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 - THES AU - Orgován, Zoltán TI - Computational investigation of the allosteric modulation of metabotropic glutamate receptor 5 PB - Budapesti Műszaki és Gazdaságtudományi Egyetem PY - 2023 SP - 163 UR - https://m2.mtmt.hu/api/publication/34738155 ID - 34738155 LA - English DB - MTMT ER - TY - JOUR AU - Orgován, Zoltán AU - Péczka, Nikolett AU - Petri, László AU - Ábrányi-Balogh, Péter AU - Randelovic, Ivan AU - Tóth, Szilárd AU - Szakács, Gergely AU - Nyíri, Kinga AU - Vértessy, Beáta (Grolmuszné) AU - Pálfy, Gyula AU - Vida, István AU - Perczel, András AU - Tóvári, József AU - Keserű, György Miklós TI - Covalent fragment mapping of KRasG12C revealed novel chemotypes with in vivo potency JF - EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY J2 - EUR J MED CHEM VL - 250 PY - 2023 PG - 7 SN - 0223-5234 DO - 10.1016/j.ejmech.2023.115212 UR - https://m2.mtmt.hu/api/publication/33647485 ID - 33647485 N1 - Medicinal Chemistry Research Group, Research Centre for Natural Sciences, and National Drug Discovery and Development Laboratory, Budapest, Hungary Department of Organic Chemistry and Technology, Faculty of Chemical Technology and Biotechnology, Budapest University of Technology and Economics, Budapest, Hungary KINETO Lab Ltd, Budapest, Hungary Institute of Enzymology, Research Centre for Natural Sciences, Budapest, Hungary Department of Applied Biotechnology and Food Science, Budapest University of Technology and Economics, Hungary Laboratory of Structural Chemistry and Biology, Eötvös Loránd University, Budapest, Hungary MTA-ELTE Protein Modelling Research Group, Eötvös Loránd University, Budapest, Hungary Department of Experimental Pharmacology and the National Tumor Biology Laboratory, National Institute of Oncology, Budapest, Hungary CODEN: EJMCA Correspondence Address: Keserű, G.M.; Medicinal Chemistry Research Group, 2 Magyar tudósok kӧrútja, Hungary; email: keseru.gyorgy@ttk.hu AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Kiss-Szemán, Anna Júlia AU - Takács, Luca AU - Orgován, Zoltán AU - Stráner, Pál AU - Jákli, Imre AU - Schlosser, Gitta (Vácziné) AU - Masiulis, Simonas AU - Harmat, Veronika AU - Karancsiné Menyhárd, Dóra AU - Perczel, András TI - A carbapenem antibiotic inhibiting a mammalian serine protease: structure of the acylaminoacyl peptidase–meropenem complex JF - CHEMICAL SCIENCE J2 - CHEM SCI VL - 13 PY - 2022 IS - 48 SP - 14264 EP - 14276 PG - 13 SN - 2041-6520 DO - 10.1039/D2SC05520A UR - https://m2.mtmt.hu/api/publication/33307131 ID - 33307131 N1 - Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University, Pázmány Péter sétány 1/A, Budapest, Hungary Medicinal Chemistry Research Group, Research Centre for Natural Sciences, Budapest, Hungary ELKH-ELTE Protein Modelling Research Group, Eötvös Loránd Research Network, Budapest, Hungary ELKH-ELTE Lendület Ion Mobility Mass Spectrometry Research Group, Institute of Chemistry, Eötvös Loránd University, Budapest, Hungary Materials and Structural Analysis Division, Thermo Fisher Scientific, Eindhoven, Netherlands Export Date: 28 March 2023 CODEN: CSHCC Correspondence Address: Harmat, V.; Laboratory of Structural Chemistry and Biology, Pázmány Péter sétány 1/A, Hungary; email: veronika.harmat@ttk.elte.hu Correspondence Address: Menyhárd, D.K.; Laboratory of Structural Chemistry and Biology, Pázmány Péter sétány 1/A, Hungary; email: dora.k.menyhard@ttk.elte.hu Correspondence Address: Perczel, A.; Laboratory of Structural Chemistry and Biology, Pázmány Péter sétány 1/A, Hungary; email: perczel.andras@ttk.elte.hu AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Péczka, Nikolett