@article{MTMT:34075046,
	title = {Structural and Biochemical Investigation of Selected Pathogenic Mutants of the Human Dihydrolipoamide Dehydrogenase},
	url = {https://m2.mtmt.hu/api/publication/34075046},
	author = {Szabó, Eszter and Nemes-Nikodém, Éva and Vass, Krisztina Rubina and Zámbó, Zsófia Melinda and Zrupko, E. and Törőcsik, Beáta and Ozohanics, Olivér and Nagy, Bálint and Ambrus, Attila},
	doi = {10.3390/ijms241310826},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {34075046},
	issn = {1661-6596},
	abstract = {Clinically relevant disease-causing variants of the human dihydrolipoamide dehydrogenase (hLADH, hE3), a common component of the mitochondrial α-keto acid dehydrogenase complexes, were characterized using a multipronged approach to unravel the molecular pathomechanisms that underlie hLADH deficiency. The G101del and M326V substitutions both reduced the protein stability and triggered the disassembly of the functional/obligate hLADH homodimer and significant FAD losses, which altogether eventually manifested in a virtually undetectable catalytic activity in both cases. The I12T-hLADH variant proved also to be quite unstable, but managed to retain the dimeric enzyme form; the LADH activity, both in the forward and reverse catalytic directions and the affinity for the prosthetic group FAD were both significantly compromised. None of the above three variants lent themselves to an in-depth structural analysis via X-ray crystallography due to inherent protein instability. Crystal structures at 2.89 and 2.44 Å resolutions were determined for the I318T- and I358T-hLADH variants, respectively; structure analysis revealed minor conformational perturbations, which correlated well with the residual LADH activities, in both cases. For the dimer interface variants G426E-, I445M-, and R447G-hLADH, enzyme activities and FAD loss were determined and compared against the previously published structural data. © 2023 by the authors.},
	keywords = {Reactive oxygen species; X-RAY CRYSTALLOGRAPHY; Lipoamide Dehydrogenase; disease-causing mutation; alpha-keto acid dehydrogenase complexes},
	year = {2023},
	eissn = {1422-0067},
	orcid-numbers = {Szabó, Eszter/0000-0002-9634-2771; Vass, Krisztina Rubina/0000-0002-1584-7154; Zámbó, Zsófia Melinda/0000-0001-8657-8556; Törőcsik, Beáta/0000-0002-9838-3710; Ozohanics, Olivér/0000-0002-2705-9921; Nagy, Bálint/0000-0003-3669-7041; Ambrus, Attila/0000-0001-6014-3175}
}

@article{MTMT:32804574,
	title = {Tumor Glucose and Fatty Acid Metabolism in the Context of Anthracycline and Taxane-Based (Neo)Adjuvant Chemotherapy in Breast Carcinomas},
	url = {https://m2.mtmt.hu/api/publication/32804574},
	author = {Tőkés, Anna-Mária and Vári-Kakas, S. and Kulka, Janina and Törőcsik, Beáta},
	doi = {10.3389/fonc.2022.850401},
	journal-iso = {FRONT ONCOL},
	journal = {FRONTIERS IN ONCOLOGY},
	volume = {12},
	unique-id = {32804574},
	issn = {2234-943X},
	year = {2022},
	eissn = {2234-943X},
	orcid-numbers = {Tőkés, Anna-Mária/0000-0002-9581-7536; Kulka, Janina/0000-0001-6498-5943; Törőcsik, Beáta/0000-0002-9838-3710}
}

@article{MTMT:31397038,
	title = {Simple binding of protein kinase A, prior to phosphorylation, allows CFTR anion channels to be opened by nucleotides},
	url = {https://m2.mtmt.hu/api/publication/31397038},
	author = {Mihályi, Csaba and Iordanov, Iordan and Törőcsik, Beáta and Csanády, László},
	doi = {10.1073/pnas.2007910117},
	journal-iso = {P NATL ACAD SCI USA},
	journal = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
	volume = {117},
	unique-id = {31397038},
	issn = {0027-8424},
	year = {2020},
	eissn = {1091-6490},
	pages = {21740-21746},
	orcid-numbers = {Mihályi, Csaba/0000-0001-7536-3066; Iordanov, Iordan/0000-0001-8251-5857; Törőcsik, Beáta/0000-0002-9838-3710; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:30775333,
	title = {Cystic fibrosis drug ivacaftor stimulates CFTR channels at picomolar concentrations},
	url = {https://m2.mtmt.hu/api/publication/30775333},
	author = {Csanády, László and Törőcsik, Beáta},
	doi = {10.7554/eLife.46450},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {8},
	unique-id = {30775333},
	issn = {2050-084X},
	abstract = {The devastating inherited disease cystic fibrosis (CF) is caused by mutations of the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) anion channel. The recent approval of the CFTR potentiator drug ivacaftor (Vx-770) for the treatment of CF patients has marked the advent of causative CF therapy. Currently, thousands of patients are being treated with the drug, and its molecular mechanism of action is under intensive investigation. Here we determine the solubility profile and true stimulatory potency of Vx-770 towards wild-type (WT) and mutant human CFTR channels in cell-free patches of membrane. We find that its aqueous solubility is ~200 fold lower (~60 nanomolar), whereas the potency of its stimulatory effect is >100 fold higher, than reported, and is unexpectedly fully reversible. Strong, but greatly delayed, channel activation by picomolar Vx-770 identifies multiple sequential slow steps in the activation pathway. These findings provide solid guidelines for the design of in vitro studies using Vx-770. © 2019, Csanády and Töröcsik.},
	keywords = {Xenopus; Solubility; cystic fibrosis; molecular biophysics; Structural biology; F508del; VX-770; G551D; potentiator drug},
	year = {2019},
	eissn = {2050-084X},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889; Törőcsik, Beáta/0000-0002-9838-3710}
}

@article{MTMT:30799456,
	title = {Underlying molecular alterations in human dihydrolipoamide dehydrogenase deficiency revealed by structural analyses of disease-causing enzyme variants},
	url = {https://m2.mtmt.hu/api/publication/30799456},
	author = {Szabó, Eszter and Wilk, Piotr and Nagy, Bálint and Zámbó, Zsófia Melinda and Bui, Dávid and Weichsel, Andrzej and Arjunan, Palaniappa and Törőcsik, Beáta and Hubert, Agnes and Furey, William and Montfort, William R and Jordan, Frank and Weiss, Manfred S and Ádám, Veronika and Ambrus, Attila},
	doi = {10.1093/hmg/ddz177},
	journal-iso = {HUM MOL GENET},
	journal = {HUMAN MOLECULAR GENETICS},
	volume = {28},
	unique-id = {30799456},
	issn = {0964-6906},
	abstract = {Human dihydrolipoamide dehydrogenase (hLADH, hE3) deficiency (OMIM# 246900) is an often prematurely lethal genetic disease usually caused by inactive or partially inactive hE3 variants. Here we report the crystal structure of wild-type hE3 at an unprecedented high resolution of 1.75 Å and the structures of six disease-causing hE3 variants at resolutions ranging from 1.44 to 2.34 Å. P453L proved to be the most deleterious substitution in structure as aberrations extensively compromised the active site. The most prevalent G194C-hE3 variant primarily exhibited structural alterations close to the substitution site, whereas the nearby cofactor-binding residues were left unperturbed. The G426E substitution mainly interfered with the local charge distribution introducing dynamics to the substitution site in the dimer interface; G194C and G426E both led to minor structural changes. The R460G, R447G, and I445M substitutions all perturbed a solvent accessible channel, the so-called H+/H2O channel, leading to the active site. Molecular pathomechanisms of enhanced reactive oxygen species (ROS) generation and impaired binding to multienzyme complexes were also addressed according to the structural data for the relevant mutations. In summary, we present here for the first time a comprehensive study that links three-dimensional structures of disease-causing hE3 variants to residual hLADH activities, altered capacities for ROS generation, compromised affinities for multienzyme complexes, and eventually clinical symptoms. Our results may serve as useful starting points for future therapeutic intervention approaches.},
	year = {2019},
	eissn = {1460-2083},
	pages = {3339-3354},
	orcid-numbers = {Szabó, Eszter/0000-0002-9634-2771; Nagy, Bálint/0000-0003-3669-7041; Zámbó, Zsófia Melinda/0000-0001-8657-8556; Bui, Dávid/0000-0003-3726-2031; Törőcsik, Beáta/0000-0002-9838-3710; Ádám, Veronika/0000-0002-8350-8701; Ambrus, Attila/0000-0001-6014-3175}
}

