@article{MTMT:34749009,
	title = {Isolation and identification of fungal biodeteriogens from the wall of a cultural heritage church and potential applicability of antifungal proteins in protection},
	url = {https://m2.mtmt.hu/api/publication/34749009},
	author = {Dán, Kinga and Kocsubé, Sándor and Tóth, Liliána and Farkas, Attila and Rákhely, Gábor and Galgóczi, László Norbert},
	doi = {10.1016/j.culher.2024.03.002},
	journal-iso = {J CULT HERIT},
	journal = {JOURNAL OF CULTURAL HERITAGE},
	volume = {67},
	unique-id = {34749009},
	issn = {1296-2074},
	year = {2024},
	eissn = {1778-3674},
	pages = {194-202},
	orcid-numbers = {Kocsubé, Sándor/0000-0001-7839-0510; Tóth, Liliána/0000-0003-1400-6174; Rákhely, Gábor/0000-0003-2557-3641; Galgóczi, László Norbert/0000-0002-6976-8910}
}

@article{MTMT:34721913,
	title = {A novel bacteriophage-based solution against Xanthomonas arboricola pv. juglandis: Natural approach for organic walnut production},
	url = {https://m2.mtmt.hu/api/publication/34721913},
	author = {T., Kovács and N., Bounedjoum and Bali, Dominika and Rákhely, Gábor},
	journal-iso = {ACTA HORTICULTURAE},
	journal = {ACTA HORTICULTURAE: TECHNICAL COMMUNICATIONS OF ISHS},
	unique-id = {34721913},
	issn = {0567-7572},
	year = {2024},
	eissn = {2406-6168},
	orcid-numbers = {Rákhely, Gábor/0000-0003-2557-3641}
}

@article{MTMT:34627084,
	title = {Rational Design of Antifungal Peptides Based on the γ-Core Motif of a Neosartorya (Aspergillus) fischeri Antifungal Protein to Improve Structural Integrity, Efficacy, and Spectrum},
	url = {https://m2.mtmt.hu/api/publication/34627084},
	author = {Váradi, Györgyi and Bende, Gábor and Borics, Attila and Dán, Kinga and Rákhely, Gábor and Tóth, Gábor and Galgóczi, László Norbert},
	doi = {10.1021/acsomega.3c09377},
	journal-iso = {ACS OMEGA},
	journal = {ACS OMEGA},
	volume = {9},
	unique-id = {34627084},
	issn = {2470-1343},
	year = {2024},
	eissn = {2470-1343},
	pages = {7206-7214},
	orcid-numbers = {Váradi, Györgyi/0000-0001-7907-8908; Rákhely, Gábor/0000-0003-2557-3641; Tóth, Gábor/0000-0002-3604-4385; Galgóczi, László Norbert/0000-0002-6976-8910}
}

@article{MTMT:34432038,
	title = {Soils in distress: The impacts and ecological risks of (micro)plastic pollution in the terrestrial environment},
	url = {https://m2.mtmt.hu/api/publication/34432038},
	author = {Bodor, Attila and Feigl, Gábor and Kolossa, Bálint and Mészáros, Enikő and Laczi, Krisztián and Kovács, Etelka and Perei, Katalin and Rákhely, Gábor},
	doi = {10.1016/j.ecoenv.2023.115807},
	journal-iso = {ECOTOX ENVIRON SAFE},
	journal = {ECOTOXICOLOGY AND ENVIRONMENTAL SAFETY},
	volume = {269},
	unique-id = {34432038},
	issn = {0147-6513},
	year = {2024},
	eissn = {1090-2414},
	orcid-numbers = {Feigl, Gábor/0000-0001-6524-9147; Laczi, Krisztián/0000-0002-9399-7406; Kovács, Etelka/0000-0003-0969-5964; Perei, Katalin/0000-0001-8989-2284; Rákhely, Gábor/0000-0003-2557-3641}
}

