Molecular cloning of cDNA encoding the Ca2+ release channel (ryanodine receptor) of rabbit cardiac muscle sarcoplasmic reticulum.
Kinya Otsu,Huntington F. Willard,Vijay K. Khanna,Francesco Zorzato,N M Green,David H. MacLennan +5 more
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TL;DR: Analysis of predicted secondary structures and hydropathy plots suggests that the two isoforms exhibit the same topology in both transmembrane and cytoplasmic domains, and suggests that a modulator binding domain in the protein lies between residues 2619 and 3016.
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About: This article is published in Journal of Biological Chemistry. The article was published on 15 Aug 1990. and is currently open access. The article focuses on the topics: Ryanodine receptor & Ryanodine receptor 2.
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Citations
Alterations in Ryanodine Receptors and Related Proteins in Heart Failure
TL;DR: The specific proteins that alter the regulation of Ca(2+) during HF are discussed, including defects in RyR2-mediated SR Ca( 2+) release and the amplitude of CICR is reduced resulting in less force production during EC coupling.
44
Temporal differences in the induction of dihydropyridine receptor subunits and ryanodine receptors during skeletal muscle development.
TL;DR: The results imply that gene expression is a major mechanism that contributes to the regulation of DHP and ryanodine receptor numbers during muscle development and suggests that these genes are under the control of distinct endogenous factors.
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Ryanodine receptor arrays: not just a pretty pattern?
TL;DR: Recent data showing structural interactions between RyR oligomers in reconstituted arrays is described and it is suggested that this provides strong evidence for direct inter-RyR communication through a novel, allosteric regulatory mechanism.
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Personal recollections on the discovery of the ryanodine receptors of muscle.
TL;DR: This minireview is to present a personal account, from the vantage point the authors' laboratory, of the discovery, isolation, and characterization of the ryanodine receptors from mammalian muscle.
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Calmodulin modulation of proteins involved in excitation-contraction coupling.
TL;DR: Calmodulin binds to a region on RyR1 corresponding to amino acids 3614-3643 and to a regions in the carboxy-terminal tail of the L-type Ca2+ channel, suggesting that they represent more general protein-protein interaction motifs.
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