@article{MTMT:34820104,
	title = {Quantifying antibody-dependent cellular cytotoxicity in a tumor spheroid model : application for drug discovery},
	url = {https://m2.mtmt.hu/api/publication/34820104},
	author = {Isotta, Sturniolo and Csongor, Váróczy and Ákos, Máté Bede and Hegedűs, Csaba and Demény, Máté Ágoston and Virág, László},
	journal-iso = {JOVE-J VIS EXP},
	journal = {JOVE-JOURNAL OF VISUALIZED EXPERIMENTS},
	unique-id = {34820104},
	issn = {1940-087X},
	year = {2024},
	eissn = {1940-087X}
}

@article{MTMT:34754751,
	title = {PARP14 contributes to the development of the tumor-associated macrophage phenotype},
	url = {https://m2.mtmt.hu/api/publication/34754751},
	author = {Sturniolo, I and Váróczy, Cs and Regdon, Zsolt and Mázló, A and Muzsai, Sz and Bácsi, A and Intili, G and Hegedűs, Csaba and Boothby, MR and Holechek, J and Ferraris, D and Schüler, H and Virág, László},
	doi = {10.3390/ijms25073601},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {25},
	unique-id = {34754751},
	issn = {1661-6596},
	year = {2024},
	eissn = {1422-0067},
	pages = {1-21}
}

@article{MTMT:34729573,
	title = {Automated high-throughput cell culture scratch assay identifies wound healing promoting and inhibiting compounds from a small compound library of redox active molecules},
	url = {https://m2.mtmt.hu/api/publication/34729573},
	author = {Virág, László and Hegedűs, Csaba and Kovács, Katalin and Polgár, Zsuzsanna and Kókai, Endre and Sturniolo, Isotta and Demény, Máté Ágoston and Virág, Bernadett and Szabó, Éva},
	doi = {10.1016/j.freeradbiomed.2023.10.328},
	journal-iso = {FREE RADICAL BIO MED},
	journal = {FREE RADICAL BIOLOGY AND MEDICINE},
	volume = {208},
	unique-id = {34729573},
	issn = {0891-5849},
	year = {2023},
	eissn = {1873-4596},
	pages = {S144-S144}
}

@article{MTMT:34108111,
	title = {High-Content Screening Assay for the Identification of Antibody-Dependent Cellular Cytotoxicity Modifying Compounds},
	url = {https://m2.mtmt.hu/api/publication/34108111},
	author = {Guti, Eliza and Bede, Ákos Máté and Váróczy, Csongor and Hegedűs, Csaba and Demény, Máté Ágoston and Virág, László},
	doi = {10.3791/64485},
	journal-iso = {JOVE-J VIS EXP},
	journal = {JOVE-JOURNAL OF VISUALIZED EXPERIMENTS},
	unique-id = {34108111},
	issn = {1940-087X},
	year = {2023},
	eissn = {1940-087X},
	pages = {1-12}
}

@article{MTMT:34020857,
	title = {Adenosine A2A Receptor Activation Regulates Niemann–Pick C1 Expression and Localization in Macrophages},
	url = {https://m2.mtmt.hu/api/publication/34020857},
	author = {Skopál, Adrienn and Ujlaki, Gyula and Gerencsér, Attila Tibor and Bankó, Csaba and Bacsó, Zsolt and Ciruela, Francisco and Virág, László and Haskó, György and Kókai, Endre},
	doi = {10.3390/cimb45060315},
	journal-iso = {CURR ISSUES MOL BIOL},
	journal = {CURRENT ISSUES IN MOLECULAR BIOLOGY},
	volume = {45},
	unique-id = {34020857},
	issn = {1467-3037},
	abstract = {Adenosine plays an important role in modulating immune cell function, particularly T cells and myeloid cells, such as macrophages and dendritic cells. Cell surface adenosine A2A receptors (A2AR) regulate the production of pro-inflammatory cytokines and chemokines, as well as the proliferation, differentiation, and migration of immune cells. In the present study, we expanded the A2AR interactome and provided evidence for the interaction between the receptor and the Niemann–Pick type C intracellular cholesterol transporter 1 (NPC1) protein. The NPC1 protein was identified to interact with the C-terminal tail of A2AR in RAW 264.7 and IPMФ cells by two independent and parallel proteomic approaches. The interaction between the NPC1 protein and the full-length A2AR was further validated in HEK-293 cells that permanently express the receptor and RAW264.7 cells that endogenously express A2AR. A2AR activation reduces the expression of NPC1 mRNA and protein density in LPS-activated mouse IPMФ cells. Additionally, stimulation of A2AR negatively regulates the cell surface expression of NPC1 in LPS-stimulated macrophages. Furthermore, stimulation of A2AR also altered the density of lysosome-associated membrane protein 2 (LAMP2) and early endosome antigen 1 (EEA1), two endosomal markers associated with the NPC1 protein. Collectively, these results suggested a putative A2AR-mediated regulation of NPC1 protein function in macrophages, potentially relevant for the Niemann–Pick type C disease when mutations in NPC1 protein result in the accumulation of cholesterol and other lipids in lysosomes.},
	year = {2023},
	eissn = {1467-3045},
	pages = {4948-4969},
	orcid-numbers = {Bacsó, Zsolt/0000-0001-6885-3796; Ciruela, Francisco/0000-0003-0832-3739}
}

