@CONFERENCE{MTMT:34506866,
	title = {Usp5, Usp34, and Otu1 deubiquitylases mediate DNA repair in Drosophila melanogaster},
	url = {https://m2.mtmt.hu/api/publication/34506866},
	author = {Páhi, Zoltán Gábor and Kovács, Levente and Szűcs, Diána and Borsos, Barbara Nikolett and Deák, Péter and Pankotai, Tibor},
	booktitle = {Ubiquitin & Friends Symposium 2023},
	unique-id = {34506866},
	year = {2023},
	pages = {67-67},
	orcid-numbers = {Páhi, Zoltán Gábor/0000-0002-3428-553X; Kovács, Levente/0000-0002-3226-3740; Pankotai, Tibor/0000-0001-9810-5465}
}

@article{MTMT:34431874,
	title = {The ubiquitin thioesterase YOD1 ameliorates mutant Huntingtin induced pathology in Drosophila},
	url = {https://m2.mtmt.hu/api/publication/34431874},
	author = {Farkas, Anita and Zsindely, Nóra and Nagy, Gábor and Kovács, Levente and Deák, Péter and Bodai, László},
	doi = {10.1038/s41598-023-49241-8},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {13},
	unique-id = {34431874},
	issn = {2045-2322},
	abstract = {Huntington’s disease (HD) is a neurodegenerative disorder caused by a dominant gain-of-function mutation in the huntingtin gene, resulting in an elongated polyglutamine repeat in the mutant Huntingtin (mHtt) that mediates aberrant protein interactions. Previous studies implicated the ubiquitin–proteasome system in HD, suggesting that restoring cellular proteostasis might be a key element in suppressing pathology. We applied genetic interaction tests in a Drosophila model to ask whether modulating the levels of deubiquitinase enzymes affect HD pathology. By testing 32 deubiquitinase genes we found that overexpression of Yod1 ameliorated all analyzed phenotypes, including neurodegeneration, motor activity, viability, and longevity. Yod1 did not have a similar effect in amyloid beta overexpressing flies, suggesting that the observed effects might be specific to mHtt. Yod1 overexpression did not alter the number of mHtt aggregates but moderately increased the ratio of larger aggregates. Transcriptome analysis showed that Yod1 suppressed the transcriptional effects of mHtt and restored the expression of genes involved in neuronal plasticity, vesicular transport, antimicrobial defense, and protein synthesis, modifications, and clearance. Furthermore, Yod1 overexpression in HD flies leads to the upregulation of genes involved in transcriptional regulation and synaptic transmission, which might be part of a response mechanism to mHtt-induced stress.},
	year = {2023},
	eissn = {2045-2322},
	orcid-numbers = {Zsindely, Nóra/0000-0002-6189-3100; Nagy, Gábor/0000-0001-5464-1135; Kovács, Levente/0000-0002-3226-3740; Bodai, László/0000-0001-8411-626X}
}

@article{MTMT:32778093,
	title = {Usp5, Usp34, and Otu1 deubiquitylases mediate DNA repair in Drosophila melanogaster},
	url = {https://m2.mtmt.hu/api/publication/32778093},
	author = {Páhi, Zoltán Gábor and Kovács, Levente and Szűcs, Diána and Borsos, Barbara Nikolett and Deák, Péter and Pankotai, Tibor},
	doi = {10.1038/s41598-022-09703-x},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {12},
	unique-id = {32778093},
	issn = {2045-2322},
	year = {2022},
	eissn = {2045-2322},
	orcid-numbers = {Páhi, Zoltán Gábor/0000-0002-3428-553X; Kovács, Levente/0000-0002-3226-3740; Pankotai, Tibor/0000-0001-9810-5465}
}

@article{MTMT:32691300,
	title = {Loss of ubiquitinated protein autophagy is compensated by persistent cnc/NFE2L2/Nrf2 antioxidant responses},
	url = {https://m2.mtmt.hu/api/publication/32691300},
	author = {Bhattacharjee, Arindam and Harmatos-Ürmösi, Adél and Jipa, András and Kovács, Levente and Deák, Péter and Szabó, Áron and Juhász, Gábor},
	doi = {10.1080/15548627.2022.2037852},
	journal-iso = {AUTOPHAGY},
	journal = {AUTOPHAGY},
	volume = {18},
	unique-id = {32691300},
	issn = {1554-8627},
	year = {2022},
	eissn = {1554-8635},
	pages = {2385-2396},
	orcid-numbers = {Jipa, András/0000-0003-4880-7666; Kovács, Levente/0000-0002-3226-3740; Juhász, Gábor/0000-0001-8548-8874}
}

