cmdc.202100569 UR - https://m2.mtmt.hu/api/publication/32476090 ID - 32476090 N1 - Plasma Chemistry Research Group, Research Centre for Natural Sciences, Magyar tudósok krt. 2, Budapest, 1117, Hungary Medicinal Chemistry Research Group, Research Centre for Natural Sciences, Magyar tudósok krt. 2, Budapest, 1117, Hungary Present affiliation: Organocatalysis Research Group, Research Centre for Natural Sciences, Magyar tudósok krt. 2, Budapest, 1117, Hungary Export Date: 3 November 2021 CODEN: CHEMG Correspondence Address: Bajusz, D.; Medicinal Chemistry Research Group, Magyar tudósok krt. 2, Hungary; email: bajusz.david@ttk.hu Funding details: Nemzeti Kutatási Fejlesztési és Innovációs Hivatal, NKFIH Funding details: Magyar Tudományos Akadémia, MTA Funding details: Hungarian Scientific Research Fund, OTKA, PD134416 Funding details: Innovációs és Technológiai Minisztérium Funding text 1: The authors thank their colleagues at the MS Metabolomics Laboratory Core Facility at RCNS for the HRMS measurements, and Károly Héberger for helpful discussions. The work of A.R. is supported by the National Research, Development and Innovation Office of Hungary (OTKA, contract no. PD134416). The work of D.B. is supported by the János Bolyai Research Scholarship of the Hungarian Academy of Sciences and the ÚNKP‐21‐5 New National Excellence Program of the Ministry for Innovation and Technology. AB - 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 LA - English DB - MTMT ER - TY - JOUR AU - Rácz, Anita AU - Mihalovits, Levente Márk AU - Bajusz, Dávid AU - Héberger, Károly AU - Miranda-Quintana, Ramón Alain TI - Molecular Dynamics Simulations and Diversity Selection by Extended Continuous Similarity Indices JF - JOURNAL OF CHEMICAL INFORMATION AND MODELING J2 - J CHEM INF MODEL VL - 62 PY - 2022 IS - 14 SP - 3415 EP - 3425 PG - 11 SN - 1549-9596 DO - 10.1021/acs.jcim.2c00433 UR - https://m2.mtmt.hu/api/publication/32992489 ID - 32992489 LA - English DB - MTMT ER - TY - JOUR AU - Rácz, Anita AU - Dunn, Timothy B. AU - Bajusz, Dávid AU - Kim, Taewon D. AU - Miranda-Quintana, Ramón Alain AU - Héberger, Károly TI - Extended continuous similarity indices: theory and application for QSAR descriptor selection JF - JOURNAL OF COMPUTER-AIDED MOLECULAR DESIGN J2 - J COMPUT AID MOL DES VL - 36 PY - 2022 IS - 3 SP - 157 EP - 173 PG - 17 SN - 0920-654X DO - 10.1007/s10822-022-00444-7 UR - https://m2.mtmt.hu/api/publication/32741735 ID - 32741735 LA - English DB - MTMT ER - TY - JOUR AU - Szedlacsek, Horea Stefan AU - Bajusz, Dávid AU - Badea, Rodica Aura AU - Pop, Andreea AU - Bică, Constantin Cătălin AU - Ravasz, Lilla AU - Mittli, Dániel Árpád AU - Mátyás, Dominik AU - Necula-Petrăreanu, Georgiana AU - Munteanu, Cristian V. A. AU - Papp, Ildikó AU - Juhász, Gábor AU - Hritcu, Lucian AU - Keserű, György Miklós AU - Szedlacsek, Stefan Eugen TI - Designed Peptide Inhibitors of STEP Phosphatase–GluA2 AMPA Receptor Interaction Enhance the Cognitive Performance in Rats JF - JOURNAL OF MEDICINAL CHEMISTRY J2 - J MED CHEM VL - 65 PY - 2022 IS - 1 SP - 217 EP - 233 PG - 17 SN - 0022-2623 DO - 10.1021/acs.jmedchem.1c01303 UR - https://m2.mtmt.hu/api/publication/32561462 ID - 32561462 LA - English DB - MTMT ER - TY - JOUR AU - Wakefield, Amanda E. AU - Bajusz, Dávid AU - Kozakov, Dima AU - Keserű, György Miklós AU - Vajda, Sandor