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1.

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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2.

001-es BibID:BIBFORM004134
Első szerző:Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:Effects of K-201 on the calcium pump and calcium release channel of rat skeletal muscle / Janos Almassy, Monika Sztretye, Balazs Lukacs, Beatrix Dienes, Laszlo Szabo, Peter Szentesi, Guy Vassort, Laszlo Csernoch, Istvan Jona
Dátum:2008
ISSN:0031-6768
Megjegyzések:The benzothiazepine derivative K-201 has been suggested as a potential therapeutic agent due to its antiarrhythmogenic action. To understand how the drug alters calcium release from the sarcoplasmic reticulum (SR), we investigated its effects on the SR calcium channel and calcium pump by single channel electrophysiology, whole-cell confocal microscopy, and ATPase activity measurements on control and post-myocardial infarcted (PMI) rat skeletal muscle. In bilayers, K-201 induced two subconductance states corresponding to approximately 24% (S(1)) and approximately 13% (S(2)) of the maximum conductance. Dependence of event frequency and of time spent in S(1) and S(2) on the drug concentration was biphasic both in control and in PMI rats, with a maximum at 50 microM. At this concentration, the channel spends 26 +/- 4% and 24 +/- 4%, respectively, of the total time in these subconductance states at positive potentials, while no subconductances are observed at negative potentials. K-201 altered the frequency of elementary calcium release events: spark frequency decreased from 0.039 +/- 0.001 to 0.023 +/- 0.001 s(-1) sarcomere(-1), while the frequency of embers increased from 0.011 +/- 0.001 to 0.023 +/- 0.001 s(-1) sarcomere(-1). Embers with different amplitude levels were observed after the addition of the drug. K-201 inhibited the Ca(2+) ATPase characterized by IC(50,contr) = 119 +/- 21 muM and n (Hill,contr) = 1.84 +/- 0.48 for control and IC(50,PMI) = 122 +/- 18 microM and n (Hill,PMI) = 1.97 +/- 0.24 for PMI animals. These results suggest that although K-201 would increase the appearance of subconductance states, the overall calcium release is reduced by the drug. In addition, the effect of K-201 is identical on calcium release channels from control and PMI rats.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Pflügers Archiv. - 457 : 1 (2008), p. 171-183. -
További szerzők:Sztretye Mónika (1981-) (élettanász, elektrofiziológus) Lukács Balázs (1978-) (élettanász) Dienes Beatrix (1972-) (élettanász, molekuláris biológus) Szabó László (Románia) Szentesi Péter (1967-) (élettanász) Vassort, Guy Csernoch László (1961-) (élettanász) Jóna István (1948-) (élettanász, fizikus)
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elektronikus változat
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3.

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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DOI
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4.

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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5.

001-es BibID:BIBFORM049406
Első szerző:Lukács Balázs (élettanász)
Cím:Effects of natural derivatives of phenol on calcium transport of sarcoplasmic reticulum / B. Lukacs, G. Nagy, N. Dobrosi, I. Gherasim, I. Jona
Dátum:2005
Megjegyzések:The effect of natural derivatives of phenol was investigated on sarcoplasmic reticulum calcium pump (SERCA) isolated from rabbit and calcium release channel (RyR1) isolated from normal and malignant hyperthermia susceptible pig (MHS) skeletal muscle. SERCA activity was determined using ♭coupled enzyme method', the decrease of NADH concentration was followed photometrically. The effects of some of these agents on the calcium release and on the 3H ryanodine binding were investigated too. Thymol and trans-anethole inhibited the Ca2+ATPase with a Kd of 224?10 lM and 168?10 lM, respectively. The vanillin, orthovanillin, 4-methyl-2-nitrophenol, meta-anisaldehyde and cineole exerted only unspecific inhibition. In calcium release measurements, the thymol and the carvacrol activated the channel with a Kd of 158?16 lM and 211?55 lM, respectively. In binding assay experiments the thymol activated both the MHS and wild type RyR1. The MHS type RyR1 showed lower Kd to ryanodine and could bind more ryanodine than the normal type RyR1both in control and in the presence of thymol.
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
calcium release
Megjelenés:Journal of Muscle Research and Cell Motility. - 26 (2005), p. 61. -
További szerzők:Nagy G. Dobrosi Nóra (1981-) (molekuláris biológus) Gherasim, Iuliana Jóna István (1948-) (élettanász, fizikus)
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6.

