{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Di M"],"funding":["NSFC","National Institutes of Health","NIGMS NIH HHS"],"pagination":["102190"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11077028"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["35(2)"],"pubmed_abstract":["RNA base editors should ideally be free of immunogenicity, compact, efficient, and specific, which has not been achieved for C > U editing. Here we first describe a compact C > U editor entirely of human origin, created by fusing the human C > U editing enzyme RESCUE-S to Cas inspired RNA targeting system (CIRTS), a tiny, human-originated programmable RNA-binding domain. This editor, CIRTS-RESCUEv1 (V1), was inefficient. Remarkably, a short histidine-rich domain (HRD), which is derived from the internal disordered region (IDR) in the human CYCT1, a protein capable of liquid-liquid phase separation (LLPS), enhanced V1 editing at on-targets as well as off-targets, the latter effect being minor. The V1-HRD fusion protein formed puncta characteristic of LLPS, and various other IDRs (but not an"],"journal":["Molecular therapy. Nucleic acids"],"pubmed_title":["Expanding RNA editing toolkit using an IDR-based strategy."],"pmcid":["PMC11077028"],"funding_grant_id":["R35 GM119840"],"pubmed_authors":["Lv J","Wu J","Di M","Yan K","Dickinson BC","Jing Z","Yang Y","Chi T","Ge J","Rauch S"],"additional_accession":[]},"is_claimable":false,"name":"Expanding RNA editing toolkit using an IDR-based strategy.","description":"RNA base editors should ideally be free of immunogenicity, compact, efficient, and specific, which has not been achieved for C > U editing. Here we first describe a compact C > U editor entirely of human origin, created by fusing the human C > U editing enzyme RESCUE-S to Cas inspired RNA targeting system (CIRTS), a tiny, human-originated programmable RNA-binding domain. This editor, CIRTS-RESCUEv1 (V1), was inefficient. Remarkably, a short histidine-rich domain (HRD), which is derived from the internal disordered region (IDR) in the human CYCT1, a protein capable of liquid-liquid phase separation (LLPS), enhanced V1 editing at on-targets as well as off-targets, the latter effect being minor. The V1-HRD fusion protein formed puncta characteristic of LLPS, and various other IDRs (but not an","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jun","modification":"2026-06-03T04:32:12.9Z","creation":"2026-04-24T03:09:42.373Z"},"accession":"S-EPMC11077028","cross_references":{"pubmed":["38721279"],"doi":["10.1016/j.omtn.2024.102190"]}}