{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sun QA"],"funding":["NHLBI NIH HHS","National Institutes of Health","National Heart Lung and Blood Institute"],"pagination":["150163"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12651786"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["723"],"pubmed_abstract":["Excitation-contraction coupling in skeletal muscle myofibers depends upon Ca<sup>2+</sup> release from the sarcoplasmic reticulum through the ryanodine receptor/Ca<sup>2+</sup>-release channel RyR1. The RyR1 contains ∼100 Cys thiols of which ∼30 comprise an allosteric network subject to posttranslational modification by S-nitrosylation, S-palmitoylation and S-oxidation. However, the role and function of these modifications is not understood. Although aberrant S-nitrosylation of multiple unidentified sites has been associated with dystrophic diseases, malignant hyperthermia and other myopathic syndromes, S-nitrosylation in physiological situations is reportedly specific to a single (1 of ∼100) Cys in RyR1, Cys<sup>3636</sup> in a manner gated by pO<sub>2</sub>. Using mice expressing a form "],"journal":["Biochemical and biophysical research communications"],"pubmed_title":["Physiological role for S-nitrosylation of RyR1 in skeletal muscle function and development."],"pmcid":["PMC12651786"],"funding_grant_id":["R01 HL059130","RO1 HL0591130"],"pubmed_authors":["Hess DT","Plummer BN","Premont RT","Sun QA","Qian Z","Laurita KR","Chaube R","Stamler JS","Venetos NM","Grimmett ZW","Perez LG"],"additional_accession":[]},"is_claimable":false,"name":"Physiological role for S-nitrosylation of RyR1 in skeletal muscle function and development.","description":"Excitation-contraction coupling in skeletal muscle myofibers depends upon Ca<sup>2+</sup> release from the sarcoplasmic reticulum through the ryanodine receptor/Ca<sup>2+</sup>-release channel RyR1. The RyR1 contains ∼100 Cys thiols of which ∼30 comprise an allosteric network subject to posttranslational modification by S-nitrosylation, S-palmitoylation and S-oxidation. However, the role and function of these modifications is not understood. Although aberrant S-nitrosylation of multiple unidentified sites has been associated with dystrophic diseases, malignant hyperthermia and other myopathic syndromes, S-nitrosylation in physiological situations is reportedly specific to a single (1 of ∼100) Cys in RyR1, Cys<sup>3636</sup> in a manner gated by pO<sub>2</sub>. Using mice expressing a form ","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Sep","modification":"2026-06-05T18:44:55.433Z","creation":"2026-05-20T03:13:12.73Z"},"accession":"S-EPMC12651786","cross_references":{"pubmed":["38820626"],"doi":["10.1016/j.bbrc.2024.150163"]}}