@{MTMT:34722580,
	title = {Aminosav-, fehérje-anyagcsere},
	url = {https://m2.mtmt.hu/api/publication/34722580},
	author = {Tretter, László},
	booktitle = {Orvosi patobiokémia},
	unique-id = {34722580},
	year = {2023},
	pages = {121-142},
	orcid-numbers = {Tretter, László/0000-0001-5638-2886}
}

@CONFERENCE{MTMT:34030843,
	title = {METABOLIKUS POLIHISZTOR VAGY EGYSZERŰ GLUTAMINGYÁR? – CITRÁTKÖR AZ ASZTROCITÁKBAN},
	url = {https://m2.mtmt.hu/api/publication/34030843},
	author = {Kokas, Márton and Kirchlechner-Farkas, Judit Mária and Gáspár, Dániel and Komlódi, Tímea and Ozohanics, Olivér and Környei, Zsuzsanna and Sváb, Gergely and Tretter, László},
	booktitle = {Membrán-Transzport konferencia : programfüzet},
	unique-id = {34030843},
	year = {2023},
	orcid-numbers = {Kokas, Márton/0000-0002-3982-4782; Komlódi, Tímea/0000-0001-9876-1411; Ozohanics, Olivér/0000-0002-2705-9921; Sváb, Gergely/0000-0002-7669-8252; Tretter, László/0000-0001-5638-2886}
}

@article{MTMT:33718236,
	title = {Oxoglutarate dehydrogenase complex controls glutamate-mediated neuronal death},
	url = {https://m2.mtmt.hu/api/publication/33718236},
	author = {Weidinger, A. and Milivojev, N. and Hosmann, A. and Duvigneau, J.C. and Szabo, C. and Törö, G. and Rauter, L. and Vaglio-Garro, A. and Mkrtchyan, G.V. and Trofimova, L. and Sharipov, R.R. and Surin, A.M. and Krasilnikova, I.A. and Pinelis, V.G. and Tretter, László and Moldzio, R. and Bayır, H. and Kagan, V.E. and Bunik, V.I. and Kozlov, A.V.},
	doi = {10.1016/j.redox.2023.102669},
	journal-iso = {REDOX BIOL},
	journal = {REDOX BIOLOGY},
	volume = {62},
	unique-id = {33718236},
	issn = {2213-2317},
	year = {2023},
	eissn = {2213-2317},
	orcid-numbers = {Tretter, László/0000-0001-5638-2886}
}

@CONFERENCE{MTMT:34030854,
	title = {AZ α-KETOGLUTARÁT-DEHIDROGENÁZ KOMPLEX DLST+/- ÉS DLD+/- ALEGYSÉGEK KIÜTÉSÉNEK HATÁSA AZ OXIGÉNFOGYASZTÁSRA ÉS REAKTÍV OXIGÉNGYÖKKÉPZŐDÉSRE EGÉR AGYI MITOKONDRIUMOKON},
	url = {https://m2.mtmt.hu/api/publication/34030854},
	author = {Kokas, Márton and Horváth, Gergő and Tretter, László},
	booktitle = {51. Membrán-Transzport Konferencia},
	unique-id = {34030854},
	year = {2022},
	orcid-numbers = {Kokas, Márton/0000-0002-3982-4782; Horváth, Gergő/0000-0001-5386-9509; Tretter, László/0000-0001-5638-2886}
}

