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RIG-I inhibition by TRBP did not require phosphorylation of sites shown to be important for inhibiting PKR, nor did it involve PACT or PKR, but it did require the dsRNA-binding ability of TRBP. These findings open the door to a complex co-regulation of RIG-I, PKR, MDA5, miRNA processing, and interferon induction.Plants encode a large number of proteases in activating intracellular signaling through proteolytic cleavages of various protein substrates. One type of the substrates is proligands, including peptide hormones, which are perceiv