id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-259246-azt5sr9w	Peng, Qi	Structural basis of SARS-CoV-2 polymerase inhibition by Favipiravir	2020-10-19		.txt	text/plain	3216	158	50	This structure provides a missing snapshot for visualizing the catalysis dynamics of coronavirus polymerase, and reveals an unexpected base-pairing pattern between Favipiravir and pyrimidine residues which may explain its capacity for mimicking both adenine and guanine nucleotides. Recently, we and other groups have determined the structures of SARS-CoV-2 core polymerase complex in both apo and RNA-bound states 26-30 , providing important information for structure-based antiviral drug design. Similar observations were also reported recently that SARS-CoV-2 polymerase is more tolerant for mismatches between template and product residues than other viral RdRps 5 , which further highlights the requirement for the proofreading nuclease nsp14 to maintain the integrity of viral genome. Interestingly, Favipiravir could be incorporated into the RNA product with similar efficiencies to those of ATP or GTP substrates guided by U or C template residues, respectively (Fig. 1c) .	./cache/cord-259246-azt5sr9w.txt	./txt/cord-259246-azt5sr9w.txt