@article{MTMT:34130955,
	title = {Regulation of the methanogenesis pathways by hydrogen at transcriptomic level in time},
	url = {https://m2.mtmt.hu/api/publication/34130955},
	author = {Szuhaj, Márk and Kakuk, Balázs and Wirth, Roland and Rákhely, Gábor and Kovács, Kornél Lajos and Bagi, Zoltán},
	doi = {10.1007/s00253-023-12700-3},
	journal-iso = {APPL MICROBIOL BIOT},
	journal = {APPLIED MICROBIOLOGY AND BIOTECHNOLOGY},
	volume = {107},
	unique-id = {34130955},
	issn = {0175-7598},
	abstract = {The biomethane formation from 4 H-2 + CO2 by pure cultures of two methanogens, Methanocaldococcus fervens and Methanobacterium thermophilum, has been studied. The goal of the study was to understand the regulation of the enzymatic steps associated with biomethane biosynthesis by H-2, using metagenomic, pan-genomic, and transcriptomic approaches. Methanogenesis in the autotrophic methanogen M. fervens could be easily "switched off" and "switched on" by H-2/CO2 within about an hour. In contrast, the heterotrophic methanogen M. thermophilum was practically insensitive to the addition of the H-2/CO2 trigger although this methanogen also converted H-2/CO2 to CH4. From practical points of view, the regulatory function of H-2/CO2 suggests that in the power-to-gas (P2G) renewable excess electricity conversion and storage systems, the composition of the biomethane-generating methanogenic community is essential for sustainable operation. In addition to managing the specific hydrogenotrophic methanogenesis biochemistry, H-2/CO2 affected several, apparently unrelated, metabolic pathways. The redox-regulated overall biochemistry and symbiotic relationships in the methanogenic communities should be explored in order to make the P2G technology more efficient.},
	keywords = {metabolism; IDENTIFICATION; HYDROGEN; REDUCTION; METHANE; ACETATE; STRAINS; ANAEROBIC-DIGESTION; methanogenesis; Dehydrogenases; Hydrogenotrophic methanogens; Power to gas; THERMOPHILICUM},
	year = {2023},
	eissn = {1432-0614},
	pages = {6315-6324},
	orcid-numbers = {Szuhaj, Márk/0000-0001-7160-3173; Kakuk, Balázs/0000-0002-4314-5707; Wirth, Roland/0000-0002-2383-2323; Rákhely, Gábor/0000-0003-2557-3641; Kovács, Kornél Lajos/0000-0002-3926-0497; Bagi, Zoltán/0000-0001-7795-2024}
}

@article{MTMT:34108330,
	title = {Bioelectrochemical Systems (BES) for Biomethane Production-Review},
	url = {https://m2.mtmt.hu/api/publication/34108330},
	author = {Horváth-Gönczi, Noémi Nikolett and Bagi, Zoltán and Szuhaj, Márk and Rákhely, Gábor and Kovács, Kornél Lajos},
	doi = {10.3390/fermentation9070610},
	journal-iso = {FERMENTATION-BASEL},
	journal = {FERMENTATION},
	volume = {9},
	unique-id = {34108330},
	abstract = {Bioelectrochemical systems (BESs) have great potential in renewable energy production technologies. BES can generate electricity via Microbial Fuel Cell (MFC) or use electric current to synthesize valuable commodities in Microbial Electrolysis Cells (MECs). Various reactor configurations and operational protocols are increasing rapidly, although industrial-scale operation still faces difficulties. This article reviews the recent BES related to literature, with special attention to electrosynthesis and the most promising reactor configurations. We also attempted to clarify the numerous definitions proposed for BESs. The main components of BES are highlighted. Although the comparison of the various fermentation systems is, we collected useful and generally applicable operational parameters to be used for comparative studies. A brief overview links the appropriate microbes to the optimal reactor design.},
	keywords = {CARBON-DIOXIDE; WASTE-WATER TREATMENT; ANAEROBIC-DIGESTION; STAINLESS-STEEL; Biomethane; FUEL-CELL; Microbial electrolysis cell (MEC); Microbial electrolysis cell; Biotechnology & Applied Microbiology; SINGLE-CHAMBER; Ion-exchange membranes; bioelectrochemical system (BES); electro-fermentation; Reactor configurations; ENHANCED METHANE PRODUCTION},
	year = {2023},
	eissn = {2311-5637},
	orcid-numbers = {Bagi, Zoltán/0000-0001-7795-2024; Szuhaj, Márk/0000-0001-7160-3173; Rákhely, Gábor/0000-0003-2557-3641; Kovács, Kornél Lajos/0000-0002-3926-0497}
}

