{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ng SK"],"funding":["Biotechnology and Biological Sciences Research Council"],"pagination":["9786-99"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3834823"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["41(21)"],"pubmed_abstract":["Long double-stranded RNA may undergo hyper-editing by adenosine deaminases that act on RNA (ADARs), where up to 50% of adenosine residues may be converted to inosine. However, although numerous RNAs may undergo hyper-editing, the role for inosine-containing hyper-edited double-stranded RNA in cells is poorly understood. Nevertheless, editing plays a critical role in mammalian cells, as highlighted by the analysis of ADAR-null mutants. In particular, the long form of ADAR1 (ADAR1(p150)) is essential for viability. Moreover, a number of studies have implicated ADAR1(p150) in various stress pathways. We have previously shown that ADAR1(p150) localized to cytoplasmic stress granules in HeLa cells following either oxidative or interferon-induced stress. Here, we show that the Z-DNA-binding doma"],"journal":["Nucleic acids research"],"pubmed_title":["Proteins that contain a functional Z-DNA-binding domain localize to cytoplasmic stress granules."],"pmcid":["PMC3834823"],"funding_grant_id":["BB/F018347/1"],"pubmed_authors":["Ng SK","Scadden AD","Weissbach R","Ronson GE"],"additional_accession":[]},"is_claimable":false,"name":"Proteins that contain a functional Z-DNA-binding domain localize to cytoplasmic stress granules.","description":"Long double-stranded RNA may undergo hyper-editing by adenosine deaminases that act on RNA (ADARs), where up to 50% of adenosine residues may be converted to inosine. However, although numerous RNAs may undergo hyper-editing, the role for inosine-containing hyper-edited double-stranded RNA in cells is poorly understood. Nevertheless, editing plays a critical role in mammalian cells, as highlighted by the analysis of ADAR-null mutants. In particular, the long form of ADAR1 (ADAR1(p150)) is essential for viability. Moreover, a number of studies have implicated ADAR1(p150) in various stress pathways. We have previously shown that ADAR1(p150) localized to cytoplasmic stress granules in HeLa cells following either oxidative or interferon-induced stress. Here, we show that the Z-DNA-binding doma","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Nov","modification":"2025-04-04T12:26:50.782Z","creation":"2019-03-27T03:08:58Z"},"accession":"S-EPMC3834823","cross_references":{"pubmed":["23982513"],"doi":["10.1093/nar/gkt750"]}}