@article{oai:repo.qst.go.jp:00046932,
 author = {Ota, Hiromitsu and Sakurai, Masayuki and Gupta, Ravi and Valente, Louis and Wulff, Bjorn-Erik and Ariyoshi, Kentaro and Iizasa, Hisashi and V, Davuluri Ramana and Nishikura, Kazuko and et.al and 有吉 健太郎},
 issue = {3},
 journal = {Cell},
 month = {Apr},
 note = {Adenosine deaminases acting on RNA (ADARs) are involved in RNA editing that converts adenosine residues to inosine specifically in double-stranded RNAs. In this study, we investigated the interaction of the RNA editing mechanism with the RNA interference (RNAi) machinery and found that ADAR1 forms a complex with Dicer through direct protein-protein interaction. Most importantly, ADAR1 increases the maximum rate (Vmax) of pre-microRNA (miRNA) cleavage by Dicer and facilitates loading of miRNA onto RNA-induced silencing complexes, identifying a new role of ADAR1 in miRNA processing and RNAi mechanisms. ADAR1 differentiates its functions in RNA editing and RNAi by the formation of either ADAR1/ADAR1 homodimer or Dicer/ADAR1 heterodimer complexes, respectively. As expected, the expression of miRNAs is globally inhibited in ADAR1-/- mouse embryos, which, in turn, alters the expression of their target genes and might contribute to their embryonic lethal phenotype.},
 pages = {575--589},
 title = {ADAR1 Forms a Complex with Dicer to Promote MicroRNA Processing and RNA-Induced Gene Silencing},
 volume = {153},
 year = {2013}
}