The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Ryanodine Receptors: Structure, Expression, Molecular Details, and Function in Calcium Release
Open accessAbstract
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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Cites
Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor
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Schäffer, D. E., Iyer, L. M., Burroughs, A. M., & Aravind, L. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00034 · Cited by 20
Ryanodine receptor inhibitor dantrolene reduces hypoxic-ischemic brain injury in neonatal mice
Ovcjak, A., Xiao, A., Kim, J.-S., Xu, B., Szeto, V., Turlova, E., Abussaud, A., Chen, N.-H., Miller, S. P., Sun, H.-S., et al. (2022) · Experimental Neurology · doi:10.1016/j.expneurol.2022.113985 · Cited by 16
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Metadata
- Authors
- Lanner, J. T., Georgiou, D. K., Joshi, A. D., & Hamilton, S. L.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2010-10-20
- Volume
- 2
- Issue
- 11
- Pages
- a003996-a003996
- ISSN
- 1943-0264 (ISSN-L)
- OpenAlex
- W2116635624
- Cited by
- 818
- References
- 2
- Type
- posted content
- Language
- en
- Open access
- bronze
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