@article{MTMT:30939202,
	title = {DJ-1 can form β-sheet structured aggregates that co-localize with pathological amyloid deposits},
	url = {https://m2.mtmt.hu/api/publication/30939202},
	author = {Solti, K. and Kuan, W.-L. and Fórizs, B. and Kustos, G. and Mihály, Judith and Varga, Zoltán and Herberth, Balázs and Moravcsik, É. and Kiss, Róbert and Kárpáti, Manuéla and Mikes, Anna and Zhao, Y. and Imre, Timea and Rochet, J.-C. and Aigbirhio, F. and Williams-Gray, C.H. and Barker, R.A. and Tóth, Gergely},
	doi = {10.1016/j.nbd.2019.104629},
	journal-iso = {NEUROBIOL DIS},
	journal = {NEUROBIOLOGY OF DISEASE},
	volume = {134},
	unique-id = {30939202},
	issn = {0969-9961},
	abstract = {The loss of native function of the DJ-1 protein has been linked to the development of Parkinson's (PD) and other neurodegenerative diseases. Here we show that DJ-1 aggregates into β-sheet structured soluble and fibrillar aggregates in vitro under physiological conditions and that this process is promoted by the oxidation of its catalytic Cys106 residue. This aggregation resulted in the loss of its native biochemical glyoxalase function and in addition oxidized DJ-1 aggregates were observed to localize within Lewy bodies, neurofibrillary tangles and amyloid plaques in human PD and Alzheimer's (AD) patients' post-mortem brain tissue. These findings suggest that the aggregation of DJ-1 may be a critical player in the development of the pathology of PD and AD and demonstrate that loss of DJ-1 function can happen through DJ-1 aggregation. This could then contribute to AD and PD disease onset and progression. © 2019 Elsevier Inc.},
	keywords = {AGGREGATION; OXIDATIVE STRESS; TISSUE DISTRIBUTION; ARTICLE; PATHOPHYSIOLOGY; PROTEIN SECONDARY STRUCTURE; human; CATALYSIS; Molecular weight; protein localization; priority journal; controlled study; Histopathology; in vitro study; protein phosphorylation; enzyme activity; cellular distribution; Protein Stability; Autopsy; Solubility; CYSTEINE; PROTEIN FUNCTION; human cell; onset age; disease exacerbation; human tissue; Parkinson disease; serine; amyloid; amyloid; upregulation; oxidation reduction reaction; Alzheimer disease; amyloid beta protein[1-42]; alpha helix; frontal cortex; protein aggregation; neurofibrillary tangle; Lewy body; alpha synuclein; Protein misfolding; tau protein; homodimer; beta sheet; protein homeostasis; Parkinson’s; Alzheimer’s; glyoxalase; amyloid plaque; protein deglycase DJ-1; DJ-1; amygdala},
	year = {2020},
	eissn = {1095-953X},
	orcid-numbers = {Varga, Zoltán/0000-0002-5741-2669}
}

@article{MTMT:2909896,
	title = {iFly: The eye of the fruit fly as a model to study autophagy and related trafficking pathways.},
	url = {https://m2.mtmt.hu/api/publication/2909896},
	author = {Lőrincz, Péter and Takáts, Szabolcs and Kárpáti, Manuéla and Juhász, Gábor},
	doi = {10.1016/j.exer.2015.06.013},
	journal-iso = {EXP EYE RES},
	journal = {EXPERIMENTAL EYE RESEARCH},
	volume = {144},
	unique-id = {2909896},
	issn = {0014-4835},
	abstract = {Autophagy is a process by which eukaryotic cells degrade and recycle their intracellular components within lysosomes. Autophagy is induced by starvation to ensure survival of individual cells, and it has evolved to fulfill numerous additional roles in animals. Autophagy not only provides nutrient supply through breakdown products during starvation, but it is also required for the elimination of damaged or surplus organelles, toxic proteins, aggregates, and pathogens, and is essential for normal organelle turnover. Because of these roles, defects in autophagy have pathological consequences. Here we summarize the current knowledge of autophagy and related trafficking pathways in a convenient model: the compound eye of the fruit fly Drosophila melanogaster. In our review, we present a general introduction of the development and structure of the compound eye. This is followed by a discussion of various neurodegeneration models including retinopathies, with special emphasis on the protective role of autophagy against these diseases.},
	year = {2016},
	eissn = {1096-0007},
	pages = {90-98},
	orcid-numbers = {Lőrincz, Péter/0000-0001-7374-667X; Takáts, Szabolcs/0000-0003-2139-7740; Juhász, Gábor/0000-0001-8548-8874}
}

