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1.

001-es BibID:BIBFORM083093
Első szerző:Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:Investigation of BK Channel Gating using Mallotoxin / Almassy Janos, Begenisich Ted
Dátum:2011
ISSN:0006-3495
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
folyóiratcikk
Megjelenés:Biophysical Journal. - 100 : 3 (2011), p. 583a. -
További szerzők:Begenisich, Ted B.
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2.

001-es BibID:BIBFORM049388
Első szerző:Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:Inhibition of Ryr1 by different lanthanides might reveal fine details of the ion conducting pore / Janos Almassy, Zsanett Topcsiov, Anett Szabo, Istvan Jona
Dátum:2008
ISSN:0006-3495
Megjegyzések:Effect of Europium on the gating of the RyR1 was investigated using Müuller-type artificial bilayer system. Europium applied on the trans side inhibited the RyR1 channel by Kd = 4.7 ? 0.1 mM (similarly to the Gd3+ effect), with a high cooperativity, as characterized by a Hill-coefficient of N = 5.9 ? 0.9 in contrast to Gadolinium, which exhibited N= 4. Inhibition of the RyR1 activity from the cis side was also different from that of Gadolinium, characterized by Kd = 167 ? 5.0 nM and Nhill = 2.0 ? 0.1. The Eu3+ inhibition was potential independent if the charge carrier moved according to the physiological direction of calcium release, while it was potential dependent (and proportional with the driving force) if the current was opposite to the current during calcium release. We assume, that theEuropium binding site is in or near to channel pore because of voltage dependence of the Europium blockade. Effect of Europium was similar on the Ryanodine binding of HSR vesicles with slightlydifferent affinity probably due to the unspecific Europium binding by the associated junctional proteins. Ryanodine exerted its characteristic effect locking the channel into its half-conductance stateon the Europium modified channel independently that Europium was applied from the cis or from the trans side. A model explaining these data - considering the different ionic diameters for calcium,gadolinium and europium - is proposed to explain these findings and to propose further investigation of the ion conducting pore of the RyR1, based on the different ion-diameters of the lanthanides
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
calcium release
Megjelenés:Biophysical Journal. - Volume 94 : Suppl. 2 (2008), p. 426a. -
További szerzők:Topcsiov Zsanett Szabó Anett (élettanász) Jóna István (1948-) (élettanász, fizikus)
Pályázati támogatás:T061442
OTKA
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3.

001-es BibID:BIBFORM049387
Első szerző:Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:Apical Ca2+-activated K+-channels in mouse parotid acinar cells / Janos Almassy, Ted Begenisich, David Yule
Dátum:2012
ISSN:0006-3495
Megjegyzések:Ca2+ activation of Cl-- and K+-channels are key events underlying stimulated fluid secretion from parotid salivary glands. Cl--channels are exclusively present on the apical plasma membrane (PM) while the localization of K+-channels has not been established. Mathematical models have suggested that localization of some K+-channels to the apical PM is optimum for fluid secretion. A combination of whole cell electrophysiology and temporally resolved digital imaging with local manipulation of intracellular [Ca2+] was used to investigate if Ca2+-activated K+-channels are present in the apical PM of parotid acinar cells. Initial experiments established Ca2+ buffering conditions that produced brief, localized increases in [Ca2+] following focal laser photolysis of caged-Ca2+. Conditions were employed to isolate K+ and Cl- conductances. Photolysis at the apical PM resulted in a robust increase in K+ and Cl- currents. A localized reduction in [Ca2+] at the apical PM following photolysis of Diazo-2, a caged-Ca2+ chelator, resulted in a decrease in both K+ and Cl- currents. The K+ currents evoked by apical photolysis were partially blocked by both paxilline and TRAM-34, specific blockers of BK and IK respectively and almost abolished by incubation with both antagonists. Apical TRAM-34 sensitive K+ currents were also observed in BK null parotid acini. In contrast, when the [Ca2+] was increased at the basal PM no increase in either K+ or Cl- currents was evoked. These data provide strong evidence that K+- and Cl--channels are similarly distributed in the apical PM. Furthermore, both IK and BK channels are present in this domain and that the density of these channels appears higher in the apical vs. basal PM. In total, this study provides support for a model in which fluid secretion is optimized following expression of K+-channels specifically in the apical PM.
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
calcium release
Megjelenés:Biophysical Journal. - 102 : 3 (2012), p. 650a-651a. -
További szerzők:Begenisich, Ted B. Yule, David I.
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4.