@article{MTMT:30723780,
	title = {Secretagogin expression in the vertebrate brainstem with focus on the noradrenergic system and implications for Alzheimer's disease},
	url = {https://m2.mtmt.hu/api/publication/30723780},
	author = {Zahola, Péter and Hanics, János and Pintér, Panka and Máté, Zoltán and Gáspárdy, Anna and Hevesi, Zsófia and Echevarria, Diego and Adori, Csaba and Barde, Swapnali and Törőcsik, Beáta and Erdélyi, Ferenc and Szabó, Gábor and Wagner, Ludwig and Kovács, Gábor Géza and Hökfelt, Tomas and Harkany, Tibor and Alpár, Alán},
	doi = {10.1007/s00429-019-01886-w},
	journal-iso = {BRAIN STRUCT FUNC},
	journal = {BRAIN STRUCTURE & FUNCTION},
	volume = {224},
	unique-id = {30723780},
	issn = {1863-2653},
	abstract = {Calcium-binding proteins are widely used to distinguish neuronal subsets in the brain. This study focuses on secretagogin, an EF-hand calcium sensor, to identify distinct neuronal populations in the brainstem of several vertebrate species. By using neural tube whole mounts of mouse embryos, we show that secretagogin is already expressed during the early ontogeny of brainstem noradrenaline cells. In adults, secretagogin-expressing neurons typically populate relay centres of special senses and vegetative regulatory centres of the medulla oblongata, pons and midbrain. Notably, secretagogin expression overlapped with the brainstem column of noradrenergic cell bodies, including the locus coeruleus (A6) and the A1, A5 and A7 fields. Secretagogin expression in avian, mouse, rat and human samples showed quasi-equivalent patterns, suggesting conservation throughout vertebrate phylogeny. We found reduced secretagogin expression in locus coeruleus from subjects with Alzheimer's disease, and this reduction paralleled the loss of tyrosine hydroxylase, the enzyme rate limiting noradrenaline synthesis. Residual secretagogin immunoreactivity was confined to small submembrane domains associated with initial aberrant tau phosphorylation. In conclusion, we provide evidence that secretagogin is a useful marker to distinguish neuronal subsets in the brainstem, conserved throughout several species, and its altered expression may reflect cellular dysfunction of locus coeruleus neurons in Alzheimer's disease.},
	keywords = {NOREPINEPHRINE; Locus coeruleus; CALCIUM-BINDING PROTEINS; Alzheimer's disease; Phylogenetic conservation},
	year = {2019},
	eissn = {1863-2661},
	pages = {2061-2078},
	orcid-numbers = {Zahola, Péter/0000-0002-5057-8252; Hanics, János/0000-0003-3305-2440; Gáspárdy, Anna/0000-0002-9698-5128; Hevesi, Zsófia/0000-0002-9341-9892; Törőcsik, Beáta/0000-0002-9838-3710; Kovács, Gábor Géza/0000-0003-3841-5511; Alpár, Alán/0000-0003-4810-0820}
}

@article{MTMT:3407990,
	title = {Crystal structures of the disease-causing D444V mutant and the relevant wild type human dihydrolipoamide dehydrogenase},
	url = {https://m2.mtmt.hu/api/publication/3407990},
	author = {Szabó, Eszter and Mizsei, Réka and Wilk, P and Zámbó, Zsófia Melinda and Törőcsik, Beáta and Weiss, MS and Ádám, Veronika and Ambrus, Attila},
	doi = {10.1016/j.freeradbiomed.2018.06.008},
	journal-iso = {FREE RADICAL BIO MED},
	journal = {FREE RADICAL BIOLOGY AND MEDICINE},
	volume = {124},
	unique-id = {3407990},
	issn = {0891-5849},
	abstract = {We report the crystal structures of the human (dihydro)lipoamide dehydrogenase (hLADH, hE3) and its disease-causing homodimer interface mutant D444V-hE3 at 2.27 and 1.84 Å resolution, respectively. The wild type structure is a unique uncomplexed, unliganded hE3 structure with the true canonical sequence. Based on the structural information a novel molecular pathomechanism is proposed for the impaired catalytic activity and enhanced capacity for reactive oxygen species generation of the pathogenic mutant. The mechanistic model involves a previously much ignored solvent accessible channel leading to the active site that might be perturbed also by other disease-causing homodimer interface substitutions of this enzyme. © 2018 Elsevier Inc.},
	keywords = {Reactive oxygen species; X-RAY CRYSTALLOGRAPHY; protein structure; Lipoamide Dehydrogenase; Pyruvate Dehydrogenase Complex; Pathogenic mutation; E3 deficiency; Alpha-ketoglutarate dehydrogenase complex; Oxidative stress},
	year = {2018},
	eissn = {1873-4596},
	pages = {214-220},
	orcid-numbers = {Szabó, Eszter/0000-0002-9634-2771; Mizsei, Réka/0000-0003-4519-4307; Zámbó, Zsófia Melinda/0000-0001-8657-8556; Törőcsik, Beáta/0000-0002-9838-3710; Ádám, Veronika/0000-0002-8350-8701; Ambrus, Attila/0000-0001-6014-3175}
}

