@article{MTMT:34874198,
	title = {The bacterial metabolite, lithocholic acid, has antineoplastic effects in pancreatic adenocarcinoma},
	url = {https://m2.mtmt.hu/api/publication/34874198},
	author = {Schwarcz, Szandra and Kovács, Patrik Bence and Nyerges, Petra and Ujlaki, Gyula and Sipos, Adrienn and Uray (Davis), Karen L. and Bay, Péter and Mikó, Edit},
	doi = {10.1038/s41420-024-02023-1},
	journal-iso = {CELL DEATH DISCOV},
	journal = {CELL DEATH DISCOVERY},
	volume = {10},
	unique-id = {34874198},
	abstract = {Lithocholic acid (LCA) is a secondary bile acid. LCA enters the circulation after bacterial synthesis in the gastrointestinal tract, reaches distantly located cancer cells, and influences their behavior. LCA was considered carcinogenic, but recent studies demonstrated that LCA has antitumor effects. We assessed the possible role of LCA in pancreatic adenocarcinoma. At the serum reference concentration, LCA induced a multi-pronged antineoplastic program in pancreatic adenocarcinoma cells. LCA inhibited cancer cell proliferation and induced mesenchymal-to-epithelial (MET) transition that reduced cell invasion capacity. LCA induced oxidative/nitrosative stress by decreasing the expression of nuclear factor, erythroid 2-like 2 (NRF2) and inducing inducible nitric oxide synthase (iNOS). The oxidative/nitrosative stress increased protein nitration and lipid peroxidation. Suppression of oxidative stress by glutathione (GSH) or pegylated catalase (pegCAT) blunted LCA-induced MET. Antioxidant genes were overexpressed in pancreatic adenocarcinoma and decreased antioxidant levels correlated with better survival of pancreatic adenocarcinoma patients. Furthermore, LCA treatment decreased the proportions of cancer stem cells. Finally, LCA induced total and ATP-linked mitochondrial oxidation and fatty acid oxidation. LCA exerted effects through the farnesoid X receptor (FXR), vitamin D receptor (VDR), and constitutive androstane receptor (CAR). LCA did not interfere with cytostatic agents used in the chemotherapy of pancreatic adenocarcinoma. Taken together, LCA is a non-toxic compound and has antineoplastic effects in pancreatic adenocarcinoma.},
	year = {2024},
	eissn = {2058-7716}
}

@article{MTMT:34864586,
	title = {Serine 39 in the GTP ‐binding domain of Drp1 is involved in shaping mitochondrial morphology},
	url = {https://m2.mtmt.hu/api/publication/34864586},
	author = {Ghani, Marvi and Szabó, Bernadett and Alkhatibe, Mahmoud and Amsalu, Hailemariam and Zohar, Peleg and Janka, Eszter Anna and Mótyán, János András and Tar, Krisztina},
	doi = {10.1002/2211-5463.13820},
	journal-iso = {FEBS OPEN BIO},
	journal = {FEBS OPEN BIO},
	unique-id = {34864586},
	issn = {2211-5463},
	abstract = {Continuous fusion and fission are critical for mitochondrial health. In this study, we further characterize the role played by dynamin‐related protein 1 (Drp1) in mitochondrial fission. We show that a single amino acid change in Drp1 at position 39 from serine to alanine (S39A) within the GTP‐binding (GTPase) domain results in a fused mitochondrial network in human SH‐SY5Y neuroblastoma cells. Interestingly, the phosphorylation of Ser‐616 and Ser‐637 of Drp1 remains unaffected by the S39A mutation, and mitochondrial bioenergetic profile and cell viability in the S39A mutant were comparable to those observed in the control. This leads us to propose that the serine 39 residue of Drp1 plays a crucial role in mitochondrial distribution through its involvement in the GTPase activity. Furthermore, this amino acid mutation leads to structural anomalies in the mitochondrial network. Taken together, our results contribute to a better understanding of the function of the Drp1 protein.},
	year = {2024},
	eissn = {2211-5463},
	orcid-numbers = {Amsalu, Hailemariam/0000-0001-5787-7872; Zohar, Peleg/0009-0004-8466-8602; Janka, Eszter Anna/0000-0003-0724-5281}
}