@article{MTMT:3010297,
	title = {Mutation in Atg5 reduces autophagy and leads to ataxia with developmental delay.},
	url = {https://m2.mtmt.hu/api/publication/3010297},
	author = {Kim, M and Sandford, E and Gatica, D and Qiu, Y and Liu, X and Zheng, Y and Schulman, BA and Xu, J and Semple, I and Ro, SH and Kim, B and Mavioglu, RN and Tolun, A and Jipa, András and Takáts, Szabolcs and Kárpáti, Manuéla and Li, JZ and Yapici, Z and Juhász, Gábor and Lee, JH and Klionsky, DJ and Burmeister, M},
	doi = {10.7554/eLife.12245},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {5},
	unique-id = {3010297},
	abstract = {Autophagy is required for the homeostasis of cellular material and is proposed to be involved in many aspects of health. Defects in the autophagy pathway have been observed in neurodegenerative disorders; however, no genetically-inherited pathogenic mutations in any of the core autophagy-related (ATG) genes have been reported in human patients to date. We identified a homozygous missense mutation, changing a conserved amino acid, in ATG5 in two siblings with congenital ataxia, mental retardation, and developmental delay. The subjects' cells display a decrease in autophagy flux and defects in conjugation of ATG12 to ATG5. The homologous mutation in yeast demonstrates a 30-50% reduction of induced autophagy. Flies in which Atg5 is substituted with the mutant human ATG5 exhibit severe movement disorder, in contrast to flies expressing the wild-type human protein. Our results demonstrate the critical role of autophagy in preventing neurological diseases and maintaining neuronal health.},
	year = {2016},
	eissn = {2050-084X},
	orcid-numbers = {Jipa, András/0000-0003-4880-7666; Takáts, Szabolcs/0000-0003-2139-7740; Juhász, Gábor/0000-0001-8548-8874}
}

@misc{MTMT:3083471,
	title = {Cas9-mediated mutagenesis of core autophagy genes in Drosophila},
	url = {https://m2.mtmt.hu/api/publication/3083471},
	author = {Jipa, András and Takáts, Szabolcs and Kárpáti, Manuéla and Juhász, Gábor},
	unique-id = {3083471},
	year = {2016},
	orcid-numbers = {Jipa, András/0000-0003-4880-7666; Takáts, Szabolcs/0000-0003-2139-7740; Juhász, Gábor/0000-0001-8548-8874}
}

@mastersthesis{MTMT:2891895,
	title = {A Drosophila Atg gének vizsgálata. a FIP200/Atg17 szerepe az autofágiában},
	url = {https://m2.mtmt.hu/api/publication/2891895},
	author = {Kárpáti, Manuéla},
	doi = {10.15476/ELTE.2014.087},
	publisher = {Eötvös Loránd University},
	unique-id = {2891895},
	year = {2015}
}

@misc{MTMT:3083487,
	title = {CRISPR/Cas9-mediated mutagenesis of core autophagy genes in Drosophila},
	url = {https://m2.mtmt.hu/api/publication/3083487},
	author = {Jipa, András and Takáts, Szabolcs and Kárpáti, Manuéla and Juhasz, G},
	unique-id = {3083487},
	year = {2015},
	orcid-numbers = {Jipa, András/0000-0003-4880-7666}
}

@CONFERENCE{MTMT:3083495,
	title = {CAS9-MEDIATED MUTAGENESIS OF CORE AUTPHAGY GENES IN DROSOPHILA},
	url = {https://m2.mtmt.hu/api/publication/3083495},
	author = {Jipa, András and Takáts, Szabolcs and Kárpáti, Manuéla and Juhasz, G},
	booktitle = {Hungarian Molecular Life Sciences 2015},
	unique-id = {3083495},
	year = {2015},
	pages = {142-143},
	orcid-numbers = {Jipa, András/0000-0003-4880-7666; Takáts, Szabolcs/0000-0003-2139-7740}
}

