id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-290218-dvyeg5fk	Jiang, Yi	RNA-dependent RNA polymerase: Structure, mechanism, and drug discovery for COVID-19	2020-09-04		.txt	text/plain	2249	143	53	Interestingly, the structure of complexed nsp12 is almost identical to nsp12 in apo RdRp, with an RMSD of 0.5 Å [17] , coinciding with the high processivity of the viral RNA polymerase, which does not need to consume extra energy for conformation changes in the active site during the replication cycle (Fig. 3B ). These "sliding poles" are stabilized by interactions formed between the positively charged residues at the extended N-terminal of nsp8 and bases in RNA backbones ( Fig. 3E ) and reported to account for the known processivity of the RdRp, which is required for replicating the long coronavirus genomes [39] . Although the sequence identity of nsp12 across the RNA viruses is low, the polymerase active site is structurally highly conserved, suggesting that RdRp inhibitors may serve as a potential J o u r n a l P r e -p r o o f broad-spectrum antiviral drug against RNA viruses.	./cache/cord-290218-dvyeg5fk.txt	./txt/cord-290218-dvyeg5fk.txt