@article{MTMT:33215047,
	title = {New ‘kids’ on the voltage‐gated proton channel block},
	url = {https://m2.mtmt.hu/api/publication/33215047},
	author = {Korpos, Éva and Papp, Ferenc},
	doi = {10.1111/febs.16670},
	journal-iso = {FEBS J},
	journal = {FEBS JOURNAL},
	volume = {290},
	unique-id = {33215047},
	issn = {1742-464X},
	year = {2023},
	eissn = {1742-4658},
	pages = {970-973},
	orcid-numbers = {Korpos, Éva/0000-0002-0438-4211}
}

@article{MTMT:31853954,
	title = {A disulfide-stabilised helical hairpin fold in acrorhagin I: an emerging structural motif in peptide toxins},
	url = {https://m2.mtmt.hu/api/publication/31853954},
	author = {Krishnarjuna, Bankala and Sunanda, Punnepalli and Villegas–Moreno, Jessica and Csóti, Ágota and A.V. Morales, Rodrigo and Wai, Dorothy C.C. and Panyi, György and Prentis, Peter and Norton, Raymond S.},
	doi = {10.1016/j.jsb.2020.107692},
	journal-iso = {J STRUCT BIOL},
	journal = {JOURNAL OF STRUCTURAL BIOLOGY},
	volume = {213},
	unique-id = {31853954},
	issn = {1047-8477},
	abstract = {Acrorhagin I (U-AITX-Aeq5a) is a disulfide-rich peptide identified in the aggressive organs (acrorhagi) of the sea anemone Actinia equina. Previous studies (Toxicon 2005, 46:768-74) found that the peptide is toxic in crabs, although the structural and functional properties of acrorhagin I have not been reported. In this work, an Escherichia coli (BL21 strain) expression system was established for the preparation of C-13,N-15-labelled acrorhagin I, and the solution structure was determined using NMR spectroscopy. Structurally, acrorhagin I is similar to B-IV toxin from the marine worm Cerebratulus lacteus (PDB id 1VIB), with a well-defined helical hairpin structure stabilised by four intramolecular disulfide bonds. The recombinant peptide was tested in patch-clamp electrophysiology assays against voltage-gated potassium and sodium channels, and in bacterial and fungal growth inhibitory and showed no activity in functional assays, indicating that this peptide may possess a different biological function. Metal ion interaction studies using NMR spectroscopy showed that acrorhagin I bound zinc and nickel, suggesting that its function might be modulated by metal ions or that it may be involved in regulating metal ion levels and their transport. The similarity between the structure of acrorhagin I and that of B-IV toxin from a marine worm suggests that this fold may prove to be a recurring motif in disulfide-rich peptides from marine organisms.},
	keywords = {NMR; Disulfides; sea anemone; Hairpin structure; Metal ion interactions; Acrorhagin I},
	year = {2021},
	eissn = {1095-8657},
	orcid-numbers = {Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:30651425,
	title = {TMEM266 is a functional voltage sensor regulated by extracellular Zn2+},
	url = {https://m2.mtmt.hu/api/publication/30651425},
	author = {Papp, Ferenc and Lomash, Suvendu and Szilagyi, Orsolya and Babikow, Erika and Smith, Jaime and Chang, Tsg-Hui and Bahamonde, Maria Isabel and Toombes, Gilman Ewan Stephen and Swartz, Kenton Jon},
	doi = {10.7554/eLife.42372},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {8},
	unique-id = {30651425},
	issn = {2050-084X},
	abstract = {Voltage-activated ion channels contain S1-S4 domains that sense membrane voltage and control opening of ion-selective pores, a mechanism that is crucial for electrical signaling. Related S1-S4 domains have been identified in voltage-sensitive phosphatases and voltage-activated proton channels, both of which lack associated pore domains. hTMEM266 is a protein of unknown function that is predicted to contain an S1-S4 domain, along with partially structured cytoplasmic termini. Here we show that hTMEM266 forms oligomers, undergoes both rapid (mu s) and slow (ms) structural rearrangements in response to changes in voltage, and contains a Zn2+ binding site that can regulate the slow conformational transition. Our results demonstrate that the S1-S4 domain in hTMEM266 is a functional voltage sensor, motivating future studies to identify cellular processes that may be regulated by the protein. The ability of hTMEM266 to respond to voltage on the mu s timescale may be advantageous for designing new genetically encoded voltage indicators.},
	year = {2019},
	eissn = {2050-084X}
}

