Author: Brisse, Morgan; Ly, Hinh
Title: Comparative Structure and Function Analysis of the RIG-I-Like Receptors: RIG-I and MDA5 Document date: 2019_7_17
ID: 1enteev7_55
Snippet: Several host factors interacting with RIG-I and MDA5 do so by yet undescribed mechanisms. PKR [which is also activated by PACT (319, 320) and is sequestered by the cellular helicase DHX36 protein to form stress granules (321, 322) along with RIG-I (323, 324) and TRIM25 (324)] appears to have a novel and yet uncharacterized function in enhancing MDA5-dependent MAVS signaling that is dependent on the kinase activity of PKR (325) . Additionally, the.....
Document: Several host factors interacting with RIG-I and MDA5 do so by yet undescribed mechanisms. PKR [which is also activated by PACT (319, 320) and is sequestered by the cellular helicase DHX36 protein to form stress granules (321, 322) along with RIG-I (323, 324) and TRIM25 (324)] appears to have a novel and yet uncharacterized function in enhancing MDA5-dependent MAVS signaling that is dependent on the kinase activity of PKR (325) . Additionally, the porcine Interferon-Inducible Oligoadenylate Synthetase-like protein (pOASL) has also been found to interact with and inhibit MDA5 by an unknown mechanism (326) .
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