@article{MTMT:33283298, title = {Safe and Efficient Continuous-Flow Synthesis and Batchwise Hydrolysis of Ethyl 5-Acetyl-1H-pyrazole-3-carboxylate: A Key Synthon of Darolutamide}, url = {https://m2.mtmt.hu/api/publication/33283298}, author = {Szilágyi, Bence and Egyed, Attila and Mándity, István and Nagy, Tamás and Kátainé Fadgyas, Katalin and Volk, Balázs and Keserű György, M.}, doi = {10.1055/s-0042-1751389}, journal-iso = {SYNTHESIS-STUTTGART}, journal = {SYNTHESIS-STUTTGART}, volume = {55}, unique-id = {33283298}, issn = {0039-7881}, year = {2023}, eissn = {1437-210X}, pages = {959-966}, orcid-numbers = {Mándity, István/0000-0003-2865-6143; Volk, Balázs/0000-0002-2019-1874} } @misc{MTMT:33106229, title = {„Semmi sem olyan egyszerű, mint amilyennek látszik”. Darolutamid intermedier generikus szemmel}, url = {https://m2.mtmt.hu/api/publication/33106229}, author = {Poszávácz, László and Szilágyi, Bence and Nagy, Tamás and Egyed, Attila and Kátainé Fadgyas, Katalin and Keserű, György Miklós and Mándity, István and Volk, Balázs}, unique-id = {33106229}, year = {2022}, orcid-numbers = {Mándity, István/0000-0003-2865-6143; Volk, Balázs/0000-0002-2019-1874} } @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} } @article{MTMT:31951354, title = {Synthesis and characterization of new fluorescent boro-β-carboline dyes}, url = {https://m2.mtmt.hu/api/publication/31951354}, author = {Szepesi Kovács, Dénes and Hajdu, Imre and Mészáros, Gergely and Wittner, Lucia and Meszéna, Domokos and Tóth, Estilla Zsófia and Hegedűs, Zita and Randelovic, Ivan and Tóvári, József and Szabó, Tímea and Szilágyi, Bence and Milen, Mátyás and Keserű, György Miklós and Ábrányi-Balogh, Péter}, doi = {10.1039/D1RA02132J}, journal-iso = {RSC ADV}, journal = {RSC ADVANCES}, volume = {11}, unique-id = {31951354}, issn = {2046-2069}, year = {2021}, eissn = {2046-2069}, pages = {12802-12807}, orcid-numbers = {Wittner, Lucia/0000-0001-6800-0953; Meszéna, Domokos/0000-0003-4042-2542; Tóth, Estilla Zsófia/0000-0003-4732-5796; Randelovic, Ivan/0000-0003-0161-0022; Tóvári, József/0000-0002-5543-3204; Szabó, Tímea/0000-0003-0700-4680; Milen, Mátyás/0000-0002-3538-8872; Keserű, György Miklós/0000-0003-1039-7809; Ábrányi-Balogh, Péter/0000-0002-9284-5160} } @mastersthesis{MTMT:31353710, title = {Design and synthesis of D-amino acid oxidase inhibitors}, url = {https://m2.mtmt.hu/api/publication/31353710}, author = {Szilágyi, Bence}, publisher = {Budapest University of Technology and Economics}, unique-id = {31353710}, year = {2019} } @article{MTMT:30392129, title = {Synthesis and Biochemical Evaluation of Lid-Open D-Amino Acid Oxidase Inhibitors}, url = {https://m2.mtmt.hu/api/publication/30392129}, author = {Szilágyi, Bence and Hargitai, Csilla Eszter and Kelemen, Ádám Andor and Rácz, Anita and Ferenczy, György and Volk, Balázs and Keserű, György Miklós}, doi = {10.3390/molecules24020290}, journal-iso = {MOLECULES}, journal = {MOLECULES}, volume = {24}, unique-id = {30392129}, issn = {1420-3049}, year = {2019}, eissn = {1420-3049}, orcid-numbers = {Ferenczy, György/0000-0002-5771-4616; Volk, Balázs/0000-0002-2019-1874} } @article{MTMT:3333356, title = {Validation of tautomeric and protomeric binding modes by free energy calculations. A case study for the structure based optimization of d-amino acid oxidase inhibitors}, url = {https://m2.mtmt.hu/api/publication/3333356}, author = {Orgován, Zoltán and Ferenczy, György and Steinbrecher, Thomas and Szilágyi, Bence and Bajusz, Dávid and Keserű, György Miklós}, doi = {10.1007/s10822-018-0097-y}, journal-iso = {J COMPUT AID MOL DES}, journal = {JOURNAL OF COMPUTER-AIDED MOLECULAR DESIGN}, volume = {32}, unique-id = {3333356}, issn = {0920-654X}, year = {2018}, eissn = {1573-4951}, pages = {331-345}, orcid-numbers = {Ferenczy, György/0000-0002-5771-4616; Bajusz, Dávid/0000-0003-4277-9481} } @article{MTMT:3375019, title = {Discovery of D-amino acid oxidase inhibitors based on virtual screening against the lid-open enzyme conformation}, url = {https://m2.mtmt.hu/api/publication/3375019}, author = {Szilágyi, Bence and Skok, Ž and Rácz, Anita and Frlan, R and Ferenczy, György and Ilaš, J and Keserű, György Miklós}, doi = {10.1016/j.bmcl.2018.04.048}, journal-iso = {BIOORG MED CHEM LETT}, journal = {BIOORGANIC & MEDICINAL CHEMISTRY LETTERS}, volume = {28}, unique-id = {3375019}, issn = {0960-894X}, abstract = {D-Amino acid oxidase (DAAO) inhibitors are typically small polar compounds with often suboptimal pharmacokinetic properties. Features of the native binding site limit the operational freedom of further medicinal chemistry efforts. We therefore initiated a structure based virtual screening campaign based on the X-ray structures of DAAO complexes where larger ligands shifted the loop (lid opening) covering the native binding site. The virtual screening of our in-house collection followed by the in vitro test of the best ranked compounds led to the identification of a new scaffold with micromolar IC50. Subsequent SAR explorations enabled us to identify submicromolar inhibitors. Docking studies supported by in vitro activity measurements suggest that compounds bind to the active site with a salt-bridge characteristic to DAAO inhibitor binding. In addition, displacement of and interaction with the loop covering the active site contributes significantly to the activity of the most potent compounds. © 2018 Elsevier Ltd}, keywords = {structure-activity relationship; Virtual screening; d-amino acid oxidase; Open-lid conformation}, year = {2018}, eissn = {1464-3405}, pages = {1693-1698}, orcid-numbers = {Ferenczy, György/0000-0002-5771-4616} } @article{MTMT:30353690, title = {Drug discovery strategies and the preclinical development of D-amino-acid oxidase inhibitors as antipsychotic therapies}, url = {https://m2.mtmt.hu/api/publication/30353690}, author = {Szilágyi, Bence and Ferenczy, György and Keserű, György Miklós}, doi = {10.1080/17460441.2018.1524459}, journal-iso = {EXPERT OPIN DRUG DIS}, journal = {EXPERT OPINION ON DRUG DISCOVERY}, volume = {13}, unique-id = {30353690}, issn = {1746-0441}, abstract = {Introduction: D-amino-acid oxidase (DAAO) degrades D-serine, a co-agonist of the NMDA receptor whose dysfunction is involved in the positive, negative, and cognitive symptoms of schizophrenia. The inhibition of DAAO appears to be a viable strategy to increase D-serine level and to have therapeutic potential in schizophrenia. Areas covered: This review describes the efforts to develop DAAO inhibitors and to optimize their in vitro and in vivo effects in preclinical settings. The structural evolution of DAAO inhibitors is presented from simple carboxylic acid derivatives via small, planar compounds with carboxylic acid