A drug and ATP binding site in type 1 ryanodine receptor
Structure, ISSN: 0969-2126, Vol: 30, Issue: 7, Page: 1025-1034.e4
2022
- 31Citations
- 26Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations31
- Citation Indexes31
- 31
- CrossRef25
- Captures26
- Readers26
- 26
Article Description
The ryanodine receptor (RyR)/calcium release channel on the sarcoplasmic reticulum (SR) is required for excitation-contraction coupling in skeletal and cardiac muscle. Inherited mutations and stress-induced post-translational modifications result in an SR Ca 2+ leak that causes skeletal myopathies, heart failure, and exercise-induced sudden death. A class of therapeutics known as Rycals prevent the RyR-mediated leak, are effective in preventing disease progression and restoring function in animal models, and are in clinical trials for patients with muscle and heart disorders. Using cryogenic-electron microscopy, we present a model of RyR1 with a 2.45-Å resolution before local refinement, revealing a binding site in the RY1&2 domain (3.10 Å local resolution), where the Rycal ARM210 binds cooperatively with ATP and stabilizes the closed state of RyR1.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S096921262200137X; http://dx.doi.org/10.1016/j.str.2022.04.010; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85133465903&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/35580609; https://linkinghub.elsevier.com/retrieve/pii/S096921262200137X; https://dx.doi.org/10.1016/j.str.2022.04.010
Elsevier BV
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