TY - JOUR AU - Nath Bhaumik, Kaushik AU - Hetényi, Anasztázia AU - Olajos, Gábor AU - Martins, Ana AU - Spohn, Réka AU - Németh, Lukács AU - Jójárt, Balázs AU - Szili, Petra AU - Dunai, Anett AU - Jangir, Pramod Kumar AU - Daruka, Lejla AU - Földesi, Imre AU - Kata, Diána AU - Pál, Csaba AU - Martinek, Tamás TI - Rationally designed foldameric adjuvants enhance antibiotic efficacy via promoting membrane hyperpolarization JF - MOLECULAR SYSTEMS DESIGN & ENGINEERING J2 - MOL SYST DES ENG VL - 7 PY - 2022 IS - 1 SP - 21 EP - 33 PG - 13 SN - 2058-9689 DO - 10.1039/D1ME00118C UR - https://m2.mtmt.hu/api/publication/32493048 ID - 32493048 N1 - Funding Agency and Grant Number: European Research CouncilEuropean Research Council (ERC)European Commission [H2020-ERC-2014-CoG 648364, H2020-ERC-2019-PoC 862077]; ELKH Lendulet Programme [LP-2017-10/2020]; National Research, Development and Innovation Office, HungaryNational Research, Development & Innovation Office (NRDIO) - Hungary [KKP 126506]; National Laboratory of Biotechnology Grant [NKFIH-871-3/2020, GINOP-2.3.2-15-2016-00014, GINOP-2.3.2-15-2016-00020]; NKFINational Research, Development & Innovation Office (NRDIO) - Hungary [PD 116222, K134754]; Ministry of Human Capacities, Hungary [20391-3/2018/FEKUSTRAT] Funding text: The study was supported by the following research grants: European Research Council H2020-ERC-2014-CoG 648364-Resistance Evolution (CP); European Research Council H2020-ERC-2019-PoC 862077-Aware (CP), ELKH Lendulet Programme LP-2017-10/2020 (CP); 'Elvonal' Programme KKP 126506 of the National Research, Development and Innovation Office, Hungary (CP), National Laboratory of Biotechnology Grant NKFIH-871-3/2020 (CP), GINOP-2.3.2-15-2016-00014 (EVOMER) (CP, TAM), GINOP-2.3.2-15-2016-00020 (MolMedEx TUMORDNS) (CP), and NKFI PD 116222 (AM), NKFI K134754 (TAM), Ministry of Human Capacities, Hungary grant 20391-3/2018/FEKUSTRAT (TAM). The authors thank Dora Bokor, PharmD, for proofreading the manuscript. AB - The negative membrane potential of bacterial cells influences crucial cellular processes. Inspired by the molecular scaffold of the antimicrobial peptide PGLa, we have developed antimicrobial foldamers with a computer-guided design strategy. The novel PGLa analogues induce sustained membrane hyperpolarization. When co-administered as an adjuvant, the resulting compounds - PGLb1 and PGLb2 - have substantially reduced the level of antibiotic resistance of multi-drug resistant Escherichia coli, Klebsiella pneumoniae and Shigella flexneri clinical isolates. The observed antibiotic potentiation was mediated by hyperpolarization of the bacterial membrane caused by the alteration of cellular ion transport. Specifically, PGLb1 and PGLb2 are selective ionophores that enhance the Goldman-Hodgkin-Katz potential across the bacterial membrane. These findings indicate that manipulating bacterial membrane electrophysiology could be a valuable tool to overcome antimicrobial resistance. LA - English DB - MTMT ER - TY - CONF AU - Fási, Laura AU - Vágvölgyi, Máté AU - Latif, Ahmed Dhahir AU - Issaadi, Halima Meriem AU - Zoofishan, Zoofishan AU - Zupkó, István AU - Spengler, Gabriella AU - Martins, Ana AU - Hunyadi, Attila TI - Natural product inspired chemical approaches against MDR cancer T2 - New Diagnostic and Therapeutic Tools against Multidrug-Resistant Tumours PY - 2019 SP - 12 EP - 13 PG - 2 UR - https://m2.mtmt.hu/api/publication/31192702 ID - 31192702 LA - English DB - MTMT ER - TY - JOUR AU - Kintses, Bálint AU - Jangir, Pramod Kumar AU - Fekete, Gergely AU - Számel, Mónika AU - Méhi, Orsolya Katinka AU - Spohn, Réka AU - Daruka, Lejla AU - Martins, Ana AU - Hosseinnia, A. AU - Gagarinova, A. AU - Kim, S. AU - Phanse, S. AU - Csörgő, Bálint AU - Györkei, Ádám AU - Ari, Eszter AU - Lázár, Viktória AU - Nagy, István AU - Babu, M. AU - Pál, Csaba AU - Papp, Balázs TI - Chemical-genetic profiling reveals limited cross-resistance between antimicrobial peptides with different modes of action JF - NATURE COMMUNICATIONS J2 - NAT COMMUN VL - 10 PY - 2019 IS - 1 SN - 2041-1723 DO - 10.1038/s41467-019-13618-z UR - https://m2.mtmt.hu/api/publication/31038930 ID - 31038930 N1 - Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Szeged, Hungary HCEMM-BRC Translational Microbiology Lab, Szeged, Hungary Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, Hungary Doctoral School of Biology, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary HCEMM-BRC Metabolic Systems Biology Lab, Szeged, Hungary Department of Biochemistry, University of Regina, Regina, SK, Canada Department of Biochemistry, University of Saskatchewan, Saskatoon, SK, Canada Department of Genetics, Eötvös Loránd University, Budapest, Hungary Sequencing Platform, Institute of Biochemistry, Biological Research Centre, Szeged, Hungary Department of Microbiology and Immunology, University of California, San Francisco, United States Faculty of Biology, Technion – Israel Institute of Technology, Haifa, Israel Export Date: 6 January 2020 Correspondence Address: Kintses, B.; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research CentreHungary; email: kintses.balint@brc.hu Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Szeged, Hungary HCEMM-BRC Translational Microbiology Lab, Szeged, Hungary Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, Hungary Doctoral School of Biology, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary HCEMM-BRC Metabolic Systems Biology Lab, Szeged, Hungary Department of Biochemistry, University of Regina, Regina, SK, Canada Department of Biochemistry, University of Saskatchewan, Saskatoon, SK, Canada Department of Genetics, Eötvös Loránd University, Budapest, Hungary Sequencing Platform, Institute of Biochemistry, Biological Research Centre, Szeged, Hungary Department of Microbiology and Immunology, University of California, San Francisco, United States Faculty of Biology, Technion – Israel Institute of Technology, Haifa, Israel Export Date: 23 January 2020 Correspondence Address: Kintses, B.; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research CentreHungary; email: kintses.balint@brc.hu Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Szeged, Hungary HCEMM-BRC Translational Microbiology Lab, Szeged, Hungary Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, Hungary Doctoral School of Biology, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary HCEMM-BRC Metabolic Systems Biology Lab, Szeged, Hungary Department of Biochemistry, University of Regina, Regina, SK, Canada Department of Biochemistry, University of Saskatchewan, Saskatoon, SK, Canada Department of Genetics, Eötvös Loránd University, Budapest, Hungary Sequencing Platform, Institute of Biochemistry, Biological Research Centre, Szeged, Hungary Department of Microbiology and Immunology, University of California, San Francisco, United States Faculty of Biology, Technion – Israel Institute of Technology, Haifa, Israel Cited By :1 Export Date: 24 August 2020 Correspondence Address: Kintses, B.; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research CentreHungary; email: kintses.balint@brc.hu Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Szeged, Hungary HCEMM-BRC Translational Microbiology Lab, Szeged, Hungary Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, Hungary Doctoral School of Biology, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary HCEMM-BRC Metabolic Systems Biology