@{MTMT:32576298,
	title = {The role of E3 ubiquitin ligases in the regulation of crinophagy},
	url = {https://m2.mtmt.hu/api/publication/32576298},
	author = {Anna, Dósa and Csizmadia, Tamás and Maddali, Asha Kiran and Laczkó-Dobos, Hajnalka and Jipa, András and Kovács, Levente and Deák, Péter and Lőw, Péter and Juhász, Gábor},
	booktitle = {Hungarian Molecular Life Sciences 2021},
	unique-id = {32576298},
	abstract = {Crinophagy is a special form of autophagy, in which damaged or no longer needed secretory granules
		directly fuse with lysosomes, independently from autophagosome formation. Our colleagues have
		previously identified the molecular components of the membrane fusion apparatus (SNARE proteins,
		small GTPases and the tethering complex), using Drosophila melanogaster as a model organism, in
		which crinophagy is part of the normal developmental program of the larval salivary gland. Despite
		these findings, our knowledge is still little about the complete mechanism, as the upstream regulation
		of the process remains mainly unclear. The well-known function of ubiquitin is the targeting of
		cytoplasmic proteins into the proteasome for degradation, maintaining normal protein turnover.
		However, it has been observed that ubiquitin plays important roles in many other cellular processes,
		such as signal transduction or proteasome-independent degradation. It has been previously shown
		that in yeast, an E3 ubiquitin ligase activity is needed for the fast degradation of the gluconeogenic
		enzymes through the Vacuolar Import and Degradation (Vid) pathway, which is mechanistically similar
		to crinophagy. According to these data, ubiquitin could potentially have a role in the regulation of
		crinophagy, too, so our group decided to investigate this possibility.
		In our work, using fluorescent and immunocytochemical labeling methods, we have found ubiquitin
		on the surface of (glue) secretory granules, when crinophagy is activated. Moreover, through a small-
		scale genetic screen that involved the genes of E3 ubiquitin ligases, we identified one E3 enzyme which
		is required for the initiation of developmentally programmed crinophagy. Importantly, the
		overexpression of this enzyme causes early induction of secretory granule-lysosome fusion. We
		observed these phenotypes using both fluorescent and electron microscopy techniques.
		According to these results, E3 ubiquitin ligase activity is likely needed for successful crinophagy, thus
		we predict that at least one ubiquitination event occurs in the process of crinophagy},
	year = {2021},
	pages = {1},
	orcid-numbers = {Csizmadia, Tamás/0000-0002-2098-9165; Jipa, András/0000-0003-4880-7666; Kovács, Levente/0000-0002-3226-3740; Lőw, Péter/0000-0003-2450-7087; Juhász, Gábor/0000-0001-8548-8874}
}

@{MTMT:32576272,
	title = {The role of ubiquitin in the secretory granule degradation in Drosophila},
	url = {https://m2.mtmt.hu/api/publication/32576272},
	author = {Csizmadia, Tamás and Dósa, Anna and Maddali, Asha Kiran and Laczkó-Dobos, Hajnalka and Jipa, András and Kovács, Levente and Deák, Péter and Lőw, Péter and Juhász, Gábor},
	booktitle = {Hungarian Molecular Life Sciences 2021},
	unique-id = {32576272},
	abstract = {In the late larval period of Drosophila salivary gland, part of the glue containing secretory granules
		evade exocytosis and are degraded via crinophagy. During this process the obsolete secretory vesicles
		directly fuse with late endosomes or lysosomes for the fast degradation and recycling of the secretory
		cargo. The mechanism of secretory granule assortment for degradation is unknown since the
		discovery of crinophagy. Here we show that, the obsolete secretory granules are designated for
		degradation by ubiquitin (Figure 1) before their fusion with late endosomes/lysosomes. Moreover, we
		have identified the molecular components (E3 and deubiquitinating enzymes), which are involved in
		the ubiquitination of secretory (glue) granule membrane proteins. Importantly, the activity of these
		components is required for the normal crinophagic degradation of unnecessary secretory vesicles.
		Our work establishes the molecular background, which directs obsolete secretory granules for
		developmentally programmed crinophagy in Drosophila and paves the way for analyzing and
		understanding the regulation of this process in Metazoan},
	year = {2021},
	pages = {0},
	orcid-numbers = {Csizmadia, Tamás/0000-0002-2098-9165; Jipa, András/0000-0003-4880-7666; Kovács, Levente/0000-0002-3226-3740; Lőw, Péter/0000-0003-2450-7087; Juhász, Gábor/0000-0001-8548-8874}
}

