Disease relevance of Dhx8

• DNA/RNA helicase gene mutations in a form of juvenile amyotrophic lateral sclerosis (ALS4) [1].
• Hepatitis C virus core protein binds to a DEAD box RNA helicase [2].
• These findings provide evidence that HCV may have evolved a distinct mechanism in alteration of host cellular gene expression regulation via the interaction of its nucleocapsid core protein and cellular putative RNA helicase known to participate in all aspects of cellular processes involving RNA metabolism [3].
• Determinants in the envelope E protein and viral RNA helicase NS3 that influence the induction of apoptosis in response to infection with dengue type 1 virus [4].
• A novel gene designated moc2, which encodes a putative RNA helicase, was isolated from Schizosaccharomyces pombe on the basis of its suppression of the sterility of two different mutant strains, one of which had elevated levels of cAMP and the other deregulated Ras functioning as a result of an ectopic expression of dominant negative RAS2 [5].

High impact information on Dhx8

• Yeast splicing factor Prp43, a DEAH box protein of the putative RNA helicase/RNA-dependent NTPase family, is a splicing factor that functions late in the pre-mRNA splicing pathway to facilitate spliceosome disassembly [6].
• Toll-like receptors (TLRs) represent a well-characterized class of membrane-bound PRRs, and the RNA helicase retinoic acid inducible gene I (RIG-I) has recently been described as a novel cytoplasmic PRR recognizing double-stranded RNA (dsRNA) [7].
• Genomic structure of newly identified paralogue of RNA helicase II/Gu: detection of pseudogenes and multiple alternatively spliced mRNAs [8].
• Our data suggest that identified amino acid substitutions in the envelope E protein and viral RNA helicase NS3 may influence DEN-1 virus pathogenicity by altering viral growth [4].
• RNA-binding proteins in mouse oocytes and embryos: expression of genes encoding Y box, DEAD box RNA helicase, and polyA binding proteins [9].

Biological context of Dhx8

• An increase in the phosphorylation of eIF-4E, its association with p220 protein, and an enhancement of RNA helicase activity were observed in the cells [10].
• rck/p54, a DEAD-box RNA helicase, is closely associated with the basic modification of RNA molecules in the process of mRNA transport, RNA decay, and translation initiation [11].
• The RNA helicase, p68, was identified as a unique Smad binding protein, and the specificity of the interaction was confirmed through various in vitro and in vivo assays [12].

Anatomical context of Dhx8

• DEAD-box Y RNA helicase (DBY) and eukaryotic initiation factor 2 gamma Y (eIF2gamma Y) were expressed only in male adipose tissue [13].

References