{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["37(1)"],"submitter":["Gaci A"],"pubmed_abstract":["Cellular uptake and intracellular distribution of phosphorothioate-modified antisense oligonucleotides (PS-ASOs) are mediated by protein interactions. While several PS-ASOs-binding proteins have been identified, mainly using gapmer designs with 2'-O-methoxyethyl (2'MOE) modifications, less is known about protein partners of splice-switching oligonucleotides (SSOs) with alternative ribose modifications. Here, using affinity purification mass spectrometry (AP-MS), we identified the intracellular protein partners of PS-SSOs of the same sequence with three distinct ribose modifications: tricyclo-DNA (tcDNA), locked nucleic acid (LNA), and 2'MOE. Interestingly, we found previously reported PS interactors, such as GRSF1, NONO, and NCL, as well as uncharacterized protein partners. Four shared int"],"journal":["Molecular therapy. Nucleic acids"],"pagination":["102832"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12860984"],"repository":["biostudies-literature"],"pubmed_title":["Identification and functional validation of intracellular protein partners of phosphorothioate splice-switching oligonucleotides using AP-MS."],"pmcid":["PMC12860984"],"pubmed_authors":["Salnot V","Bruce J","Pedeux R","Menchon G","Gaci A","Goyenvalle A"],"additional_accession":[]},"is_claimable":false,"name":"Identification and functional validation of intracellular protein partners of phosphorothioate splice-switching oligonucleotides using AP-MS.","description":"Cellular uptake and intracellular distribution of phosphorothioate-modified antisense oligonucleotides (PS-ASOs) are mediated by protein interactions. While several PS-ASOs-binding proteins have been identified, mainly using gapmer designs with 2'-O-methoxyethyl (2'MOE) modifications, less is known about protein partners of splice-switching oligonucleotides (SSOs) with alternative ribose modifications. Here, using affinity purification mass spectrometry (AP-MS), we identified the intracellular protein partners of PS-SSOs of the same sequence with three distinct ribose modifications: tricyclo-DNA (tcDNA), locked nucleic acid (LNA), and 2'MOE. Interestingly, we found previously reported PS interactors, such as GRSF1, NONO, and NCL, as well as uncharacterized protein partners. Four shared int","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Mar","modification":"2026-06-19T04:44:57.935Z","creation":"2026-06-19T03:07:05.352Z"},"accession":"S-EPMC12860984","cross_references":{"pubmed":["41630988"],"doi":["10.1016/j.omtn.2026.102832"]}}