Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5.
Wu, Bin; Peisley, Alys; Richards, Claire; Yao, Hui; Zeng, Xiaohui; Lin, Cecilie; Chu, Feixia; Walz, Thomas; Hur, Sun.
; 152(1-2): 276-89, 2013 Jan 17.
Artigo em Inglês | MEDLINE | ID: mdl-23273991
Structural insights into RNA recognition by RIG-I.
The DEAD-box protein DDX43 (HAGE) is a dual RNA-DNA helicase and has a K-homology domain required for full nucleic acid unwinding activity.
RIG-I forms signaling-competent filaments in an ATP-dependent, ubiquitin-independent manner.
The innate immune sensor LGP2 activates antiviral signaling by regulating MDA5-RNA interaction and filament assembly.
MDA5 cooperatively forms dimers and ATP-sensitive filaments upon binding double-stranded RNA.
DNA-Demethylating Agents Target Colorectal Cancer Cells by Inducing Viral Mimicry by Endogenous Transcripts.
Structural mechanism of RNA recognition by the RIG-I-like receptors.
Kinetic discrimination of self/non-self RNA by the ATPase activity of RIG-I and MDA5.
MDA5 assembles into a polar helical filament on dsRNA.
ATP-dependent effector-like functions of RIG-I-like receptors.