001-es BibID:BIBFORM049379
Első szerző:Lukács Balázs (élettanász)
Cím:Effect of maurocalcine on the skeletal type ryanodine receptor / Lukacs B., Sarkozi S., Almassy J., Jona I.
Dátum:2012
Megjegyzések:Maurocalcine (MCa) is a 33 amino acid long scorpion toxin which shows high homology with dihydropyridine receptor constituent peptide-A (pepA). The latter is believed to directly interact with ryanodine receptor (RyR1) and plays important role in the electromechanical coupling. The position and the positive charge of given amino acids residues of MCa are determinative in this interaction.We studied the effect of pepA and potassium ion on the MCa evoked Long Lasting Subconductance State (LLSS) type RyR1 operation assuming that both of them may have access to MCa binding sites of the channel. To investigate the binding of these peptides to RyR1, we used heavy sarcoplasmic reticulum vesicles (HSR) and CHAPS solubilized ryanodine receptor complex of rabbit skeletal muscle. Gating of RyR1 was monitored on channels incorporated into a planar lipid bilayer under voltage clamp conditions. Ca2+-release measurements were performed on HSR, where changes in extravesicular Ca2+ concentration were followed as changes in the absorption of APIII Ca2+-sensitive dye (?=710 nm).In single channel experiments LLSS type RyR1 gating was evoked applying of 5 and 10 nM MCa in the cytoplasmic side of the channel. The length and frequency of the characteristic subconductance states gradually ceased by consecutively added K+. The half effective concentration of K+ was higher at 10 nM MCa concentration which refers to a possible competition between MCa and potassium ion in biding to the same site on RyR1. A similar competitive-like effect of pepA was observed, when in the presence of 26 ?M pepA, much higher concentration of MCa was able to evoke LLSSs. In Ca2+ release measurements 5 nM MCa induced Ca2+-release at 100 mM K+, but release was completely eliminated at 250 mM K+. High concentration of K+inhibited only the MCa induced Ca2+-release but had no effect on the 4-CMC induced Ca2+-release suggesting specific effect of K+ on MCa-RyR1 interaction. Suppression of release in the presence of 250 mM K+ was inhibited by addition of higher concentration of MCa suggesting charge driven interaction between MCa and RyR1.Our data put forward a possible mode of MCa action with 3 binding sites at the cytosolic side on RyR1. The first binding site located on the surface of the channel, and is responsible for the Po increase at low MCa concentration. The second binding site in the pore of the channel induces potential- and voltage dependent LLSS-s at higher toxin concentration. Occupy of third one which located presumably in the pore, close to the selectivity filter results in closed states of RyR1.Supported by: OTKA 81923
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
calcium release
Megjelenés:Acta Physiologica. - 205 : Suppl. 690 (2012), 26. p. -
További szerzők:Sárközi Sándor (1966-) (élettanász) Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító) Jóna István (1948-) (élettanász, fizikus)
Pályázati támogatás:81923
OTKA
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7.

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
elektronikus változat
DOI
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8.

001-es BibID:BIBFORM052874
Első szerző:Nagy Miklós (vegyész)
Cím:Glükóz oldalláncokat tartalmazó poli(naftalén-fenilén) fényemittáló kopolimer előállítása és vizsgálata / Nagy Miklós, Rácz Dávid, Daróczi Lajos, Lukács Balázs, Jóna István, Zsuga Miklós, Kéki Sándor
Dátum:2011
ISSN:0027-2914
Tárgyszavak:Orvostudományok Elméleti orvostudományok magyar nyelvű folyóiratközlemény hazai lapban
Egészség- és Környezettudomány
Megjelenés:Műanyag és Gumi. - 48 : 12 (2011), p. 456-461. -
További szerzők:Rácz Dávid (1987-) (vegyész) Daróczi Lajos (1965-) (fizikus) Lukács Balázs (1978-) (élettanász) Jóna István (1948-) (élettanász, fizikus) Zsuga Miklós (1944-) (polimer kémikus) Kéki Sándor (1964-) (polimer kémikus)
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Multimodális képalkotás
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9.

