@article{MTMT:34840361,
	title = {Intracellular acidity impedes KCa3.1 activation by Riluzole and SKA-31},
	url = {https://m2.mtmt.hu/api/publication/34840361},
	author = {Cozzolino, Marco and Panyi, György},
	doi = {10.3389/fphar.2024.1380655},
	journal-iso = {FRONT PHARMACOL},
	journal = {FRONTIERS IN PHARMACOLOGY},
	volume = {15},
	unique-id = {34840361},
	year = {2024},
	eissn = {1663-9812},
	pages = {1-23},
	orcid-numbers = {Panyi, György/0000-0001-6227-3301}
}

@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:34565926,
	title = {Activity of Potassium Channels in CD8+ T Lymphocytes: Diagnostic and Prognostic Biomarker in Ovarian Cancer?},
	url = {https://m2.mtmt.hu/api/publication/34565926},
	author = {Jusztus, Vivien and Medyouni, Ghofrane and Bagosi, Adrienn and Lampé, Rudolf and Panyi, György and Matolay, Orsolya and Maka, Eszter and Krasznai, Zoárd Tibor and Vörös, Orsolya and Hajdu, Péter Béla},
	doi = {10.3390/ijms25041949},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {25},
	unique-id = {34565926},
	issn = {1661-6596},
	abstract = {CD8+ T cells play a role in the suppression of tumor growth and immunotherapy. Ion channels control the Ca2+-dependent function of CD8+ lymphocytes such as cytokine/granzyme production and tumor killing. Kv1.3 and KCa3.1 K+ channels stabilize the negative membrane potential of T cells to maintain Ca2+ influx through CRAC channels. We assessed the expression of Kv1.3, KCa3.1 and CRAC in CD8+ cells from ovarian cancer (OC) patients (n = 7). We found that the expression level of Kv1.3 was higher in patients with malignant tumors than in control or benign tumor groups while the KCa3.1 activity was lower in the malignant tumor group as compared to the others. We demonstrated that the Ca2+ response in malignant tumor patients is higher compared to control groups. We propose that altered Kv1.3 and KCa3.1 expression in CD8+ cells in OC could be a reporter and may serve as a biomarker in diagnostics and that increased Ca2+ response through CRAC may contribute to the impaired CD8+ function.},
	year = {2024},
	eissn = {1422-0067},
	pages = {1949},
	orcid-numbers = {Lampé, Rudolf/0000-0002-8230-7692; Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:34320587,
	title = {Structure-function relationships in ShKT domain peptides: ShKT-Ts1 from the sea anemone Telmatactis stephensoni},
	url = {https://m2.mtmt.hu/api/publication/34320587},
	author = {Sanches, Karoline and Ashwood, Lauren M. and Olushola-Siedoks, Abisola Ave-Maria and Wai, Dorothy C. C. and Rahman, Arfatur and Shakeel, Kashmala and Naseem, Muhammad Umair and Panyi, György and Prentis, Peter J. and Norton, Raymond S.},
	doi = {10.1002/prot.26594},
	journal-iso = {PROTEINS},
	journal = {PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS},
	volume = {92},
	unique-id = {34320587},
	issn = {0887-3585},
	abstract = {Diverse structural scaffolds have been described in peptides from sea anemones, with the ShKT domain being a common scaffold first identified in ShK toxin from Stichodactyla helianthus. ShK is a potent blocker of voltage-gated potassium channels (K-V 1.x), and an analog, ShK-186 (dalazatide), has completed Phase 1 clinical trials in plaque psoriasis. The ShKT domain has been found in numerous other species, but only a tiny fraction of ShKT domains has been characterized functionally. Despite adopting the canonical ShK fold, some ShKT peptides from sea anemones inhibit K-V 1.x, while others do not. Mutagenesis studies have shown that a Lys-Tyr (KY) dyad plays a key role in K-V 1.x blockade, although a cationic residue followed by a hydrophobic residue may also suffice. Nevertheless, ShKT peptides displaying an ShK-like fold and containing a KY dyad do not necessarily block potassium channels, so additional criteria are needed to determine whether new ShKT peptides might show activity against potassium channels. In this study, we used a combination of NMR and molecular dynamics (MD) simulations to assess the potential activity of a new ShKT peptide. We determined