@article{MTMT:31879664,
	title = {Condition-dependent functional shift of two Drosophila Mtmr lipid phosphatases in autophagy control},
	url = {https://m2.mtmt.hu/api/publication/31879664},
	author = {Manzéger, Anna and Tagscherer, Kinga and Lőrincz, Péter and Szaker, Henrik Mihály and Lukácsovich, T and Pliz, P and Kméczik, R and Csikós, György and Erdélyi, Miklós and Sass, Miklós and Kovács, Tibor and Vellai, Tibor and Billes, Viktor András},
	doi = {10.1080/15548627.2021.1899681},
	journal-iso = {AUTOPHAGY},
	journal = {AUTOPHAGY},
	volume = {17},
	unique-id = {31879664},
	issn = {1554-8627},
	year = {2021},
	eissn = {1554-8635},
	pages = {4010-4028},
	orcid-numbers = {Manzéger, Anna/0000-0002-3655-8335; Lőrincz, Péter/0000-0001-7374-667X; Szaker, Henrik Mihály/0000-0001-8340-8287; Csikós, György/0000-0002-5881-5363; Sass, Miklós/0000-0002-4559-8216; Kovács, Tibor/0000-0002-0632-9128; Vellai, Tibor/0000-0002-3520-2572; Billes, Viktor András/0000-0003-0030-6221}
}

@article{MTMT:31409031,
	title = {Interplay of Structural Disorder and Short Binding Elements in the Cellular Chaperone Function of Plant Dehydrin ERD14},
	url = {https://m2.mtmt.hu/api/publication/31409031},
	author = {Murvai, Nikoletta and Kalmár, Lajos and Szalainé Ágoston, Bianka and Szabó, Beáta and Tantos, Ágnes and Csikós, György and Micsonai, András and Kardos, József and Vertommen, Didier and Nguyen, Phuong N. and Hristozova, Nevena and Lang, Andras and Kovacs, Denes and Buday, László and Han, Kyou-Hoon and Perczel, András and Tompa, Péter},
	doi = {10.3390/cells9081856},
	journal-iso = {CELLS-BASEL},
	journal = {CELLS},
	volume = {9},
	unique-id = {31409031},
	abstract = {Details of the functional mechanisms of intrinsically disordered proteins (IDPs) in living cells is an area not frequently investigated. Here, we dissect the molecular mechanism of action of an IDP in cells by detailed structural analyses based on an in-cell nuclear magnetic resonance experiment. We show that the ID stress protein (IDSP) A. thaliana Early Response to Dehydration (ERD14) is capable of protecting E. coli cells under heat stress. The overexpression of ERD14 increases the viability of E. coli cells from 38.9% to 73.9% following heat stress (50 °C × 15 min). We also provide evidence that the protection is mainly achieved by protecting the proteome of the cells. In-cell NMR experiments performed in E. coli cells show that the protective activity is associated with a largely disordered structural state with conserved, short sequence motifs (K- and H-segments), which transiently sample helical conformations in vitro and engage in partner binding in vivo. Other regions of the protein, such as its S segment and its regions linking and flanking the binding motifs, remain unbound and disordered in the cell. Our data suggest that the cellular function of ERD14 is compatible with its residual structural disorder in vivo.},
	year = {2020},
	eissn = {2073-4409},
	orcid-numbers = {Murvai, Nikoletta/0000-0001-7477-0911; Szalainé Ágoston, Bianka/0000-0002-9666-8608; Csikós, György/0000-0002-5881-5363; Micsonai, András/0000-0002-2539-4080; Kardos, József/0000-0002-2135-2932; Buday, László/0000-0003-3518-5757; Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:30848725,
	title = {No Correlation between Endo- and Exoskeletal Regenerative Capacities in Teleost Species},
	url = {https://m2.mtmt.hu/api/publication/30848725},
	author = {Pápai, Nóra and Kagan, Ferenc and Csikós, György and Kosztelnik, Mónika and Vellai, Tibor and Varga, Máté},
	doi = {10.3390/fishes4040051},
	journal-iso = {FISHES-BASEL},
	journal = {FISHES},
	volume = {4},
	unique-id = {30848725},
	keywords = {regenerációs medicina},
	year = {2019},
	eissn = {2410-3888},
	orcid-numbers = {Csikós, György/0000-0002-5881-5363; Kosztelnik, Mónika/0000-0001-6735-3597; Vellai, Tibor/0000-0002-3520-2572; Varga, Máté/0000-0003-4289-1705}
}

@article{MTMT:2983461,
	title = {Function of desiccate in gustatory sensilla of drosophila melanogaster},
	url = {https://m2.mtmt.hu/api/publication/2983461},
	author = {Kawano, T and Ryuda, M and Matsumoto, H and Ochiai, M and Oda, Y and Tanimura, T and Csikós, György and Moriya, M and Hayakawa, Y},
	doi = {10.1038/srep17195},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {5},
	unique-id = {2983461},
	year = {2015},
	eissn = {2045-2322},
	orcid-numbers = {Csikós, György/0000-0002-5881-5363}
}