Lab, Szeged, Hungary Department of Biochemistry, University of Regina, Regina, SK, Canada Department of Biochemistry, University of Saskatchewan, Saskatoon, SK, Canada Department of Genetics, Eötvös Loránd University, Budapest, Hungary Sequencing Platform, Institute of Biochemistry, Biological Research Centre, Szeged, Hungary Department of Microbiology and Immunology, University of California, San Francisco, United States Faculty of Biology, Technion – Israel Institute of Technology, Haifa, Israel Cited By :3 Export Date: 8 December 2020 Correspondence Address: Kintses, B.; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research CentreHungary; email: kintses.balint@brc.hu LA - English DB - MTMT ER - TY - JOUR AU - Spohn, Réka AU - Daruka, Lejla AU - Lázár, Viktória AU - Martins, Ana AU - Vidovics, Fanni AU - Grézal, Gábor AU - Méhi, Orsolya Katinka AU - Kintses, Bálint AU - Számel, Mónika AU - Jangir, Pramod Kumar AU - Csörgő, Bálint AU - Györkei, Ádám AU - Bódi, Zoltán AU - Faragó, Anikó AU - Bodai, László AU - Földesi, Imre AU - Kata, Diána AU - Maróti, Gergely AU - Pap, Bernadett AU - Wirth, Roland AU - Papp, Balázs AU - Pál, Csaba TI - Integrated evolutionary analysis reveals antimicrobial peptides with limited resistance JF - NATURE COMMUNICATIONS J2 - NAT COMMUN VL - 10 PY - 2019 PG - 13 SN - 2041-1723 DO - 10.1038/s41467-019-12364-6 UR - https://m2.mtmt.hu/api/publication/30865039 ID - 30865039 N1 - Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Szeged, Hungary Doctoral School of Biology, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary HCEMM-BRC Metabolic Systems Biology Lab, Szeged, Hungary Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, Hungary Department of Laboratory Medicine, University of Szeged, Szeged, Hungary Institute of Plant Biology, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary Department of Biotechnology, University of Szeged, Szeged, Hungary Faculty of Biology, Technion - Israel Institute of Technology, Haifa, Israel University of California, San Francisco, Department of Microbiology and Immunology, San Francisco, CA, United States Cited By :19 Export Date: 24 August 2020 Correspondence Address: Pál, C.; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research CentreHungary; email: cpal@brc.hu Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Szeged, Hungary Doctoral School of Biology, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary HCEMM-BRC Metabolic Systems Biology Lab, Szeged, Hungary Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, Hungary Department of Laboratory Medicine, University of Szeged, Szeged, Hungary Institute of Plant Biology, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary Department of Biotechnology, University of Szeged, Szeged, Hungary Faculty of Biology, Technion - Israel Institute of Technology, Haifa, Israel University of California, San Francisco, Department of Microbiology and Immunology, San Francisco, CA, United States Cited By :32 Export Date: 14 January 2021 Correspondence Address: Pál, C.; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research CentreHungary; email: cpal@brc.hu Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Szeged, Hungary Doctoral School of Biology, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary HCEMM-BRC Metabolic Systems Biology Lab, Szeged, Hungary Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, Hungary Department of Laboratory Medicine, University of Szeged, Szeged, Hungary Institute of Plant Biology, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary Department of Biotechnology, University of Szeged, Szeged, Hungary Faculty of Biology, Technion - Israel Institute of Technology, Haifa, Israel University of