{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["9"],"submitter":["Kazmierczak K"],"pubmed_abstract":["In this study, we investigated the rescue potential of two phosphomimetic mutants of the myosin regulatory light chain (RLC, <i>MYL2</i> gene), S15D, and T160D RLCs. S15D-RLC mimics phosphorylation of the established serine-15 site of the human cardiac RLC. T160D-RLC mimics the phosphorylation of threonine-160, identified by computational analysis as a high-score phosphorylation site of myosin RLC. Cardiac myosin and left ventricular papillary muscle (LVPM) fibers were isolated from a previously generated model of hypertrophic cardiomyopathy (HCM), Tg-R58Q, and Tg-wild-type (WT) mice. Muscle specimens were first depleted of endogenous RLC and then reconstituted with recombinant human cardiac S15D and T160D phosphomimetic RLCs. Preparations reconstituted with recombinant human cardiac WT-RL"],"journal":["Frontiers in cardiovascular medicine"],"pagination":["988066"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9530205"],"repository":["biostudies-literature"],"pubmed_title":["Functional comparison of phosphomimetic S15D and T160D mutants of myosin regulatory light chain exchanged in cardiac muscle preparations of HCM and WT mice."],"pmcid":["PMC9530205"],"pubmed_authors":["Kazmierczak K","Liang J","Gomez-Guevara M","Szczesna-Cordary D"],"additional_accession":[]},"is_claimable":false,"name":"Functional comparison of phosphomimetic S15D and T160D mutants of myosin regulatory light chain exchanged in cardiac muscle preparations of HCM and WT mice.","description":"In this study, we investigated the rescue potential of two phosphomimetic mutants of the myosin regulatory light chain (RLC, <i>MYL2</i> gene), S15D, and T160D RLCs. S15D-RLC mimics phosphorylation of the established serine-15 site of the human cardiac RLC. T160D-RLC mimics the phosphorylation of threonine-160, identified by computational analysis as a high-score phosphorylation site of myosin RLC. Cardiac myosin and left ventricular papillary muscle (LVPM) fibers were isolated from a previously generated model of hypertrophic cardiomyopathy (HCM), Tg-R58Q, and Tg-wild-type (WT) mice. Muscle specimens were first depleted of endogenous RLC and then reconstituted with recombinant human cardiac S15D and T160D phosphomimetic RLCs. Preparations reconstituted with recombinant human cardiac WT-RL","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2025-04-05T07:08:33.029Z","creation":"2024-11-12T02:43:24.512Z"},"accession":"S-EPMC9530205","cross_references":{"pubmed":["36204565"],"doi":["10.3389/fcvm.2022.988066"]}}