@article{MTMT:3287727,
	title = {Asymmetry of movements in CFTR's two ATP sites during pore opening serves their distinct functions},
	url = {https://m2.mtmt.hu/api/publication/3287727},
	author = {Sorum, Ben and Törőcsik, Beáta and Csanády, László},
	doi = {10.7554/eLife.29013},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {6},
	unique-id = {3287727},
	issn = {2050-084X},
	abstract = {CFTR, the chloride channel mutated in cystic fibrosis (CF) patients, is opened by ATP binding to two cytosolic nucleotide binding domains (NBDs), but pore-domain mutations may also impair gating. ATP-bound NBDs dimerize occluding two nucleotides at interfacial binding sites; one site hydrolyzes ATP, the other is inactive. The pore opens upon tightening, and closes upon disengagement, of the catalytic site following ATP hydrolysis. Extent, timing, and role of non-catalytic-site movements are unknown. Here we exploit equilibrium gating of a hydrolysis-deficient mutant and apply Phi value analysis to compare timing of opening-associated movements at multiple locations, from the cytoplasmic ATP sites to the extracellular surface. Marked asynchrony of motion in the two ATP sites reveals their distinct roles in channel gating. The results clarify the molecular mechanisms of functional cross-talk between canonical and degenerate ATP sites in asymmetric ABC proteins, and of the gating defects caused by two common CF mutations.},
	year = {2017},
	eissn = {2050-084X},
	orcid-numbers = {Sorum, Ben/0000-0001-6742-1094; Törőcsik, Beáta/0000-0002-9838-3710; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:3114546,
	title = {Structural alterations induced by ten disease-causing mutations of human dihydrolipoamide dehydrogenase analyzed by hydrogen/deuterium-exchange mass spectrometry: Implications for the structural basis of E3 deficiency},
	url = {https://m2.mtmt.hu/api/publication/3114546},
	author = {Ambrus, Attila and Wang, J and Mizsei, Réka and Zámbó, Zsófia Melinda and Törőcsik, Beáta and Jordan, F and Ádám, Veronika},
	doi = {10.1016/j.bbadis.2016.08.013},
	journal-iso = {BBA-MOL BASIS DIS},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE},
	volume = {1862},
	unique-id = {3114546},
	issn = {0925-4439},
	abstract = {Pathogenic amino acid substitutions of the common E3 component (hE3) of the human alpha-ketoglutarate dehydrogenase and the pyruvate dehydrogenase complexes lead to severe metabolic diseases (E3 deficiency), which usually manifest themselves in cardiological and/or neurological symptoms and often cause premature death. To date, 14 disease-causing amino acid substitutions of the hE3 component have been reported in the clinical literature. None of the pathogenic protein variants has lent itself to high-resolution structure elucidation by X-ray or NMR. Hence, the structural alterations of the hE3 protein caused by the disease-causing mutations and leading to dysfunction, including the enhanced generation of reactive oxygen species by selected disease-causing variants, could only be speculated. Here we report results of an examination of the effects on the protein structure of ten pathogenic mutations of hE3 using hydrogen/deuterium-exchange mass spectrometry (HDX-MS), a new and state-of-the-art approach of solution structure elucidation. On the basis of the results, putative structural and mechanistic conclusions were drawn regarding the molecular pathogenesis of each disease-causing hE3 mutation addressed in this study. © 2016 Elsevier B.V.},
	keywords = {Mass spectrometry; Dihydrolipoamide dehydrogenase; Hydrogen/deuterium exchange; Pathogenic mutation; E3 deficiency},
	year = {2016},
	eissn = {1879-260X},
	pages = {2098-2109},
	orcid-numbers = {Ambrus, Attila/0000-0001-6014-3175; Mizsei, Réka/0000-0003-4519-4307; Zámbó, Zsófia Melinda/0000-0001-8657-8556; Törőcsik, Beáta/0000-0002-9838-3710; Ádám, Veronika/0000-0002-8350-8701}
}

@article{MTMT:3069984,
	title = {Alterations in voltage-sensing of the mitochondrial permeability transition pore in ANT1-deficient cells},
	url = {https://m2.mtmt.hu/api/publication/3069984},
	author = {Dóczi, Judit and Törőcsik, Beáta and Echaniz-Laguna, A and Mousson, de Camaret B and Starkov, A and Starkova, N and Gál, Anikó and Molnár, Mária Judit and Kawamata, H and Manfredi, G and Ádám, Veronika and Chinopoulos, Christos},
	doi = {10.1038/srep26700},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {6},
	unique-id = {3069984},
	issn = {2045-2322},
	abstract = {The probability of mitochondrial permeability transition (mPT) pore opening is inversely related to the magnitude of the proton electrochemical gradient. The module conferring sensitivity of the pore to this gradient has not been identified. We investigated mPT's voltage-sensing properties elicited by calcimycin or H2O2 in human fibroblasts exhibiting partial or complete lack of ANT1 and in C2C12 myotubes with knocked-down ANT1 expression. mPT onset was assessed by measuring in situ mitochondrial volume using the 'thinness ratio' and the 'cobalt-calcein' technique. De-energization hastened calcimycin-induced swelling in control and partially-expressing ANT1 fibroblasts, but not in cells lacking ANT1, despite greater losses of mitochondrial membrane potential. Matrix Ca(2+) levels measured by X-rhod-1 or mitochondrially-targeted ratiometric biosensor 4mtD3cpv, or ADP-ATP exchange rates did not differ among cell types. ANT1-null fibroblasts were also resistant to H2O2-induced mitochondrial swelling. Permeabilized C2C12 myotubes with knocked-down ANT1 exhibited higher calcium uptake capacity and voltage-thresholds of mPT opening inferred from cytochrome c release, but intact cells showed no differences in calcimycin-induced onset of mPT, irrespective of energization and ANT1 expression, albeit the number of cells undergoing mPT increased less significantly upon chemically-induced hypoxia than control cells. We conclude that ANT1 confers sensitivity of the pore to the electrochemical gradient.},
	year = {2016},
	eissn = {2045-2322},
	orcid-numbers = {Dóczi, Judit/0000-0002-5797-5074; Törőcsik, Beáta/0000-0002-9838-3710; Gál, Anikó/0000-0002-2059-5748; Molnár, Mária Judit/0000-0001-9350-1864; Ádám, Veronika/0000-0002-8350-8701; Chinopoulos, Christos/0000-0003-0183-4149}
}

@article{MTMT:3083629,
	title = {Obligate coupling of CFTR pore opening to tight nucleotide-binding domain dimerization},
	url = {https://m2.mtmt.hu/api/publication/3083629},
	author = {Mihályi, Csaba and Törőcsik, Beáta and Csanády, László},
	doi = {10.7554/eLife.18164},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {5},
	unique-id = {3083629},
	issn = {2050-084X},
	abstract = {In CFTR, the chloride channel mutated in cystic fibrosis (CF) patients, ATP-binding-induced dimerization of two cytosolic nucleotide binding domains (NBDs) opens the pore, and dimer disruption following ATP hydrolysis closes it. Spontaneous openings without ATP are rare in wild-type CFTR, but in certain CF mutants constitute the only gating mechanism, stimulated by ivacaftor, a clinically approved CFTR potentiator. The molecular motions underlying spontaneous gating are unclear. Here we correlate energetic coupling between residues across the dimer interface with spontaneous pore opening/closure in single CFTR channels. We show that spontaneous openings are also strictly coupled to NBD dimerization, which may therefore occur even without ATP. Coordinated NBD/pore movements are therefore intrinsic to CFTR: ATP alters the stability, but not the fundamental structural architecture, of open- and closed-pore conformations. This explains correlated effects of phosphorylation, mutations, and drugs on ATP-driven and spontaneous activity, providing insights for understanding CF mutation and drug mechanisms.},
	year = {2016},
	eissn = {2050-084X},
	orcid-numbers = {Mihályi, Csaba/0000-0001-7536-3066; Törőcsik, Beáta/0000-0002-9838-3710; Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:3262509,
	title = {Crystal structure of the D444V disease-causing mutant of human dihydrolipoamide dehydrogenase},
	url = {https://m2.mtmt.hu/api/publication/3262509},
	author = {Szabó, Eszter and Mizsei, Réka and Zámbó, Zsófia Melinda and Törőcsik, Beáta and Weiss, Manfred S and Ádám, Veronika and Ambrus, Attila},
	doi = {10.1016/j.bbabio.2016.04.337},
	journal-iso = {BBA-BIOENERGETICS},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS},
	volume = {1857},
	unique-id = {3262509},
	issn = {0005-2728},
	year = {2016},
	eissn = {1879-2650},
	pages = {e100},
	orcid-numbers = {Szabó, Eszter/0000-0002-9634-2771; Mizsei, Réka/0000-0003-4519-4307; Zámbó, Zsófia Melinda/0000-0001-8657-8556; Törőcsik, Beáta/0000-0002-9838-3710; Ádám, Veronika/0000-0002-8350-8701; Ambrus, Attila/0000-0001-6014-3175}
}