001-es BibID:BIBFORM049386
Első szerző:Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:Effect of scorpion toxins on the CRC/RyR function / Janos Almassy, Balazs Lukacs, Sandor Sarkozi, Istvan Jona
Dátum:2012
ISSN:0006-3495
Megjegyzések:It was shown previously that maurocalcin (MCa) induces long lasting subconductance states (LLSS) investigating the RyR function by single channel electrophysiology. These LLSSs are polarity and potential dependent and caused by the distinct positively charged surface formed by 5 amino acids corresponding to the peptide A binding site. We tested the effect of beta scorpion toxins - having a similar structure - on the RyR1 function. Charibdotoxin (CHTX) elicits close state at 20 nM in an all or none and voltage dependent manner because of smaller surface charge. Smaller size makes it easier to reach the most inner toxin binding site (out of the three) which causes the closure of the channel. MCa and CHTX share a common binding site which is identical to the peptide A binding site. Noxiustoxin has a similar effect at slightly higher toxin concentration. At nanomolar concentration Kaliotoxin evokes "flickering" of the channel in subconductance state which is occasionally interrupted by long lasting closed states, while locks the channel in closed state at micromolar concentration. Iberiotoxin induces a slight increase of the open probability accompanied by normal gating while Slotoxin has no effect. With the exception of MCa all toxins are effective only at one side, at the preferred side. Iberiotoxin and Slotoxin - ion spite of similar structure - have no large positive surfaces, they exhibit random surface charge distribution. A model has been proposed for the possible mode of action which accounts for the above effect of the tested toxins. Supported by Hungarian Research Found OTKA 81923.1563-PosB333
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
calcium release
Megjelenés:Biophysical Journal. - 102 : 3 (2012), p. 306a-307a. -
További szerzők:Lukács Balázs (1978-) (élettanász) Sárközi Sándor (1966-) (élettanász) Jóna István (1948-) (élettanász, fizikus)
Pályázati támogatás:81923
OTKA
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5.

001-es BibID:BIBFORM049383
Első szerző:Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:Apical Ca2+ activated K+ channels in mouse lacrimal acinar cells / Janos Almassy, David I. Yule
Dátum:2013
Megjegyzések:During the contraction of a skeletal muscle fiber an action potential running along the fiber surface membrane results in the conformational change of the dihydropyridine receptors which in turn causes the opening of the sarcoplasmic reticulum (SR) calcium channels (RyR1). Calcium ions - released from the SR through the channels ? increase the myoplasmic calcium concentration that finally evokes the contraction of the fibre. The decrease in the myoplasmic calcium concentration causing relaxation of the fiber is achieved by the action of the SR Ca2+-ATPase (SERCA).It's known from the literature and our earlier results that thymol and its structural analogues ? which are widely used in the food, cosmetic and pharmaceutical industry as preservatives ? have influence on the activity of the RyR1 and SERCA. Continuing our previous work our aim was to study the effect of further phenol derivatives on the SERCA.Light SR (LSR) vesicles were prepared from rabbit skeletal muscle (m. longissimus dorsi) containing the SR Ca2+-pump in their membrane. ATP dependent hydrolytic activity of LSR vesicles was measured using "coupled enzyme assay" at 37oC. Specific activity of SERCA was calculated after determination of the non-specific activity in the presence of 20 ?M cyclopiazonic acid which specifically blocks SERCA.Pump activities were plotted against the concentration values of different drugs, dots were fitted by Hill-equation revealing the following parametes:4-Chloro-meta-crezol IC50=167 ? 8 ?M, nHill ~3;5-Chloro-orho-crezol IC50=554 ? 45 ?M, nHill ~2,4-Chloro-ortho-crezol IC50=1370 ? 88 ?M, nHill ~8.Almost all the compounds investigated here inhibited the pump except cresol which didn't exert any effect in concentration range 0?3 mM. Other compounds inhibited SERCA activity, but affinity and the number of ligands differed from each other.Our results prove that phenol derivative structural analogues have an inhibitory effect on SERCA activity but this effect is significantly modified by the relative position of the different substituent groups and the presence of cloride is also required for inhibition. The alterations in the shape of the pi electron cloud caused by the different substituents can be also involved in the effect of these compounds.Supported by: OTKA 81923
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
calcium release
calcium pump
Lacrimal Acinar Cell
Megjelenés:Biophysical Journal. - 104 : 2 (2013), p. 474a. -
További szerzők:Yule, David I.
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6.