@article{MTMT:34043893,
	title = {Hard nut to crack: Solving the disulfide linkage pattern of the Neosartorya (Aspergillus) fischeri antifungal protein 2},
	url = {https://m2.mtmt.hu/api/publication/34043893},
	author = {Váradi, Györgyi and Kele, Zoltán and Czajlik, András and Borics, Attila and Bende, Gábor and Papp, Csaba Gergő and Rákhely, Gábor and Tóth, Gábor and Batta, Gyula and Galgóczi, László Norbert},
	doi = {10.1002/pro.4692},
	journal-iso = {PROTEIN SCI},
	journal = {PROTEIN SCIENCE},
	volume = {32},
	unique-id = {34043893},
	issn = {0961-8368},
	abstract = {As a consequence of the fast resistance spreading, a limited number of drugs are available to treat fungal infections. Therefore, there is an urgent need to develop new antifungal treatment strategies. The features of a disulfide bond-stabilized antifungal protein, NFAP2 secreted by the mold Neosartorya (Aspergillus) fischeri render it to be a promising template for future protein-based antifungal drug design, which requires knowledge about the native disulfide linkage pattern as it is one of the prerequisites for biological activity. However, in the lack of tryptic and chymotryptic proteolytic sites in the ACNCPNNCK sequence, the determination of the disulfide linkage pattern of NFAP2 is not easy with traditional mass spectrometry-based methods. According to in silico predictions working with a preliminary nuclear magnetic resonance (NMR) solution structure, two disulfide isomers of NFAP2 (abbacc and abbcac) were possible. Both were chemically synthesized; and comparative reversed-phase high-performance liquid chromatography, electronic circular dichroism and NMR spectroscopy analyses, and antifungal susceptibility and efficacy tests indicated that the abbcac is the native pattern. This knowledge allowed rational modification of NAFP2 to improve the antifungal efficacy and spectrum through the modulation of the evolutionarily conserved gamma-core region, which is responsible for the activity of several antimicrobial peptides. Disruption of the steric structure of NFAP2 upon gamma-core modification led to the conclusions that this motif may affect the formation of the biologically active three-dimensional structure, and that the gamma-core modulation is not an efficient tool to improve the antifungal efficacy or to change the antifungal spectrum of NFAP2.},
	keywords = {DYNAMICS; PREDICTION; DRUG DESIGN; BONDS; protein structure; ANTIFUNGAL PROTEIN; disulfide linkage pattern},
	year = {2023},
	eissn = {1469-896X},
	orcid-numbers = {Váradi, Györgyi/0000-0001-7907-8908; Kele, Zoltán/0000-0002-4401-0302; Papp, Csaba Gergő/0000-0003-4450-0667; Rákhely, Gábor/0000-0003-2557-3641; Tóth, Gábor/0000-0002-3604-4385; Batta, Gyula/0000-0002-0442-1828; Galgóczi, László Norbert/0000-0002-6976-8910}
}

@{MTMT:34012624,
	title = {Intracellular ProteinTargets of Neosartorya (Aspergillus) fischeri Antifungal Proteins},
	url = {https://m2.mtmt.hu/api/publication/34012624},
	author = {Dán, Kinga and Zoltán, Kele and Tóth, Liliána and Fanni, Marcsisák and Gábor, K. Tóth and Rákhely, Gábor and Galgóczi, László Norbert},
	booktitle = {Power of Microbes in Industry and Environment 2023},
	unique-id = {34012624},
	year = {2023},
	pages = {92-93},
	orcid-numbers = {Tóth, Liliána/0000-0003-1400-6174; Rákhely, Gábor/0000-0003-2557-3641; Galgóczi, László Norbert/0000-0002-6976-8910}
}