@article{MTMT:2953634,
	title = {Formation of reactive oxygen species by human and bacterial pyruvate and 2- oxoglutarate dehydrogenase multienzyme complexes reconstituted from recombinant components},
	url = {https://m2.mtmt.hu/api/publication/2953634},
	author = {Ambrus, Attila and Nemeria, NS and Törőcsik, Beáta and Tretter, László and Nilsson, M and Jordan, F and Ádám, Veronika},
	doi = {10.1016/j.freeradbiomed.2015.10.001},
	journal-iso = {FREE RADICAL BIO MED},
	journal = {FREE RADICAL BIOLOGY AND MEDICINE},
	volume = {89},
	unique-id = {2953634},
	issn = {0891-5849},
	year = {2015},
	eissn = {1873-4596},
	pages = {642-650},
	orcid-numbers = {Ambrus, Attila/0000-0001-6014-3175; Törőcsik, Beáta/0000-0002-9838-3710; Tretter, László/0000-0001-5638-2886; Ádám, Veronika/0000-0002-8350-8701}
}

@article{MTMT:2761953,
	title = {Structure-activity analysis of a CFTR channel potentiator: Distinct molecular parts underlie dual gating effects.},
	url = {https://m2.mtmt.hu/api/publication/2761953},
	author = {Csanády, László and Törőcsik, Beáta},
	doi = {10.1085/jgp.201411246},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {144},
	unique-id = {2761953},
	issn = {0022-1295},
	abstract = {The cystic fibrosis (CF) transmembrane conductance regulator (CFTR) is a member of the ATP-binding cassette transporter superfamily that functions as an epithelial chloride channel. Gating of the CFTR ion conduction pore involves a conserved irreversible cyclic mechanism driven by ATP binding and hydrolysis at two cytosolic nucleotide-binding domains (NBDs): formation of an intramolecular NBD dimer that occludes two ATP molecules opens the pore, whereas dimer disruption after ATP hydrolysis closes it. CFTR dysfunction resulting from inherited mutations causes CF. The most common CF mutation, deletion of phenylalanine 508 (DeltaF508), impairs both protein folding and processing and channel gating. Development of DeltaF508 CFTR correctors (to increase cell surface expression) and potentiators (to enhance open probability, Po) is therefore a key focus of CF research. The practical utility of 5-nitro-2-(3-phenylpropylamino)benzoate (NPPB), one of the most efficacious potentiators of DeltaF508 CFTR identified to date, is limited by its pore-blocking side effect. NPPB-mediated stimulation of Po is unique in that it involves modulation of gating transition state stability. Although stabilization by NPPB of the transition state for pore opening enhances both the rate of channel opening and the very slow rate of nonhydrolytic closure, because of CFTR's cyclic gating mechanism, the net effect is Po stimulation. In addition, slowing of ATP hydrolysis by NPPB delays pore closure, further enhancing Po. Here we show that NPPB stimulates gating at a site outside the pore and that these individual actions of NPPB on CFTR are fully attributable to one or the other of its two complementary molecular parts, 3-nitrobenzoate (3NB) and 3-phenylpropylamine (3PP), both of which stimulate Po: the pore-blocking 3NB selectively stabilizes the transition state for opening, whereas the nonblocking 3PP selectively slows the ATP hydrolysis step. Understanding structure-activity relationships of NPPB might prove useful for designing potent, clinically relevant CFTR potentiators.},
	year = {2014},
	eissn = {1540-7748},
	pages = {321-336},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889; Törőcsik, Beáta/0000-0002-9838-3710}
}

@article{MTMT:2496247,
	title = {Catalyst-like Modulation of Transitions States for CFTR Channel Opening and Closing: New Stimulation Strategy Exploits Nonequilibrium Gating},
	url = {https://m2.mtmt.hu/api/publication/2496247},
	author = {Csanády, László and Törőcsik, Beáta},
	doi = {10.1085/jgp.201311089},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {143},
	unique-id = {2496247},
	issn = {0022-1295},
	year = {2014},
	eissn = {1540-7748},
	pages = {269-287},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889; Törőcsik, Beáta/0000-0002-9838-3710}
}

@article{MTMT:2333381,
	title = {Conformational changes in the catalytically inactive nucleotide-binding site of CFTR},
	url = {https://m2.mtmt.hu/api/publication/2333381},
	author = {Csanády, László and Mihályi, Csaba and Szöllősi, András and Törőcsik, Beáta and Vergani, P},
	doi = {10.1085/jgp.201210954},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {142},
	unique-id = {2333381},
	issn = {0022-1295},
	abstract = {A central step in the gating of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel is the association of its two cytosolic nucleotide-binding domains (NBDs) into a head-to-tail dimer, with two nucleotides bound at the interface. Channel opening and closing, respectively, are coupled to formation and disruption of this tight NBD dimer. CFTR is an asymmetric adenosine triphosphate (ATP)-binding cassette protein in which the two interfacial-binding sites (composite sites 1 and 2) are functionally different. During gating, the canonical, catalytically active nucleotide-binding site (site 2) cycles between dimerized prehydrolytic (state O1), dimerized post-hydrolytic (state O2), and dissociated (state C) forms in a preferential C-->O1-->O2-->C sequence. In contrast, the catalytically inactive nucleotide-binding site (site 1) is believed to remain associated, ATP-bound, for several gating cycles. Here, we have examined the possibility of conformational changes in site 1 during gating, by studying gating effects of perturbations in site 1.Previous work showed that channel closure is slowed, both under hydrolytic and nonhydrolytic conditions, by occupancy of site 1 by N6-(2-phenylethyl)-ATP (P-ATP) as well as by the site-1 mutation H1348A (NBD2 signature sequence). Here, we found that P-ATP prolongs wild-type (WT) CFTR burst durations by selectively slowing (>2x) transition O1-->O2 and decreases the nonhydrolytic closing rate (transition O1-->C) of CFTR mutants K1250A ( approximately 4x) and E1371S ( approximately 3x). Mutation H1348A also slowed ( approximately 3x) the O1-->O2 transition in the WT background and decreased the nonhydrolytic closing rate of both K1250A ( approximately 3x) and E1371S ( approximately 3x) background mutants. Neither P-ATP nor the H1348A mutation affected the 1:1 stoichiometry between ATP occlusion and channel burst events characteristic to WT CFTR gating in ATP. The marked effect that different structural perturbations at site 1 have on both steps O1-->C and O1-->O2 suggests that the overall conformational changes that CFTR undergoes upon opening and coincident with hydrolysis at the active site 2 include significant structural rearrangement at site 1.},
	year = {2013},
	eissn = {1540-7748},
	pages = {61-73},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889; Mihályi, Csaba/0000-0001-7536-3066; Szöllősi, András/0000-0002-5570-4609; Törőcsik, Beáta/0000-0002-9838-3710}
}