001-es BibID:BIBFORM049392
Első szerző:Csernoch László (élettanász)
Cím:The Low Affinity Calcium Buffer TPEN Alters Calcium Release From the Sarcoplasmic Reticulum (SR) of Mammalian Skeletal Muscle / Laszlo Csernoch, Cecilia Simut, János Almássy, Carole Jung, Ernst Niggli, István Jona
Dátum:2005
ISSN:0006-3495
Megjegyzések:Recent experiments suggested that chelating calcium within the SR using phosphate in the intracellular solution of skinned mammalian skeletal muscle fibers leads to the increase in the frequency of elementary calcium release events (ECRE) as observed under laser scanning confocal microscopy (Csernoch et al. 2003. Biophys. J. 84, 386a). To understand if this phenomenon was solely due to the buffering of intra SR calcium we incubated our saponin skinned, Fluo-4 loaded fibers with the low affinity membrane permeant buffer N,N,N',N'-tetrakis (2-pyridylmethyl)ethylene diamine (TPEN) and measured ECRE in the line-scan mode using a confocal scanner. In the concentration of 0.2 mM TPEN suppressed, rather than increased the frequency of ECRE sometimes to the point that no events were detectable. To determine whether this effect was due to chelating calcium or to a direct inhibition of ryanodine receptors (RyR1) by TPEN, the effects of the drug were studied on isolated RyR1-s incorporated into planar lipid bilayers. TPEN increased channel activity (open probability) at negative (cis compared to trans) holding potentials in a concentration and calcium dependent manner. In contrast, at positive holding potentials an inhibition was observed. Channel inhibition exhibited a voltage dependence resulting in a full inhibition at and above 40 mV. On the other hand, no potential dependence was observed when negative holding potentials were applied. In addition, the activity of the calcium pump was also inhibited by TPEN with a Kd of 639?44 ?M and a Hill coefficient of 0.87 ? 0.06. It is concluded that chelation alone of intra SR calcium will not increase ECRE frequency.This work was supported by OTKA T034894, T037727 and ETT 250/2003.
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
calcium release
Megjelenés:Biophysical Journal. - 88 : Supplement 2 (2005), p. 636a. -
További szerzők:Simut, Cecilia Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító) Jung, Carole Niggli, Ernst Jóna István (1948-) (élettanász, fizikus)
Pályázati támogatás:T037727
OTKA
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7.

001-es BibID:BIBFORM049385
Első szerző:Csernoch László (élettanász)
Cím:Estimation of Pore Geometry of RyR1 using Lanthanide Ruler / Laszlo Csernoch, Janos Almassy, Sandor Sarkozi, Balazs Lukacs, Istvan Jona
Dátum:2012
ISSN:0006-3495
Megjegyzések:It was shown previously that the Ca analogue Gd inhibits RyR1 gating symmetrically with a Kd about 5.5 microM and Hill coefficient (nH) of 4 both on cis and trans side using single channel electrophysiology. We further tested the RyR1-lanthanide interaction using two lanthanides - having an ionic radii between Ca2+ and Gd3+ - by bilayer measurements and ryanodine binding experiments. Cis inhibition of RyR1 by Eu was characterized by a binding constant of Kd=167?5 nM and an nH of 2?0.1 while trans inhibition exhibits Kd=4.8?0.2 microM and nN of 5.2?1.2. The inhibition constants for Sm on the cis side are Kd=64.3?2.5 nM and nH=2.2?0.2 while on the trans side Kd=6.15?0.13 microM and nH=4.68?0.45. Inhibition by Eu and Sm are potential and polarity dependent in contrast to Gd due to the differences in ionic radii of these lanthanides. Increasing the ionic radius from 0.938 (Gd) to 0.964 (Sm) increased the binding affinity from 5.6 microM to 64.3 nM revealing that the size of Ca binding pocket is only slightly higher than the ionic radius of Sm. Ryanodine (Ry) binding experiments revealed that lanthanides bind - at least partially - to the regulatory Ca binding site because the dose response curve of 3H Ry binding starts with an increase of Ry binding, which amounts to about 40% for Eu and 70% for Sm of basic Ry binding. A model has been proposed for one possible spatial arrangement of lanthanide and calcium binding sites of the RyR1 pore based on the ionic radii of Ca and the tested lanthanides. Supported by OTKA 81923.1557-PosB327
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
calcium release
Megjelenés:Biophysical Journal. - 102 : 3 Supplement (2012), p. 305a. -
További szerzők:Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító) Sárközi Sándor (1966-) (élettanász) Lukács Balázs (1978-) (élettanász) Jóna István (1948-) (élettanász, fizikus)
Pályázati támogatás:81923
OTKA
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8.

