id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-103924-mhgnqi80	Shin, Donghyuk	Novel class of OTU deubiquitinases regulate substrate ubiquitination upon Legionella infection	2020-04-28		.txt	text/plain	2096	220	67	MS analysis of catalytically inactive LotB and LotC identified different categories of host-substrates for these two related DUBs. Together, our results provide new structural insights of bacterial OTU deubiquitinases and indicate distinct roles of bacterial deubiquitinases in host-pathogen interactions. Whereas the overall fold of the 174 catalytic core of LotB and LotC resembles that of other OTU-deubiquitinases, both showed clear 175 differences in the helical arm region, which has been shown to interact with ubiquitin and it serves 176 as an S1 binding site (Mevissen et al., 2013) . To address this, we performed ubiquitin 192 docking into both LotB and LotC, followed by molecular dynamics (MD) simulations for 600 ns 193 ( Fig. 4aTo gain better insights into the physiological roles of LotB and LotC, we decided to identify their 216 interacting proteins or substrates.	./cache/cord-103924-mhgnqi80.txt	./txt/cord-103924-mhgnqi80.txt