@article{MTMT:2528949,
	title = {SAL1 modulates sensitivity of heterologously expressed artemia ADP/ATP carrier to bongkrekate in yeast},
	url = {https://m2.mtmt.hu/api/publication/2528949},
	author = {Kucharczyk, Roza and Wysocka-Kapcinska, M and Törőcsik, Beáta and Turiák, Lilla and Tsaprailis, G and David, C L and Hunt, A and Vékey, Károly and Ádám, Veronika and Chinopoulos, Christos},
	journal-iso = {YEAST},
	journal = {YEAST},
	volume = {30},
	unique-id = {2528949},
	issn = {0749-503X},
	year = {2013},
	eissn = {1097-0061},
	pages = {164-164},
	orcid-numbers = {Törőcsik, Beáta/0000-0002-9838-3710; Ádám, Veronika/0000-0002-8350-8701; Chinopoulos, Christos/0000-0003-0183-4149}
}

@article{MTMT:2420731,
	title = {The Suppressor of AAC2 Lethality SAL1 Modulates Sensitivity of Heterologously Expressed Artemia ADP/ATP Carrier to Bongkrekate in Yeast},
	url = {https://m2.mtmt.hu/api/publication/2420731},
	author = {Wysocka-Kapcinska, M and Törőcsik, Beáta and Turiák, Lilla and Tsaprailis, G and David, CL and Hunt, AM and Vékey, Károly and Ádám, Veronika and Kucharczyk, R and Chinopoulos, Christos},
	doi = {10.1371/journal.pone.0074187},
	journal-iso = {PLOS ONE},
	journal = {PLOS ONE},
	volume = {8},
	unique-id = {2420731},
	issn = {1932-6203},
	abstract = {The ADP/ATP carrier protein (AAC) expressed in Artemia franciscana is refractory to bongkrekate. We generated two strains of Saccharomyces cerevisiae where AAC1 and AAC3 were inactivated and the AAC2 isoform was replaced with Artemia AAC containing a hemagglutinin tag (ArAAC-HA). In one of the strains the suppressor of ΔAAC2 lethality, SAL1, was also inactivated but a plasmid coding for yeast AAC2 was included, because the ArAACΔsal1Δ strain was lethal. In both strains ArAAC-HA was expressed and correctly localized to the mitochondria. Peptide sequencing of ArAAC expressed in Artemia and that expressed in the modified yeasts revealed identical amino acid sequences. The isolated mitochondria from both modified strains developed 85% of the membrane potential attained by mitochondria of control strains, and addition of ADP yielded bongkrekate-sensitive depolarizations implying acquired sensitivity of ArAAC-mediated adenine nucleotide exchange to this poison, independent from SAL1. However, growth of ArAAC-expressing yeasts in glycerol-containing media was arrested by bongkrekate only in the presence of SAL1. We conclude that the mitochondrial environment of yeasts relying on respiratory growth conferred sensitivity of ArAAC to bongkrekate in a SAL1-dependent manner. © 2013 Wysocka-Kapcinska et al.},
	year = {2013},
	eissn = {1932-6203},
	orcid-numbers = {Törőcsik, Beáta/0000-0002-9838-3710; 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}
}

@article{MTMT:1980192,
	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/1980192},
	author = {Konrád, Csaba and Kiss, Gergely and Törőcsik, Beáta and Ádám, Veronika and Chinopoulos, Christos},
	doi = {10.1371/journal.pone.0039839},
	journal-iso = {PLOS ONE},
	journal = {PLOS ONE},
	volume = {7},
	unique-id = {1980192},
	issn = {1932-6203},
	year = {2012},
	eissn = {1932-6203},
	orcid-numbers = {Törőcsik, Beáta/0000-0002-9838-3710; Ádám, Veronika/0000-0002-8350-8701; Chinopoulos, Christos/0000-0003-0183-4149}
}

@article{MTMT:1666747,
	title = {Stimulation of reactive oxygen species generation by disease-causing mutations of lipoamide dehydrogenase},
	url = {https://m2.mtmt.hu/api/publication/1666747},
	author = {Ambrus, Attila and Törőcsik, Beáta and Tretter, László and Ozohanics, Olivér and Ádám, Veronika},
	doi = {10.1093/hmg/ddr202},
	journal-iso = {HUM MOL GENET},
	journal = {HUMAN MOLECULAR GENETICS},
	volume = {20},
	unique-id = {1666747},
	issn = {0964-6906},
	keywords = {Humans; Escherichia coli; Mass spectrometry; Chromatography, Gel; hydrogen peroxide; Reactive oxygen species; Circular Dichroism; Dihydrolipoamide dehydrogenase},
	year = {2011},
	eissn = {1460-2083},
	pages = {2984-2995},
	orcid-numbers = {Ambrus, Attila/0000-0001-6014-3175; Törőcsik, Beáta/0000-0002-9838-3710; Tretter, László/0000-0001-5638-2886; Ozohanics, Olivér/0000-0002-2705-9921; Ádám, Veronika/0000-0002-8350-8701}
}

@article{MTMT:1502467,
	title = {Modulation of F0F1-ATP synthase activity by cyclophilin D regulates matrix adenine nucleotide levels},
	url = {https://m2.mtmt.hu/api/publication/1502467},
	author = {Chinopoulos, Christos and Konrád, Csaba and Kiss, Gergely and Metelkin, E and Törőcsik, Beáta and Zhang, SF and Starkov, AA},
	doi = {10.1111/j.1742-4658.2011.08026.x},
	journal-iso = {FEBS J},
	journal = {FEBS JOURNAL},
	volume = {278},
	unique-id = {1502467},
	issn = {1742-464X},
	year = {2011},
	eissn = {1742-4658},
	pages = {1112-1125},
	orcid-numbers = {Chinopoulos, Christos/0000-0003-0183-4149; Törőcsik, Beáta/0000-0002-9838-3710}
}

@article{MTMT:1479724,
	title = {Complex Contribution of Cyclophilin D to Ca2+-induced Permeability Transition in Brain Mitochondria, with Relation to the Bioenergetic State},
	url = {https://m2.mtmt.hu/api/publication/1479724},
	author = {Dóczi, Judit and Turiák, Lilla and Sisa-Vajda, Szilvia and Mándi, Miklós and Törőcsik, Beáta and Gerencsér, Ákos and Kiss, Gergely and Konrád, Csaba and Ádám, Veronika and Chinopoulos, Christos},
	doi = {10.1074/jbc.M110.196600},
	journal-iso = {J BIOL CHEM},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {286},
	unique-id = {1479724},
	issn = {0021-9258},
	year = {2011},
	eissn = {1083-351X},
	pages = {6345-6353},
	orcid-numbers = {Dóczi, Judit/0000-0002-5797-5074; Törőcsik, Beáta/0000-0002-9838-3710; Ádám, Veronika/0000-0002-8350-8701; Chinopoulos, Christos/0000-0003-0183-4149}
}