@article{MTMT:34836717,
	title = {Microcystin-LR, a cyanotoxin, modulates division of higher plant chloroplasts through protein phosphatase inhibition and affects cyanobacterial division},
	url = {https://m2.mtmt.hu/api/publication/34836717},
	author = {Máthé, Csaba and Bóka, Károly and Kónya, Zoltán and Erdődi, Ferenc and Vasas, Gábor and Freytag, Csongor and Garda, Tamás},
	doi = {10.1016/j.chemosphere.2024.142125},
	journal-iso = {CHEMOSPHERE},
	journal = {CHEMOSPHERE},
	volume = {358},
	unique-id = {34836717},
	issn = {0045-6535},
	keywords = {PROTEIN PHOSPHATASE; microcystin-LR; Arabidopsis.; chloroplast division/fission},
	year = {2024},
	eissn = {1879-1298},
	orcid-numbers = {Bóka, Károly/0000-0002-1324-3592; Freytag, Csongor/0000-0002-3356-4182}
}

@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:34817464,
	title = {Specific and shared biological functions of PARP2 – is PARP2 really a lil’ brother of PARP1?},
	url = {https://m2.mtmt.hu/api/publication/34817464},
	author = {Szántó, Magdolna and Yélamos, J and Bay, Péter},
	doi = {10.1017/erm.2024.14},
	journal-iso = {EXPERT REV MOL MED},
	journal = {EXPERT REVIEWS IN MOLECULAR MEDICINE},
	volume = {26},
	unique-id = {34817464},
	issn = {1462-3994},
	year = {2024},
	eissn = {1462-3994},
	pages = {1-21}
}

@article{MTMT:34813914,
	title = {Synthesis, in silico and kinetics evaluation of N-(beta-D-glucopyranosyl)-2-arylimidazole-4(5)-carboxamides and N-(beta-D-glucopyranosyl)-4(5)-arylimidazole-2-carboxamides as glycogen phosphorylase inhibitors},
	url = {https://m2.mtmt.hu/api/publication/34813914},
	author = {Homolya, Levente and Mathomes, Rachel T. and Fodor-Varga, Luca Anna and Docsa, Tibor and Juhász, László and Hayes, Joseph M. and Somsák, László},
	doi = {10.3390/ijms25094591},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {25},
	unique-id = {34813914},
	issn = {1661-6596},
	abstract = {Recently studied N-(β-D-glucopyranosyl)-3-aryl-1,2,4-triazole-5-carboxamides have proven to be low micromolar inhibitors of glycogen phosphorylase (GP), a validated target for the treatment of type 2 diabetes mellitus. Since in other settings, the bioisosteric replacement of the 1,2,4-triazole moiety with imidazole resulted in significantly more efficient GP inhibitors, in silico calculations using Glide molecular docking along with unbound state DFT calculations were performed on N-(β-Dglucopyranosyl)-arylimidazole-carboxamides, revealing their potential for strong GP inhibition. The syntheses of the target compounds involved the formation of an amide bond between per-O-acetylated β-D-glucopyranosylamine and the corresponding arylimidazole-carboxylic acids. Kinetics experiments on rabbit muscle GPb revealed low micromolar inhibitors, with the best inhibition constants (Kis) of ~3–4 µM obtained for 1- and 2-naphthyl-substituted N-(β-D-glucopyranosyl)-imidazolecarboxamides, 2b–c. The predicted protein–ligand interactions responsible for the observed potencies are discussed and will facilitate the structure-based design of other inhibitors targeting this important therapeutic target. Meanwhile, the importance of the careful consideration of ligand tautomeric states in binding calculations is highlighted, with the usefulness of DFT calculations in this regard proposed.},
	keywords = {Glycogen phosphorylase inhibitor; Tautomers; type 2 diabetes; glucose analogues},
	year = {2024},
	eissn = {1422-0067},
	pages = {1-21},
	orcid-numbers = {Juhász, László/0000-0002-7462-7944; Somsák, László/0000-0002-9103-9845}
}

