@article{MTMT:34722791,
	title = {A synthetic flavonoid derivate in the plasma membrane transforms the voltage‐clamp fluorometry signal of CiHv1},
	url = {https://m2.mtmt.hu/api/publication/34722791},
	author = {Pethő, Zoltán Dénes and Pajtás, Dávid and Piga, Martina and Magyar, Zsuzsanna Édua and Zákány, Florina and Kovács, Tamás and Zidar, Nace and Panyi, György and Varga, Zoltán and Papp, Ferenc},
	doi = {10.1111/febs.17105},
	journal-iso = {FEBS J},
	journal = {FEBS JOURNAL},
	unique-id = {34722791},
	issn = {1742-464X},
	abstract = {Voltage‐clamp fluorometry (VCF) enables the study of voltage‐sensitive proteins through fluorescent labeling accompanied by ionic current measurements for voltage‐gated ion channels. The heterogeneity of the fluorescent signal represents a significant challenge in VCF. The VCF signal depends on where the cysteine mutation is incorporated, making it difficult to compare data among different mutations and different studies and standardize their interpretation. We have recently shown that the VCF signal originates from quenching amino acids in the vicinity of the attached fluorophores, together with the effect of the lipid microenvironment. Based on these, we performed experiments to test the hypothesis that the VCF signal could be altered by amphiphilic quenching molecules in the cell membrane. Here we show that a phenylalanine‐conjugated flavonoid (4‐oxo‐2‐phenyl‐4H‐chromene‐7‐yl)‐phenylalanine, (later Oxophench) has potent effects on the VCF signals of the Ciona intestinalis H V 1 (CiHv1) proton channel. Using spectrofluorimetry, we showed that Oxophench quenches TAMRA (5(6)‐carboxytetramethylrhodamine‐(methane thiosulfonate)) fluorescence. Moreover, Oxophench reduces the baseline fluorescence in oocytes and incorporates into the cell membrane while reducing the membrane fluidity of HEK293 cells. Our model calculations confirmed that Oxophench, a potent membrane‐bound quencher, modifies the VCF signal during conformational changes. These results support our previously published model of VCF signal generation and point out that a change in the VCF signal may not necessarily indicate an altered conformational transition of the investigated protein.},
	year = {2024},
	eissn = {1742-4658},
	orcid-numbers = {Piga, Martina/0009-0006-8549-3386; Kovács, Tamás/0000-0002-1084-9847; Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:33398474,
	title = {Mapping the functional expression of auxiliary subunits of KCa1.1 in glioblastoma},
	url = {https://m2.mtmt.hu/api/publication/33398474},
	author = {Fehér, Ádám and Pethő, Zoltán Dénes and Szántó, Gábor Tibor and Klekner, Álmos and Tajti, Gábor and Batta, Gyula Gábor (Ifj.) and Hortobágyi, Tibor and Varga, Zoltán and Schwab, Albrecht and Panyi, György},
	doi = {10.1038/s41598-022-26196-w},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {12},
	unique-id = {33398474},
	issn = {2045-2322},
	abstract = {Glioblastoma (GBM) is the most aggressive glial tumor, where ion channels, including K Ca 1.1, are candidates for new therapeutic options. Since the auxiliary subunits linked to K Ca 1.1 in GBM are largely unknown we used electrophysiology combined with pharmacology and gene silencing to address the functional expression of K Ca 1.1/ β subunits complexes in both primary tumor cells and in the glioblastoma cell line U-87 MG. The pattern of the sensitivity (activation/inhibition) of the whole-cell currents to paxilline, lithocholic acid, arachidonic acid, and iberiotoxin; the presence of inactivation of the whole-cell current along with the loss of the outward rectification upon exposure to the reducing agent DTT collectively argue that K Ca 1.1/β3 complex is expressed in U-87 MG. Similar results were found using human primary glioblastoma cells isolated from patient samples. Silencing the β3 subunit expression inhibited carbachol-induced Ca 2+ transients in U-87 MG thereby indicating the role of the K Ca 1.1/β3 in the Ca 2+ signaling of glioblastoma cells. Functional expression of the K Ca 1.1/β3 complex, on the other hand, lacks cell cycle dependence. We suggest that the K Ca 1.1/β3 complex may have diagnostic and therapeutic potential in glioblastoma in the future.},
	year = {2022},
	eissn = {2045-2322},
	orcid-numbers = {Batta, Gyula Gábor (Ifj.)/0000-0001-8735-6920; Hortobágyi, Tibor/0000-0001-5732-7942; Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:33209098,
	title = {Multiple mechanisms contribute to fluorometry signals from the voltage-gated proton channel},
	url = {https://m2.mtmt.hu/api/publication/33209098},
	author = {Papp, Ferenc and Toombes, Gilman E. S. and Pethő, Zoltán Dénes and Bagosi, Adrienn and Fehér, Ádám and Almássy, János and Borrego Terrazas, Jesus Angel and Kuki, Ákos and Kéki, Sándor and Panyi, György and Varga, Zoltán},
	doi = {10.1038/s42003-022-04065-6},
	journal-iso = {COMMUN BIOL},
	journal = {COMMUNICATIONS BIOLOGY},
	volume = {5},
	unique-id = {33209098},
	abstract = {Voltage-clamp fluorometry (VCF) supplies information about the conformational changes of voltage-gated proteins. Changes in the fluorescence intensity of the dye attached to a part of the protein that undergoes a conformational rearrangement upon the alteration of the membrane potential by electrodes constitute the signal. The VCF signal is generated by quenching and dequenching of the fluorescence as the dye traverses various local environments. Here we studied the VCF signal generation, using the Hv1 voltage-gated proton channel as a tool, which shares a similar voltage-sensor structure with voltage-gated ion channels but lacks an ion-conducting pore. Using mutagenesis and lipids added to the extracellular solution we found that the signal is generated by the combined effects of lipids during movement of the dye relative to the plane of the membrane and by quenching amino acids. Our 3-state model recapitulates the VCF signals of the various mutants and is compatible with the accepted model of two major voltage-sensor movements.},
	year = {2022},
	eissn = {2399-3642},
	orcid-numbers = {Toombes, Gilman E. S./0000-0001-8346-1790; Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:32812792,
	title = {Multiple mechanisms contribute to fluorometry signals from the voltage-gated proton channel},
	url = {https://m2.mtmt.hu/api/publication/32812792},
	author = {Papp, Ferenc and Toombes, Gilman E. and Pethő, Zoltán Dénes and Bagosi, Adrienn and Fehér, Ádám and Almássy, János and Kuki, Ákos and Kéki, Sándor and Panyi, György and Varga, Zoltán},
	doi = {10.1016/j.bpj.2021.11.1481},
	journal-iso = {BIOPHYS J},
	journal = {BIOPHYSICAL JOURNAL},
	volume = {121},
	unique-id = {32812792},
	issn = {0006-3495},
	year = {2022},
	eissn = {1542-0086},
	pages = {247A-247A},
	orcid-numbers = {Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:32080243,
	title = {Effect of E2 and long control region polymorphisms on disease severity in human papillomavirus type 11 mediated mucosal disease: Protein modelling and functional analysis},
	url = {https://m2.mtmt.hu/api/publication/32080243},
	author = {Nagy, Zsófia and Pethő, Zoltán Dénes and Kardos, Gábor and Major, Tamás and Szűcs, Attila and Szarka, Krisztina Zsuzsanna},
	doi = {10.1016/j.meegid.2021.104948},
	journal-iso = {INFECT GENET EVOL},
	journal = {INFECTION GENETICS AND EVOLUTION},
	volume = {93},
	unique-id = {32080243},
	issn = {1567-1348},
	abstract = {Interaction of the long control region (LCR) and the E2 protein of HPV11s was studied by in silico modelling and in vitro functional analysis.
		
