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Article

Structural determination of the phosphorylation domain of the ryanodine receptor.

The FEBS journal - 1 Oct 2012

Sharma Parveen, Ishiyama Noboru, Nair Usha, Li Wenping, Dong Aiping, Miyake Tetsuaki, Wilson Aaron, Ryan Tim, MacLennan David H, Kislinger Thomas, Ikura Mitsuhiko, Dhe-Paganon Sirano, Gramolini Anthony O

Abstract excerpt

The ryanodine receptor (RyR) is a large, homotetrameric sarcoplasmic reticulum membrane protein that is essential for Ca(2+) cycling in both skeletal and cardiac muscle. Genetic mutations in RyR1 are associated with severe conditions including malignant hyperthermia (MH) and central core disease. One phosphorylation site (Ser 2843) has been identified in a segment of RyR1 flanked by two RyR motifs, which are...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 22913516
DOI: 10.1111/j.1742-4658.2012.08755.x
PMCID: PMC3712973

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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