id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-342653-bpyc2gbl	Wang, Hai-Tao	Substrate recognition by TRIM and TRIM-like proteins in innate immunity	2020-10-20		.txt	text/plain	8560	478	49	While E3 ligases are often thought to negatively regulate the stability of the target molecule by Ub-mediated proteasomal targeting, many TRIMs have been shown to enhance innate immune signaling pathways [15] , through both proteasome-dependent and -independent mechanisms. The study of RIG-I and RIPLET interaction provides a detailed example of how TRIM-like proteins utilize bivalency and CC for regulating substrate selectivity, higher-order oligomerization and innate immune function. Given that an increasing number of receptors and signaling molecules in the innate immune system are shown to multimerize upon activation [77] , it is tempting to speculate that TRIM/TRIM-like proteins may utilize multimer-specific substrate recognition as a common mechanism for regulating their immune functions. The avidity-driven substrate recognition mechanism of TRIM/TRIM-like proteins would thus ensure more precise control of innate immune signaling and restriction functions.	./cache/cord-342653-bpyc2gbl.txt	./txt/cord-342653-bpyc2gbl.txt