@book{MTMT:3165682,
	title = {Állatszervezettani Gyakorlatok},
	url = {https://m2.mtmt.hu/api/publication/3165682},
	author = {Csikós, György and Csizmadia, Tamás and Csörgő, Tibor and Kárpáti, Manuéla and Kis, Viktor and Dr. Kovács, Attila and Molnár, Kinga and Pálfia, Zsolt},
	editor = {Lippai, Mónika},
	publisher = {ELTE TTK},
	unique-id = {3165682},
	year = {2015},
	orcid-numbers = {Csikós, György/0000-0002-5881-5363; Csizmadia, Tamás/0000-0002-2098-9165; Csörgő, Tibor/0000-0002-7060-9853; Molnár, Kinga/0000-0002-7196-5331; Pálfia, Zsolt/0000-0002-4277-8131; Lippai, Mónika/0000-0002-7307-4233}
}

@article{MTMT:2766653,
	title = {Immunoevasive protein (IEP)-containing surface layer covering polydnavirus particles is essential for viral infection},
	url = {https://m2.mtmt.hu/api/publication/2766653},
	author = {Furihata, S and Tanaka, K and Ryuda, M and Ochiai, M and Matsumoto, H and Csikós, György and Hayakawa, Y},
	doi = {10.1016/j.jip.2013.10.013},
	journal-iso = {J INVERTEBR PATHOL},
	journal = {JOURNAL OF INVERTEBRATE PATHOLOGY},
	volume = {115},
	unique-id = {2766653},
	issn = {0022-2011},
	year = {2014},
	eissn = {1096-0805},
	pages = {26-32},
	orcid-numbers = {Csikós, György/0000-0002-5881-5363}
}

@CONFERENCE{MTMT:2968782,
	title = {Endosymbiont bacteria in Arcella species. An overview},
	url = {https://m2.mtmt.hu/api/publication/2968782},
	author = {Török, Júlia Katalin and Molnár, O and Csikós, György},
	booktitle = {7th International Symposium on Testate Amoebae},
	unique-id = {2968782},
	year = {2014},
	pages = {50-50},
	orcid-numbers = {Török, Júlia Katalin/0000-0001-5303-2610; Csikós, György/0000-0002-5881-5363}
}

@article{MTMT:1880280,
	title = {Plasma membrane H+-ATPase gene expression, protein level and activity in growing and non-growing regions of barley (Hordeum vulgare L.) leaves},
	url = {https://m2.mtmt.hu/api/publication/1880280},
	author = {Visnovitz, Tamás and Solti, Ádám and Csikós, György and Fricke, Wieland},
	doi = {10.1111/j.1399-3054.2012.01578.x},
	journal-iso = {PHYSIOL PLANTARUM},
	journal = {PHYSIOLOGIA PLANTARUM},
	volume = {144},
	unique-id = {1880280},
	issn = {0031-9317},
	keywords = {POTASSIUM CHANNELS; light; ROOTS; Cell elongation; auxin; COLEOPTILES; ACID GROWTH; APOPLASTIC PH; LEAF GROWTH; INDUCED ELONGATION GROWTH},
	year = {2012},
	eissn = {1399-3054},
	pages = {382-393},
	orcid-numbers = {Visnovitz, Tamás/0000-0002-7962-5083; Solti, Ádám/0000-0003-1479-5492; Csikós, György/0000-0002-5881-5363}
}

@article{MTMT:1925102,
	title = {PP2A regulates autophagy in two alternative ways in Drosophila.},
	url = {https://m2.mtmt.hu/api/publication/1925102},
	author = {Bánréti, Ágnes Regina and Lukacsovich, T and Csikós, György and Erdélyi, Miklós and Sass, Miklós},
	doi = {10.4161/auto.19081},
	journal-iso = {AUTOPHAGY},
	journal = {AUTOPHAGY},
	volume = {8},
	unique-id = {1925102},
	issn = {1554-8627},
	abstract = {Protein phosphatase 2A (PP2A) holoenzyme is a heterotrimeric complex, consisting of A, B and C subunits. The catalytic subunit PP2A-C (microtubule star/mts) binds to the C-terminal part of the scaffold protein PP2A-A (PP2A-29B). In Drosophila, there are three different forms of B subunits (widerborst/wdb, twins/tws and PP2A-B'), which determine the subcellular localization and substrate specificity of the holoenzyme. Previous studies demonstrated that PP2A is involved in the control of TOR-dependent autophagy both in yeast and mammals. Furthermore, in Drosophila, wdb genetically interacts with the PtdIns3K/PTEN/Akt signaling cascade, which is a main upstream regulatory system of dTOR. Here we demonstrate that in Drosophila, two different PP2A complexes (containing B' or wdb subunit) play essential roles in the regulation of starvation-induced autophagy. The PP2A-A/wdb/C complex acts upstream of dTOR, whereas the PP2A-A/B'/C complex functions as a target of dTOR and may regulate the elongation of autophagosomes and their subsequent fusion with lysosomes. We also identified three Drosophila Atg orthologs (Atg14, Atg17 and Atg101), which represent potential targets of the PP2A-A/B'/C complex during autophagy.},
	keywords = {DROSOPHILA; Autophagy; TOR; Larval fat body; wdb; srp; PP2A; mts},
	year = {2012},
	eissn = {1554-8635},
	pages = {623-636},
	orcid-numbers = {Csikós, György/0000-0002-5881-5363; Sass, Miklós/0000-0002-4559-8216}
}

@mastersthesis{MTMT:30707192,
	title = {Az autofágia folyamatának vizsgálata rovar modellszervezeteken},
	url = {https://m2.mtmt.hu/api/publication/30707192},
	author = {Csikós, György},
	unique-id = {30707192},
	year = {2012},
	orcid-numbers = {Csikós, György/0000-0002-5881-5363}
}