the structure of ShKT-Ts1, from the sea anemone Telmatactis stephensoni, examined its tissue localization, and investigated its activity against a range of ion channels. As ShKT-Ts1 showed no activity against K-V 1.x channels, we used MD simulations to investigate whether solvent exposure of the dyad residues may be informative in rationalizing and potentially predicting the ability of ShKT peptides to block K-V 1.x channels. We show that either a buried dyad that does not become exposed during MD simulations, or a partially exposed dyad that becomes buried during MD simulations, correlates with weak or absent activity against K-V 1.x channels. Therefore, structure determination coupled with MD simulations, may be used to predict whether new sequences belonging to the ShKT family may act as potassium channel blockers.},
	keywords = {PEPTIDE; NMR; molecular dynamics; potassium channel; Structure Determination; sea anemone; ShKT domain},
	year = {2024},
	eissn = {1097-0134},
	pages = {192-205},
	orcid-numbers = {Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:34151641,
	title = {Structural and functional characterisation of Tst2, a novel TRPV1 inhibitory peptide from the Australian sea anemone Telmatactis stephensoni},
	url = {https://m2.mtmt.hu/api/publication/34151641},
	author = {Elnahriry, Khaled A. and Wai, Dorothy C.C. and Ashwood, Lauren M. and Naseem, Muhammad Umair and Szántó, Gábor Tibor and Guo, Shaodong and Panyi, György and Prentis, Peter J. and Norton, Raymond S.},
	doi = {10.1016/j.bbapap.2023.140952},
	journal-iso = {BBA-PROTEINS PROTEOM},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS},
	volume = {1872},
	unique-id = {34151641},
	issn = {1570-9639},
	year = {2024},
	eissn = {1878-1454},
	orcid-numbers = {Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:34775337,
	title = {AB0237 EFFECTS OF ONE-YEAR TOFACITINIB THERAPY ON ANGIOGENIC BIOMARKERS IN RHEUMATOID ARTHRITIS},
	url = {https://m2.mtmt.hu/api/publication/34775337},
	author = {Kerekes, György and Bodoki, Levente and Hamar, Attila and Karancsiné Pusztai, Anita and Tajti, Gábor and Katkó, Mónika and Végh, Edit and Pethő, Zsófia and Bodnár, Nóra and Horváth, Ágnes and Soós, B. and Szamosi, Szilvia and Hascsi, Z. and Harangi, Mariann and Panyi, György and Szűcs, Gabriella and Szekanecz, Zoltán},
	doi = {10.1136/annrheumdis-2023-eular.2331},
	journal-iso = {ANN RHEUM DIS},
	journal = {ANNALS OF THE RHEUMATIC DISEASES},
	volume = {82},
	unique-id = {34775337},
	issn = {0003-4967},
	year = {2023},
	eissn = {1468-2060},
	pages = {1303-1303},
	orcid-numbers = {Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:34763840,
	title = {Novel loss-of-function mutations in KV7.2, and their possible involvement in epilepsy},
	url = {https://m2.mtmt.hu/api/publication/34763840},
	author = {Szántó, Gábor Tibor and Balogh, István and Panyi, György},
	journal-iso = {EUR BIOPHYS J},
	journal = {EUROPEAN BIOPHYSICS JOURNAL},
	volume = {52},
	unique-id = {34763840},
	issn = {0175-7571},
	year = {2023},
	eissn = {1432-1017},
	pages = {S161-S161},
	orcid-numbers = {Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:34215318,
	title = {Effects of 1-year tofacitinib therapy on angiogenic biomarkers in rheumatoid arthritis},
	url = {https://m2.mtmt.hu/api/publication/34215318},
	author = {Kerekes, György and Czókolyová, Monika and Hamar, Attila and Karancsiné Pusztai, Anita and Tajti, Gábor and Katkó, Mónika and Végh, Edit and Pethő, Zsófia and Bodnár, Nóra and Horváth, Ágnes and Soós, Boglárka and Szamosi, Szilvia and Hascsi, Zsolt and Harangi, Mariann and Hodosi, Katalin and Panyi, György and Seres, Tamás and Szűcs, Gabriella and Szekanecz, Zoltán},
	doi = {10.1093/rheumatology/kead502},
	journal-iso = {RHEUMATOLOGY},
	journal = {RHEUMATOLOGY (UNITED KINGDOM)},
	volume = {62},
	unique-id = {34215318},
	issn = {1462-0324},
	year = {2023},
	eissn = {1462-0332},
	pages = {SI304-SI312},
	orcid-numbers = {Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:34151535,
