Journal ClubRIG-I: an essential regulator of virus-induced interferon production
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Cited by (19)
Identification of a retinoic acid-inducible gene I from grass carp (Ctenopharyngodon idella) and expression analysis in vivo and in vitro
2011, Fish and Shellfish ImmunologyCitation Excerpt :Analysis of MDA5 or RIG-I knockout mice demonstrates that this pathway is central for innate immunity against viral infection [17]. RIG-I is a cytosolic sensor of viral RNA that plays crucial roles in the induction of type I IFNs [24–27]. Next-generation RNA sequencing shows that RIG-I preferentially associates with shorter 5′ppp containing viral RNA molecules in infected cells as well as subgenomic defective interfering particles [11].
Modulation of the interferon antiviral response by the TBK1/IKKi adaptor protein TANK
2007, Journal of Biological ChemistryCytokine modulation of retinoic acid-inducible gene-I (RIG-I) expression in human epidermal keratinocytes
2007, Journal of Dermatological ScienceCitation Excerpt :These results suggest that the helicase domain suppresses downstream signaling through the CARD domains in non-viral condition [5]. Considering the binding ability of the helicase domain to poly(I:C), RIG-I is an essential component of the signaling pathway upstream of IRF-3 and NF-κB, and probably the direct sensor of viral double-stranded RNA [5,23]. Interestingly, it has been demonstrated that RIG-I is expressed by the induction of inflammatory cytokines in various types of human cells, including endothelial cells, vascular smooth muscle cells, urinary bladder epithelial cells, gingival fibroblasts, and bronchial epithelial cells [9,17–22].
The hepatitis C virus NS3/4A protease complex interferes with pathways of the innate immune response
2005, Journal of HepatologyCrystallization and preliminary crystallographic studies of human RIG-I in complex with double-stranded RNA
2009, Acta Crystallographica Section F: Structural Biology and Crystallization Communications