@article{MTMT:32866658,
	title = {Real-world evidence on methotrexate-free subcutaneous tocilizumab therapy in patients with rheumatoid arthritis : 24-week data from the SIMPACT study},
	url = {https://m2.mtmt.hu/api/publication/32866658},
	author = {Nagy, György and Géher, Pál and Tamási, László and Drescher, Edit and Keszthelyi, Péter and Pulai, Judit and Czirják, László and Szekanecz, Zoltán and Kiss, Gergely and Kovács, László},
	doi = {10.1093/rap/rkac038},
	journal-iso = {RHEUMATOL ADV PRACT},
	journal = {RHEUMATOLOGY ADVANCES IN PRACTICE},
	volume = {6},
	unique-id = {32866658},
	abstract = {The aim of the SIMPACT study was to evaluate the efficacy and safety of MTX-free s.c. tocilizumab (TCZ) therapy in RA patients.SIMPACT was an open-label, non-controlled, non-randomized, non-interventional study, in which RA patients for whom the treating physicians ordered s.c. TCZ were observed during a 24-week treatment period in Hungarian centres. Although the use of MTX was avoided during the study period, other conventional synthetic DMARDs, oral CSs and NSAIDs were allowed. Study endpoints included the change in DAS28 and clinical activity index (CDAI) scores, the proportion of patients achieving remission in the whole population and in subgroups defined based on prior RA treatment history, and age, weight or biological sex post hoc. The extent of supplementary medication use was monitored.Three hundred and thirty-seven RA patients were enrolled in 18 study centres. TCZ therapy significantly decreased the disease activity measured by both DAS28 (P = 0.0001) and CDAI (P = 0.0001). Clinical response was more pronounced in biologic-naïve patients and was lower in patients >75 years of age. In the whole population, DAS28 ESR or CRP and CDAI remission rates were 70.10%, 78.95% and 33.59%, respectively. In patients <45 years of age, the CDAI remission rate doubled (67.86%). A significant decrease in the frequency of co-administered medication was reported, including oral CSs and DMARDs.Real-world clinical evidence on s.c. TCZ reported here is in line with the efficacy outcomes of randomized clinical trials. Subgroup analysis revealed that TCZ was more effective in biologic-naïve patients and in those <75 years old.ClinicalTrials.gov, http://www.clinicaltrials.gov, NCT02402686.},
	keywords = {steroid; rheumatoid arthritis; monotherapy; tocilizumab; DAS28; Subcutaneous; clinical activity index},
	year = {2022},
	eissn = {2514-1775},
	orcid-numbers = {Nagy, György/0000-0003-1198-3228; Géher, Pál/0000-0002-4543-9629; Kovács, László/0000-0003-4457-1430}
}

@article{MTMT:3037329,
	title = {Divalent cation chelators citrate and EDTA unmask an intrinsic uncoupling pathway in isolated mitochondria.},
	url = {https://m2.mtmt.hu/api/publication/3037329},
	author = {Starkov, AA and Chinopoulos, Christos and Starkova, NN and Konrád, Csaba and Kiss, Gergely and Stepanova, A and Popov, VN},
	doi = {10.1007/s10863-016-9656-x},
	journal-iso = {J BIOENERG BIOMEMBR},
	journal = {JOURNAL OF BIOENERGETICS AND BIOMEMBRANES},
	volume = {49},
	unique-id = {3037329},
	issn = {0145-479X},
	abstract = {We demonstrate a suppression of ROS production and uncoupling of mitochondria by exogenous citrate in Mg2+ free medium. Exogenous citrate suppressed H2O2 emission and depolarized mitochondria. The depolarization was paralleled by the stimulation of respiration of mitochondria. The uncoupling action of citrate was independent of the presence of sodium, potassium, or chlorine ions, and it was not mediated by the changes in permeability of the inner mitochondrial membrane to solutes. The citrate transporter was not involved in the citrate effect. Inhibitory analysis data indicated that several well described mitochondria carriers and channels (ATPase, IMAC, ADP/ATP translocase, mPTP, mKATP) were not involved in citrate's effect. Exogenous MgCl2 strongly inhibited citrate-induced depolarization. The uncoupling effect of citrate was demonstrated in rat brain, mouse brain, mouse liver, and human melanoma cells mitochondria. We interpreted the data as an evidence to the existence of a hitherto undescribed putative inner mitochondrial membrane channel that is regulated by extramitochondrial Mg2+ or other divalent cations.},
	year = {2017},
	eissn = {1573-6881},
	pages = {3-11},
	orcid-numbers = {Chinopoulos, Christos/0000-0003-0183-4149}
}