@article{MTMT:33070137,
	title = {Reverse and Forward Electron Flow-Induced H2O2 Formation Is Decreased in α-Ketoglutarate Dehydrogenase (α-KGDH) Subunit (E2 or E3) Heterozygote Knock Out Animals},
	url = {https://m2.mtmt.hu/api/publication/33070137},
	author = {Horváth, Gergő and Sváb, Gergely and Komlódi, Tímea and Ravasz, Dóra and Kacsó, Gergely and Dóczi, Judit and Chinopoulos, Christos and Ambrus, Attila and Tretter, László},
	doi = {10.3390/antiox11081487},
	journal-iso = {ANTIOXIDANTS-BASEL},
	journal = {ANTIOXIDANTS},
	volume = {11},
	unique-id = {33070137},
	abstract = {α-ketoglutarate dehydrogenase complex (KGDHc), or 2-oxoglutarate dehydrogenase complex (OGDHc) is a rate-limiting enzyme in the tricarboxylic acid cycle, that has been identified in neurodegenerative diseases such as in Alzheimer’s disease. The aim of the present study was to establish the role of the KGDHc and its subunits in the bioenergetics and reactive oxygen species (ROS) homeostasis of brain mitochondria. To study the bioenergetic profile of KGDHc, genetically modified mouse strains were used having a heterozygous knock out (KO) either in the dihydrolipoyl succinyltransferase (DLST+/−) or in the dihydrolipoyl dehydrogenase (DLD+/−) subunit. Mitochondrial oxygen consumption, hydrogen peroxide (H2O2) production, and expression of antioxidant enzymes were measured in isolated mouse brain mitochondria. Here, we demonstrate that the ADP-stimulated respiration of mitochondria was partially arrested in the transgenic animals when utilizing α-ketoglutarate (α-KG or 2-OG) as a fuel substrate. Succinate and α-glycerophosphate (α-GP), however, did not show this effect. The H2O2 production in mitochondria energized with α-KG was decreased after inhibiting the adenine nucleotide translocase and Complex I (CI) in the transgenic strains compared to the controls. Similarly, the reverse electron transfer (RET)-evoked H2O2 formation supported by succinate or α-GP were inhibited in mitochondria isolated from the transgenic animals. The decrease of RET-evoked ROS production by DLST+/− or DLD+/− KO-s puts the emphasis of the KGDHc in the pathomechanism of ischemia-reperfusion evoked oxidative stress. Supporting this notion, expression of the antioxidant enzyme glutathione peroxidase was also decreased in the KGDHc transgenic animals suggesting the attenuation of ROS-producing characteristics of KGDHc. These findings confirm the contribution of the KGDHc to the mitochondrial ROS production and in the pathomechanism of ischemia-reperfusion injury.},
	year = {2022},
	eissn = {2076-3921},
	orcid-numbers = {Horváth, Gergő/0000-0001-5386-9509; Sváb, Gergely/0000-0002-7669-8252; Komlódi, Tímea/0000-0001-9876-1411; Ravasz, Dóra/0000-0002-0510-3282; Kacsó, Gergely/0000-0003-0428-3645; Dóczi, Judit/0000-0002-5797-5074; Chinopoulos, Christos/0000-0003-0183-4149; Ambrus, Attila/0000-0001-6014-3175; Tretter, László/0000-0001-5638-2886}
}

@article{MTMT:32989211,
	title = {The effect of Cyclophilin D depletion on liver regeneration following associating liver partition and portal vein ligation for staged hepatectomy},
	url = {https://m2.mtmt.hu/api/publication/32989211},
	author = {Daradics, Noémi and Horváth, Gergő and Tretter, László and Paál, Ágnes and Fülöp, András and Budai, András and Szijártó, Attila},
	doi = {10.1371/journal.pone.0271606},
	journal-iso = {PLOS ONE},
	journal = {PLOS ONE},
	volume = {17},
	unique-id = {32989211},
	issn = {1932-6203},
	abstract = {Associating Liver Partition and Portal vein ligation for Staged hepatectomy (ALPPS) is a modification of two-stage hepatectomy profitable for patients with inoperable hepatic tumors by standard techniques. Unfortunately, initially poor postoperative outcome was associated with ALPPS, in which mitochondrial dysfunction played an essential role. Inhibition of cyclophilins has been already proposed to be efficient as a mitochondrial therapy in liver diseases. To investigate the effect of Cyclophilin D (CypD) depletion on mitochondrial function, biogenesis and liver regeneration following ALPPS a CypD knockout (KO) mice model was created.Male wild type (WT) (n = 30) and CypD KO (n = 30) mice underwent ALPPS procedure. Animals were terminated pre-operatively and 24, 48, 72 or 168 h after the operation. Mitochondrial functional studies and proteomic analysis were performed. Regeneration rate and mitotic activity were assessed.The CypD KO group displayed improved mitochondrial function, as both ATP production (P < 0.001) and oxygen consumption (P < 0.05) were increased compared to the WT group. The level of mitochondrial biogenesis coordinator peroxisome proliferator-activated receptor γ co-activator 1-α (PGC1-α) was also elevated in the CypD KO group (P < 0.001), which resulted in the induction of the mitochondrial oxidative phosphorylation system. Liver growth increased in the CypD KO group compared to the WT group (P < 0.001).Our study demonstrates the beneficial effect of CypD depletion on the mitochondrial vulnerability following ALPPS. Based on our results we propose that CypD inhibition should be further investigated as a possible mitochondrial therapy following ALPPS.},
	year = {2022},
	eissn = {1932-6203},
	orcid-numbers = {Daradics, Noémi/0000-0001-6918-7406; Horváth, Gergő/0000-0001-5386-9509; Tretter, László/0000-0001-5638-2886; Paál, Ágnes/0000-0003-2292-3714; Budai, András/0000-0002-4634-2140}
}