mimetics to extended compounds whose binding is possible owing to DAAO flexibility. Inhibitory potency and pharmacokinetic properties are discussed in the context of compounds’ ability to increase D-serine level and to show efficacy in animal models of schizophrenia. Expert opinion: The accumulated knowledge on the structural requirements of DAAO inhibitors and on their in vitro and in vivo effects provides appropriate basis to develop inhibitors with optimized potency, selectivity and pharmacokinetic profile including blood-brain penetration. In addition, the validation of DAAO inhibition therapy in alleviating the symptoms of schizophrenia requires further studies on the efficacy of DAAO inhibitors in behavioral assays of animals and on the species differences in D-serine metabolism. © 2018, © 2018 Informa UK Limited, trading as Taylor & Francis Group.}, keywords = {SCHIZOPHRENIA; D-SERINE; D-amino-acid oxidase}, year = {2018}, eissn = {1746-045X}, pages = {973-982}, orcid-numbers = {Ferenczy, György/0000-0002-5771-4616} } @article{MTMT:3344151, title = {Discovery of isatin and 1H-indazol-3-ol derivatives as d-amino acid oxidase (DAAO) inhibitors}, url = {https://m2.mtmt.hu/api/publication/3344151}, author = {Szilágyi, Bence and Kovacs, P and Ferenczy, György and Rácz, Anita and Németh, Krisztina and Benéné Visy, Júlia and Szabó, Pál Tamás and Ilas, J and Balogh, György Tibor and Monostory, Katalin and Vincze, István and Tábi, Tamás and Szökő, Éva and Keserű, György Miklós}, doi = {10.1016/j.bmc.2018.02.004}, journal-iso = {BIOORGAN MED CHEM}, journal = {BIOORGANIC & MEDICINAL CHEMISTRY}, volume = {26}, unique-id = {3344151}, issn = {0968-0896}, abstract = {d-Amino acid oxidase (DAAO) is a potential target in the treatment of schizophrenia as its inhibition increases brain d-serine level and thus contributes to NMDA receptor activation. Inhibitors of DAAO were sought testing [6+5] type heterocycles and identified isatin derivatives as micromolar DAAO inhibitors. A pharmacophore and structure-activity relationship analysis of isatins and reported DAAO inhibitors led us to investigate 1H-indazol-3-ol derivatives and nanomolar inhibitors were identified. The series was further characterized by pKa and isothermal titration calorimetry measurements. Representative compounds exhibited beneficial properties in in vitro metabolic stability and PAMPA assays. 6-fluoro-1H-indazol-3-ol (37) significantly increased plasma d-serine level in an in vivo study on mice. These results show that the 1H-indazol-3-ol series represents a novel class of DAAO inhibitors with the potential to develop drug candidates.}, year = {2018}, eissn = {1464-3391}, pages = {1579-1587}, orcid-numbers = {Ferenczy, György/0000-0002-5771-4616; Szabó, Pál Tamás/0000-0003-2260-4641; Balogh, György Tibor/0000-0003-3347-1880; Vincze, István/0000-0002-6843-7159; Tábi, Tamás/0000-0001-5343-0205; Szökő, Éva/0000-0003-1464-6403} } @CONFERENCE{MTMT:2517810, title = {N-(β-D-Glucopyranosyl) Oxadiazole- and 1,2,4-Triazolecarboxamides as Glycogen Phosphorylase Inhibitors: Synthesis, Enzyme Kinetics and Computational Evaluation}, url = {https://m2.mtmt.hu/api/publication/2517810}, author = {Somsák, László and M, Polyák and G, Varga and J, Begum and Szilágyi, Bence and Juhász, László and T, Docsa and P, Gergely and J M, Hayes}, booktitle = {27th International