@misc{MTMT:33288185,
	title = {Haladó genetikai szemelvények},
	url = {https://m2.mtmt.hu/api/publication/33288185},
	author = {Pankotai, Tibor and Boros, Imre Miklós and Henn, László and Deák, Péter},
	unique-id = {33288185},
	year = {2020},
	orcid-numbers = {Pankotai, Tibor/0000-0001-9810-5465; Boros, Imre Miklós/0000-0001-8504-9687}
}

@article{MTMT:31364575,
	title = {Multidrug Resistance (MDR) and Collateral Sensitivity in Bacteria, with Special Attention to Genetic and Evolutionary Aspects and to the Perspectives of Antimicrobial Peptides—A Review},
	url = {https://m2.mtmt.hu/api/publication/31364575},
	author = {Fodor, András and Abate, Birhan Addisie and Deák, Péter and Fodor, László and Gyenge, Ervin and Klein, Michael G. and Koncz, Zsuzsanna and Muvevi, Josephat and Ötvös, László and Székely, Gyöngyi and Vozik, Dávid and Makrai, László},
	doi = {10.3390/pathogens9070522},
	journal-iso = {PATHOGENS},
	journal = {PATHOGENS},
	volume = {9},
	unique-id = {31364575},
	year = {2020},
	eissn = {2076-0817}
}

@article{MTMT:31158977,
	title = {Usp14 is required for spermatogenesis and ubiquitin stress responses in Drosophila melanogaster.},
	url = {https://m2.mtmt.hu/api/publication/31158977},
	author = {Kovács, Levente and Nagy, Ágota and Pál, Margit and Deák, Péter},
	doi = {10.1242/jcs.237511},
	journal-iso = {J CELL SCI},
	journal = {JOURNAL OF CELL SCIENCE},
	volume = {133},
	unique-id = {31158977},
	issn = {0021-9533},
	abstract = {Deubiquitylating (DUB) enzymes free covalently linked ubiquitin moieties from ubiquitin-ubiquitin and ubiquitin-protein conjugates, and thereby maintain the equilibrium between free and conjugated ubiquitin moieties and regulate ubiquitin-mediated cellular processes. Here, we performed genetic analyses of mutant phenotypes in Drosophila melanogaster and demonstrate that loss of Usp14 function results in male sterility, with defects in spermatid individualization and reduced testicular free monoubiquitin levels. These phenotypes were rescued by germline-specific overexpression of wild-type Usp14. Synergistic genetic interactions with Ubi-p63E and cycloheximide sensitivity suggest that ubiquitin shortage is a primary cause of male sterility. In addition, Usp14 is predominantly expressed in testes in Drosophila, indicating a higher demand for this DUB in testes that is also reflected by testis-specific loss-of-function Usp14 phenotypes. Collectively, these results suggest a major role of Usp14 in maintaining normal steady state free monoubiquitin levels during the later stages of Drosophila spermatogenesis.This article has an associated First Person interview with the first author of the paper.},
	keywords = {deubiquitination; USP14; Deubiquitylaton; Drosophila spermatogenesis; Ubiquitin equilibrium},
	year = {2020},
	eissn = {1477-9137},
	orcid-numbers = {Kovács, Levente/0000-0002-3226-3740}
}

@misc{MTMT:30355860,
	title = {An Overview of Multi-Antibiotic Resistance in Pathogenic Bacteria - From Selected Genetic and Evolutionary Aspects - A Review},
	url = {https://m2.mtmt.hu/api/publication/30355860},
	author = {Fodor, András and Birhan, Addisie Abate and Deák, Péter and László, Fodor and Michael, G. Klein and László, Makrai and Josephat, Muvevi and Dávid, Vozik},
	doi = {10.20944/preprints201808.0036.v1},
	unique-id = {30355860},
	year = {2018},
	pages = {1-33}
}