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FKBP12 Modulates Gating of the Ryanodine Receptor/Calcium Release Channela
Annals of the New York Academy of Sciences, 1998Excitation-contraction (EC) coupling in muscle requires the activation of intracellular calcium release channels (CRC). Four type 1 ryanodine receptor (RyR1) molecules form each tetrameric CRC. Each RyR1 contains a binding site for the FK506 binding protein (FKBP12), a cis-trans peptidyl-prolyl isomerase that is required for coordinated gating of the ...
K, Ondrias +3 more
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Calcium Release Channels (Ryanodine Receptors) and Arrhythmogenesis
2008Intracellular calcium release channels (ryanodine receptors, RyR) are present on the sarcoplasmic reticulum (SR) in cardiomyocytes and are required for excitation-contraction (EC) coupling in cardiac muscle. Each RyR channel consists of four pore-forming subunits that contain large cytoplasmic domains, which serve as scaffolds for proteins that ...
Subeena Sood, Xander H.T. Wehrens
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Expression and regulation of ryanodine receptor/calcium release channels
Trends in Cardiovascular Medicine, 1996Intracellular calcium release channels on the endoplasmic or sarcoplasmic reticula (ryanodine receptors, RyR, and inositol 1,4,5-trisphosphate receptors, IP(3)R) comprise a unique family of molecules that are structurally and functionally distinct from all other known ion channels.
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Membrane Topology and Membrane Retention of the Ryanodine Receptor Calcium Release Channel
Cell Biochemistry and Biophysics, 2004The ryanodine receptor (RyR) is a Ca2+ release channel located in the sarcoplasmic/endoplasmic reticulum (ER) membrane and plays a critical role in excitation-contraction coupling of skeletal and cardiac muscles. RyR normally exists in a tetrameric structure and contains two functional domains: a carboxyl-terminal hydrophobic domain that contains the ...
Jianjie, Ma +2 more
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Ryanodine Receptor Calcium Release Channels: An Evolutionary Perspective
2012Ryanodine receptors (RyRs), along with the related inositol 1,4,5-trisphosphate receptors (IP(3)Rs), mediate the release of Ca(2+) from intracellular organelles of eukaryotes. As discussed in other chapters, such increases in intracellular Ca(2+) levels act a fundamental second messenger, regulating a diverse array of cellular processes.
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Inactivation of the cardiac ryanodine receptor calcium release channel by nitric oxide
Cell Calcium, 1997We have recently reported [Mészáros L.G., Minarovic I., Zahradníková A. Inhibition of the skeletal muscle ryanodine receptor calcium release channel by nitric oxide. FEBS Lett 1996; 380: 49-52] that nitric oxide (NO) reduces the activity of the skeletal muscle ryanodine receptor Ca2+ release channel (RyRC), a principal component of the excitation ...
A, Zahradníková +3 more
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Regulation of the ryanodine receptor calcium release channel: a molecular complex system
Biophysical Chemistry, 1999Skeletal muscle contraction is regulated by Ca(2+) released from the sarcoplasmic reticulum (SR). The Ca(2+) release channel in the SR has been identified as the ryanodine receptor (RyR). Recently, it was found that the RyR is a large transmembrane protein that is regulated by many intrinsic factors. In this review, we mainly summarize our experimental
M, Kasai, T, Kawasaki, N, Yamaguchi
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The Ryanodine Receptor Family of Intracellular Calcium Release Channels
1995Publisher Summary Molecular studies have provided data on the nature and function of the intracellular calcium release channels. Two distinct classes of channels that mediate release of calcium from intracellular stores have been identified. The first is sensitive to InsP 3 and is referred to as the InsP 3 receptor family and the second is ...
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Characterization of the Calcium-release Channel/Ryanodine Receptor from Zebrafish Skeletal Muscle
Journal of Membrane Biology, 2001Calcium (Ca2+)-mediated signaling is fueled by two sources for Ca2+: Ca2+ can enter through Ca2+ channels located in the plasma membrane and can also be released from intracellular stores. In the present study the intracellular Ca2+ release channel/ryanodine receptor (RyR) from zebrafish skeletal muscle was characterized.
P, Koulen +3 more
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Biochemical and Biophysical Research Communications, 1995
In this study terminal cisternae vesicles from rabbit skeletal muscle were fused into planar bilayers and the effect of calmodulin on single Ca2+ release channel currents was investigated. In the presence of 10(-7) and 10(-9) M free [Ca2+], nanomolar concentrations of calmodulin activated the channel by increasing the open probability of single-channel
Buratti R +4 more
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In this study terminal cisternae vesicles from rabbit skeletal muscle were fused into planar bilayers and the effect of calmodulin on single Ca2+ release channel currents was investigated. In the presence of 10(-7) and 10(-9) M free [Ca2+], nanomolar concentrations of calmodulin activated the channel by increasing the open probability of single-channel
Buratti R +4 more
openaire +3 more sources