1. RIG-I Holds the CARDs in a Game of Self versus Nonself
Karl-Peter Hopfner 
Molecular Cell 
Volume 55, Issue 4, Pages (August 2014)
DOI: /j.molcel
Copyright © 2014 Elsevier Inc. Terms and Conditions

2. Figure 1 Model for RIG-I-Mediated Formation of MAVS Filaments
Viral 5′ triphosphate-containing double-stranded RNA (ppp-dsRNA) triggers a conformational change in the antiviral innate immune sensor RIG-I that unmasks and, in the presence of K63-linked ubiquitin (Ub) chain, leads to the oligomerization of its tandem CARDs (yellow/orange). RIG-I CARDs assemble in the same way as the CARDs of the MAVS filament. They thereby form a nucleus onto which MAVS can polymerize. MAVS polymerization amplifies the signal and provides an interaction hub for the concentration and activation of downstream signaling factors such as TRAFs (TNF-α receptor-associated factors).
Molecular Cell  , DOI: ( /j.molcel )
Copyright © 2014 Elsevier Inc. Terms and Conditions