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001-es BibID:	BIBFORM077738
035-os BibID:	(WoS)000469213300008 (Scopus)85066271383 (PubMed)30517027
Első szerző:	Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:	Brief structural insight into the allosteric gating mechanism of BK (Slo1) channel / János Almássy, Péter P. Nánási
Dátum:	2019
ISSN:	0008-4212
Megjegyzések:	The big conductance Ca2+-dependent K+ channel, also known as BK, MaxiK, Slo1, or KCa1.1, is a ligand- and voltage-gated K+ channel. Although structure-function studies of the past decades, involving mutagenesis and electrophysiological measurements, revealed fine details of the mechanism of BK channel gating, the exact molecular details remained unknown until the quaternary structure of the protein has been solved at a resolution of 3.5 ?A using cryo-electron microscopy. In this short review, we are going to summarize these results and interpret the gating model of the BK channel in the light of the recent structural results.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk BK channel
Megjelenés:	Canadian Journal Of Physiology And Pharmacology. - 97 : 6 (2019), p. 498-502. -
További szerzők:	Nánási Péter Pál (1956-) (élettanász)
Pályázati támogatás:	OTKA K115307 OTKA GINOP-2.3.2-15-2016-00040 GINOP EFOP-3.6.2-16-2017-00006 EFOP
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM076044
035-os BibID:	(WoS)000436909600011 (Scopus)85054071643 (PubMed)29769426
Első szerző:	Horváth Balázs (élettanász)
Cím:	Effect of the intracellular calcium concentration chelator BAPTA acetoxy-methylester on action potential duration in canine ventricular myocytes / B. Horvath, N. Szentandrassy, R. Veress, D. Baranyai, K. Kistamas, J. Almassy, A. Toth, J. Magyar, T. Banyasz, P. P. Nanasi
Dátum:	2018
Megjegyzések:	Intracellular calcium concentration ([Ca2+]i) is often buffered by using the cell-permeant acetoxy-methylester form of the Ca2+ chelator BAPTA (BAPTA-AM) under experimental conditions. This study was designed to investigate the time-dependent actions of extracellularly applied BAPTA-AM on action potential duration (APD) in cardiac cells. Action potentials were recorded from enzymatically isolated canine ventricular myocytes with conventional sharp microelectrodes. The effect of BAPTA-AM on the rapid delayed rectifier K+ current (IKr) was studied using conventional voltage clamp and action potential voltage clamp techniques. APD was lengthened by 5 ?M BAPTA-AM - but not by BAPTA - and shortened by the Ca2+ ionophore A23187 in a time-dependent manner. The APD-lengthening effect of BAPTA-AM was strongly suppressed in the presence of nisoldipine, and enhanced in the presence of BAY K8644, suggesting that a shift in the [Ca2+]i-dependent inactivation of L-type Ca2+ current may be an important underlying mechanism. However, in the presence of the IKr-blocker dofetilide or E-4031 APD was shortened rather than lengthened by BAPTA-AM. Similarly, the APD-lengthening effect of 100 nM dofetilide was halved by the pretreatment with BAPTA-AM. In line with these results, IKr was significantly reduced by extracellularly applied BAPTA-AM under both conventional voltage clamp and action potential voltage clamp conditions. This inhibition of IKr was partially reversible and was not related to the Ca2+ chelator effect BAPTA-AM. The possible mechanisms involved in the APD-modifying effects of BAPTA-AM are discussed. It is concluded that BAPTA-AM has to be applied carefully to control [Ca2+]i in whole cell systems because of its direct inhibitory action on IKr.
Tárgyszavak:	idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk calcium chelators intracellular calcium concentration action potential duration cardiac ion currents potassium ion currents ventricular myocytes
Megjelenés:	Journal of Physiology and Pharmacology. - 69 : 1 (2018), p. 99-107. -
További szerzők:	Szentandrássy Norbert (1976-) (élettanász) Veress Roland (1992-) (molekuláris biológus) Baranyai Dóra Kistamás Kornél (1986-) (biológus) Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító) Tóth A. (farmakológus) Magyar János (1961-) (élettanász) Bányász Tamás (1960-) (élettanász) Nánási Péter Pál (1956-) (élettanász)
Pályázati támogatás:	NKFIHK-115397 NKFIH NKFIH-K109736 NKFIH NKFIH-PD120794 NKFIH OTKA ANN-113273 OTKA GINOP-2.3.2-15-2016-00040 GINOP EFOP-3.6.2-16-2017-00006 EFOP UNKP-17-4-III-DE-201 UNKP
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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001-es BibID:	BIBFORM077837
035-os BibID:	(PMID)29792814 (WoS)000438114100006 (Scopus)85049826983
Első szerző:	Nánási Péter Pál ifj. (sejtbiológus)
Cím:	Perspectives of a myosin motor activator agent with increased selectivity / Péter Nánási Jr., István Komáromi, János Almássy
Dátum:	2018
ISSN:	0008-4212
Megjegyzések:	Clinical treatment of heart failure is still not fully solved. A novel class of agents, the myosin motor activators, acts directly on cardiac myosin resulting in an increased force generation and prolongation of contraction. Omecamtiv mecarbil, the lead molecule of this group, is now in human 3 phase displaying promising clinical performance. However, omecamtiv mecarbil is not selective to myosin, since it readily binds to and activates cardiac ryanodine receptors (RyR-2), an effect that may cause complications is case of overdose. In this study, in silico analysis was performed to investigate the docking of omecamtiv mecarbil and other structural analogues to cardiac myosin heavy chain and RyR-2 in order to select the structure which has a higher selectivity to myosin over RyR-2. In silico docking studies revealed that omecamtiv mecarbil has comparable affinity to myosin and RyR-2: the respective K values are 0.60 and 0.87 ?M. Another compound CK-1032100 has much lower affinity to RyR-2 than omecamtiv mecarbil, while it still has a moderate affinity to myosin. It was concluded that further research starting from the chemical structure of CK-1032100 may result a better myosin activator burdened probably less by the RyR-2 binding side effect. It also is possible, however, that the selectivity of omecamtiv mecarbil to myosin over RyR-2 cannot be substantially improved, because similar moieties seem to be responsible for the high affinity to both myosin and RyR-2.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Inotropic agents Myosin activators Omecamtiv mecarbil Ryanodine receptor Cytosolic Ca 2+
Megjelenés:	Canadian Journal of Physiology and Pharmacology. - 96 : 7 (2018), p. 676-680. -
További szerzők:	Komáromi István (1957-) (vegyész, molekuláris biológus, biokémikus) Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító)
Pályázati támogatás:	NKFIH PD112199 Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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