001-es BibID:BIBFORM041437
035-os BibID:WOS:000315759900028
Első szerző:Nagy Miklós (vegyész)
Cím:A new and simple polycondensation method for the synthesis of sulfur-linked isoindole-phenylene based blue light-emitting copolymers / Miklós Nagy, Dávid Rácz, Pál Herczegh, Gyula Batta, György Deák, Balázs Lukács, István Jóna, Miklós Zsuga, Sándor Kéki
Dátum:2013
ISSN:0014-3057
Megjegyzések:New isoindole containing blue light-emitting copolymers, poly[(1,2-isoindolene)-(1-sulfane-4-phenylene)] and poly[(1,2-isoindolene)-(1-sulfane-3-phenylene)] were prepared by a simple polycondensation method between ortho-phthalaldehyde and para-, or meta-aminothiophenol. The reaction proceeds under mild conditions, giving pure copolymers with high yields and does not require a catalyst. The formation of both linear and cyclic products was observed. The polymerization is largely solvent dependent and the maximum obtainable molecular weight is limited by the solubility of the copolymers. Detailed NMR study revealed orthogonal sigma?pi interactions between the chain segments of the 1,4-copolymer. The optical properties were also studied and it was found that both copolymers emitted blue light in solution with relatively narrow emission band. Unlike their simple isoindole derivatives, the copolymers proved to be stable for several weeks and can serve as model compounds for the synthesis of new and versatile isoindole-containing light-emitting polymers.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Copolymer
Isoindole
Light-emitting polymer
Polycondensation
Conjugated polymers
Doktori iskola
egyetemen (Magyarországon) készült közlemény
Megjelenés:European Polymer Journal. - 49 : 2 (2013), p. 549-557. -
További szerzők:Rácz Dávid (1987-) (vegyész) Deák György (1954-) (polimer kémikus) Lukács Balázs (1978-) (élettanász) Jóna István (1948-) (élettanász, fizikus) Zsuga Miklós (1944-) (polimer kémikus) Herczegh Pál (1947-) (vegyész, antibiotikumkémikus) Batta Gyula (1953-) (molekula-szerkezet kutató) Kéki Sándor (1964-) (polimer kémikus)
Pályázati támogatás:K-72524
OTKA
K-79126
OTKA
K-101850
OTKA
T-81923
OTKA
TÁMOP-4.2.2/B-10/1-2010-0024
TÁMOP
Fizikai Tudományok Doktori Iskola
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10.

001-es BibID:BIBFORM018654
035-os BibID:(WOS)000294229700007
Első szerző:Nagy Miklós (vegyész)
Cím:Synthesis and characterization of an amphiphilic blue?light?emitting glycosylated poly(naphthalene/phenylene) copolymer / Miklós Nagy, Dávid Rácz, Lajos Daróczi, Balázs Lukács, István Jóna, Miklós Zsuga, Sándor Kéki
Dátum:2011
ISSN:1022-1352
Megjegyzések:The preparation and self-assembly of poly(2-glucopyranosyl-1,6-naphthalene-1,4-phenylene), P16NP2Glu, an amphiphilic, blue-light-emitting copolymer, is reported. The copolymer is soluble in polar solvents such as methanol/THF mixtures and even in water. The emission spectrum of P16NP2Glu shows a maximum at approximate to 400 nm for solutions containing the above solvents. Owing to the highly polar nature of the glucopyranose rings of P16NP2Glu, the formation of aggregates is observed. Uniform-size nanospheres capable of emitting blue light are prepared in the solid phase. The critical micelle concentration and micelle sizes are determined by light-scattering measurements. It is found that the emission maximum and fluorescence quantum yields depend on the aggregate formation of the copolymer.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Fizikai-, Számítás- és Anyagtudomány
glucose
light emission
nanoparticles
naphthalene
self assembly
Megjelenés:Macromolecular Chemistry And Physics. - 212 : 17 (2011), p. 1891-1899. -
További szerzők:Rácz Dávid (1987-) (vegyész) Daróczi Lajos (1965-) (fizikus) Lukács Balázs (1978-) (élettanász) Jóna István (1948-) (élettanász, fizikus) Zsuga Miklós (1944-) (polimer kémikus) Kéki Sándor (1964-) (polimer kémikus)
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Kémiai anyagtudományi csoport
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11.