California, San Francisco, Department of Microbiology and Immunology, San Francisco, CA, United States Cited By :54 Export Date: 30 July 2021 Correspondence Address: Pál, C.; Synthetic and Systems Biology Unit, Hungary; email: cpal@brc.hu Chemicals/CAS: chloramphenicol, 134-90-7, 2787-09-9, 56-75-7; indolicidin, 140896-21-5; pexiganan, 172820-23-4, 147664-63-9; polymyxin B, 1404-26-8, 1405-20-5; pr 39, 139637-11-9; protamine, 11061-43-1, 9007-31-2, 9012-00-4; tachyplesin, 118231-04-2; Anti-Infective Agents; Antimicrobial Cationic Peptides Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Szeged, Hungary Doctoral School of Biology, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary HCEMM-BRC Metabolic Systems Biology Lab, Szeged, Hungary Department of Biochemistry and Molecular Biology, University of Szeged, Szeged, Hungary Department of Laboratory Medicine, University of Szeged, Szeged, Hungary Institute of Plant Biology, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary Department of Biotechnology, University of Szeged, Szeged, Hungary Faculty of Biology, Technion - Israel Institute of Technology, Haifa, Israel University of California, San Francisco, Department of Microbiology and Immunology, San Francisco, CA, United States Cited By :58 Export Date: 25 August 2021 Correspondence Address: Pál, C.; Synthetic and Systems Biology Unit, Hungary; email: cpal@brc.hu AB - Antimicrobial peptides (AMPs) are promising antimicrobials, however, the potential of bacterial resistance is a major concern. Here we systematically study the evolution of resistance to 14 chemically diverse AMPs and 12 antibiotics in Escherichia coli. Our work indicates that evolution of resistance against certain AMPs, such as tachyplesin II and cecropin P1, is limited. Resistance level provided by point mutations and gene amplification is very low and antibiotic-resistant bacteria display no cross-resistance to these AMPs. Moreover, genomic fragments derived from a wide range of soil bacteria confer no detectable resistance against these AMPs when introduced into native host bacteria on plasmids. We have found that simple physicochemical features dictate bacterial propensity to evolve resistance against AMPs. Our work could serve as a promising source for the development of new AMP-based therapeutics less prone to resistance, a feature necessary to avoid any possible interference with our innate immune system. LA - English DB - MTMT ER - TY - JOUR AU - Fási, Laura AU - Di Meo, Florent AU - Kuo, Ching-Ying AU - Stojkovic Buric, Sonja AU - Martins, Ana AU - Kúsz, Norbert AU - Béni, Zoltán AU - Dékány, Miklós AU - Balogh, György Tibor AU - Pesic, Milica AU - Wang, Hui-Chun AU - Trouillas, Patrick AU - Hunyadi, Attila TI - Antioxidant-inspired drug discovery: antitumor metabolite is formed in situ from a hydroxycinnamic acid derivative upon free radical scavenging JF - JOURNAL OF MEDICINAL CHEMISTRY J2 - J MED CHEM VL - 62 PY - 2019 IS - 3 SP - 1657 EP - 1668 PG - 12 SN - 0022-2623 DO - 10.1021/acs.jmedchem.8b01994 UR - https://m2.mtmt.hu/api/publication/30380633 ID - 30380633 AB - Cancer cells generally possess higher levels of reactive oxygen species than normal cells, and this can serve as a possible therapeutic target. In this proof-of-concept study, an antioxidant-inspired drug discovery strategy was evaluated using a hydroxycinnamic acid derivative. The processing of oxidized mixtures of p-coumaric acid methyl ester (pcm) revealed a new antitumor lead, graviquinone. Graviquinone bypassed ABCB1-mediated resistance, induced DNA damage in lung carcinoma cells but exerted DNA protective activity in normal keratinocytes, and modulated DNA damage response in MCF-7 cells. The cytotoxic effect