		Genomes of HPV11s from fifteen (six known and nine novel) patients (two solitary papillomas, eleven respiratory papillomatoses of different severity, one condyloma acuminatum and one cervical atypia) were sequenced; E2 polymorphisms were analysed in silico by protein modelling. E2 and LCR variants were cloned into pcDNA3.1+ expression vector and into pALuc reporter vector, respectively, transfected to HEp2 cells alone or in different combinations and the luciferase activity was measured.
		
		In the E2, the ubiquitous polymorphism K308R caused stronger binding between the dimers but did not alter DNA binding; E2s with this polymorphism were significantly less efficient than the reference in promoting LCR activity. The unique polymorphism Q86K changed the negative surface charge of E2 (Q86) to positive (K86). The unique polymorphisms S245F and N247T in the hinge region disrupt a probable phosphorylation site in a RXXS motif targeted by protein kinase A and B, but do not affect directly the amino acids critical to nuclear transport. Both unique patterns partly restored the LCR activating potential disrupted by K308R. A unique E2/E4 ORF with a 58-bp deletion leading to a frameshift and an early stop codon resulted in a practically nonfunctional E2, and was associated with a papillomatosis with dysplasia.
		
		When testing existing LCR-E2 combinations, LCR with intrinsically lower enhancer capacity was only marginally activated by its E2 (R308 and the deletion mutant), and did not significantly exceed the activity of the reference LCR without E2. Combined with more potent LCRs associated with more severe disease, the activity was significantly higher, but still significantly lower than LCRs with reference E2.
		
		In summary, LCR-E2 interaction determined by their polymorphisms may explain, at least partly, differences in disease severity.},
	keywords = {Long Control Region; Recurrent respiratory papillomatosis; Low-risk human papillomavirus; Genome polymorphisms; Transactivating potential},
	year = {2021},
	eissn = {1567-7257}
}