001-es BibID:BIBFORM049380
Első szerző:Sárközi Sándor (élettanász)
Cím:Altered modulation of the skeletal type ryanodine receptor / calcium release channel by ATP in malignant hyperthermia / Sarkozi S., Lukacs B., Bardi M., Jona I.
Dátum:2012
Megjegyzések:We have shown previously that the activity of the Ryanodine Receptor / Calcium release channel (RyR/CRC) is modulated by ATP. Increasing ATP concentration results in an increase of open probability of the RyR/CRC and the dose response curve of the phenomena is biphasic having two distinctive activatory processes. The amplitude ratio of the two steps are 1:3 suggesting strong cooperation between the ATP binding sites and independent but cooperative binding of the ATP on the RyR1 monomers. It was also shown by several laboratories that mutations leading to malignant hyperthermia (MH) also increases the calcium sensitivity of the channel. Our aim was to test whether the ATP pharmacology is affected in MH and if this is the case in what way.Heavy SR vesicle was prepared as described previously using longissimus dorsi of a swine (Pietrin strain), which carries an MH causing homozygous arg615cysmutation. Following CHAPS+lipid solubilization, the functional RyR1 tetramer - the channel complex - was incorporated into a lipid bilayer. The bathing medium contained symmetrical 250 mM KCl ? 20mM PIPES ? pH:7.4. Free (ionized) calcium concentration was established using Ca-EGTA calcium buffer, calculated by Fabiato's method. Under voltage clamp conditions the channel current was recorded and the channel parameters were determined: such as open probability (Po), mean open time and specific conductance. The ATP pharmacology of the RyR/CRC was determined using 50 ?M Ca2+ free trans and 472 nM Ca2+ free cis, applying increasing Na2ATP concentration on the cis side.The mutant channel showed higher open probability compared to the wild type even in the absence of ATP. The mean open time was slightly higher in the mutant, but not significantly different from the wt. The ATP pharmacology of the mutant channel was different from the wt: the pronounced two phases disappeared from the ATP dependence of the open probability function. The increase of the open probability has two components: the mean open time increased significantly above 100 ?M, and the number of open events increased even more pronounced above 150 ?M ATP. The majority of the Po increase was attributed to the increase of the number of open events. All point histograms showed clearly two peaks without a trace of subconductance state: meaning that the synchrony of the four RyR1 monomers has not been changed due to the given mutation.Supported by: OTKA 81923
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
calcium release
Megjelenés:Acta Physiologica. - 205 : Suppl. 690 (2012), p. L9. -
További szerzők:Lukács Balázs (1978-) (élettanász) Bárdi Miklós Jóna István (1948-) (élettanász, fizikus)
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12.

001-es BibID:BIBFORM049070
Első szerző:Sárközi Sándor (élettanász)
Cím:Effect of gadolinium on the ryanodine receptor/sarcoplasmic reticulum calcium release channel of skeletal muscle / Sándor Sárközi, Csaba Szegedi, Balázs Lukács, Michel Ronjat, István Jóna
Dátum:2005
ISSN:1742-464X
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Febs Journal. - 272 : 2 (2005), p. 464-471. -
További szerzők:Szegedi Csaba Lukács Balázs (1978-) (élettanász) Ronjat, Michel Jóna István (1948-) (élettanász, fizikus)
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DOI
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