@misc{MTMT:34036737,
	title = {A metilénkék hatása a citokróm-c redox állapotára in vivo és in vitro körülmények között},
	url = {https://m2.mtmt.hu/api/publication/34036737},
	author = {Kokas, Márton and Sváb, Gergely and Tretter, László},
	unique-id = {34036737},
	year = {2021},
	orcid-numbers = {Kokas, Márton/0000-0002-3982-4782; Sváb, Gergely/0000-0002-7669-8252; Tretter, László/0000-0001-5638-2886}
}

@article{MTMT:31887594,
	title = {Methylene Blue Bridges the Inhibition and Produces Unusual Respiratory Changes in Complex III-Inhibited Mitochondria. Studies on Rats, Mice and Guinea Pigs},
	url = {https://m2.mtmt.hu/api/publication/31887594},
	author = {Sváb, Gergely and Kokas, Márton and Sipos, Ildikó and Ambrus, Attila and Tretter, László},
	doi = {10.3390/antiox10020305},
	journal-iso = {ANTIOXIDANTS-BASEL},
	journal = {ANTIOXIDANTS},
	volume = {10},
	unique-id = {31887594},
	year = {2021},
	eissn = {2076-3921},
	orcid-numbers = {Sváb, Gergely/0000-0002-7669-8252; Kokas, Márton/0000-0002-3982-4782; Sipos, Ildikó/0000-0003-2861-1439; Ambrus, Attila/0000-0001-6014-3175; Tretter, László/0000-0001-5638-2886}
}

@article{MTMT:31822211,
	title = {Cyclophilin D-dependent mitochondrial permeability transition amplifies inflammatory reprogramming in endotoxemia},
	url = {https://m2.mtmt.hu/api/publication/31822211},
	author = {Veres, Balázs and Erős, Krisztián and Antus, Csenge Petra and Kálmán, Nikoletta and Fónai, Fruzsina and Jakus, Péter and Boros, Éva and Hegedűs, Zoltán and Nagy, István and Tretter, László and Gallyas, Ferenc and Sümegi, Balázs},
	doi = {10.1002/2211-5463.13091},
	journal-iso = {FEBS OPEN BIO},
	journal = {FEBS OPEN BIO},
	volume = {11},
	unique-id = {31822211},
	issn = {2211-5463},
	abstract = {Microorganisms or LPS (lipopolysaccharide), an outer membrane component of Gram-negative bacteria, can induce a systemic inflammatory response that leads to sepsis, multiple organ dysfunction, and mortality. Here, we investigated the role of cyclophilin D (CypD)-dependent mitochondrial permeability transition (mPT) in the immunosuppressive phase of LPS-induced endotoxic shock. The liver plays an important role in immunity and organ dysfunction; therefore, we used liver RNA sequencing (RNAseq) data, Ingenuity® Pathway Analysis (IPA ® ) to investigate the complex role of mPT formation in inflammatory reprogramming and disease progression. LPS induced significant changes in the expression of 2844 genes, affecting 179 pathways related to mitochondrial dysfunction, defective oxidative phosphorylation, nitric oxide (NO) and reactive oxygen species (ROS) accumulation, nuclear factor, erythroid 2 like 2 (Nrf2), Toll-like receptors (TLRs), and tumor necrosis factor α receptor (TNFR)-mediated processes in wild-type mice. The disruption of CypD reduced LPS-induced alterations in gene expression and pathways involving TNFRs and TLRs, in addition to improving survival and attenuating oxidative liver damage and the related NO- and ROS-producing pathways. CypD deficiency diminished the suppressive effect of LPS on mitochondrial function, nuclear- and mitochondrial-encoded genes, and mitochondrial DNA (mtDNA) quantity, which could be critical in improving survival. Our data propose that CypD-dependent mPT is an amplifier in inflammatory reprogramming and promotes disease progression. The mortality in human sepsis and shock is associated with mitochondrial dysfunction. Prevention of mPT by CypD disruption reduces inflammatory reprogramming, mitochondrial dysfunction, and lethality; therefore, CypD can be a novel drug target in endotoxic shock and related inflammatory diseases.},
	keywords = {Inflammation; LIVER; ENDOTOXIN; ANTIOXIDANT; Mitochondria; Gene Expression; Toll-like receptor; Reprogramming; cyclophilin D; Oxidative stress},
	year = {2021},
	eissn = {2211-5463},
	pages = {684-704},
	orcid-numbers = {Tretter, László/0000-0001-5638-2886; Gallyas, Ferenc/0000-0002-1906-4333}
}

