{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["36(1)"],"submitter":["Anwar S"],"pubmed_abstract":["Dysferlinopathies are debilitating autosomal recessive muscular dystrophies caused by mutations in the <i>DYSF</i> gene, encoding dysferlin, a protein crucial for sarcolemmal homeostasis and membrane resealing. Currently, no therapies exist for dysferlinopathies. Dysferlin features a modular structure with multiple calcium-dependent C2 lipid-binding domains. Clinical reports of mild, late-onset phenotypes suggest partial retention of functionality despite missing C2 domains, supporting exon-skipping therapies using antisense oligonucleotides (ASOs). In this study, we identified a patient-derived muscle cell line with a splice site mutation in <i>DYSF</i> intron 26, causing exon 26 exclusion, an out-of-frame transcript, and no detectable dysferlin protein. We hypothesized that skipping <i>D"],"journal":["Molecular therapy. Nucleic acids"],"pagination":["102443"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11834094"],"repository":["biostudies-literature"],"pubmed_title":["Antisense oligonucleotide-mediated exon 27 skipping restores dysferlin function in dysferlinopathy patient-derived muscle cells."],"pmcid":["PMC11834094"],"pubmed_authors":["Roshmi RR","Bigot A","Woo S","Haque US","Anwar S","Arthur Lee JJ","Duddy WJ","Maruyama R","Yokota T"],"additional_accession":[]},"is_claimable":false,"name":"Antisense oligonucleotide-mediated exon 27 skipping restores dysferlin function in dysferlinopathy patient-derived muscle cells.","description":"Dysferlinopathies are debilitating autosomal recessive muscular dystrophies caused by mutations in the <i>DYSF</i> gene, encoding dysferlin, a protein crucial for sarcolemmal homeostasis and membrane resealing. Currently, no therapies exist for dysferlinopathies. Dysferlin features a modular structure with multiple calcium-dependent C2 lipid-binding domains. Clinical reports of mild, late-onset phenotypes suggest partial retention of functionality despite missing C2 domains, supporting exon-skipping therapies using antisense oligonucleotides (ASOs). In this study, we identified a patient-derived muscle cell line with a splice site mutation in <i>DYSF</i> intron 26, causing exon 26 exclusion, an out-of-frame transcript, and no detectable dysferlin protein. We hypothesized that skipping <i>D","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Mar","modification":"2025-04-03T23:16:54.328Z","creation":"2025-04-03T23:16:54.328Z"},"accession":"S-EPMC11834094","cross_references":{"pubmed":["39967852"],"doi":["10.1016/j.omtn.2024.102443"]}}