ArticleThe Journal of biological chemistry2005
Localization of a disease-associated mutation site in the three-dimensional structure of the cardiac muscle ryanodine receptor.
Article in The Journal of biological chemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.
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Who cites it
27 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Calcium and arrhythmogenesis.Physiological reviews · 2007Pooled it
- Loss of SPEG Inhibitory Phosphorylation of Ryanodine Receptor Type-2 Promotes Atrial Fibrillation.Circulation · 2020Article
- Single-particle cryo-EM of the ryanodine receptor channel in an aqueous environment.European journal of translational myology · 2015Article
- TRP channels as sensors of oxygen availability.Pflugers Archiv : European journal of physiology · 2013Review
- Ligand-dependent conformational changes in the clamp region of the cardiac ryanodine receptor.The Journal of biological chemistry · 2013Article
- FRET-based localization of fluorescent protein insertions within the ryanodine receptor type 1.PloS one · 2012Article
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- Localization of the dantrolene-binding sequence near the FK506-binding protein-binding site in the three-dimensional structure of the ryanodine receptor.The Journal of biological chemistry · 2011Article
- Ryanodine receptors: structure, expression, molecular details, and function in calcium release.Cold Spring Harbor perspectives in biology · 2010Review
- Dissociation of calmodulin from cardiac ryanodine receptor causes aberrant Ca(2+) release in heart failure.Cardiovascular research · 2010Article
- Dynamic, inter-subunit interactions between the N-terminal and central mutation regions of cardiac ryanodine receptor.Journal of cell science · 2010Article
- Catecholaminergic polymorphic ventricular tachycardia is caused by mutation-linked defective conformational regulation of the ryanodine receptor.Circulation research · 2010Article
- Defective calmodulin binding to the cardiac ryanodine receptor plays a key role in CPVT-associated channel dysfunction.Biochemical and biophysical research communications · 2010Article
- Luminal Ca(2+) activation of cardiac ryanodine receptors by luminal and cytoplasmic domains.European biophysics journal : EBJ · 2009Review
- The RYR2-encoded ryanodine receptor/calcium release channel in patients diagnosed previously with either catecholaminergic polymorphic ventricular tachycardia or genotype negative, exercise-induced long QT syndrome: a comprehensive open reading frame mutational analysis.Journal of the American College of Cardiology · 2009Article
- Förster resonance energy transfer measurements of ryanodine receptor type 1 structure using a novel site-specific labeling method.PloS one · 2009Article
- Ryanodine receptor-mediated arrhythmias and sudden cardiac death.Pharmacology & therapeutics · 2009Review
- CLIC2-RyR1 interaction and structural characterization by cryo-electron microscopy.Journal of molecular biology · 2009Article
- Ryanodine receptor structure: progress and challenges.The Journal of biological chemistry · 2009Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The cardiac muscle ryanodine receptor (RyR2) functions as a calcium release channel in the heart. Up to 40 mutations in RyR2 have been linked to genetic forms of sudden cardiac death. These mutations are largely clustered in three regions of the sequence of the polypeptide: one near the N terminus, one in the central region, and the third in the C-terminal region. The central region includes 11 mutations, and an isoleucine-proline motif (positions 2427 and 2428) in the same region is predicted to contribute to the binding of FKBP12.6 protein. We have mapped the central mutation site in the three-dimensional structure of RyR2 by green fluorescent protein insertion, cryoelectron microscopy, and single-particle image processing. The central mutation site was mapped to a "bridge" of density that connects cytoplasmic domains 5 and 6, which have been suggested to undergo conformational changes during channel gating. Moreover, the location of this central mutation site is not close to that of the FKBP12.6-binding site mapped previously by cryoelectron microscopy.
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Registered trials
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