Adenosine deaminases acting on RNA (ADARs): RNA-editing enzymes

By L. Keegan, Anne Leroy, Duncan Sproul, Mary A O'Connell. Genome Biology, 2004

702 citations recorded by the source corpus.

SummaryAdenosine deaminases acting on RNA (ADARs) were discovered as a result of their ability extensively to deaminate adenosines in any long double-stranded RNA, converting them to inosines. Subsequently, ADARs were found to deaminate adenosines site-specifically within the coding sequences of transcripts encoding ion-channel subunits, increasing the diversity of these proteins in the central nervous system. ADAR1 is now known to be involved in defending the genome against viruses, and it may affect RNA interference. ADARs are found in animals but are not known in other organisms. It appears that ADARs evolved from a member of another family, adenosine deaminases acting on tRNAs (ADATs), by steps including fusion of two or more double-stranded-RNA binding domains to a common type of zinc-containing adenosine-deaminase domain.

Subfields: Cardiology and Cardiovascular Medicine, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/b822dc6f6a942f4ef4416f4f260f21edb6df5897

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Citations in the corpus

Interferon-Stimulated Genes: A Complex Web of Host Defenses (2014, neutral): “Following IFN signaling, transcription initiates from an upstream alternative transcriptional start site, giving rise to an extended protein that is predominantly localized to the cytoplasm (240).”
Protein Molecular Function Prediction by Bayesian Phylogenomics (2005, positive): “4) modifies posttranscriptional RNA, converting adenosine to inosine, resulting in a protein with a sequence different from that coded in the genome by the standard codon table [49].”