{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Washburn MC"],"funding":["NHGRI NIH HHS","NCI NIH HHS","NINDS NIH HHS","NIGMS NIH HHS"],"pagination":["599-607"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3959997"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["6(4)"],"pubmed_abstract":["Inadequate adenosine-to-inosine editing of noncoding regions occurs in disease but is often uncorrelated with ADAR levels, underscoring the need to study deaminase-independent control of editing. C. elegans have two ADAR proteins, ADR-2 and the theoretically catalytically inactive ADR-1. Using high-throughput RNA sequencing of wild-type and adr mutant worms, we expand the repertoire of C. elegans edited transcripts over 5-fold and confirm that ADR-2 is the only active deaminase in vivo. Despite lacking deaminase function, ADR-1 affects editing of over 60 adenosines within the 3' UTRs of 16 different mRNAs. Furthermore, ADR-1 interacts directly with ADR-2 substrates, even in the absence of ADR-2, and mutations within its double-stranded RNA (dsRNA) binding domains abolish both binding and e"],"journal":["Cell reports"],"pubmed_title":["The dsRBP and inactive editor ADR-1 utilizes dsRNA binding to regulate A-to-I RNA editing across the C. elegans transcriptome."],"pmcid":["PMC3959997"],"funding_grant_id":["R01 NS075449","P30 CA023100","T32 GM008666","R01 HG004659","T32 GM007757"],"pubmed_authors":["Kakaradov B","Wheeler E","Hoon S","Sundararaman B","Yeo GW","Hundley HA","Washburn MC"],"additional_accession":[]},"is_claimable":false,"name":"The dsRBP and inactive editor ADR-1 utilizes dsRNA binding to regulate A-to-I RNA editing across the C. elegans transcriptome.","description":"Inadequate adenosine-to-inosine editing of noncoding regions occurs in disease but is often uncorrelated with ADAR levels, underscoring the need to study deaminase-independent control of editing. C. elegans have two ADAR proteins, ADR-2 and the theoretically catalytically inactive ADR-1. Using high-throughput RNA sequencing of wild-type and adr mutant worms, we expand the repertoire of C. elegans edited transcripts over 5-fold and confirm that ADR-2 is the only active deaminase in vivo. Despite lacking deaminase function, ADR-1 affects editing of over 60 adenosines within the 3' UTRs of 16 different mRNAs. Furthermore, ADR-1 interacts directly with ADR-2 substrates, even in the absence of ADR-2, and mutations within its double-stranded RNA (dsRNA) binding domains abolish both binding and e","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Feb","modification":"2026-04-29T12:39:28.604Z","creation":"2019-03-27T01:23:41Z"},"accession":"S-EPMC3959997","cross_references":{"pubmed":["24508457"],"doi":["10.1016/j.celrep.2014.01.011"]}}