@article{MTMT:1479725,
	title = {A distinct sequence in the adenine nucleotide translocase from Artemia franciscana embryos is associated with insensitivity to bongkrekate and atypical effects of adenine nucleotides on Ca2+ uptake and sequestration},
	url = {https://m2.mtmt.hu/api/publication/1479725},
	author = {Konrád, Csaba and Kiss, Gergely and Törőcsik, Beáta and Lábár, János and Gerencsér, Ákos and Mándi, Miklós and Ádám, Veronika and Chinopoulos, Christos},
	doi = {10.1111/j.1742-4658.2010.08001.x},
	journal-iso = {FEBS J},
	journal = {FEBS JOURNAL},
	volume = {278},
	unique-id = {1479725},
	issn = {1742-464X},
	year = {2011},
	eissn = {1742-4658},
	pages = {822-836},
	orcid-numbers = {Törőcsik, Beáta/0000-0002-9838-3710; Lábár, János/0000-0002-3944-8350; Ádám, Veronika/0000-0002-8350-8701; Chinopoulos, Christos/0000-0003-0183-4149}
}

@article{MTMT:1327780,
	title = {Forward operation of adenine nucleotide translocase during F0F1-ATPase reversal: critical role of matrix substrate-level phosphorylation},
	url = {https://m2.mtmt.hu/api/publication/1327780},
	author = {Chinopoulos, Christos and Gerencsér, Ákos and Mándi, Miklós and Mathe, K and Törőcsik, Beáta and Dóczi, Judit and Turiák, Lilla and Kiss, Gergely and Konrád, Csaba and Sisa-Vajda, Szilvia and Vereczki, Viktória and Oh, RJ and Ádám, Veronika},
	doi = {10.1096/fj.09-149898},
	journal-iso = {FASEB J},
	journal = {FASEB JOURNAL},
	volume = {24},
	unique-id = {1327780},
	issn = {0892-6638},
	keywords = {Oxygen Consumption; Animals; Male; PHOSPHORYLATION; RABBITS; NEURONS; RATS; ARTICLE; Rats, Sprague-Dawley; priority journal; Cell Membrane; Mitochondria; nonhuman; animal tissue; animal cell; Cercopithecus aethiops; COS Cells; THERMODYNAMICS; Rabbit; Adenosine Triphosphate; MITOCHONDRIAL RESPIRATION; enzyme phosphorylation; liver mitochondrion; potassium channel; enzyme substrate; BIOLUMINESCENCE; enzyme analysis; computer model; Proton-Translocating ATPases; Bioenergetics; mitochondrial membrane potential; Membrane Potential, Mitochondrial; adenine nucleotide carrier; Mitochondrial ADP, ATP Translocases; adenine nucleotide translocase; proton transporting adenosine triphosphate synthase; SUCLA2; ATP synthasome; Systems biology of mitochondria; rat},
	year = {2010},
	eissn = {1530-6860},
	pages = {2405-2416},
	orcid-numbers = {Chinopoulos, Christos/0000-0003-0183-4149; Törőcsik, Beáta/0000-0002-9838-3710; Dóczi, Judit/0000-0002-5797-5074; Ádám, Veronika/0000-0002-8350-8701}
}

@article{MTMT:1404329,
	title = {Mitochondria from Artemia franciscana embryos exhibit a truncated form of ant, associated with atypical effects of its ligands on Ca2+ uptake capacity and unique morphology of matrix Ca2+ precipitates},
	url = {https://m2.mtmt.hu/api/publication/1404329},
	author = {Konrád, Csaba and Kiss, Gergely and Törőcsik, Beáta and Lábár, János and Gerencser, AA and Mándi, Miklós and Ádám, Veronika and Chinopoulos, Christos},
	doi = {10.1016/j.bbabio.2010.04.426},
	journal-iso = {BBA-BIOENERGETICS},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS},
	volume = {1797},
	unique-id = {1404329},
	issn = {0005-2728},
	year = {2010},
	eissn = {1879-2650},
	pages = {142-143},
	orcid-numbers = {Törőcsik, Beáta/0000-0002-9838-3710; Lábár, János/0000-0002-3944-8350; Ádám, Veronika/0000-0002-8350-8701; Chinopoulos, Christos/0000-0003-0183-4149}
}

@article{MTMT:1264449,
	title = {Refolding of the human dihydrolipoamide dehydrogenase},
	url = {https://m2.mtmt.hu/api/publication/1264449},
	author = {Ambrus, Attila and Törőcsik, Beáta and Ádám, Veronika},
	doi = {10.1016/j.bej.2009.03.004},
	journal-iso = {BIOCHEM ENG J},
	journal = {BIOCHEMICAL ENGINEERING JOURNAL},
	volume = {45},
	unique-id = {1264449},
	issn = {1369-703X},
	year = {2009},
	eissn = {1873-295X},
	pages = {120-125},
	orcid-numbers = {Ambrus, Attila/0000-0001-6014-3175; Törőcsik, Beáta/0000-0002-9838-3710; Ádám, Veronika/0000-0002-8350-8701}
}

@article{MTMT:244260,
	title = {Periplasmic cold expression and one-step purification of human dihydrolipoamide dehydrogenase},
	url = {https://m2.mtmt.hu/api/publication/244260},
	author = {Ambrus, Attila and Törőcsik, Beáta and Ádám, Veronika},
	doi = {10.1016/j.pep.2008.09.009},
	journal-iso = {PROTEIN EXPRES PURIF},
	journal = {PROTEIN EXPRESSION AND PURIFICATION},
	volume = {63},
	unique-id = {244260},
	issn = {1046-5928},
	abstract = {Dihydrolipoamide dehydrogenase (LADH) is a FAD-linked subunit of 
		alpha-ketoglutarate, pyruvate and branched-chain amino acid 
		dehydrogenases and the glycine cleavage system. As an 
		oxidoreductase it transfers electrons from the dihydrolipoic 
		acid prosthetic group to the NAD(+) cofactor via its FAD center. 
		Besides its physiological function it is capable of generating 
		harmful reactive oxygen species (ROS) in pathological settings 
		therefore it is implicated in neurodegeneration, ischemia-
		reperfusion, cancer and several other disorders. Pathological 
		mutants of the enzyme cause severe, sometimes lethal syndromes 
		like hypotonia, metabolic acidosis or inefficiency in 
		development. Recently it has been revealed that LADH is a 
		moonlighting protease when specific mutations in the 
		dimerization surface destabilize the functional homodimer and 
		expose a serine-protease-like catalytic dyad. As the basis of 
		versatile functions of LADH is far from elucidation, there is a 
		constant need for a pure and functional enzyme product for 
		investigations. Several studies used recombinant human LADH 
		before, however, it was generated by more complicated and/or 
		physiologically less compatible protocols than reported here; 
		most papers on functional and structural studies do not even 
		report detailed protocols and characteristics (most importantly 
		the purity) of their protein products. Here we describe the 
		details of an optimized, easy-to-use periplasmic expression and 
		one-step purification protocol for obtaining a highly pure, 
		active and authentic (tag-cleaved) enzyme with the 
		characterization of the protein product. The purified LADH can 
		be used in biophysical and structural studies while the 
		published protocol is easily convertible to a protein labeling 
		procedure. (c) 2008 Elsevier Inc. All rights reserved.},
	year = {2009},
	eissn = {1096-0279},
	pages = {50-57},
	orcid-numbers = {Ambrus, Attila/0000-0001-6014-3175; Törőcsik, Beáta/0000-0002-9838-3710; Ádám, Veronika/0000-0002-8350-8701}
}

