The ryanodine receptor/Ca2+ release channel
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چکیده
منابع مشابه
Nitric oxide and the ryanodine receptor Ca-release channel.
Nitric Oxide and the Ryanodine Receptor Ca-Release Channel To the Editor: I have read with interest the recent review on the role of S-nitrosylation in cardiovascular signaling, in which Lima et al1 provide a very useful digest on the current status of research in this important but burgeoning field of cardiovascular physiology. On the other hand, I believe that one of the many functions of a s...
متن کاملRedox regulation of the ryanodine receptor/calcium release channel.
The RyR (ryanodine receptor)/calcium release channel contains a number of highly reactive thiol groups that endow it with redox sensitivity. In general, oxidizing conditions favour channel opening, while reducing conditions have the opposite effect. Thiol modification affects the channel sensitivity to its principal effectors, Ca2+, Mg2+ and ATP, and alters RyR protein interactions. Here, we gi...
متن کاملModification of ryanodine receptor/Ca2+ release channel with dinitrofluorobenzene.
Modification of the ryanodine receptor (RyR)/Ca(2+) release channel with 2,4-dinitrofluorobenzene (DNFB) indicated that two classes of amino group interact with the reagent, as can be distinguished on the basis of their reactivity/accessibility and the effects on ryanodine binding and single channel activities. One group interacted very rapidly (t(1/2)<30 s) at 25 degrees C with low concentrati...
متن کاملResidue Gln within a Predicted Transmembrane Sequence of the Ca Release Channel (Ryanodine Receptor) Is Critical for Ryanodine Interaction*
From the ‡Cardiovascular Research Group, Departments of Physiology and Biophysics and of Biochemistry and Molecular Biology, University of Calgary, Calgary, Alberta T2N 4N1, Canada, the §Department of Chemistry, University of Sherbrooke, Sherbrooke, Quebec J1K 2R1, Canada, the ¶Department of Biochemistry, University of Nevada School of Medicine, Reno, Nevada 89557, and Cardiac Medicine, Nationa...
متن کاملResidue Gln4863 within a predicted transmembrane sequence of the Ca2+ release channel (ryanodine receptor) is critical for ryanodine interaction.
Despite the pivotal role of ryanodine in ryanodine receptor (RyR) research, the molecular basis of ryanodine-RyR interaction remains largely undefined. We investigated the role of the proposed transmembrane helix TM10 in ryanodine interaction and channel function. Each amino acid residue within the TM10 sequence, 4844IIFDITFFFFVIVILLAIIQGLII4867, of the mouse RyR2 was mutated to either alanine ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1993
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)85166-9