001-es BibID:BIBFORM049390
Első szerző:Jóna István (élettanász, fizikus)
Cím:Effect of maurocalcine on RyR1 and RyR2 is substantially different / Istvan Jona, Janos Almassy, Michel Ronjat, Balazs Lukacs
Dátum:2007
ISSN:0006-3495
Megjegyzések:Effect of a scorpion toxin (maurocalcine, MCa) on the RyR was studied using Müller-Rudin type bilayer. Canine cardiac SR calcium channel (RyR2) was isolated, solubilized and incorporated into lipid bilayer. Channel parameters were determined under voltage clamp conditions, using charge carrier of 250 mM KCl while ionized calcium buffered to 274 nM and 50 microM. It is shown that MCa evokes long lasting subconductance state (LLSS) events if the current is opposite of the physiological calcium movement - similarly to RyR1 (as prviously reported), but these events in case of RyR2 are more frequent [63.5 ? 5.7 versus 17.3 ? 2.7 in a minute] and about 10 times shorter [12 ? 0.9 sec versus 193 ? 14 ms] than in case of RyR1. During these LLSS events, the channel frequently goes into the close state - for a short period - end returns to the subconductance state. These intra-LLSS closings are longer for the RyR2-MCa interaction than for the RyR1-MCa interaction. The open probability (Po) - determined between the LLSS events - is also effected. In case of physiological current MCa does not evoke LLSS at all, however there is a slight increase of the open probability. Similarly to the RyR1, the effect of the toxin on RyR2 is voltage independent and its concentration dependence indicates one binding site. The MCa effect is calcium independent. These findings indicate that the region of the RyR2 which interacts with the 2-3 loop of the DHPR is different from that of the RyR1.
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
calcium release
Megjelenés:Biophysical Journal. - 91 : Suppl. (2007), p. 87a. -
További szerzők:Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító) Ronjat, Michel Lukács Balázs (1978-) (élettanász)
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9.

001-es BibID:BIBFORM004115
Első szerző:Lukács Balázs (élettanász)
Cím:Charged surface area of maurocalcine determines its interaction with the skeletal ryanodine receptor / Balazs Lukacs, Monika Sztretye, Janos Almassy, Sandor Sarkozi, Beatrix Dienes, Kamel Mabrouk, Cecilia Simut, Laszlo Szabo, Peter Szentesi, Michel De Waard, Michel Ronjat, Istvan Jona, Laszlo Csernoch
Dátum:2008
Megjegyzések:The 33 amino acid scorpion toxin maurocalcine (MCa) has been shown to modify the gating of the skeletal-type ryanodine receptor (RyR1). Here we explored the effects of MCa and its mutants ([Ala(8)]MCa, [Ala(19)]MCa, [Ala(20)]MCa, [Ala(22)]MCa, [Ala(23)]MCa, and [Ala(24)]MCa) on RyR1 incorporated into artificial lipid bilayers and on elementary calcium release events (ECRE) in rat and frog skeletal muscle fibers. The peptides induced long-lasting subconductance states (LLSS) on RyR1 that lasted for several seconds. However, their average length and frequency were decreased if the mutation was placed farther away in the 3D structure from the critical (24)Arg residue. The effect was strongly dependent on the direction of the current through the channel. If the direction was similar to that followed by calcium during release, the peptides were 8- to 10-fold less effective. In fibers long-lasting calcium release events were observed after the addition of the peptides. The average length of these events correlated well with the duration of LLSS. These data suggest that the effect of the peptide is governed by the large charged surface formed by residues Lys(20), Lys(22), Arg(23), Arg(24), and Lys(8). Our observations also indicate that the results from bilayer experiments mimic the in situ effects of MCa on RyR1.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biophysical Journal. - 95 : 7 (2008), p. 3497-3509. -
További szerzők:Sztretye Mónika (1981-) (élettanász, elektrofiziológus) Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító) Sárközi Sándor (1966-) (élettanász) Dienes Beatrix (1972-) (élettanász, molekuláris biológus) Mabrouk, Kamel Simut, Cecilia Szabó László (Románia) Szentesi Péter (1967-) (élettanász) De Waard, Michel Ronjat, Michel Jóna István (1948-) (élettanász, fizikus) Csernoch László (1961-) (élettanász)
Internet cím:elektronikus változat
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10.

