ArticleThe Journal of general physiology2002
Interdomain interactions within ryanodine receptors regulate Ca2+ spark frequency in skeletal muscle.
Article in The Journal of general physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
23 citing papers in PubMed, 53 citations in OpenAlex.
- Article
- FKBP12 binds to the cardiac ryanodine receptor with negative cooperativity: implications for heart muscle physiology in health and disease.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023Article
- Molecular Changes in the Cardiac RyR2 With Catecholaminergic Polymorphic Ventricular Tachycardia (CPVT).Frontiers in physiology · 2022Article
- CaTrends in biochemical sciences · 2017Review
- Mice expressing T4826I-RYR1 are viable but exhibit sex- and genotype-dependent susceptibility to malignant hyperthermia and muscle damage.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012Article
- Effects of conformational peptide probe DP4 on bidirectional signaling between DHPR and RyR1 calcium channels in voltage-clamped skeletal muscle fibers.Biophysical journal · 2011Article
- Dynamic, inter-subunit interactions between the N-terminal and central mutation regions of cardiac ryanodine receptor.Journal of cell science · 2010Article
- Bioinformatic mapping and production of recombinant N-terminal domains of human cardiac ryanodine receptor 2.Protein expression and purification · 2010Article
- Ubiquitous SPRY domains and their role in the skeletal type ryanodine receptor.European biophysics journal : EBJ · 2009Review
- Ryanodine receptor-mediated arrhythmias and sudden cardiac death.Pharmacology & therapeutics · 2009Review
- Alternative splicing of RyR1 alters the efficacy of skeletal EC coupling.Cell calcium · 2009Article
- Modulation of the local SR Ca2+ release by intracellular Mg2+ in cardiac myocytes.The Journal of general physiology · 2008Article
- Structural and functional characterization of ryanodine receptor-natrin toxin interaction.Biophysical journal · 2008Article
- Postulated role of interdomain interaction between regions 1 and 2 within type 1 ryanodine receptor in the pathogenesis of porcine malignant hyperthermia.The Biochemical journal · 2007Article
- Malignant hyperthermia mutation sites in the Leu2442-Pro2477 (DP4) region of RyR1 (ryanodine receptor 1) are clustered in a structurally and functionally definable area.The Biochemical journal · 2007Article
- Sorcin modulation of Ca2+ sparks in rat vascular smooth muscle cells.The Journal of physiology · 2006Article
- Effects of peptide C corresponding to the Glu724-Pro760 region of the II-III loop of the DHP (dihydropyridine) receptor alpha1 subunit on the domain- switch-mediated activation of RyR1 (ryanodine receptor 1) Ca2+ channels.The Biochemical journal · 2006Article
- Novel regulators of RyR Ca2+ release channels: insight into molecular changes in genetically-linked myopathies.Journal of muscle research and cell motility · 2006Review
- Differential effects of maurocalcine on Ca2+ release events and depolarization-induced Ca2+ release in rat skeletal muscle.The Journal of physiology · 2005Article
- Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM.Nature structural & molecular biology · 2005Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
DP4 is a 36-residue synthetic peptide that corresponds to the Leu(2442)-Pro(2477) region of RyR1 that contains the reported malignant hyperthermia (MH) mutation site. It has been proposed that DP4 disrupts the normal interdomain interactions that stabilize the closed state of the Ca(2)+ release channel (Yamamoto, T., R. El-Hayek, and N. Ikemoto. 2000. J. Biol. Chem. 275:11618-11625). We have investigated the effects of DP4 on local SR Ca(2)+ release events (Ca(2)+ sparks) in saponin-permeabilized frog skeletal muscle fibers using laser scanning confocal microscopy (line-scan mode, 2 ms/line), as well as the effects of DP4 on frog SR vesicles and frog single RyR Ca(2)+ release channels reconstituted in planar lipid bilayers. DP4 caused a significant increase in Ca(2)+ spark frequency in muscle fibers. However, the mean values of the amplitude, rise time, spatial half width, and temporal half duration of the Ca(2)+ sparks, as well as the distribution of these parameters, remained essentially unchanged in the presence of DP4. Thus, DP4 increased the opening rate, but not the open time of the RyR Ca(2)+ release channel(s) generating the sparks. DP4 also increased [(3)H]ryanodine binding to SR vesicles isolated from frog and mammalian skeletal muscle, and increased the open probability of frog RyR Ca(2)+ release channels reconstituted in bilayers, without changing the amplitude of the current through those channels. However, unlike in Ca(2)+ spark experiments, DP4 produced a pronounced increase in the open time of channels in bilayers. The same peptide with an Arg(17) to Cys(17) replacement (DP4mut), which corresponds to the Arg(2458)-to-Cys(2458) mutation in MH, did not produce a significant effect on RyR activation in muscle fibers, bilayers, or SR vesicles. Mg(2)+ dependence experiments conducted with permeabilized muscle fibers indicate that DP4 preferentially binds to partially Mg(2)+-free RyR(s), thus promoting channel opening and production of Ca(2)+ sparks.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.