BIOLOGICAL MODEL;
CHEMICAL STRUCTURE;
CHEMISTRY;
DRUG POTENTIATION;
GENETICS;
HUMAN;
METABOLISM;
NOTE;
PHYSIOLOGY;
PROTEIN BINDING;
PROTEIN DOMAIN;
REGULATOR GENE;
GENES, SWITCH;
HUMANS;
MODELS, BIOLOGICAL;
MODELS, MOLECULAR;
PROTEIN BINDING;
PROTEIN INTERACTION DOMAINS AND MOTIFS;
RECEPTORS, RETINOIC ACID;
RNA HELICASES;
RNA, VIRAL;
Interplay between innate immunity and negative strand RNA viruses: Towards a rational model
Gerlier D, Lyles DS. Interplay between innate immunity and negative strand RNA viruses: towards a rational model. Microbiol Mol Biol Rev 2011; 75: 468-90.
Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA
Kowalinski E, Lunardi T, McCarthy AA, et al. Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. Cell 2011; 147: 423-35.
The RIG-I ATPase domain structure reveals insights into ATP-dependent antiviral signalling
Civril F, Bennett M, Moldt M, et al. The RIG-I ATPase domain structure reveals insights into ATP-dependent antiviral signalling. EMBO Rep 2011; 12: 1127-34.
The structural basis of 5’ triphosphate double-stranded RNA recognition by RIG-I C-terminal domain
Lu C, Xu H, Ranjith-Kumar CT, et al. The structural basis of 5’ triphosphate double-stranded RNA recognition by RIG-I C-terminal domain. Structure 2010; 18: 1032-43.
Regulation of innate antiviral defenses through a shared repressor domain in RIG-I and LGP2
Saito T, Hirai R, Loo YM, et al. Regulation of innate antiviral defenses through a shared repressor domain in RIG-I and LGP2. Proc Natl Acad Sci USA 2007; 104: 582-7.