@article{MTMT:1502468,
	title = {Four Ca2+ Ions Activate TRPM2 Channels by Binding in Deep Crevices near the Pore but Intracellularly of the Gate},
	url = {https://m2.mtmt.hu/api/publication/1502468},
	author = {Csanády, László and Törőcsik, Beáta},
	doi = {10.1085/jgp.200810109},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {133},
	unique-id = {1502468},
	issn = {0022-1295},
	year = {2009},
	eissn = {1540-7748},
	pages = {189-203},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889; Törőcsik, Beáta/0000-0002-9838-3710}
}

@article{MTMT:1131095,
	title = {Mitochondrial swelling measurement in situ by optimized spatial filtering: Astrocyte-neuron differences},
	url = {https://m2.mtmt.hu/api/publication/1131095},
	author = {Gerencsér, Ákos and Dóczi, Judit and Törőcsik, Beáta and Bossy, B and Bossy-Wetzel, E and Ádám, Veronika},
	doi = {10.1529/biophysj.107.118620},
	journal-iso = {BIOPHYS J},
	journal = {BIOPHYSICAL JOURNAL},
	volume = {95},
	unique-id = {1131095},
	issn = {0006-3495},
	year = {2008},
	eissn = {1542-0086},
	pages = {2583-2598},
	orcid-numbers = {Dóczi, Judit/0000-0002-5797-5074; Törőcsik, Beáta/0000-0002-9838-3710; Ádám, Veronika/0000-0002-8350-8701}
}

@article{MTMT:1428260,
	title = {Role of phospholipase C-gamma in NGF-stimulated differentiation and gene induction},
	url = {https://m2.mtmt.hu/api/publication/1428260},
	author = {Feketéné Kiss, Katalin and Salamon, S and Törőcsik, Beáta and Szeberényi, József},
	doi = {10.1556/ABiol.57.2006.2.2},
	journal-iso = {ACTA BIOL HUNG},
	journal = {ACTA BIOLOGICA HUNGARICA (1983-2018)},
	volume = {57},
	unique-id = {1428260},
	issn = {0236-5383},
	abstract = {The PC12 phaeochromocytoma cell line provides a useful model to study nerve growth factor-induced neuronal differentiation. The central signaling route of this process is mediated by the Ras-dependent extracellular signal-regulated kinase cascade. However, Ras-independent pathways are also stimulated by nerve growth factor and may contribute to differentiation signaling. One mediator for Ras-independent signal transduction in PC12 cells is phospholipase C-gamma that generates the second messengers diacylglycerol and inositol- trisphosphate. To probe the possible involvement of this enzyme in nerve growth factor-promoted differentiation, we used the phospholipase C inhibitor U73122 and the inositol-trisphosphatereceptor inhibitor Xestospongin C. Our results show that both chemicals block nerve growth factor-promoted neurite out-growth, but the blockage of phospholipase C does not inhibit nerve growth factor-induced expression of c-fos, zif268 and transin genes. In addition, induction of these genes by nerve growth factor plus dibutyryl-cAMP is comparable in wild-type PC12 cells as well as in cells in which both Ras- and phospholipase C-gamma-mediated pathways are inhibited. The phospholipase C-gamma pathway thus belongs to those nerve growth factor receptor-originated signaling routes that contribute to the biological response of PC12 cells to nerve growth factor, but its gene activating potential does not have a major role in its neuritogenic effect.},
	year = {2006},
	eissn = {1588-256X},
	pages = {147-155},
	orcid-numbers = {Törőcsik, Beáta/0000-0002-9838-3710}
}

@article{MTMT:1030894,
	title = {Impaired regulation of pH homeostasis by oxidative stress in rat brain capillary endothelial cells},
	url = {https://m2.mtmt.hu/api/publication/1030894},
	author = {Sipos, Ildikó and Törőcsik, Beáta and Tretter, László and Ádám, Veronika},
	doi = {10.1007/s10571-004-1379-6},
	journal-iso = {CELL MOL NEUROBIOL},
	journal = {CELLULAR AND MOLECULAR NEUROBIOLOGY},
	volume = {25},
	unique-id = {1030894},
	issn = {0272-4340},
	year = {2005},
	eissn = {1573-6830},
	pages = {141-151},
	orcid-numbers = {Sipos, Ildikó/0000-0003-2861-1439; Törőcsik, Beáta/0000-0002-9838-3710; Tretter, László/0000-0001-5638-2886; Ádám, Veronika/0000-0002-8350-8701}
}

@article{MTMT:1586978,
	title = {Newcastle disease virus-induced apoptosis in PC12 pheochromocytoma cells},
	url = {https://m2.mtmt.hu/api/publication/1586978},
	author = {Szeberényi, József and Fábián, Zsolt and Törőcsik, Beáta and Feketéné Kiss, Katalin and Csatáry, L. K.},
	doi = {10.1097/00045391-200307000-00008},
	journal-iso = {AM J THER},
	journal = {AMERICAN JOURNAL OF THERAPEUTICS},
	volume = {10},
	unique-id = {1586978},
	issn = {1075-2765},
	year = {2003},
	eissn = {1536-3686},
	pages = {282-288},
	orcid-numbers = {Törőcsik, Beáta/0000-0002-9838-3710}
}

@article{MTMT:1502471,
	title = {Blue-white selection step enhances the yield of SAGE concatemers},
	url = {https://m2.mtmt.hu/api/publication/1502471},
	author = {Angelastro, JM and Ryu, EJ and Törőcsik, Beáta and Fiske, BK and Greene, LA},
	doi = {10.2144/02323bm02},
	journal-iso = {BIOTECHNIQUES},
	journal = {BIOTECHNIQUES},
	volume = {32},
	unique-id = {1502471},
	issn = {0736-6205},
	year = {2002},
	eissn = {1940-9818},
	pages = {484, 486},
	orcid-numbers = {Törőcsik, Beáta/0000-0002-9838-3710}
}

@article{MTMT:1502469,
	title = {Nerve growth factor selectively regulates expression of transcripts encoding ribosomal proteins},
	url = {https://m2.mtmt.hu/api/publication/1502469},
	author = {Angelastro, JM and Törőcsik, Beáta and Greene, LA},
	doi = {10.1186/1471-2202-3-3},
	journal-iso = {BMC NEUROSCI},
	journal = {BMC NEUROSCIENCE},
	volume = {3},
	unique-id = {1502469},
	issn = {1471-2202},
	year = {2002},
	eissn = {1471-2202},
	orcid-numbers = {Törőcsik, Beáta/0000-0002-9838-3710}
}

@article{MTMT:1502470,
	title = {The basic region and leucine zipper transcription factor MafK is a new nerve growth factor-responsive immediate early gene that regulates neurite outgrowth},
	url = {https://m2.mtmt.hu/api/publication/1502470},
	author = {Törőcsik, Beáta and Angelastro, JM and Greene, LA},
	journal-iso = {J NEUROSCI},
	journal = {JOURNAL OF NEUROSCIENCE},
	volume = {22},
	unique-id = {1502470},
	issn = {0270-6474},
	year = {2002},
	eissn = {1529-2401},
	pages = {8971-8980},
	orcid-numbers = {Törőcsik, Beáta/0000-0002-9838-3710}
}