@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:34747207,
	title = {Ünnepelt a Debreceni Egyetem Orvosi Vegytani Intézete: 70 éves Dombrádi Viktor és Erdődi Ferenc},
	url = {https://m2.mtmt.hu/api/publication/34747207},
	author = {Lontay, Beáta},
	journal-iso = {BIOKÉMIA},
	journal = {BIOKÉMIA: A MAGYAR BIOKÉMIAI EGYESÜLET FOLYÓIRATA},
	volume = {XLVIII},
	unique-id = {34747207},
	issn = {0133-8455},
	year = {2024},
	eissn = {2060-8152},
	pages = {96-100}
}

@article{MTMT:34738061,
	title = {Stable knockdown of Drp1 improves retinoic acid-BDNF-induced neuronal differentiation through global transcriptomic changes and results in reduced phosphorylation of ERK1/2 independently of DUSP1 and 6},
	url = {https://m2.mtmt.hu/api/publication/34738061},
	author = {Ghani, Marvi and Zohar, Peleg and Ujlaki, Gyula and Tóth, Melinda and Amsalu, Hailemariam and Póliska, Szilárd and Tar, Krisztina},
	doi = {10.3389/fcell.2024.1342741},
	journal-iso = {FRONT CELL DEV BIOL},
	journal = {FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY},
	volume = {12},
	unique-id = {34738061},
	issn = {2296-634X},
	abstract = {Background: Dynamin-related protein Drp1 —a major mitochondrial fission protein— is widely distributed in the central nervous system and plays a crucial role in regulating mitochondrial dynamics, specifically mitochondrial fission and the organelle's shaping. Upregulated Drp1 function may contribute to the pathological progression of neurodegenerative diseases by dysregulating mitochondrial fission/ fusion. The study aims to investigate the effects of Drp1 on retinoic acid-BDNF-induced (RA-BDNF) neuronal differentiation and mitochondrial network reorganization in SH-SY5Y neuroblastoma cells.},
	year = {2024},
	eissn = {2296-634X},
	pages = {1-25}
}

@article{MTMT:34573513,
	title = {PP2A Affects Angiogenesis via Its Interaction with a Novel Phosphorylation Site of TSP1},
	url = {https://m2.mtmt.hu/api/publication/34573513},
	author = {Thalwieser, Zsófia and Fonódi, Márton and Király, Nikolett and Csortos, Csilla and Boratkó, Anita},
	doi = {10.3390/ijms25031844},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {25},
	unique-id = {34573513},
	issn = {1661-6596},
	abstract = {Alterations in angiogenic properties play a pivotal role in the manifestation and onset of various pathologies, including vascular diseases and cancer. Thrombospondin-1 (TSP1) protein is one of the master regulators of angiogenesis. This study unveils a novel aspect of TSP1 regulation through reversible phosphorylation. The silencing of the B55α regulatory subunit of protein phosphatase 2A (PP2A) in endothelial cells led to a significant decrease in TSP1 expression. Direct interaction between TSP1 and PP2A-B55α was confirmed via various methods. Truncated TSP1 constructs were employed to identify the phosphorylation site and the responsible kinase, ultimately pinpointing PKC as the enzyme phosphorylating TSP1 on Ser93. The biological effects of B55α–TSP1 interaction were also analyzed. B55α silencing not only counteracted the increase in TSP1 expression during wound closure but also prolonged wound closure time. Although B55α silenced cells initiated tube-like structures earlier than control cells, their spheroid formation was disrupted, leading to disintegration. Cells transfected with phosphomimic TSP1 S93D exhibited smaller spheroids and reduced effectiveness in tube formation, revealing insights into the effects of TSP1 phosphorylation on angiogenic properties. In this paper, we introduce a new regulatory mechanism of angiogenesis by reversible phosphorylation on TSP1 S93 by PKC and PP2A B55α.},
	year = {2024},
	eissn = {1422-0067},
	pages = {1844}
}