@article{MTMT:2940351,
	title = {Abolition of mitochondrial substrate-level phosphorylation by itaconic acid produced by LPS-induced Irg1 expression in cells of murine macrophage lineage},
	url = {https://m2.mtmt.hu/api/publication/2940351},
	author = {Németh, Beáta and Dóczi, Judit and Csete, Dániel and Kacsó, Gergely and Ravasz, Dóra and Daniel, Adams and Kiss, Gergely and Nagy, Ádám Miklós and Horváth, Gergő and Tretter, László and Mócsai, Attila and Csépányi-Kömi, Roland and Iordanov, Iordan and Ádám, Veronika and Chinopoulos, Christos},
	doi = {10.1096/fj.15-279398},
	journal-iso = {FASEB J},
	journal = {FASEB JOURNAL},
	volume = {30},
	unique-id = {2940351},
	issn = {0892-6638},
	year = {2016},
	eissn = {1530-6860},
	pages = {286-300},
	orcid-numbers = {Németh, Beáta/0000-0002-2334-9796; Dóczi, Judit/0000-0002-5797-5074; Csete, Dániel/0000-0001-8057-225X; Kacsó, Gergely/0000-0003-0428-3645; Ravasz, Dóra/0000-0002-0510-3282; Nagy, Ádám Miklós/0000-0002-9568-2555; Horváth, Gergő/0000-0001-5386-9509; Tretter, László/0000-0001-5638-2886; Mócsai, Attila/0000-0002-0512-1157; Csépányi-Kömi, Roland/0000-0001-6825-7142; Iordanov, Iordan/0000-0001-8251-5857; Ádám, Veronika/0000-0002-8350-8701; Chinopoulos, Christos/0000-0003-0183-4149}
}

@mastersthesis{MTMT:2955220,
	title = {The role of matrix substrate-level phosphorylation during anoxia},
	url = {https://m2.mtmt.hu/api/publication/2955220},
	author = {Kiss, Gergely},
	doi = {10.14753/SE.2015.1713},
	publisher = {Semmelweis Egyetem},
	unique-id = {2955220},
	year = {2015}
}

@article{MTMT:2594473,
	title = {Measurement of ADP-ATP Exchange in Relation to Mitochondrial Transmembrane Potential and Oxygen Consumption.},
	url = {https://m2.mtmt.hu/api/publication/2594473},
	author = {Chinopoulos, Christos and Kiss, Gergely and Kawamata, H and Starkov, AA},
	doi = {10.1016/B978-0-12-416618-9.00017-0},
	journal-iso = {METHOD ENZYMOL},
	journal = {METHODS IN ENZYMOLOGY},
	volume = {542},
	unique-id = {2594473},
	issn = {0076-6879},
	abstract = {We have previously described a fluorometric method to measure ADP-ATP exchange rates in mitochondria of permeabilized cells, in which several enzymes that consume substantial amounts of ATP and other competing reactions interconverting adenine nucleotides are present. This method relies on recording changes in free extramitochondrial Mg(2+) with the Mg(2+)-sensitive fluorescent indicator Magnesium Green (MgGr), exploiting the differential affinity of ADP and ATP for Mg(2+). In particular, cells are permeabilized with digitonin in the presence of [Formula: see text] and Na3VO4, inhibiting all ATP- and ADP-utilizing reactions but mitochondrial exchange of ATP with ADP catalyzed by the adenine nucleotide translocase. The rate of ATP appearing in the medium upon the addition of ADP to energized mitochondria is then calculated from the rate of change in free extramitochondrial Mg(2+) using standard binding equations. Here, we describe a variant of this method involving an improved calibration step. This step minimizes errors that may be introduced during the conversion of the MgGr signal into free extramitochondrial [Mg(2+)] and ATP. Furthermore, we describe an approach for combining this methodology with the measurement of mitochondrial membrane potential and oxygen consumption in the same sample. The method described herein is useful for the study of malignant cells, which are known to thrive in hypoxic environments and to harbor mitochondria with profound functional alterations.},
	year = {2014},
	eissn = {1557-7988},
	pages = {333-348},
	orcid-numbers = {Chinopoulos, Christos/0000-0003-0183-4149}
}

