TY - JOUR AU - Tóth, Ádám Viktor AU - Bartók, Ádám TI - Reviewing critical TRPM2 variants through a structure-function lens JF - JOURNAL OF BIOTECHNOLOGY J2 - J BIOTECHNOL VL - 385 PY - 2024 SP - 49 EP - 57 PG - 9 SN - 0168-1656 DO - 10.1016/j.jbiotec.2024.02.017 UR - https://m2.mtmt.hu/api/publication/34720489 ID - 34720489 LA - English DB - MTMT ER - TY - JOUR AU - Zboray, Katalin AU - Tóth, Ádám Viktor AU - Miskolczi, Tímea D. AU - Pesti, Krisztina AU - Casanova, Emilio AU - Kreidl, Emanuel AU - Mike, Árpád AU - Szenes, Áron AU - Sági, László AU - Lukács, Péter TI - High-throughput ligand profile characterization in novel cell lines expressing seven heterologous insect olfactory receptors for the detection of volatile plant biomarkers JF - SCIENTIFIC REPORTS J2 - SCI REP VL - 13 PY - 2023 IS - 1 PG - 11 SN - 2045-2322 DO - 10.1038/s41598-023-47455-4 UR - https://m2.mtmt.hu/api/publication/34431632 ID - 34431632 AB - Agriculturally important crop plants emit a multitude of volatile organic compounds (VOCs), which are excellent indicators of their health status and their interactions with pathogens and pests. In this study, we have developed a novel cellular olfactory panel for detecting fungal pathogen-related VOCs we had identified in the field, as well as during controlled inoculations of several crop plants. The olfactory panel consists of seven stable HEK293 cell lines each expressing a functional Drosophila olfactory receptor as a biosensing element along with GCaMP6, a fluorescent calcium indicator protein. An automated 384-well microplate reader was used to characterize the olfactory receptor cell lines for their sensitivity to reference VOCs. Subsequently, we profiled a set of 66 VOCs on all cell lines, covering a concentration range from 1 to 100 μM. Results showed that 49 VOCs (74.2%) elicited a response in at least one olfactory receptor cell line. Some VOCs activated the cell lines even at nanomolar (ppb) concentrations. The interaction profiles obtained here will support the development of biosensors for agricultural applications. Additionally, the olfactory receptor proteins can be purified from these cell lines with sufficient yields for further processing, such as structure determination or integration with sensor devices. LA - English DB - MTMT ER - TY - JOUR AU - Mike, Árpád AU - Pesti, Krisztina AU - Földi, Mátyás Csaba AU - Tóth, Ádám Viktor AU - Zboray, Katalin AU - Lukács, Péter TI - Automated patch-clamp with automated analysis: extracting compound-specific, concentration-independent biophysical properties of inhibition for sodium channel inhibitors JF - BIOPHYSICAL JOURNAL J2 - BIOPHYS J VL - 121 PY - 2022 IS - 3 Suppl. 1 SP - 92 EP - 92 PG - 1 SN - 0006-3495 DO - 10.1016/j.bpj.2021.11.2238 UR - https://m2.mtmt.hu/api/publication/32676587 ID - 32676587 LA - English DB - MTMT ER - TY - JOUR AU - Lukács, Péter AU - Pesti, Krisztina AU - Földi, Mátyás Csaba AU - Zboray, Katalin AU - Tóth, Ádám Viktor AU - Papp, Gábor AU - Mike, Árpád TI - An Advanced Automated Patch Clamp Protocol Design to Investigate Drug—Ion Channel Binding Dynamics JF - FRONTIERS IN PHARMACOLOGY J2 - FRONT PHARMACOL VL - 12 PY - 2021 PG - 14 SN - 1663-9812 DO - 10.3389/fphar.2021.738260 UR - https://m2.mtmt.hu/api/publication/32468284 ID - 32468284 N1 - Funding Agency and Grant Number: Hungarian Brain Research Program Funding text: Funding This work was supported by the Hungarian Brain Research Program (KTIA-NAP-1322014002), and by Hungarys Economic Development, and Innovation Operative Programme (GINOP-2.3.2-15-2016-00051). LA - English DB - MTMT ER - TY - JOUR AU - Pesti, Krisztina AU - Földi, Mátyás Csaba AU - Zboray, Katalin AU - Tóth, Ádám Viktor AU - Lukács, Péter AU - Mike, Árpád TI - Characterization of Compound-Specific, Concentration-Independent Biophysical Properties of Sodium Channel Inhibitor Mechanism of Action Using Automated Patch-Clamp Electrophysiology JF - FRONTIERS IN PHARMACOLOGY J2 - FRONT PHARMACOL VL - 12 PY - 2021 PG - 13 SN - 1663-9812 DO - 10.3389/fphar.2021.738460 UR - https://m2.mtmt.hu/api/publication/32218209 ID - 32218209 N1 - Összes idézések száma a WoS-ban: 0 LA - English DB - MTMT ER - TY - JOUR AU - Földi, Mátyás Csaba AU - Pesti, Krisztina AU - Zboray, Katalin AU - Tóth, Ádám Viktor AU - Hegedűs, Tamás AU - Málnási Csizmadia, András AU - Lukács, Péter AU - Mike, Árpád TI - The mechanism of non-blocking inhibition of sodium channels revealed by conformation-selective photolabeling JF - BRITISH JOURNAL OF PHARMACOLOGY J2 - BR J PHARMACOL VL - 178 PY - 2021 IS - 5 SP - 1200 EP - 1217 PG - 18 SN - 0007-1188 DO - 10.1111/bph.15365 UR - https://m2.mtmt.hu/api/publication/31821613 ID - 31821613 N1 - MTA-ELTE NAP B Opto-Neuropharmacology Group, Budapest, Hungary Plant Protection Institute, Centre for Agricultural