TI - Conservation of Allosteric Ligand Binding Sites in G-Protein Coupled Receptors JF - JOURNAL OF CHEMICAL INFORMATION AND MODELING J2 - J CHEM INF MODEL VL - 62 PY - 2022 IS - 20 SP - 4937 EP - 4954 PG - 18 SN - 1549-9596 DO - 10.1021/acs.jcim.2c00209 UR - https://m2.mtmt.hu/api/publication/33129525 ID - 33129525 LA - English DB - MTMT ER - TY - JOUR AU - Bajusz, Dávid AU - Bognár, Zsolt AU - Ebner, Jessica AU - Grebien, Florian AU - Keserű, György Miklós TI - Discovery of a Non-Nucleoside SETD2 Methyltransferase Inhibitor against Acute Myeloid Leukemia JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 22 PY - 2021 IS - 18 SN - 1661-6596 DO - 10.3390/ijms221810055 UR - https://m2.mtmt.hu/api/publication/32216560 ID - 32216560 LA - English DB - MTMT ER - TY - JOUR AU - Bajusz, Dávid TI - Gyógyszertervezés számítógéppel - Hogyan tervezhetünk új hatóanyagokat? JF - ÉLET ÉS TUDOMÁNY J2 - ÉLET ÉS TUDOMÁNY VL - 76 PY - 2021 IS - 35 SP - 1097 EP - 1099 PG - 3 SN - 0013-6077 UR - https://m2.mtmt.hu/api/publication/32173932 ID - 32173932 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Bajusz, Dávid AU - Miranda-Quintana, Ramón Alain AU - Rácz, Anita AU - Héberger, Károly TI - Extended many-item similarity indices for sets of nucleotide and protein sequences JF - COMPUTATIONAL AND STRUCTURAL BIOTECHNOLOGY JOURNAL J2 - CSBJ VL - 19 PY - 2021 SP - 3628 EP - 3639 PG - 12 SN - 2001-0370 DO - 10.1016/j.csbj.2021.06.021 UR - https://m2.mtmt.hu/api/publication/32089303 ID - 32089303 LA - English DB - MTMT ER - TY - JOUR AU - Bajusz, Dávid AU - Wade, Warren S. AU - Satała, Grzegorz AU - Bojarski, Andrzej J. AU - Ilaš, Janez AU - Ebner, Jessica AU - Grebien, Florian AU - Papp, Henrietta AU - Jakab, Ferenc AU - Douangamath, Alice AU - Fearon, Daren AU - von Delft, Frank AU - Schuller, Marion AU - Ahel, Ivan AU - Wakefield, Amanda AU - Vajda, Sándor AU - Gerencsér, János AU - Pallai, Péter AU - Keserű, György Miklós TI - Exploring protein hotspots by optimized fragment pharmacophores JF - NATURE COMMUNICATIONS J2 - NAT COMMUN VL - 12 PY - 2021 IS - 1 PG - 10 SN - 2041-1723 DO - 10.1038/s41467-021-23443-y UR - https://m2.mtmt.hu/api/publication/32044302 ID - 32044302 LA - English DB - MTMT ER - TY - JOUR AU - Bakai-Bereczki, Ilona AU - Papp, Henrietta AU - Kuczmog, Anett AU - Madai, Mónika AU - Nagy, Veronika AU - Agócs, Attila AU - Batta, Gyula AU - Milánkovits, Márton AU - Ostorházi, Eszter AU - Mitrović, Ana AU - Kos, Janko AU - Zsigmond, Áron AU - Hajdú, István AU - Lőrincz, Zsolt AU - Bajusz, Dávid AU - Keserű, György Miklós AU - Hodek, Jan AU - Weber, Jan AU - Jakab, Ferenc AU - Herczegh, Pál AU - Borbás, Anikó TI - Natural Apocarotenoids and Their Synthetic Glycopeptide Conjugates Inhibit SARS-CoV-2 Replication JF - PHARMACEUTICALS J2 - PHARMACEUTICALS-BASE VL - 14 PY - 2021 IS - 11 PG - 25 SN - 1424-8247 DO - 10.3390/ph14111111 UR - https://m2.mtmt.hu/api/publication/32473976 ID - 32473976 N1 - * Megosztott szerzőség AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Gere, Attila AU - Bajusz, Dávid AU - Biró, Barbara AU - Rácz, Anita TI - Discrimination Ability of Assessors in Check-All-That-Apply Tests: Method and Product Development JF - FOODS J2 - FOODS VL - 10 PY - 2021 IS - 5 PG - 14 SN - 2304-8158 DO - 10.3390/foods10051123 UR - https://m2.mtmt.hu/api/publication/32030041 