	title = {Of Seven New K+ Channel Inhibitor Peptides of Centruroides bonito, α-KTx 2.24 Has a Picomolar Affinity for Kv1.2},
	url = {https://m2.mtmt.hu/api/publication/34151535},
	author = {Shakeel, Kashmala and Olamendi-Portugal, Timoteo and Naseem, Muhammad Umair and Becerril, Baltazar and Zamudio, Fernando Z. and Delgado-Prudencio, Gustavo and Possani, Lourival Domingos and Panyi, György},
	doi = {10.3390/toxins15080506},
	journal-iso = {TOXINS},
	journal = {TOXINS},
	volume = {15},
	unique-id = {34151535},
	issn = {2072-6651},
	abstract = {Seven new peptides denominated CboK1 to CboK7 were isolated from the venom of the Mexican scorpion Centruroides bonito and their primary structures were determined. The molecular weights ranged between 3760.4 Da and 4357.9 Da, containing 32 to 39 amino acid residues with three putative disulfide bridges. The comparison of amino acid sequences with known potassium scorpion toxins (KTx) and phylogenetic analysis revealed that CboK1 (α-KTx 10.5) and CboK2 (α-KTx 10.6) belong to the α-KTx 10.x subfamily, whereas CboK3 (α-KTx 2.22), CboK4 (α-KTx 2.23), CboK6 (α-KTx 2.21), and CboK7 (α-KTx 2.24) bear > 95% amino acid similarity with members of the α-KTx 2.x subfamily, and CboK5 is identical to Ce3 toxin (α-KTx 2.10). Electrophysiological assays demonstrated that except CboK1, all six other peptides blocked the Kv1.2 channel with Kd values in the picomolar range (24–763 pM) and inhibited the Kv1.3 channel with comparatively less potency (Kd values between 20–171 nM). CboK3 and CboK4 inhibited less than 10% and CboK7 inhibited about 42% of Kv1.1 currents at 100 nM concentration. Among all, CboK7 showed out-standing affinity for Kv1.2 (Kd = 24 pM), as well as high selectivity over Kv1.3 (850-fold) and Kv1.1 (~6000-fold). These characteristics of CboK7 may provide a framework for developing tools to treat Kv1.2-related channelopathies.},
	year = {2023},
	eissn = {2072-6651},
	pages = {506},
	orcid-numbers = {Delgado-Prudencio, Gustavo/0000-0002-7977-9269; Possani, Lourival Domingos/0000-0001-6357-2661; Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:34037015,
	title = {Effect of the Lipid Landscape on the Efficacy of Cell-Penetrating Peptides},
	url = {https://m2.mtmt.hu/api/publication/34037015},
	author = {Zákány, Florina and Mándity, István and Varga, Zoltán and Panyi, György and Nagy, Péter and Kovács, Tamás},
	doi = {10.3390/cells12131700},
	journal-iso = {CELLS-BASEL},
	journal = {CELLS},
	volume = {12},
	unique-id = {34037015},
	abstract = {Every cell biological textbook teaches us that the main role of the plasma membrane is to separate cells from their neighborhood to allow for a controlled composition of the intracellular space. The mostly hydrophobic nature of the cell membrane presents an impenetrable barrier for most hydrophilic molecules larger than 1 kDa. On the other hand, cell-penetrating peptides (CPPs) are capable of traversing this barrier without compromising membrane integrity, and they can do so on their own or coupled to cargos. Coupling biologically and medically relevant cargos to CPPs holds great promise of delivering membrane-impermeable drugs into cells. If the cargo is able to interact with certain cell types, uptake of the CPP–drug complex can be tailored to be cell-type-specific. Besides outlining the major membrane penetration pathways of CPPs, this review is aimed at deciphering how properties of the membrane influence the uptake mechanisms of CPPs. By summarizing an extensive body of experimental evidence, we argue that a more ordered, less flexible membrane structure, often present in the very diseases planned to be treated with CPPs, decreases their cellular uptake. These correlations are not only relevant for understanding the cellular biology of CPPs, but also for rationally improving their value in translational or clinical applications.},
	year = {2023},
	eissn = {2073-4409},
	orcid-numbers = {Mándity, István/0000-0003-2865-6143; Panyi, György/0000-0001-6227-3301; Nagy, Péter/0000-0002-7466-805X; Kovács, Tamás/0000-0002-1084-9847}
}