@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:2502657,
	title = {Atg17/FIP200 localizes to perilysosomal Ref(2)P aggregates and promotes autophagy by activation of Atg1 in Drosophila},
	url = {https://m2.mtmt.hu/api/publication/2502657},
	author = {Nagy, Péter and Kárpáti, Manuéla and Varga, Ágnes and Pircs, Karolina Milena and Venkei, Z and Takáts, Szabolcs and Varga, Kata and Érdi, Balázs and Hegedűs, Krisztina and Juhász, Gábor},
	doi = {10.4161/auto.27442},
	journal-iso = {AUTOPHAGY},
	journal = {AUTOPHAGY},
	volume = {10},
	unique-id = {2502657},
	issn = {1554-8627},
	abstract = {Phagophore-derived autophagosomes deliver cytoplasmic material to lysosomes for degradation and reuse. Autophagy mediated by the incompletely characterized actions of Atg proteins is involved in numerous physiological and pathological settings including stress resistance, immunity, aging, cancer, and neurodegenerative diseases. Here we characterized Atg17/FIP200, the Drosophila ortholog of mammalian RB1CC1/FIP200, a proposed functional equivalent of yeast Atg17. Atg17 disruption inhibits basal, starvation-induced and developmental autophagy, and interferes with the programmed elimination of larval salivary glands and midgut during metamorphosis. Upon starvation, Atg17-positive structures appear at aggregates of the selective cargo Ref(2)P/p62 near lysosomes. This location may be similar to the perivacuolar PAS (phagophore assembly site) described in yeast. Drosophila Atg17 is a member of the Atg1 kinase complex as in mammals, and we showed that it binds to the other subunits including Atg1, Atg13 and Atg101 (C12orf44 in humans, 9430023L20Rik in mice and RGD1359310 in rats). Atg17 is required for the kinase activity of endogenous Atg1 in vivo, as loss of Atg17 prevents the Atg1-dependent shift of endogenous Atg13 to hyperphosphorylated forms, and also blocks punctate Atg1 localization during starvation. Finally, we found that Atg1 overexpression induces autophagy and reduces cell size in Atg17-null mutant fat body cells, and that overexpression of Atg17 promotes endogenous Atg13 phosphorylation and enhances autophagy in an Atg1-dependent manner in the fat body. We propose a model according to which the relative activity of Atg1, estimated by the ratio of hyper- to hypophosphorylated Atg13, contributes to setting low (basal) vs. high (starvation-induced) autophagy levels in Drosophila.},
	year = {2014},
	eissn = {1554-8635},
	pages = {453-467},
	orcid-numbers = {Nagy, Péter/0000-0002-5053-0646; Pircs, Karolina Milena/0000-0001-8281-4785; Takáts, Szabolcs/0000-0003-2139-7740; Juhász, Gábor/0000-0001-8548-8874}
}

@article{MTMT:2527687,
	title = {Interaction of the HOPS complex with Syntaxin 17 mediates autophagosome clearance in Drosophila},
	url = {https://m2.mtmt.hu/api/publication/2527687},
	author = {Takáts, Szabolcs and Pircs, Karolina Milena and Nagy, Péter and Varga, Ágnes and Kárpáti, Manuéla and Hegedűs, Krisztina and Kramer, H and Kovács, Attila Lajos and Sass, Miklós and Juhász, Gábor},
	doi = {10.1091/mbc.E13-08-0449},
	journal-iso = {MOL BIOL CELL},
	journal = {MOLECULAR BIOLOGY OF THE CELL},
	volume = {25},
	unique-id = {2527687},
	issn = {1059-1524},
	year = {2014},
	eissn = {1939-4586},
	pages = {1338-1354},
	orcid-numbers = {Takáts, Szabolcs/0000-0003-2139-7740; Pircs, Karolina Milena/0000-0001-8281-4785; Nagy, Péter/0000-0002-5053-0646; Sass, Miklós/0000-0002-4559-8216; Juhász, Gábor/0000-0001-8548-8874}
}