Carbohydrate Symposium}, unique-id = {2517810}, abstract = {I-P-58 (Abstracts p. 91)}, year = {2014}, orcid-numbers = {Somsák, László/0000-0002-9103-9845; Juhász, László/0000-0002-7462-7944} } @CONFERENCE{MTMT:2382460, title = {Synthesis and enzyme kinetic evaluation of heterocyclic bioisosteric analogues of N-acyl-N’-β-D-glucopyranosyl urea type glycogen phosphorylase inhibitors}, url = {https://m2.mtmt.hu/api/publication/2382460}, author = {Mária, Polyák and Gergő, Varga and Szilágyi, Bence and Tibor, Docsa and Pál, Gergely and Juhász, László and Somsák, László}, booktitle = {5th European Conference on Chemistry for Life Sciences, Abstract Book}, unique-id = {2382460}, year = {2013}, pages = {93}, orcid-numbers = {Juhász, László/0000-0002-7462-7944; Somsák, László/0000-0002-9103-9845} } @article{MTMT:2381496, title = {Synthesis, enzyme kinetics and computational evaluation of N-(beta-D-glucopyranosyl) oxadiazolecarboxamides as glycogen phosphorylase inhibitors}, url = {https://m2.mtmt.hu/api/publication/2381496}, author = {Polyák, M and Varga, G and Szilágyi, Bence and Juhász, László and Docsa, Tibor and Gergely, Pál and Begum, J and Hayes, JM and Somsák, László}, doi = {10.1016/j.bmc.2013.07.024}, journal-iso = {BIOORGAN MED CHEM}, journal = {BIOORGANIC & MEDICINAL CHEMISTRY}, volume = {21}, unique-id = {2381496}, issn = {0968-0896}, year = {2013}, eissn = {1464-3391}, pages = {5738-5747}, orcid-numbers = {Juhász, László/0000-0002-7462-7944; Somsák, László/0000-0002-9103-9845} } @{MTMT:2382468, title = {N-Acil-N’-β-D-glükopiranozil-karbamid típusú glikogén foszforiláz inhibitorok heterociklusos bioizosztér analógjainak szintézise és enzimkinetikai vizsgálata}, url = {https://m2.mtmt.hu/api/publication/2382468}, author = {Polyák, Mária and Varga, Gergely and Szilágyi, Bence and Docsa, Tibor and Gergely, Pál and Juhász, László and Somsák, László}, booktitle = {Vegyészkonferencia 2013}, unique-id = {2382468}, year = {2013}, pages = {114}, orcid-numbers = {Juhász, László/0000-0002-7462-7944; Somsák, László/0000-0002-9103-9845} } @CONFERENCE{MTMT:2314255, title = {SAR study of glycogen phosphorylase inhibitors: heterocycles as bioisosteric amide replacements in N-acyl-beta-D-glucopyranosylamines and N-acyl-N’-beta-D-glucopyranosyl ureas}, url = {https://m2.mtmt.hu/api/publication/2314255}, author = {Vágvölgyiné Tóth, Marietta and Gergely, Tibor Varga and Mária, Polyák and Szilágyi, Bence and Kun, Sándor and I, Takács and Juhász, László and Tibor, Docsa and Pál, Gergely and Somsák, László}, booktitle = {26th International Carbohydrate Symposium}, unique-id = {2314255}, year = {2012}, orcid-numbers = {Juhász, László/0000-0002-7462-7944; Somsák, László/0000-0002-9103-9845} } @CONFERENCE{MTMT:2034044, title = {SAR Study of Glycogen Phosphorylase Inhibitors: Heterocycles as Bioisosteric Amide Replacements in N-Acyl-beta-D-Glucopyranosylamines and N-Acyl-N’-beta-D-Glucopyranosyl Ureas}, url = {https://m2.mtmt.hu/api/publication/2034044}, author = {Vágvölgyiné Tóth, Marietta and Varga, G T and Polyák, M and Szilágyi, Bence and Kun, Sándor and Takács, I and Juhász, László and Docsa, T and Gergely, P and Somsák, László}, booktitle = {26th International Carbohydrate Symposium}, unique-id = {2034044}, year = {2012}, pages = {F80-F80}, orcid-numbers = {Juhász, László/0000-0002-7462-7944; Somsák, László/0000-0002-9103-9845} }