@article{MTMT:34774200,
	title = {Analysis of intact venom proteins with capillary zone electrophoresis - mass spectrometry},
	url = {https://m2.mtmt.hu/api/publication/34774200},
	author = {Vishwakarma, Gayatri and Andrási, Melinda and Szabó, Dávid Ruben and Hajdu, Péter Béla and Petrilla, Vladimir and Petrillová, Monika and Legath, Jaroslav and Gáspár, Attila},
	doi = {10.1016/j.microc.2024.110290},
	journal-iso = {MICROCHEM J},
	journal = {MICROCHEMICAL JOURNAL},
	volume = {200},
	unique-id = {34774200},
	issn = {0026-265X},
	year = {2024},
	eissn = {1095-9149}
}

@article{MTMT:34762667,
	title = {Universal CAR T cells targeted to HER2 with a biotin-trastuzumab soluble linker penetrate spheroids and large tumor xenografts that are inherently resistant to trastuzumab mediated ADCC},
	url = {https://m2.mtmt.hu/api/publication/34762667},
	author = {Nagy, Lőrinc and Mezősi-Csaplár, Marianna and Rebenku, István and Vereb, György and Szöőr, Árpád},
	doi = {10.3389/fimmu.2024.1365172},
	journal-iso = {FRONT IMMUNOL},
	journal = {FRONTIERS IN IMMUNOLOGY},
	volume = {15},
	unique-id = {34762667},
	issn = {1664-3224},
	abstract = {CAR T cell therapies face challenges in combating solid tumors due to their single-target approach, which becomes ineffective if the targeted antigen is absent or lost. Universal CAR T cells (UniCAR Ts) provide a promising solution by utilizing molecular tags (linkers), such as biotin conjugated to monoclonal antibodies, enabling them to target a variety of tumor antigens. Recently, we showed that conventional CAR T cells could penetrate the extracellular matrix (ECM) of ADCC-resistant tumors, which forms a barrier to therapeutic antibodies. This finding led us to investigate whether UniCAR T cells, targeted by soluble antibody-derived linkers, could similarly tackle ADCC-resistant tumors where ECM restricts antibody penetration. We engineered UniCAR T cells by incorporating a biotin-binding monomeric streptavidin 2 (mSA2) domain for targeting HER2 via biotinylated trastuzumab (BT). The activation and cytotoxicity of UniCAR T cells in the presence or absence of BT were evaluated in conventional immunoassays. A 3D spheroid coculture was set up to test the capability of UniCAR Ts to access ECM-masked HER2 + cells. For in vivo analysis, we utilized a HER2 + xenograft model in which intravenously administered UniCAR T cells were supplemented with intraperitoneal BT treatments. In vitro , BT-guided UniCAR T cells showed effective activation and distinct anti-tumor response. Upon target recognition, IFNγ secretion correlated with BT concentration. In the presence of BT, UniCAR T cells effectively penetrated HER2 + spheroids and induced cell death in their core regions. In vivo , upon intravenous administration of UniCAR Ts, circulating BT linkers immediately engaged the mSA2 domain and directed effector cells to the HER2 + tumors. However, these co-treated mice died early, possibly due to the lung infiltration of UniCAR T cells that could recognize both native biotin and HER2. Our results suggest that UniCAR T cells guided with soluble linkers present a viable alternative to conventional CAR T cells, especially for patients resistant to antibody therapy and those with solid tumors exhibiting high antigenic variability. Critical to their success, however, is the choice of an appropriate binding domain for the CAR and the corresponding soluble linker, ensuring both efficacy and safety in therapeutic applications.},
	year = {2024},
	eissn = {1664-3224},
	pages = {1664-3224},
	orcid-numbers = {Nagy, Lőrinc/0000-0001-5278-1898}
}

@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:34767238,
	title = {Examinations of cellular uptake of cell penetrating peptides in vitro and in vivo},
	url = {https://m2.mtmt.hu/api/publication/34767238},
	author = {Toth, Gabriella and Batta, Gyula Gábor (Ifj.) and Karpati, Levente and Szöőr, Árpád and Mandity, Istvan and Nagy, Péter},
	journal-iso = {EUR BIOPHYS J},
	journal = {EUROPEAN BIOPHYSICS JOURNAL},
	volume = {52},
	unique-id = {34767238},
	issn = {0175-7571},
	year = {2023},
	eissn = {1432-1017},
	pages = {S163-S163},
	orcid-numbers = {Batta, Gyula Gábor (Ifj.)/0000-0001-8735-6920; Nagy, Péter/0000-0002-7466-805X}
}

@article{MTMT:34766294,
	title = {Effect of Erbb2 Missense Mutations on Dimer Formation},
	url = {https://m2.mtmt.hu/api/publication/34766294},
	author = {Serrano Cano, Tayde Gabriela and Yasari, Atena and Tiemann-Boege, Irene and Nagy, Péter},
	journal-iso = {EUR BIOPHYS J},
	journal = {EUROPEAN BIOPHYSICS JOURNAL},
	volume = {52},
	unique-id = {34766294},
	issn = {0175-7571},
	year = {2023},
	eissn = {1432-1017},
	pages = {S105-S105},
	orcid-numbers = {Nagy, Péter/0000-0002-7466-805X}
}

@article{MTMT:34764950,
	title = {Probes for Single-Molecule Microscopy Analysis of ErbB4 Biophysical Properties},
	url = {https://m2.mtmt.hu/api/publication/34764950},
	author = {Kalouskova, Barbora and Serrano Cano, Tayde Gabriela and Nagy, Péter and Brameshuber, Mario},
	journal-iso = {EUR BIOPHYS J},
	journal = {EUROPEAN BIOPHYSICS JOURNAL},
	volume = {52},
	unique-id = {34764950},
	issn = {0175-7571},
	year = {2023},
	eissn = {1432-1017},
	pages = {S87-S87},
	orcid-numbers = {Nagy, Péter/0000-0002-7466-805X}
}