@article{MTMT:1502472,
	title = {Induction of apoptosis by a Newcastle disease virus vaccine (MTH-68/H) in PC12 rat phaeochromocytoma cells},
	url = {https://m2.mtmt.hu/api/publication/1502472},
	author = {Fábián, Zsolt and Törőcsik, Beáta and Feketéné Kiss, Katalin and Csatary, LK and Bodey, B and Tigyi, József and Csatary, C and Szeberényi, József},
	journal-iso = {ANTICANCER RES},
	journal = {ANTICANCER RESEARCH},
	volume = {21},
	unique-id = {1502472},
	issn = {0250-7005},
	year = {2001},
	eissn = {1791-7530},
	pages = {125-135},
	orcid-numbers = {Törőcsik, Beáta/0000-0002-9838-3710}
}

@article{MTMT:1427998,
	title = {Regulation of activator protein-1-DNA binding activity by opioid peptides in estrogen-sensitive cells of rat hypothalamus and uterus},
	url = {https://m2.mtmt.hu/api/publication/1427998},
	author = {Oszter, Angéla and Törőcsik, Beáta and Vértes, Zsuzsanna and Környei, József László and Kovács, Kálmán András and Vértes, Marietta},
	doi = {10.1016/S0014-2999(00)00214-4},
	journal-iso = {EUR J PHARMACOL},
	journal = {EUROPEAN JOURNAL OF PHARMACOLOGY},
	volume = {395},
	unique-id = {1427998},
	issn = {0014-2999},
	year = {2000},
	eissn = {1879-0712},
	pages = {103-106},
	orcid-numbers = {Törőcsik, Beáta/0000-0002-9838-3710}
}

@article{MTMT:1427993,
	title = {Antiestrogenic effect of opioid peptides in rat uterus.},
	url = {https://m2.mtmt.hu/api/publication/1427993},
	author = {Oszter, Angéla and Vértes, Zsuzsanna and Törőcsik, Beáta and Környei, József László and Kovács, Kálmán András and Vértes, Marietta},
	doi = {10.1016/S0960-0760(00)00085-6},
	journal-iso = {J STEROID BIOCHEM MOL BIOL},
	journal = {JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY},
	volume = {74},
	unique-id = {1427993},
	issn = {0960-0760},
	year = {2000},
	eissn = {1879-1220},
	pages = {25-32},
	orcid-numbers = {Törőcsik, Beáta/0000-0002-9838-3710}
}

@article{MTMT:1428299,
	title = {Anisomycin uses multiple mechanisms to stimulate mitogen-activated protein kinases and gene expression and to inhibit neuronal differentiation in PC12 phaeochromocytoma cells},
	url = {https://m2.mtmt.hu/api/publication/1428299},
	author = {Törőcsik, Beáta and Szeberényi, József},
	doi = {10.1046/j.1460-9568.2000.00933.x},
	journal-iso = {EUR J NEUROSCI},
	journal = {EUROPEAN JOURNAL OF NEUROSCIENCE},
	volume = {12},
	unique-id = {1428299},
	issn = {0953-816X},
	abstract = {Treatment of PC12 cells with nerve growth factor (NGF) stimulates extracellular signal-regulated kinases (ERKs), as well as stress-activated c-Jun N-terminal kinases (JNKs) and p38 kinase, and induces neuronal differentiation. While the pivotal role of ERKs in NGF-induced morphological differentiation is well established, the contribution of JNK- and p38-pathways is less clear. The role of the JNK- and p38-pathway in PC12 cells was analysed by using anisomycin, a protein synthesis inhibitor that activates JNKs and p38. Non-toxic concentrations of anisomycin were found to stimulate these enzyme activities as well as the expression of the early response genes c-jun, c-fos and zif268, and to inhibit NGF-induced neurite formation. These effects of anisomycin appear to be mediated by the generation of reactive oxygen species (ROS), which in turn act through both TrkA/Ras-dependent and -independent signalling pathways. In addition, cross-talk between the p38- and ERK-pathways appears to play a role in the action of anisomycin.},
	year = {2000},
	eissn = {1460-9568},
	pages = {527-532},
	orcid-numbers = {Törőcsik, Beáta/0000-0002-9838-3710}
}

@article{MTMT:1428298,
	title = {Anisomycin affects both pro- and antiapoptotic mechanisms in PC12 cells},
	url = {https://m2.mtmt.hu/api/publication/1428298},
	author = {Törőcsik, Beáta and Szeberényi, József},
	doi = {10.1006/bbrc.2000.3836},
	journal-iso = {BIOCHEM BIOPH RES CO},
	journal = {BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS},
	volume = {278},
	unique-id = {1428298},
	issn = {0006-291X},
	abstract = {Survival and differentiation of PC12 cells depend on the proper balance between the activities of several mitogen-activated protein kinase (MAPK) pathways. We have previously shown that low, nontoxic doses of anisomycin stimulated these MAPKs as well. as the expression of several early-response genes and inhibited NC;F-induced neurite formation. In the present work we show that protein synthesis-inhibiting concentrations of anisomycin, in contrast, cause apoptosis of PC12 cells. To try to characterize the apoptosis-inducing mechanisms of anisomycin we compared the signaling effects of subinhibitory and inhibitory drug concentrations. Anisomycin in a nontoxic dosis activates the same MAPK pathways and early-response genes as in protein synthesis inhibiting concentrations. In contrast, while the subinhibitory anisomycin treatment stimulates Akt and induces Bcl-2, two anti-apoptotic proteins, the translation-inhibiting concentration of the drug prevents these survival-promoting biochemical events. Anisomycin thus triggers both pro- and anti-apoptotic processes in PC12 cells; stimulation of stress-responsive MAPK cascades is not sufficient to mediate apoptotic signaling: the inhibition of key antiapoptotic proteins appears to be more important for PC12 cell death by anisomycin treatment. (C) 2000 Academic Press.},
	year = {2000},
	eissn = {1090-2104},
	pages = {550-556},
	orcid-numbers = {Törőcsik, Beáta/0000-0002-9838-3710}
}

@article{MTMT:1339176,
	title = {Beneficial treatment of patients with advanced cancer using a Newcastle disease virus vaccine (MTH-68/H)},
	url = {https://m2.mtmt.hu/api/publication/1339176},
	author = {Csatary, LK and Moss, RW and Beuth, J and Törőcsik, Beáta and Szeberényi, József and Bakács, Tibor},
	journal-iso = {ANTICANCER RES},
	journal = {ANTICANCER RESEARCH},
	volume = {19},
	unique-id = {1339176},
	issn = {0250-7005},
	abstract = {Newcastle Disease Virus Vaccine (MTH-68/H) was administered to patients suffering from advanced neoplastic diseases after non-efficient tumor-destructive treatment. Case reports of selected patients suggest promising effects of this treatment. A prospectively-randomized clinical study (phase III; in accordance with Good Clinical Practice, GCP) was proposed to confirm these results and is currently under consideration.},
	year = {1999},
	eissn = {1791-7530},
	pages = {635-638},
	orcid-numbers = {Törőcsik, Beáta/0000-0002-9838-3710}
}