ID - 32030041 LA - English DB - MTMT ER - TY - JOUR AU - Gere, Attila AU - Rácz, Anita AU - Bajusz, Dávid AU - Héberger, Károly TI - Multicriteria decision making for evergreen problems in food science by sum of ranking differences JF - FOOD CHEMISTRY J2 - FOOD CHEM VL - 344 PY - 2021 PG - 10 SN - 0308-8146 DO - 10.1016/j.foodchem.2020.128617 UR - https://m2.mtmt.hu/api/publication/31664103 ID - 31664103 LA - English DB - MTMT ER - TY - JOUR AU - Kemenesi, Gábor AU - Tóth, Gábor Endre AU - Bajusz, Dávid AU - Keserű, György Miklós AU - Terhes, Gabriella AU - Burián, Katalin AU - Zeghbib, Safia AU - Somogyi, Balázs Antal AU - Jakab, Ferenc TI - 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 JF - GENES J2 - GENES-BASEL VL - 12 PY - 2021 IS - 2 PG - 10 SN - 2073-4425 DO - 10.3390/genes12020194 UR - https://m2.mtmt.hu/api/publication/31836393 ID - 31836393 N1 - D.B. and G.K. are supported by the János Bolyai Research Scholarship of the Hungarian Academy of Sciences. The research was partially performed (4150 Tapestation system measurements) with the help of the Genomics and Bioinformatics Core Facility at the Szentágothai Research Centre, University of Pécs. Journal Article; Research Support, Non-U.S. Gov't Funding Agency and Grant Number: Hungarian Scientific Research FundOrszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [OTKA KH129599]; National Research, Development and Innovation Office-National Laboratory of Virology program; European UnionEuropean Commission; European Social Fund: Comprehensive Development for Implementing Smart Specialization Strategies at the University of Pecs [EFOP-3.6.1.-16-2016-00004]; Higher Education Institutional Excellence Program of the Ministry for Innovation and Technology in Hungary, within University of Pecs [TUDFO/47138/2019-ITM]; Foreign Commonwealth and Development Office (UK) Funding text: This research was funded by the Hungarian Scientific Research Fund OTKA KH129599 and by National Research, Development and Innovation Office-National Laboratory of Virology program. The project was supported by the European Union, and co-financed by the European Social Fund: Comprehensive Development for Implementing Smart Specialization Strategies at the University of Pecs (EFOP-3.6.1.-16-2016-00004). The research was financed by the Higher Education Institutional Excellence Program of the Ministry for Innovation and Technology in Hungary, within the framework of the "Innovation for a sustainable life and environment" and "Multidisciplinary approach to brain function and disease" thematic programs of the University of Pecs (TUDFO/47138/2019-ITM). G.M.K. is grateful for the support of the Foreign Commonwealth and Development Office (UK). LA - English DB - MTMT ER - TY - JOUR AU - Kollár, Levente AU - Gobec, Martina AU - Szilágyi, Bence AU - Proj, Matic AU - Knez, Damijan AU - Ábrányi-Balogh, Péter AU - Petri, László AU - Imre, Timea AU - Bajusz, Dávid AU - Ferenczy, György AU - Gobec, Stanislav AU - Keserű, György Miklós AU - Sosič, Izidor TI - Discovery of selective fragment-sized immunoproteasome inhibitors JF - EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY J2 - EUR J MED CHEM VL - 219 PY - 2021 PG - 23 SN - 0223-5234 DO - 10.1016/j.ejmech.2021.113455 UR - https://m2.mtmt.hu/api/publication/31984014 ID - 31984014 LA - English DB - MTMT ER -