ReviewCold Spring Harbor perspectives in biology2010
Ryanodine receptors: structure, expression, molecular details, and function in calcium release.
Review in Cold Spring Harbor perspectives in biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 422 papers.
What it found
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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
422 citing papers in PubMed, 791 citations in OpenAlex.
- Remimazolam-Based Total Intravenous Anesthesia for Cardiac Surgery in an Infant With a Pathogenic RYR1 Variant.Journal of medical cases · 2026Article
- The nonexcitable smooth muscle: remodeling the smooth muscle ion transport toolkit in disease.Physiological reviews · 2026Review
- An INF2-dependent actin-mediated step in inositol 1,4,5-trisphosphate receptor cluster formation and activity.Current biology : CB · 2026Article
- VMP1 forms a CaScience advances · 2026Article
- HuR-dependent expression of RyR2 contributes to calcium-mediated thermogenesis in murine brown adipocytes.Scientific reports · 2026Article
- Ablation of ACSS2 drives alteration to cardiac and hepatic proteomic landscapes in a tissue- and sex-specific manner.Journal of proteomics · 2026Article
- Phage RyR-domain proteins degrade ADPR-based immune signals and fuel NADbioRxiv : the preprint server for biology · 2026Article
- Serum proteomic signatures and an immune-calcium signaling cascade associated with antipsychotic-related erectile dysfunction in schizophrenia.Scientific reports · 2026Article
- Article
- A single-cell multiomic analysis identifies molecular and gene-regulatory mechanisms dysregulated in developing Down syndrome neocortex.Science (New York, N.Y.) · 2026Article
- Intracellular calcium handling dysfunction contributes to behavioural deficits leading to mortality of honey bees after acute contact exposure to the insecticide cyantraniliprole.Scientific reports · 2026Article
- Review
- Gne-Depletion in C2C12 Myoblasts Leads to Alterations in Glycosylation and Myopathogene Expression.Cells · 2026Article
- Case Report: RYR1-related myopathy with hypoxic ischemic encephalopathy-a case of severe neonatal presentation due to aFrontiers in pediatrics · 2026Article
- Lipid Metabolism in Relation to Calcium Homeostasis.Advances in experimental medicine and biology · 2026Review
- Ryanodine-1-Calstabin Complex Stabilizers in Antidoping Research: Synthesis, Metabolism, and Characterization.ChemPlusChem · 2026Article
- Gut microbeFrontiers in immunology · 2026Article
- Monocellular and Multicellular Parasites Infesting Humans: A Review of Calcium Ion Mechanisms.Biomedicines · 2025Review
- Adaptation without Dominance in Pseudomonas syringae Pathovars.Microbial ecology · 2025Article
- Potentiation of ryanodine receptor-mediated calcium release by MAPK is responsible for epidermal transformation and carcinogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
362 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ryanodine receptors (RyRs) are located in the sarcoplasmic/endoplasmic reticulum membrane and are responsible for the release of Ca(2+) from intracellular stores during excitation-contraction coupling in both cardiac and skeletal muscle. RyRs are the largest known ion channels (> 2MDa) and exist as three mammalian isoforms (RyR 1-3), all of which are homotetrameric proteins that interact with and are regulated by phosphorylation, redox modifications, and a variety of small proteins and ions. Most RyR channel modulators interact with the large cytoplasmic domain whereas the carboxy-terminal portion of the protein forms the ion-conducting pore. Mutations in RyR2 are associated with human disorders such as catecholaminergic polymorphic ventricular tachycardia whereas mutations in RyR1 underlie diseases such as central core disease and malignant hyperthermia. This chapter examines the current concepts of the structure, function and regulation of RyRs and assesses the current state of understanding of their roles in associated disorders.
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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.