of pcm in MCF-7 cells was potentiated under H2O2-induced oxidative stress, and the formation of graviquinone was confirmed by Fenton's reaction on pcm. In silico density functional theory calculations suggested graviquinone as a kinetic product of pcm-scavenging (OH)-O-center dot radicals. Our results demonstrate the pharmacological value of an in situ-formed, oxidative stress-related metabolite of an antioxidant. This might be of particular importance for designing new strategies for antioxidant-based drug discovery. LA - English DB - MTMT ER - TY - JOUR AU - Lázár, Viktória AU - Martins, Ana AU - Spohn, Réka AU - Daruka, Lejla AU - Grézal, Gábor AU - Fekete, Gergely AU - Számel, Mónika AU - Jangir, Pramod Kumar AU - Kintses, Bálint AU - Csörgő, Bálint AU - Nyerges, Ákos AU - Györkei, Ádám AU - Kincses, András AU - Dér, András AU - Walter, Fruzsina AU - Deli, Mária Anna AU - Zsoldiné Urbán, Edit AU - Hegedüs, Zsófia AU - Olajos, Gábor AU - Méhi, Orsolya Katinka AU - Bálint, Balázs AU - Nagy, István AU - Martinek, Tamás AU - Papp, Balázs AU - Pál, Csaba TI - Antibiotic-resistant bacteria show widespread collateral sensitivity to antimicrobial peptides JF - NATURE MICROBIOLOGY J2 - NAT MICROBIOL VL - 3 PY - 2018 IS - 6 SP - 718 EP - 731 PG - 14 SN - 2058-5276 DO - 10.1038/s41564-018-0164-0 UR - https://m2.mtmt.hu/api/publication/3378998 ID - 3378998 N1 - Megosztott első szerzőség. These authors contributed equally to this work: Viktória Lázár and Ana Martins. AB - Antimicrobial peptides are promising alternative antimicrobial agents. However, little is known about whether resistance to small-molecule antibiotics leads to cross-resistance (decreased sensitivity) or collateral sensitivity (increased sensitivity) to antimicrobial peptides. We systematically addressed this question by studying the susceptibilities of a comprehensive set of 60 antibiotic-resistant Escherichia coli strains towards 24 antimicrobial peptides. Strikingly, antibiotic-resistant bacteria show a high frequency of collateral sensitivity to antimicrobial peptides, whereas cross-resistance is relatively rare. We identify clinically relevant multidrug-resistance mutations that increase bacterial sensitivity to antimicrobial peptides. Collateral sensitivity in multidrug-resistant bacteria arises partly through regulatory changes shaping the lipopolysaccharide composition of the bacterial outer membrane. These advances allow the identification of antimicrobial peptide-antibiotic combinations that enhance antibiotic activity against multidrug-resistant bacteria and slow down de novo evolution of resistance. In particular, when co-administered as an adjuvant, the antimicrobial peptide glycine-leucine-amide caused up to 30-fold decrease in the antibiotic resistance level of resistant bacteria. Our work provides guidelines for the development of efficient peptide-based therapies of antibiotic-resistant infections. LA - English DB - MTMT ER - TY - JOUR AU - Lentz, F AU - Reiling, N AU - Martins, Ana AU - Molnár, József AU - Hilgeroth, A TI - Discovery of Novel Enhancers of Isoniazid Toxicity in Mycobacterium tuberculosis JF - MOLECULES J2 - MOLECULES VL - 23 PY - 2018 IS - 4 PG - 9 SN - 1420-3049 DO - 10.3390/molecules23040825 UR - https://m2.mtmt.hu/api/publication/3370143 ID - 3370143 N1 - Acknowledgments: We acknowledge the support of the Szeged Foundation for Cancer Research and the financial support within the funding programme Open Access Publishing by the German Research Foundation (DFG) AB - The number of effective first-line antibiotics for the treatment of Mycobacterium tuberculosis infection is strongly limited to a few drugs. Due to emerging resistance against those drugs, second- and third-line