@article{MTMT:31878487,
	title = {Effects of one-year tofacitinib therapy on bone metabolism in rheumatoid arthritis},
	url = {https://m2.mtmt.hu/api/publication/31878487},
	author = {Hamar, Attila and Szekanecz, Zoltán and Karancsiné Pusztai, Anita and Czókolyová, Monika and Végh, E. and Pethő, Zoltán Dénes and Bodnár, Nóra and Gulyás, Katalin and Horváth, Á. and Soós, B. and Bodoki, Levente and Bhattoa Harjit, Pál and Nagy, Gábor and Tajti, Gábor and Panyi, György and Szekanecz, Éva and Domján, A. and Hodosi, K. and Szántó, Sándor Zoltán and Szűcs, Gabriella and Szamosi, Szilvia},
	doi = {10.1007/s00198-021-05871-0},
	journal-iso = {OSTEOPOROSIS INT},
	journal = {OSTEOPOROSIS INTERNATIONAL},
	volume = {32},
	unique-id = {31878487},
	issn = {0937-941X},
	year = {2021},
	eissn = {1433-2965},
	pages = {1621-1629},
	orcid-numbers = {Bhattoa Harjit, Pál/0000-0002-4909-0065; Nagy, Gábor/0000-0002-2943-2750; Panyi, György/0000-0001-6227-3301; Szántó, Sándor Zoltán/0000-0001-5030-6292}
}

@article{MTMT:30660660,
	title = {The Origin of the Voltage Clamp Fluorometry Signal in Ci-Hvl Proton Channel},
	url = {https://m2.mtmt.hu/api/publication/30660660},
	author = {Pethő, Zoltán Dénes and Bagosi, Adrienn and Varga, Zoltán and Panyi, György and Papp, Ferenc},
	doi = {10.1016/j.bpj.2018.11.1334},
	journal-iso = {BIOPHYS J},
	journal = {BIOPHYSICAL JOURNAL},
	volume = {116},
	unique-id = {30660660},
	issn = {0006-3495},
	year = {2019},
	eissn = {1542-0086},
	pages = {243A-243A},
	orcid-numbers = {Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:30530360,
	title = {The Role of TRP Channels in the Metastatic Cascade},
	url = {https://m2.mtmt.hu/api/publication/30530360},
	author = {Fels, Benedikt and Bulk, Etmar and Pethő, Zoltán Dénes and Schwab, Albrecht},
	doi = {10.3390/ph11020048},
	journal-iso = {PHARMACEUTICALS-BASE},
	journal = {PHARMACEUTICALS},
	volume = {11},
	unique-id = {30530360},
	abstract = {A dysregulated cellular Ca2+ homeostasis is involved in multiple pathologies including cancer. Changes in Ca2+ signaling caused by altered fluxes through ion channels and transporters (the transportome) are involved in all steps of the metastatic cascade. Cancer cells thereby re-program and misuse the cellular transportome to regulate proliferation, apoptosis, metabolism, growth factor signaling, migration and invasion. Cancer cells use their transportome to cope with diverse environmental challenges during the metastatic cascade, like hypoxic, acidic and mechanical cues. Hence, ion channels and transporters are key modulators of cancer progression. This review focuses on the role of transient receptor potential (TRP) channels in the metastatic cascade. After briefly introducing the role of the transportome in cancer, we discuss TRP channel functions in cancer cell migration. We highlight the role of TRP channels in sensing and transmitting cues from the tumor microenvironment and discuss their role in cancer cell invasion. We identify open questions concerning the role of TRP channels in circulating tumor cells and in the processes of intra- and extravasation of tumor cells. We emphasize the importance of TRP channels in different steps of cancer metastasis and propose cancer-specific TRP channel blockade as a therapeutic option in cancer treatment.},
	keywords = {TRP CHANNELS; Tumor microenvironment; metastatic cascade; transportome},
	year = {2018},
	eissn = {1424-8247}
}

@mastersthesis{MTMT:3381580,
	title = {The functional role of Ca2+- and voltage-gated potassium channels in activated human T cells and fibroblast-like synoviocytes},
	url = {https://m2.mtmt.hu/api/publication/3381580},
	author = {Pethő, Zoltán Dénes},
	unique-id = {3381580},
	year = {2018}
}

@article{MTMT:3245969,
	title = {Optimization of the Synthesis of Flavone–Amino Acid and Flavone–Dipeptide Hybrids via Buchwald–Hartwig Reaction},
	url = {https://m2.mtmt.hu/api/publication/3245969},
	author = {Pajtás, Dávid and Kónya, Krisztina and Kiss, Attila and Džubák, Petr and Pethő, Zoltán Dénes and Varga, Zoltán and Panyi, György and Patonay, Tamás},
	doi = {10.1021/acs.joc.7b00124},
	journal-iso = {J ORG CHEM},
	journal = {JOURNAL OF ORGANIC CHEMISTRY},
	volume = {82},
	unique-id = {3245969},
	issn = {0022-3263},
	abstract = {The article describes the development of Buchwald–Hartwig amination of different bromoflavones with amino acid and peptide derivatives as nitrogen source giving unique structures. The previously observed racemization, which occurred during the synthesis of flavone-amino acid hybrids, was successfully prevented in most cases. The biological assays of these novel structures showed cytotoxic effects on different cancer cell lines.},
	year = {2017},
	eissn = {1520-6904},
	pages = {4578-4587},
	orcid-numbers = {Kiss, Attila/0000-0003-3601-5143; Panyi, György/0000-0001-6227-3301}
}