<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Ng SK</submitter><funding>Biotechnology and Biological Sciences Research Council</funding><pagination>9786-99</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3834823</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>41(21)</volume><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</pubmed_abstract><journal>Nucleic acids research</journal><pubmed_title>Proteins that contain a functional Z-DNA-binding domain localize to cytoplasmic stress granules.</pubmed_title><pmcid>PMC3834823</pmcid><funding_grant_id>BB/F018347/1</funding_grant_id><pubmed_authors>Ng SK</pubmed_authors><pubmed_authors>Scadden AD</pubmed_authors><pubmed_authors>Weissbach R</pubmed_authors><pubmed_authors>Ronson GE</pubmed_authors></additional><is_claimable>false</is_claimable><name>Proteins that contain a functional Z-DNA-binding domain localize to cytoplasmic stress granules.</name><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</description><dates><release>2013-01-01T00:00:00Z</release><publication>2013 Nov</publication><modification>2025-04-04T12:26:50.782Z</modification><creation>2019-03-27T03:08:58Z</creation></dates><accession>S-EPMC3834823</accession><cross_references><pubmed>23982513</pubmed><doi>10.1093/nar/gkt750</doi></cross_references></HashMap>