@article{MTMT:30378432,
	title = {Determining the target of membrane sterols on voltage-gated potassium channels},
	url = {https://m2.mtmt.hu/api/publication/30378432},
	author = {Zákány, Florina and Pap, Pál and Papp, Ferenc and Kovács, Tamás and Nagy, Péter and Péter, Mária and Szente, Lajos and Panyi, György and Varga, Zoltán},
	doi = {10.1016/j.bbalip.2018.12.006},
	journal-iso = {BBA-MOL CELL BIOL L},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS},
	volume = {1864},
	unique-id = {30378432},
	issn = {1388-1981},
	year = {2019},
	eissn = {1879-2618},
	pages = {312-325},
	orcid-numbers = {Kovács, Tamás/0000-0002-1084-9847; Nagy, Péter/0000-0002-7466-805X; Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:3320951,
	title = {Mechanisms of noncovalent β subunit regulation of NaV channel gating},
	url = {https://m2.mtmt.hu/api/publication/3320951},
	author = {Zhu, W and Voelker, TL and Varga, Zoltán and Schubert, AR and Nerbonne, JM and Silva, JR},
	doi = {10.1085/jgp.201711802},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {149},
	unique-id = {3320951},
	issn = {0022-1295},
	year = {2017},
	eissn = {1540-7748},
	pages = {813-831}
}

@article{MTMT:3272305,
	title = {Sterol Regulation of Voltage-Gated K+ Channels},
	url = {https://m2.mtmt.hu/api/publication/3272305},
	author = {Balajthy, András and Hajdu, Péter Béla and Panyi, György and Varga, Zoltán},
	doi = {10.1016/bs.ctm.2017.05.006},
	journal-iso = {CURR TOP MEMBR},
	journal = {CURRENT TOPICS IN MEMBRANES},
	volume = {80},
	unique-id = {3272305},
	issn = {1063-5823},
	year = {2017},
	pages = {255-292},
	orcid-numbers = {Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:3192921,
	title = {Regulation of Na+ channel inactivation by the DIII and DIV voltage-sensing domains.},
	url = {https://m2.mtmt.hu/api/publication/3192921},
	author = {Hsu, EJ and Zhu, W and Schubert, AR and Voelker, T and Varga, Zoltán and Silva, JR},
	doi = {10.1085/jgp.201611678},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {149},
	unique-id = {3192921},
	issn = {0022-1295},
	abstract = {Functional eukaryotic voltage-gated Na+ (NaV) channels comprise four domains (DI-DIV), each containing six membrane-spanning segments (S1-S6). Voltage sensing is accomplished by the first four membrane-spanning segments (S1-S4), which together form a voltage-sensing domain (VSD). A critical NaV channel gating process, inactivation, has previously been linked to activation of the VSDs in DIII and DIV. Here, we probe this interaction by using voltage-clamp fluorometry to observe VSD kinetics in the presence of mutations at locations that have been shown to impair NaV channel inactivation. These locations include the DIII-DIV linker, the DIII S4-S5 linker, and the DIV S4-S5 linker. Our results show that, within the 10-ms timeframe of fast inactivation, the DIV-VSD is the primary regulator of inactivation. However, after longer 100-ms pulses, the DIII-DIV linker slows DIII-VSD deactivation, and the rate of DIII deactivation correlates strongly with the rate of recovery from inactivation. Our results imply that, over the course of an action potential, DIV-VSDs regulate the onset of fast inactivation while DIII-VSDs determine its recovery.},
	year = {2017},
	eissn = {1540-7748},
	pages = {389-403}
}

@article{MTMT:3099238,
	title = {7DHC-induced changes of Kv1.3 operation contributes to modified T cell function in Smith-Lemli-Opitz syndrome},
	url = {https://m2.mtmt.hu/api/publication/3099238},
	author = {Balajthy, András and Somodi, Sándor and Pethő, Z and Péter, Mária and Varga, Zoltán and P. Szabó, Gabriella and Paragh, György and Vigh, László and Panyi, György and Hajdu, Péter Béla},
	doi = {10.1007/s00424-016-1851-4},
	journal-iso = {PFLUG ARCH EUR J PHY},
	journal = {PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY},
	volume = {468},
	unique-id = {3099238},
	issn = {0031-6768},
	abstract = {In vitro manipulation of membrane sterol level affects the regulation of ion channels and consequently certain cellular functions; however, a comprehensive study that confirms the pathophysiological significance of these results is missing. The malfunction of 7-dehydrocholesterol (7DHC) reductase in Smith-Lemli-Opitz syndrome (SLOS) leads to the elevation of the 7-dehydrocholesterol level in the plasma membrane. T lymphocytes were isolated from SLOS patients to assess the effect of the in vivo altered membrane sterol composition on the operation of the voltage-gated Kv1.3 channel and the ion channel-dependent mitogenic responses. We found that the kinetic and equilibrium parameters of Kv1.3 activation changed in SLOS cells. Identical changes in Kv1.3 operation were observed when control/healthy T cells were loaded with 7DHC. Removal of the putative sterol binding sites on Kv1.3 resulted in a phenotype that was not influenced by the elevation in membrane sterol level. Functional assays exhibited impaired activation and proliferation rate of T cells probably partially due to the modified Kv1.3 operation. We concluded that the altered membrane sterol composition hindered the operation of Kv1.3 as well as the ion channel-controlled T cell functions. © 2016, Springer-Verlag Berlin Heidelberg.},
	keywords = {cholesterol; Kv1.3; 7-Dehydrocholesterol; Smith-Lemli-Opitz syndrome; Voltage-gated ion channel},
	year = {2016},
	eissn = {1432-2013},
	pages = {1403-1418},
	orcid-numbers = {Somodi, Sándor/0000-0002-3615-2300; Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:3023309,
	title = {Molecular motions that shape the cardiac action potential: Insights from voltage clamp fluorometry},
	url = {https://m2.mtmt.hu/api/publication/3023309},
	author = {Zhu, W and Varga, Zoltán and Silva, J R},
	doi = {10.1016/j.pbiomolbio.2015.12.003},
	journal-iso = {PROG BIOPHYS MOL BIO},
	journal = {PROGRESS IN BIOPHYSICS AND MOLECULAR BIOLOGY},
	volume = {120},
	unique-id = {3023309},
	issn = {0079-6107},
	year = {2016},
	eissn = {1873-1732},
	pages = {3-17}
}

