id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-297044-tpp40j0g	Jin, Zhenming	Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug Carmofur	2020-04-28		.txt	text/plain	1146	84	62	title: Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug Carmofur The antineoplastic drug Carmofur was shown to inhibit SARS-CoV-2 main protease (Mpro). The antineoplastic drug Carmofur was shown to inhibit SARS-CoV-2 main protease 24 (M pro ). Here the X-ray crystal structure of M pro in complex with Carmofur reveals that 25 the carbonyl reactive group of Carmofur is covalently bound to catalytic Cys145, 26 whereas its fatty acid tail occupies the hydrophobic S2 subsite. Here, we present the 1.6 Å X-ray crystal structure of SARS-CoV-2 M pro in complex 49 with Carmofur (Fig. 1b, domain II feature the catalytic dyad residues Cys145 and His41 (Fig. 1c, d) . Here we determined the inhibitory 94 effect of Carmofur against SARS-CoV-2 infection on Vero E6 cells, as previously 95 described 20 (Fig. 2) .	./cache/cord-297044-tpp40j0g.txt	./txt/cord-297044-tpp40j0g.txt