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lüll The NFAR s (nuclear factors associated with dsRNA): evolutionarily conserved members of the dsRNA binding protein family Barber GNRNA Biol 2009[Jan]; 6 (1): 35-9The dsRNA binding protein (DRBP) family comprise one or more evolutionarily conserved dsRNA-binding domains (DRBD) of approximately 65-68 amino acids, are found in both eukaryotes and prokaryotes and are even encoded by plants and viruses. DRBP's do not recognize specific nucleotide sequences and primarily interact with approximately 11-16 base pairs present within A-form double helix RNAs, which can include ssRNA's with extensive secondary structure. The DRBP family include TRBP (TAR RNA binding protein), PKR (protein kinase activated by dsRNA), PACT (Protein Activator of PKR), ADAR (Adenosine deaminases acting on RNA), and the RNase III family including DICER, which collectively play important roles in mRNA elongation, RNA interference (RNAi), mRNA editing, stability, splicing and/or export and translation. Here, we focus on the role of DRBP's referred to as the NFARs (Nuclear Factors associated with dsRNA) which are translated from two major alternatively spliced products encoded from a single gene. Evidence indicates that the NFAR proteins play crucial roles in mRNA post-transcriptional regulation, including mRNA stability, export and translation and may also have an important function in host defense.|Animals[MESH]|Cell Nucleus/*metabolism[MESH]|Evolution, Molecular[MESH]|Exons[MESH]|Introns[MESH]|Mice[MESH]|Models, Biological[MESH]|Models, Genetic[MESH]|Nucleic Acid Conformation[MESH]|Oxidative Stress[MESH]|RNA Processing, Post-Transcriptional[MESH]|RNA, Double-Stranded/*chemistry[MESH]|RNA, Messenger/metabolism[MESH]|RNA-Binding Proteins/chemistry[MESH]|RNA/chemistry[MESH] |