AU - Orgován, Zoltán AU - Ábrányi-Balogh, Péter AU - Keserű, György Miklós TI - Electrophilic warheads in covalent drug discovery: an overview JF - EXPERT OPINION ON DRUG DISCOVERY J2 - EXPERT OPIN DRUG DIS VL - 17 PY - 2022 SP - 413 EP - 422 PG - 10 SN - 1746-0441 DO - 10.1080/17460441.2022.2034783 UR - https://m2.mtmt.hu/api/publication/32756662 ID - 32756662 N1 - CAplus AN 2022:310212; MEDLINE PMID: 35129005 (Journal; General Review; Article); LA - English DB - MTMT ER - TY - JOUR AU - Orgován, Zoltán AU - Ferenczy, György AU - Keserű, György Miklós TI - Allosteric Molecular Switches in Metabotropic Glutamate Receptors JF - CHEMMEDCHEM J2 - CHEMMEDCHEM VL - 16 PY - 2021 IS - 1 SP - 81 EP - 93 PG - 14 SN - 1860-7179 DO - 10.1002/cmdc.202000444 UR - https://m2.mtmt.hu/api/publication/31698584 ID - 31698584 AB - 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.. LA - English DB - MTMT ER - TY - JOUR AU - Jójárt, Balázs AU - Orgován, Zoltán AU - Márki, Árpád AU - Pándy-Szekeres, Gáspár AU - Ferenczy, György AU - Keserű, György Miklós TI - Allosteric activation of metabotropic glutamate receptor 5 JF - JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS J2 - J BIOMOL STRUCT DYN VL - 38 PY - 2020 IS - 9 SP - 2624 EP - 2632 PG - 10 SN - 0739-1102 DO - 10.1080/07391102.2019.1638302 UR - https://m2.mtmt.hu/api/publication/30834454 ID - 30834454 LA - English DB - MTMT ER - TY - JOUR AU - Karancsiné Menyhárd, Dóra AU - Pálfy, Gyula AU - Orgován, Zoltán AU - Vida, István AU - Keserű, György Miklós AU - Perczel, András TI - Structural impact of GTP binding on downstream KRAS signaling JF - CHEMICAL SCIENCE J2 - CHEM SCI VL - 11 PY - 2020 IS - 34 SP - 9272 EP - 9289 PG - 18 SN - 2041-6520 DO - 10.1039/d0sc03441j UR - https://m2.mtmt.hu/api/publication/31605838 ID - 31605838 N1 - Funding Agency and Grant Number: National Research, Development and Innovation Office of Hungary [NVKP_16-1-2016-0020, OTKA K116904, OTKA K116305]; Hungarian Ministry of Human Capacities; European Regional Development FundEuropean Union (EU) [VEKOP-2.3.2-16-2017-00014]; HunProtEx Funding text: The National Research, Development and Innovation Office of Hungary (grant numbers: NVKP_16-1-2016-0020, OTKA K116904, and OTKA K116305) and the Hungarian Ministry of Human Capacities and co-financed by the European Regional Development Fund (VEKOP-2.3.2-16-2017-00014) and HunProtEx. Funding Agency and Grant Number: National Research, Development and Innovation Office of Hungary [NVKP_16-1-2016-0020, OTKA K116904, OTKA K116305]; Hungarian Ministry of Human Capacities; European Regional Development FundEuropean Commission [VEKOP-2.3.2-16-2017-00014]; HunProtEx Funding text: The National Research, Development and Innovation Office of Hungary (grant numbers: NVKP_16-1-2016-0020, OTKA K116904, and OTKA K116305) and the Hungarian Ministry of Human Capacities and co-financed by the European Regional Development Fund (VEKOP-2.3.2-16-2017-00014) and HunProtEx. AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Orgován, Zoltán AU - Keserű, György Miklós TI - Small molecule inhibitors of RAS proteins with oncogenic mutations JF - CANCER AND METASTASIS REVIEWS J2 - CANCER METAST REV VL - 39 PY - 2020 SP - 1107 EP - 1126 PG - 20 SN - 0167-7659 DO - 10.1007/s10555-020-09911-9 UR - https://m2.mtmt.hu/api/publication/31473660 ID - 31473660 N1 - Export Date: 28 August 2020 CODEN: CMRED Correspondence Address: Keserű, G.M.; Medicinal Chemistry Research Group, Research Centre for Natural Sciences, 2 Magyar tudósok körútja, Hungary; email: gy.keseru@ttk.mta.hu Funding details: NVKP_16-1-2016-0020 Funding text 1: This work has been