@article{MTMT:33687467,
	title = {Spectral and Redox Properties of a Recombinant Mouse Cytochrome b561 Protein Suggest Transmembrane Electron Transfer Function},
	url = {https://m2.mtmt.hu/api/publication/33687467},
	author = {Bérczi, Alajos and Márton, Zsuzsanna and Laskay, Krisztina and Tóth, András and Rákhely, Gábor and Duzs, Ágnes and Sebőkné Nagy, Krisztina and Páli, Tibor and Zimányi, László},
	doi = {10.3390/molecules28052261},
	journal-iso = {MOLECULES},
	journal = {MOLECULES},
	volume = {28},
	unique-id = {33687467},
	issn = {1420-3049},
	abstract = {Cytochrome b561 proteins (CYB561s) are integral membrane proteins with six trans-membrane domains, two heme-b redox centers, one on each side of the host membrane. The major characteristics of these proteins are their ascorbate reducibility and trans-membrane electron transferring capability. More than one CYB561 can be found in a wide range of animal and plant phyla and they are localized in membranes different from the membranes participating in bioenergization. Two homologous proteins, both in humans and rodents, are thought to participate—via yet unidentified way—in cancer pathology. The recombinant forms of the human tumor suppressor 101F6 protein (Hs_CYB561D2) and its mouse ortholog (Mm_CYB561D2) have already been studied in some detail. However, nothing has yet been published about the physical-chemical properties of their homologues (Hs_CYB561D1 in humans and Mm_CYB561D1 in mice). In this paper we present optical, redox and structural properties of the recombinant Mm_CYB561D1, obtained based on various spectroscopic methods and homology modeling. The results are discussed in comparison to similar properties of the other members of the CYB561 protein family.},
	year = {2023},
	eissn = {1420-3049},
	orcid-numbers = {Rákhely, Gábor/0000-0003-2557-3641; Páli, Tibor/0000-0003-1649-1097; Zimányi, László/0000-0002-5101-2023}
}

@article{MTMT:33641641,
	title = {Reversal of Multidrug Resistance by Symmetrical Selenoesters in Colon Adenocarcinoma Cells},
	url = {https://m2.mtmt.hu/api/publication/33641641},
	author = {Rácz, Bálint and Kincses, Annamária and Laczi, Krisztián and Rákhely, Gábor and Domínguez-Álvarez, Enrique and Spengler, Gabriella},
	doi = {10.3390/pharmaceutics15020610},
	journal-iso = {PHARMACEUTICS},
	journal = {PHARMACEUTICS},
	volume = {15},
	unique-id = {33641641},
	issn = {1999-4923},
	abstract = {Recently, selenium containing derivatives have attracted more attention in medicinal chemistry. In the present work, the anticancer activity of symmetrical selenoesters was investigated by studying the reversal of efflux pump-related and apoptosis resistance in sensitive and resistant human colon adenocarcinoma cells expressing the ABCB1 protein. The combined effect of the compounds with doxorubicin was demonstrated with a checkerboard assay. The ABCB1 inhibitory and the apoptosis-inducing effects of the derivatives were measured with flow cytometry. Whole transcriptome sequencing was carried out on Illumina platform upon the treatment of resistant cells with the most potent derivatives. One ketone and three methyl ester selenoesters showed synergistic or weak synergistic interaction with doxorubicin, respectively. Ketone selenoesters were the most potent ABCB1 inhibitors and apoptosis inducers. Nitrile selenoesters could induce moderate early and late apoptotic processes that could be explained by their ABCB1 modulating properties. The transcriptome analysis revealed that symmetrical selenoesters may influence the redox state of the cells and interfere with metastasis formation. It can be assumed that these symmetrical selenocompounds possess toxic, DNA-damaging effects due to the presence of two selenium atoms in the molecule, which may be augmented by the presence of symmetrical groups.},
	year = {2023},
	eissn = {1999-4923},
	orcid-numbers = {Rácz, Bálint/0000-0003-0088-3408; Kincses, Annamária/0000-0002-1591-1419; Laczi, Krisztián/0000-0002-9399-7406; Rákhely, Gábor/0000-0003-2557-3641; Domínguez-Álvarez, Enrique/0000-0003-2655-1575; Spengler, Gabriella/0000-0001-8085-0950}
}