@misc{MTMT:33806508,
	title = {Optimization of tumor cell killing by chimeric antigen receptor expressing macrophages},
	url = {https://m2.mtmt.hu/api/publication/33806508},
	author = {Gerencsér, A and Tóth, PÁ and Vígh, D and Kókai, Endre and Virág, László},
	unique-id = {33806508},
	year = {2023}
}

@article{MTMT:33153168,
	title = {OGG1 Inhibition Reduces Acinar Cell Injury in a Mouse Model of Acute Pancreatitis},
	url = {https://m2.mtmt.hu/api/publication/33153168},
	author = {Hajnády, Zoltán and Nagy-Pénzes, Máté and Demény, Máté Ágoston and Kovács, Katalin and El-Hamoly, Tarek and Maléth, József and Hegyi, Péter and Polgár, Zsuzsanna and Hegedűs, Csaba and Virág, László},
	doi = {10.3390/biomedicines10102543},
	journal-iso = {BIOMEDICINES},
	journal = {BIOMEDICINES},
	volume = {10},
	unique-id = {33153168},
	abstract = {Acute pancreatitis (AP) is a potentially life-threatening gastrointestinal disease with a complex pathology including oxidative stress. Oxidative stress triggers oxidative DNA lesions such as formation of 7,8-dihydro-8-oxo-2′-oxoguanine (8-oxoG) and also causes DNA strand breaks. DNA breaks can activate the nuclear enzyme poly(ADP-ribose) polymerase 1 (PARP1) which contributes to AP pathology. 8-oxoG is recognized by 8-oxoG glycosylase 1 (OGG1) resulting in the removal of 8-oxoG from DNA as an initial step of base excision repair. Since OGG1 also possesses a DNA nicking activity, OGG1 activation may also trigger PARP1 activation. In the present study we investigated the role played by OGG1 in AP. We found that the OGG1 inhibitor compound TH5487 reduced edema formation, inflammatory cell migration and necrosis in a cerulein-induced AP model in mice. Moreover, TH5487 caused 8-oxoG accumulation and reduced tissue poly(ADP-ribose) levels. Consistent with the indirect PARP inhibitory effect, TH5487 shifted necrotic cell death (LDH release and Sytox green uptake) towards apoptosis (caspase activity) in isolated pancreatic acinar cells. In the in vivo AP model, TH5487 treatment suppressed the expression of various cytokine and chemokine mRNAs such as those of TNF, IL-1β, IL1ra, IL6, IL16, IL23, CSF, CCL2, CCL4, CCL12, IL10 and TREM as measured with a cytokine array and verified by RT-qPCR. As a potential mechanism underlying the transcriptional inhibitory effect of the OGG1 inhibitor we showed that while 8-oxoG accumulation in the DNA facilitates NF-κB binding to its consensus sequence, when OGG1 is inhibited, target site occupancy of NF-κB is impaired. In summary, OGG1 inhibition provides protection from tissue injury in AP and these effects are likely due to interference with the PARP1 and NF-κB activation pathways.},
	year = {2022},
	eissn = {2227-9059},
	orcid-numbers = {Demény, Máté Ágoston/0000-0003-4623-4091; Maléth, József/0000-0001-5768-3090; Hegyi, Péter/0000-0003-0399-7259}
}

@article{MTMT:33140473,
	title = {100 éves a Debreceni Egyetem Orvosi Vegytani Intézete},
	url = {https://m2.mtmt.hu/api/publication/33140473},
	author = {Virág, László},
	doi = {10.29116/gerundium/2022/1-2/13},
	journal-iso = {GERUNDIUM},
	journal = {GERUNDIUM: EGYETEMTÖRTÉNETI KÖZLEMÉNYEK},
	volume = {MMXXII},
	unique-id = {33140473},
	issn = {2061-5132},
	year = {2022},
	eissn = {2061-7097},
	pages = {203-216}
}

@article{MTMT:32886684,
	title = {Tricetin Reduces Inflammation and Acinar Cell Injury in Cerulein-Induced Acute Pancreatitis: The Role of Oxidative Stress-Induced DNA Damage Signaling},
	url = {https://m2.mtmt.hu/api/publication/32886684},
	author = {Nagy-Pénzes, Máté and Hajnády, Zoltán and Regdon, Zsolt and Demény, Máté Ágoston and Kovács, Katalin and El-Hamoly, Tarek and Maléth, József and Hegyi, Péter and Hegedűs, Csaba and Virág, László},
	doi = {10.3390/biomedicines10061371},
	journal-iso = {BIOMEDICINES},
	journal = {BIOMEDICINES},
	volume = {10},
	unique-id = {32886684},
	year = {2022},
	eissn = {2227-9059},
	orcid-numbers = {Maléth, József/0000-0001-5768-3090; Hegyi, Péter/0000-0003-0399-7259}
}

@article{MTMT:32799560,
	title = {Cathepsin D interacts with adenosine A2A receptors in mouse macrophages to modulate cell surface localization and inflammatory signalling},
	url = {https://m2.mtmt.hu/api/publication/32799560},
	author = {Skopál, Adrienn and Kéki, T and Tóth, PÁ and Csóka, B and Koscsó, B and Német, ZH and Antonioli, L and Ivessa, A and Ciruela, F and Virág, László and Haskó, György and Kókai, Endre},
	doi = {10.1016/j.jbc.2022.101888},
	journal-iso = {J BIOL CHEM},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {298},
	unique-id = {32799560},
	issn = {0021-9258},
	year = {2022},
	eissn = {1083-351X}
}