supported by the National Research, Development and Innovation Office under the contract number NVKP_16-1-2016-0020. Open access funding provided by ELKH Research Centre for Natural Sciences. AB - 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). LA - English DB - MTMT ER - TY - JOUR AU - Szabó, György AU - Kolok, Sándor AU - Orgován, Zoltán AU - Vastag, Monika AU - Béni, Zoltán AU - Kóti, János AU - Sághy, Katalin AU - Lévay, György István AU - Greiner, István AU - Keserű, György Miklós TI - Discovery of dihydropyrazino-benzimidazole derivatives as metabotropic glutamate receptor-2 (mGluR2) positive allosteric modulators (PAMs) JF - EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY J2 - EUR J MED CHEM VL - 186 PY - 2020 SN - 0223-5234 DO - 10.1016/j.ejmech.2019.111881 UR - https://m2.mtmt.hu/api/publication/30928052 ID - 30928052 LA - English DB - MTMT ER - TY - JOUR AU - Christopher, John A. AU - Orgován, Zoltán AU - Congreve, Miles AU - Doré, Andrew S. AU - Errey, James C. AU - Marshall, Fiona H. AU - Mason, Jonathan S. AU - Okrasa, Krzysztof AU - Rucktooa, Prakash AU - Serrano-Vega, Maria J. AU - Ferenczy, György AU - Keserű, György Miklós TI - 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 JF - JOURNAL OF MEDICINAL CHEMISTRY J2 - J MED CHEM VL - 62 PY - 2019 IS - 1 SP - 207 EP - 222 PG - 16 SN - 0022-2623 DO - 10.1021/acs.jmedchem.7b01722 UR - https://m2.mtmt.hu/api/publication/30334026 ID - 30334026 LA - English DB - MTMT ER - TY - JOUR AU - Nyíri, Kinga AU - Koppány, Gergely AU - Pálfy, Gyula AU - Vida, István AU - Tóth, Szilárd AU - Orgován, Zoltán AU - Randelovic, Ivan AU - Baranyi, Marcell AU - Molnár, Eszter AU - Keserű, György Miklós AU - Tóvári, József AU - Perczel, András AU - Vértessy, Beáta (Grolmuszné) AU - Tímár, József TI - Allélspecifikus inhibitorok nyomában: a RASopátia konzorcium célpontjában a KRAS fehérje onkogén mutációi JF - MAGYAR ONKOLÓGIA J2 - MAGYAR ONKOLÓGIA VL - 63 PY - 2019 IS - 4 SP - 310 EP - 323 PG - 10 SN - 0025-0244 UR - https://m2.mtmt.hu/api/publication/31038395 ID - 31038395 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Orgován, Zoltán AU - Ferenczy, György AU - Keserű, György Miklós TI - Fragment-Based Approaches for Allosteric Metabotropic Glutamate Receptor (mGluR) Modulators JF - CURRENT TOPICS IN MEDICINAL CHEMISTRY J2 - CURR TOP MED CHEM VL - 19 PY - 2019 IS - 19 SP - 1768 EP - 1781 PG - 14 SN - 1568-0266 DO - 10.2174/1568026619666190808150039 UR - https://m2.mtmt.hu/api/publication/30834430 ID - 30834430 LA - English DB - MTMT ER - TY - JOUR AU - Orgován, Zoltán AU - Ferenczy, György AU - Keserű, György Miklós TI - The role of water and protein flexibility in the structure-based virtual screening of allosteric GPCR modulators: an mGlu5 receptor case study JF - JOURNAL OF COMPUTER-AIDED MOLECULAR DESIGN J2 - J COMPUT AID MOL DES VL - 33 PY - 2019 IS - 9 SP - 787 EP - 797 PG - 11 SN - 0920-654X DO - 10.1007/s10822-019-00224-w UR - https://m2.mtmt.hu/api/publication/30834424 ID - 30834424 LA - English DB - MTMT ER - TY - JOUR AU - Orgován, Zoltán AU - Ferenczy, György AU - Steinbrecher, Thomas AU - Szilágyi, Bence AU - Bajusz, Dávid AU - Keserű, György Miklós TI - 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 JF - JOURNAL OF COMPUTER-AIDED MOLECULAR DESIGN J2 - J COMPUT AID MOL DES VL - 32 PY - 2018 IS - 2 SP - 331 EP - 345 PG - 15 SN - 0920-654X DO - 10.1007/s10822-018-0097-y UR - https://m2.mtmt.hu/api/publication/3333356 ID - 3333356 N1 - Megjegyzés-27191071 N1 Funding details: K111862, AHF, American Hungarian Foundation N1 Funding text: Program (project KTIA NAP_13) and by the Hungarian Science Foundation OTKA (project K111862) is gratefully acknowledged. Megjegyzés-27191022 N1 Funding details: K111862, AHF, American Hungarian Foundation N1 Funding text: Program (project KTIA NAP_13) and by the Hungarian Science Foundation OTKA (project K111862) is gratefully acknowledged. Medicinal Chemistry Research Group, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok krt. 2, Budapest, 1117, Hungary Schrödinger GmbH, Dynamostr. 