@article{MTMT:31595275,
	title = {Bioenergetic impairment of triethylene glycol dimethacrylate- (TEGDMA-) treated dental pulp stem cells (DPSCs) and isolated brain mitochondria are amended by redox compound methylene blue},
	url = {https://m2.mtmt.hu/api/publication/31595275},
	author = {Mikulás, Krisztina Ágnes and Komlódi, Tímea and Földes, Anna and Sváb, Gergely and Horváth, Gergő and Nagy, Ádám Miklós and Ambrus, Attila and Gyulai-Gaál, Szabolcs and Gera, István and Hermann, Péter and Varga, Gábor and Tretter, László},
	doi = {10.3390/ma13163472},
	journal-iso = {MATERIALS},
	journal = {MATERIALS},
	volume = {13},
	unique-id = {31595275},
	abstract = {Background: Triethylene glycol dimethacrylate (TEGDMA) monomers released from resin matrix are toxic to dental pulp cells, induce apoptosis, oxidative stress and decrease viability. Recently, mitochondrial complex I (CI) was identified as a potential target of TEGDMA. In isolated mitochondria supported by CI, substrates oxidation and ATP synthesis were inhibited, reactive oxygen species production was stimulated. Contrary to that, respiratory Complex II was not impaired by TEGDMA. The beneficial effects of electron carrier compound methylene blue (MB) are proven in many disease models where mitochondrial involvement has been detected. In the present study, the bioenergetic effects of MB on TEGDMA-treated isolated mitochondria and on human dental pulp stem cells (DPSC) were analyzed. Methods: Isolated mitochondria and DPSC were acutely exposed to low millimolar concentrations of TEGDMA and 2 μM concentration of MB. Mitochondrial and cellular respiration and glycolytic flux were measured by high resolution respirometry and by Seahorse XF extracellular analyzer. Mitochondrial membrane potential was measured fluorimetrically. Results: MB partially restored the mitochondrial oxidation, rescued membrane potential in isolated mitochondria and significantly increased the impaired cellular O2 consumption in the presence of TEGDMA. Conclusion: MB is able to protect against TEGDMA-induced CI damage, and might provide protective effects in resin monomer exposed cells. © 2020 by the authors.},
	keywords = {Oxygen Consumption; Stem Cells; Mitochondria; Mitochondria; Substrates; Cell Death; Aromatic compounds; methylene blue; Resins; Acrylic monomers; Glycols; Triethylene glycol dimethacrylate; mitochondrial membrane potential; Mitochondrial complex; Millimolar concentrations; Dental pulp stem cells; TEGDMA; DPSC; Cellular respiration; Dental pulp stem cell (DPSC); Substrates oxidation},
	year = {2020},
	eissn = {1996-1944},
	orcid-numbers = {Mikulás, Krisztina Ágnes/0000-0002-0259-9761; Komlódi, Tímea/0000-0001-9876-1411; Földes, Anna/0000-0002-4182-7886; Sváb, Gergely/0000-0002-7669-8252; Horváth, Gergő/0000-0001-5386-9509; Nagy, Ádám Miklós/0000-0002-9568-2555; Ambrus, Attila/0000-0001-6014-3175; Gyulai-Gaál, Szabolcs/0000-0003-2419-4236; Gera, István/0000-0002-4355-7613; Hermann, Péter/0000-0002-9148-0139; Varga, Gábor/0000-0002-5506-8198; Tretter, László/0000-0001-5638-2886}
}