@article{MTMT:3023306,
	title = {The anti-proliferative effect of cation channel blockers in T lymphocytes depends on the strength of mitogenic stimulation},
	url = {https://m2.mtmt.hu/api/publication/3023306},
	author = {Pethő, Zoltán Dénes and Balajthy, András and Bartók, Ádám and Bene, Krisztián and Somodi, Sándor and Szilagyi, O and Rajnavölgyi, Éva and Panyi, György and Varga, Zoltán},
	doi = {10.1016/j.imlet.2016.02.003},
	journal-iso = {IMMUNOL LETT},
	journal = {IMMUNOLOGY LETTERS},
	volume = {171},
	unique-id = {3023306},
	issn = {0165-2478},
	abstract = {Ion channels are crucially important for the activation and 
		proliferation of T lymphocytes, and thus, for
		the function of the immune system. Previous studies on the 
		effects of channel blockers on T cell proliferation
		reported variable effectiveness due to differing experimental 
		systems. Therefore our aim was
		to investigate how the strength of the mitogenic stimulation 
		influences the efficiency of cation channel
		blockers in inhibiting activation, cytokine secretion and 
		proliferation of T cells under standardized
		conditions.
		Human peripheral blood lymphocytes were activated via 
		monoclonal antibodies targeting the TCR-CD3
		complex and the co-stimulator CD28. We applied the blockers 
		of Kv1.3 (Anuroctoxin), KCa3.1 (TRAM-
		34) and CRAC (2-Apb) channels of T cells either alone or in 
		combination with rapamycin, the inhibitor
		of the mammalian target of rapamycin (mTOR). Five days after 
		the stimulation ELISA and flow cytometric
		measurements were performed to determine IL-10 and IFN- 
		secretion, cellular viability and
		proliferation.
		Our results showed that ion channel blockers and rapamycin 
		inhibit IL-10 and IFN- secretion and cell
		division in a dose-dependent manner. Simultaneous application 
		of the blockers for each channel along
		with rapamycin was the most effective, indicating synergy 
		among the various activation pathways. Upon
		increasing the extent of mitogenic stimulation the anti-
		proliferative effect of the ion channel blockers
		diminished. This phenomenon may be important in understanding 
		the fine-tuning of T cell activation.
		© 2016 European Federation of Immunological Societies. 
		Published by Elsevier B.V. All rights reserved.},
	keywords = {Humans; Drug Synergism; Cells, Cultured; Pyrazoles/pharmacology; Cell Proliferation/*drug effects; Interleukin-4/metabolism; Interferon-gamma/metabolism; Lymphocyte Activation/*drug effects; T-Lymphocytes/*drug effects/physiology; Calcium Channel Blockers/*pharmacology; Receptors, Antigen, T-Cell/metabolism; Sirolimus/pharmacology; Immunosuppressive Agents/pharmacology; Intermediate-Conductance Calcium-Activated Potassium Channels/*antagonists &; Boron Compounds/pharmacology; Mitogens/immunology; Kv1.3 Potassium Channel/*antagonists & inhibitors; Calcium Release Activated Calcium Channels/*antagonists & inhibitors},
	year = {2016},
	eissn = {1879-0542},
	pages = {60-69},
	orcid-numbers = {Bartók, Ádám/0000-0002-1232-5246; Bene, Krisztián/0000-0002-9963-8172; Somodi, Sándor/0000-0002-3615-2300; Panyi, György/0000-0001-6227-3301}
}