13, Mannheim, 68165, Germany Cited By :7 Export Date: 6 September 2021 CODEN: JCADE Correspondence Address: Keserű, G.M.; Medicinal Chemistry Research Group, Magyar tudósok krt. 2, Hungary; email: gy.keseru@ttk.mta.hu LA - English DB - MTMT ER - TY - JOUR AU - Galambos, J AU - Bielik, A AU - Wágner, G AU - Domány, G AU - Kóti, János AU - Béni, Zoltán AU - Szigetvári, Á AU - Sánta, Z AU - Orgován, Zoltán AU - Bobok, A AU - Kiss, Béla AU - Mikó-Bakk, ML AU - Vastag, M AU - Sághy, K AU - Krasavin, M AU - Gál, K AU - Greiner, István AU - Szombathelyi, Zsolt AU - Keserű, György Miklós TI - Discovery of 4-amino-3-arylsulfoquinolines, a novel non-acetylenic chemotype of metabotropic glutamate 5 (mGlu5) receptor negative allosteric modulators JF - EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY J2 - EUR J MED CHEM VL - 133 PY - 2017 SP - 240 EP - 254 PG - 15 SN - 0223-5234 DO - 10.1016/j.ejmech.2017.03.071 UR - https://m2.mtmt.hu/api/publication/3291826 ID - 3291826 LA - English DB - MTMT ER - TY - JOUR AU - Galambos, J AU - Bielik, A AU - Krasavin, M AU - Orgován, Zoltán AU - Domány, G AU - Nógrádi, K AU - Wágner, G AU - Balogh, György Tibor AU - Béni, Zoltán AU - Kóti, János AU - Szakács, Zoltán AU - Bobok, A AU - Kolok, S AU - Mikó-Bakk, ML AU - Vastag, Monika AU - Sághy, K AU - Laszy, J AU - Halász, AS AU - Balázs, O AU - Gál, K AU - Greiner, István AU - Szombathelyi, Zsolt AU - Keserű, György Miklós TI - 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 JF - JOURNAL OF MEDICINAL CHEMISTRY J2 - J MED CHEM VL - 60 PY - 2017 IS - 6 SP - 2470 EP - 2484 PG - 15 SN - 0022-2623 DO - 10.1021/acs.jmedchem.6b01858 UR - https://m2.mtmt.hu/api/publication/3291825 ID - 3291825 LA - English DB - MTMT ER - TY - JOUR AU - Karancsiné Menyhárd, Dóra AU - Orgován, Zoltán AU - Szeltner, Zoltán AU - Szamosi, Ildikó AU - Harmat, Veronika TI - Catalytically distinct states captured in a crystal lattice: the substrate-bound and scavenger states of acylaminoacyl peptidase and their implications for functionality JF - ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY J2 - ACTA CRYSTALLOGR D VL - 71 PY - 2015 SP - 461 EP - 472 PG - 12 SN - 0907-4449 DO - 10.1107/S1399004714026819 UR - https://m2.mtmt.hu/api/publication/2832195 ID - 2832195 N1 - Megjegyzés-26265240 PN 3 MTA-ELTE Protein Modelling Research Group, Pázmány Péter Sétány 1/A, Budapest, 1117, Hungary Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University, Pázmány Péter Sétány 1/A, Budapest, 1117, Hungary Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok körútja 2, Budapest, 1117, Hungary Cited By :4 Export Date: 16 December 2019 CODEN: ABCRE Correspondence Address: Harmat, V.; MTA-ELTE Protein Modelling Research Group, Pázmány Péter Sétány 1/A, Hungary MTA-ELTE Protein Modelling Research Group, Pázmány Péter Sétány 1/A, Budapest, 1117, Hungary Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University, Pázmány Péter Sétány 1/A, Budapest, 1117, Hungary Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok körútja 2, Budapest, 1117, Hungary Cited By :4 Export Date: 17 December 2019 CODEN: ABCRE Correspondence Address: Harmat, V.; MTA-ELTE Protein Modelling Research Group, Pázmány Péter Sétány 1/A, Hungary LA - English DB - MTMT ER -