id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-318222-o9kc3x6z	Saraswat, Shweta	Hepatitis E Virus Cysteine Protease Has Papain Like Properties Validated by in silico Modeling and Cell-Free Inhibition Assays	2020-01-23		.txt	text/plain	8555	493	53	title: Hepatitis E Virus Cysteine Protease Has Papain Like Properties Validated by in silico Modeling and Cell-Free Inhibition Assays The enzyme activity and the inhibition studies were conducted using Zymography, FTC-casein based protease assay and ORF1 polyprotein digestion. Hence, we propose that HEV-protease has characteristics of "Papain-like cysteine protease," as determined through structural homology, active site residues and class-specific inhibition. Four inhibitors (E64, Chymostatin, Leupeptin, and ALLN) showed good ligandreceptor interactions that correlated better with the enzyme inhibition activity of recombinant HEV PCP protein with Glide docking ( Table 2 ). On the basis of structural homology, active site residue and class specific inhibition we have classified HEV-protease as a "Papain-like cysteine protease." Molecular characterization of hepatitis E virus ORF1 gene supports a papain-like cysteine protease (PCP)-domain activity Molecular modeling and analysis of hepatitis E virus (HEV) papain-like cysteine protease	./cache/cord-318222-o9kc3x6z.txt	./txt/cord-318222-o9kc3x6z.txt