id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-023766-qx0qdjmt	Nirwan, Sonam	Rhinovirus RNA Polymerase: Structure, Function, and Inhibitors	2018-11-02		.txt	text/plain	10466	477	51	Differences observed in the secondary structure of these polymerases reflect not only the substrate diversity but also divergent mechanisms for initiation of RNA synthesis (primer dependent for HRV and RHDV but primer independent for HCV and bacteriophage ϕ6). Conserved aspartic acid residues in the polymerase palm domains coordinate the two magnesium ions needed for the catalytic polymerization reaction of the enzyme, with one metal activating the primer 3 0 OH for the attack of the nucleotide α-phosphate, and the other metal serving to stabilize the triphosphate moiety ( Fig. 11 .1). The EC of PV polymerase provided a required view about how the template and the RNA strand interact as they thread through the active site and showed that viral RdRPs use a unique palm-based structural change to close their active site for catalysis (Gong and Peersen, 2010) .	./cache/cord-023766-qx0qdjmt.txt	./txt/cord-023766-qx0qdjmt.txt