@article{MTMT:2497374,
	title = {Mitochondrial diaphorases as NAD+ donors to segments of the citric acid cycle that support substrate-level phosphorylation yielding ATP during respiratory inhibition.},
	url = {https://m2.mtmt.hu/api/publication/2497374},
	author = {Kiss, Gergely and Konrád, Csaba and Pour-Ghaz, I and Mansour, JJ and Németh, Beáta and Starkov, AA and Ádám, Veronika and Chinopoulos, Christos},
	doi = {10.1096/fj.13-243030},
	journal-iso = {FASEB J},
	journal = {FASEB JOURNAL},
	volume = {28},
	unique-id = {2497374},
	issn = {0892-6638},
	abstract = {Substrate-level phosphorylation mediated by succinyl-CoA ligase in the mitochondrial matrix produces high-energy phosphates in the absence of oxidative phosphorylation. Furthermore, when the electron transport chain is dysfunctional, provision of succinyl-CoA by the alpha-ketoglutarate dehydrogenase complex (KGDHC) is crucial for maintaining the function of succinyl-CoA ligase yielding ATP, preventing the adenine nucleotide translocase from reversing. We addressed the source of the NAD+ supply for KGDHC under anoxic conditions and inhibition of complex I. Using pharmacologic tools and specific substrates and by examining tissues from pigeon liver exhibiting no diaphorase activity, we showed that mitochondrial diaphorases in the mouse liver contribute up to 81% to the NAD+ pool during respiratory inhibition. Under these conditions, KGDHC's function, essential for the provision of succinyl-CoA to succinyl-CoA ligase, is supported by NAD+ derived from diaphorases. Through this process, diaphorases contribute to the maintenance of substrate-level phosphorylation during respiratory inhibition, which is manifested in the forward operation of adenine nucleotide translocase. Finally, we show that reoxidation of the reducible substrates for the diaphorases is mediated by complex III of the respiratory chain.-Kiss, G., Konrad, C., Pour-Ghaz, I., Mansour, J. J., Nemeth, B., Starkov, A. A., Adam-Vizi, V., Chinopoulos, C. Mitochondrial diaphorases as NAD+ donors to segments of the citric acid cycle that support substrate-level phosphorylation yielding ATP during respiratory inhibition.},
	year = {2014},
	eissn = {1530-6860},
	pages = {1682-1697},
	orcid-numbers = {Németh, Beáta/0000-0002-2334-9796; Ádám, Veronika/0000-0002-8350-8701; Chinopoulos, Christos/0000-0003-0183-4149}
}

@article{MTMT:2528926,
	title = {A reduction in the activity of alpha-ketoglutarate dehydrogenase complex decreases matrix substrate-level phosphorylation and prompts respiration-impaired mitochondria towards extramitochondrial ATP consumption},
	url = {https://m2.mtmt.hu/api/publication/2528926},
	author = {Kiss, Gergely and Konrád, Csaba and Starkov, Anatoly A and Kawamata, Hibiki and Manfredi, Giovanni and Zhang, Steven F and Gibson, Gary E and Beal, M Flint and Ádám, Veronika and Chinopoulos, Christos},
	journal-iso = {J NEUROSCI RES},
	journal = {JOURNAL OF NEUROSCIENCE RESEARCH},
	volume = {91},
	unique-id = {2528926},
	issn = {0360-4012},
	year = {2013},
	eissn = {1097-4547},
	pages = {1099-1100},
	orcid-numbers = {Ádám, Veronika/0000-0002-8350-8701; Chinopoulos, Christos/0000-0003-0183-4149}
}