antibiotics have been established in therapy with certain problems and also increasing mycobacterial resistance. An alternative to such novel drugs or combined therapeutic regimes which may reduce resistance development is finding enhancers of mycobacterial drug effectiveness, especially enhancers that counteract causative resistance mechanisms. Such enhancers may reduce the extracellular drug efflux mediated by bacterial efflux pumps and thus enhance the intracellular drug toxicity. We developed novel 1,4-dihydropyridines (DHPs) as potential efflux pump inhibitors with some determined P-gp affinities. The influence on the antituberculotic drug toxicity has been investigated for three prominent antituberculotic drugs. Exclusive and selective toxicity enhancing effects have been detected for isoniazid (INH) which could be related to certain substituent effects of the 1,4-DHPs. So, structure-dependent activities have been found. Thus, promising enhancers could be identified and a suggested efflux pump inhibition is discussed. LA - English DB - MTMT ER - TY - JOUR AU - Vágvölgyi, Máté AU - Martins, Ana AU - Kulmány, Ágnes Erika AU - Zupkó, István AU - Gáti, Tamás AU - Simon, András AU - Tóth, Gábor AU - Hunyadi, Attila TI - Nitrogen-containing ecdysteroid derivatives vs. multi-drug resistance in cancer: Preparation and antitumor activity of oximes, oxime ethers and a lactam JF - EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY J2 - EUR J MED CHEM VL - 144 PY - 2018 SP - 730 EP - 739 PG - 10 SN - 0223-5234 DO - 10.1016/j.ejmech.2017.12.032 UR - https://m2.mtmt.hu/api/publication/3302693 ID - 3302693 N1 - Institute of Pharmacognosy, Faculty of Pharmacy, University of Szeged, Szeged, Hungary Department of Medical Microbiology and Immunobiology, Faculty of Medicine, University of Szeged, Szeged, Hungary Institute of Pharmacodynamics and Biopharmacy, Faculty of Pharmacy, University of Szeged, Szeged, Hungary Servier Research Institute of Medicinal Chemistry (SRIMC), Budapest, Hungary NMR group, Department of Inorganic and Analytical Chemistry, University of Technology and Economics, Budapest, Hungary Interdisciplinary Centre for Natural Products, University of Szeged, Szeged, Hungary Synthetic Systems Biology Unit, Institute of Biochemistry, Biological Research Centre, Temesvári krt. 62, Szeged, H-6726, Hungary Cited By :7 Export Date: 2 November 2020 CODEN: EJMCA Correspondence Address: Hunyadi, A.; Institute of Pharmacognosy, Faculty of Pharmacy, University of Szeged, Eötvös u. 6, Hungary; email: hunyadi.a@pharm.u-szeged.hu LA - English DB - MTMT ER - TY - JOUR AU - Vágvölgyi, Máté AU - Martins, Ana AU - Kulmány, Ágnes Erika AU - Zupkó, István AU - Tóth, Gábor AU - Hunyadi, Attila TI - Preparation and chemo-sensitizing activity of nitrogen-containing ecdysteroid derivatives: 6-oximes, oxime ethers, and a lactam JF - PLANTA MEDICA INTERNATIONAL OPEN J2 - PLANTA MEDICA INT OPEN VL - 4 PY - 2017 IS - S 01 SN - 2509-6656 DO - 10.1055/s-0037-1608147 UR - https://m2.mtmt.hu/api/publication/3287862 ID - 3287862 LA - English DB - MTMT ER - TY - JOUR AU - Balázs, Attila AU - Hunyadi, Attila AU - Csábi, József AU - Tillekeratne, LMV AU - Martins, Ana AU - Tóth, Gábor TI - New cyclic 2,3-sulfite ester derivatives of poststerone – Discriminating diastereomers and probing spatial proximities by NMR and DFT calculations JF - MAGNETIC RESONANCE IN CHEMISTRY J2 - MAGN RESON CHEM VL - 55 PY - 2017 IS - 12 SP - 1102 EP - 1107 PG - 6 SN - 0749-1581 DO - 10.1002/mrc.4641 UR - https://m2.mtmt.hu/api/publication/3253009 ID - 3253009 N1 - Besorolása rövid közlemény, mert idézettsége eléri a folyóirat adott évi impakt faktorának kétszeresét. (BCS, SZTE admin4) LA - English DB - MTMT ER -