001-es BibID:BIBFORM113945
035-os BibID:(Scopus)85168002058
Első szerző:Magyar Zsuzsanna Édua (molekuláris biológus)
Cím:Eu3+ detects two functionally distinct luminal Ca2+ binding sites in ryanodine receptors / Magyar Zsuzsanna É., Bauer Jacob, Bauerová-Hlinková Vladena, Jóna István, Gaburjakova Jana, Gaburjakova Marta, Almássy János
Dátum:2023
ISSN:0006-3495
Megjegyzések:Ryanodine receptors (RyRs) are Ca2+ release channels, gated by Ca2+ in the cytosol and the sarcoplasmic reticulum lumen. Their regulation is impaired in certain cardiac and muscle diseases. Although a lot of data is available on the luminal Ca2+ regulation of RyR, its interpretation is complicated by the possibility that the divalent ions used to probe the luminal binding sites may contaminate the cytoplasmic sites by crossing the channel pore. In this study, we used Eu3+, an impermeable agonist of Ca2+ binding sites, as a probe to avoid this complication and to gain more specific information about the function of the luminal Ca2+ sensor. Single-channel currents were measured from skeletal muscle and cardiac RyRs (RyR1 and RyR2) using the lipid bilayer technique. We show that RyR2 is activated by the luminal addition of Ca2+, whereas RyR1 is inhibited. These results were qualitatively reproducible using Eu3+. The luminal regulation of RyR1 carrying a mutation associated with malignant hyperthermia was not different from that of the wild-type. RyR1 inhibition by Eu3+ was extremely voltage dependent, whereas RyR2 activation did not depend on the membrane potential. These results suggest that the RyR1 inhibition site is in the membrane's electric field (channel pore), whereas the RyR2 activation site is outside. Using in silico analysis and previous results, we predicted putative Ca2+ binding site sequences. We propose that RyR2 bears an activation site, which is missing in RyR1, but both isoforms share the same inhibitory Ca2+ binding site near the channel gate.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Biophysical Journal. - 122 : 17 (2023), p. 3516-3531. -
További szerzők:Bauer, Jacob Bauerová-Hlinková, Vladena Jóna István (1948-) (élettanász, fizikus) Gaburjakova, Jana Gaburjakova, Marta Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító)
Pályázati támogatás:NKFIH FK144576
Egyéb
ÚNKP-22-4-I-DE-28
Egyéb
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11.

001-es BibID:BIBFORM069230
035-os BibID:(WoS)000402119300013 (Scopus)85019695207
Első szerző:Sárközi Sándor (élettanász)
Cím:Lanthanides Report Calcium Sensor in the Vestibule of Ryanodine Receptor / Sárközi Sándor, Komáromi István, Jóna István, Almássy János
Dátum:2017
ISSN:0006-3495
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Biophysical Journal. - 112 : 10 (2017), p. 2127-2137. -
További szerzők:Komáromi István (1957-) (vegyész, molekuláris biológus, biokémikus) Jóna István (1948-) (élettanász, fizikus) Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító)
Pályázati támogatás:PD 112199
OTKA
81923
OTKA
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12.

001-es BibID:BIBFORM049397
Első szerző:Szegedi Csaba
Cím:Effect of maurocalcine on the calcium release channel / Csaba Szegedi, János Almássy, Jan-Marc Sabatier, István Jóna
Dátum:2004
ISSN:0006-3495
Megjegyzések:The toxin Maurocalcine (MCa) isolated from scorpion Scorpio maurus palmatus contains 33 amino acids and three important disulphide bridges. This compound was chemically synthesized and its effect studied using purified RyR1 incorporated into bilayer under voltage clamp condition. Application of MCa on the cis side of the bilayer induces characteristic long lasting subconductance state (LLSSs), representing 60% of the full conductance. The channel spend 54.8% of the time in this LLSSs at 472 nM calcium using 50 nM of MCa. Duration distribution analysis reveals one single exponential component, showing 363?42 ms mean LLSS duration. Exchanging AA24 of MCa for alanine result in the loss of LLSSs. Exchanging AA23 of MCa for alanine result a decrease of the overall LLSS effect by several fold influencing the frequency and the duration of the LLSS in different way. The frequency and the duration of LLSS induced by wtMCa is polarity dependent, however still ohmic and the "inter LLSS" open probability is increased tenfold at 200 nM MCa concentrations. The first order concentration dependence of the mean duration of the LLSSs suggests one effective binding site per functional channel. Interestingly, exchanging AA22 of MCa for alanine result a decrease of the overall LLSS effect resulting about 686?31 ms mean duration at 200 nM 22MCa concentrations, accompanied by substantially lower frequency. The MCa treated RyR1 still sensitive for ryanodine showing three conductance levels corresponding to the closed, ryanodine effected and ryanodine + MCa affected states. Nor the wild type, nor the mutants altered the SERCA1 ATPase activity. Supported by EU (HPRN-CT-2002-00331) and by OTKA (037727).
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
calcium release
Megjelenés:Biophysical Journal. - 84 : Suppl. 2 (2004), p. 224a. -
További szerzők:Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító) Sabatier, Jean Marc Jóna István (1948-) (élettanász, fizikus)
Pályázati támogatás:T037727
OTKA
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