@article{MTMT:2528925,
	title = {Functional importance of mitochondrial diaphorases in maintaining phosphorylation potential during inhibition of electron transport chain.},
	url = {https://m2.mtmt.hu/api/publication/2528925},
	author = {Kiss, Gergely and Konrád, Csaba and Ádám, Veronika and Chinopoulos, Christos},
	journal-iso = {J NEUROSCI RES},
	journal = {JOURNAL OF NEUROSCIENCE RESEARCH},
	volume = {91},
	unique-id = {2528925},
	issn = {0360-4012},
	year = {2013},
	eissn = {1097-4547},
	pages = {1088-1088},
	orcid-numbers = {Ádám, Veronika/0000-0002-8350-8701; Chinopoulos, Christos/0000-0003-0183-4149}
}

@article{MTMT:2228167,
	title = {The negative impact of alpha-ketoglutarate dehydrogenase complex deficiency on matrix substrate-level phosphorylation},
	url = {https://m2.mtmt.hu/api/publication/2228167},
	author = {Kiss, Gergely and Konrád, Csaba and Dóczi, Judit and Starkov, AA and Kawamata, H and Manfredi, G and Zhang, SF and Gibson, GE and Beal, MF and Ádám, Veronika and Chinopoulos, Christos},
	doi = {10.1096/fj.12-220202},
	journal-iso = {FASEB J},
	journal = {FASEB JOURNAL},
	volume = {27},
	unique-id = {2228167},
	issn = {0892-6638},
	abstract = {A decline in alpha-ketoglutarate dehydrogenase complex (KGDHC) activity has been associated with neurodegeneration. Provision of succinyl-CoA by KGDHC is essential for generation of matrix ATP (or GTP) by substrate-level phosphorylation catalyzed by succinyl-CoA ligase. Here, we demonstrate ATP consumption in respiration-impaired isolated and in situ neuronal somal mitochondria from transgenic mice with a deficiency of either dihydrolipoyl succinyltransferase (DLST) or dihydrolipoyl dehydrogenase (DLD) that exhibit a 20-48% decrease in KGDHC activity. Import of ATP into the mitochondrial matrix of transgenic mice was attributed to a shift in the reversal potential of the adenine nucleotide translocase toward more negative values due to diminished matrix substrate-level phosphorylation, which causes the translocase to reverse prematurely. Immunoreactivity of all three subunits of succinyl-CoA ligase and maximal enzymatic activity were unaffected in transgenic mice as compared to wild-type littermates. Therefore, decreased matrix substrate-level phosphorylation was due to diminished provision of succinyl-CoA. These results were corroborated further by the finding that mitochondria from wild-type mice respiring on substrates supporting substrate-level phosphorylation exhibited approximately 30% higher ADP-ATP exchange rates compared to those obtained from DLST+/- or DLD+/- littermates. We propose that KGDHC-associated pathologies are a consequence of the inability of respiration-impaired mitochondria to rely on "in-house" mitochondrial ATP reserves.-Kiss, G., Konrad, C., Doczi, J., Starkov, A. A., Kawamata, H., Manfredi, G., Zhang, S. F., Gibson, G. E., Beal, M. F., Adam-Vizi, V., Chinopoulos, C. The negative impact of alpha-ketoglutarate dehydrogenase complex deficiency on matrix substrate-level phosphorylation.},
	year = {2013},
	eissn = {1530-6860},
	pages = {2392-2406},
	orcid-numbers = {Dóczi, Judit/0000-0002-5797-5074; Ádám, Veronika/0000-0002-8350-8701; Chinopoulos, Christos/0000-0003-0183-4149}
}

@article{MTMT:2529232,
	title = {Absence of Ca2+-induced mitochondrial permeability transition but presence of bongkrekate-sensitive nucleotide exchange in C. crangon and P. serratus},
	url = {https://m2.mtmt.hu/api/publication/2529232},
	author = {Konrád, Csaba and Kiss, Gergely and Törőcsik, Beáta and Ádám, Veronika and Chinopoulos, Christos},
	doi = {10.1016/j.bbabio.2012.06.325},
	journal-iso = {BBA-BIOENERGETICS},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS},
	volume = {1817},
	unique-id = {2529232},
	issn = {0005-2728},
	year = {2012},
	eissn = {1879-2650},
	pages = {S121-S121},
	orcid-numbers = {Törőcsik, Beáta/0000-0002-9838-3710; Ádám, Veronika/0000-0002-8350-8701; Chinopoulos, Christos/0000-0003-0183-4149}
}