Research, Martonvásár, Hungary Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary School of PhD Studies, Semmelweis University, Budapest, Hungary Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary Motor Pharmacology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary Export Date: 20 March 2021 CODEN: BJPCB Correspondence Address: Mike, A.; MTA-ELTE NAP B Opto-Neuropharmacology GroupHungary; email: arpadmike1@gmail.com Correspondence Address: Mike, A.; Plant Protection Institute, Hungary; email: arpadmike1@gmail.com Correspondence Address: Mike, A.; Department of Biochemistry, Hungary; email: arpadmike1@gmail.com Funding details: KTIA‐NAP‐13‐2‐2014‐002 Funding details: GINOP‐2.3.2‐15‐2016‐00051 Funding details: Nemzeti Kutatási Fejlesztési és Innovációs Hivatal, NKFIH, K127961 Funding text 1: This work was supported by the Hungarian Brain Research Program (KTIA‐NAP‐13‐2‐2014‐002), Hungary's Economic Development and Innovation Operative Programme (GINOP‐2.3.2‐15‐2016‐00051), NKFIH K127961, and the Semmelweis Science and Innovation Fund. MTA-ELTE NAP B Opto-Neuropharmacology Group, Budapest, Hungary Plant Protection Institute, Centre for Agricultural Research, Martonvásár, Hungary Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary School of PhD Studies, Semmelweis University, Budapest, Hungary Department of Biophysics and Radiation Biology, Semmelweis University, Budapest, Hungary Motor Pharmacology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary Export Date: 26 April 2021 CODEN: BJPCB Correspondence Address: Mike, A.; MTA-ELTE NAP B Opto-Neuropharmacology GroupHungary; email: arpadmike1@gmail.com Correspondence Address: Mike, A.; Plant Protection Institute, Hungary; email: arpadmike1@gmail.com Correspondence Address: Mike, A.; Department of Biochemistry, Hungary; email: arpadmike1@gmail.com Funding details: KTIA‐NAP‐13‐2‐2014‐002 Funding details: GINOP‐2.3.2‐15‐2016‐00051 Funding details: Nemzeti Kutatási Fejlesztési és Innovációs Hivatal, NKFIH, K127961 Funding text 1: This work was supported by the Hungarian Brain Research Program (KTIA‐NAP‐13‐2‐2014‐002), Hungary's Economic Development and Innovation Operative Programme (GINOP‐2.3.2‐15‐2016‐00051), NKFIH K127961, and the Semmelweis Science and Innovation Fund. AB - Sodium channel inhibitors can be used to treat hyperexcitability-related diseases, including epilepsies, pain syndromes, neuromuscular disorders, and cardiac arrhythmias. The applicability of these drugs is limited by their nonspecific effect on physiological function. They act mainly by sodium channel block and in addition by modulation of channel kinetics. While channel block inhibits healthy and pathological tissue equally, modulation can preferentially inhibit pathological activity. An ideal drug designed to target the sodium channels of pathological tissue would act predominantly by modulation. Thus far, no such drug has been described.Patch-clamp experiments with ultra-fast solution exchange and photolabeling-coupled electrophysiology were applied to describe the unique mechanism of riluzole on Nav1.4 sodium channels. In silico docking experiments were used to study the molecular details of binding.We present evidence that riluzole acts predominantly by non-blocking modulation. We propose that, being a relatively small molecule, riluzole is able to stay bound to the binding site, but nonetheless stay off the conduction pathway, by residing in one of the fenestrations. We demonstrate how this mechanism can be recognized.Our results identify riluzole as the prototype of this new class of sodium channel inhibitors. Drugs of this class are expected to selectively prevent hyperexcitability, while having minimal effect on cells firing at a normal rate from a normal resting potential. LA - English DB - MTMT ER - TY - JOUR AU - Tóth, Ádám Viktor AU - Lukács, Péter AU - Mike, Árpád TI - What Makes a Compound a Sodium Channel Inhibitor JF - BIOPHYSICAL JOURNAL J2 - BIOPHYS J VL - 118 PY - 2020 IS - 3 Suppl. 1 SP - 577A EP - 577A PG - 1 SN - 0006-3495 DO - 10.1016/j.bpj.2019.11.3132 UR - https://m2.mtmt.hu/api/publication/31196565 ID - 31196565 LA - English DB - MTMT ER - TY - JOUR AU - Miskolczi, Tímea Dóra AU - Zboray, Katalin AU - Keszőcze, Anikó Zsófia AU - Quddoos, Zainab AU - Ambrózy, Zsuzsanna AU - Hamow, Kamirán Áron AU - Tóth, Ádám Viktor AU - Sági, László AU - Szelényi, Magdolna Olívia AU - Radványi, Dalma AU - Földi, Mátyás Csaba AU - Molnár, Béla Péter AU - Pesti, Krisztina AU - Mike, Árpád AU - Lukács, Péter TI - Development of a Smell Biosensor System for Early Detection of Plant Diseases JF - BIOPHYSICAL JOURNAL J2 - BIOPHYS J VL - 118 PY - 2020 IS - 3 Suppl. 1 SP - 315A EP - 315A PG - 1 SN - 0006-3495 DO - 10.1016/j.bpj.2019.11.1774 UR - https://m2.mtmt.hu/api/publication/31180515 ID - 31180515 LA - English DB - MTMT ER -