id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-022290-p0l1kv6n	Bergmann, Ernst M.	Proteolytic Enzymes of the Viruses of the Family Picornaviridae	2007-05-09		.txt	text/plain	9450	480	56	The primary function of the picornaviral proteinases is the cotranslational, specific cleavage of the viral polyprotein into the structural and nonstructural proteins. This is true even for some families of + RNA viruses which have developed additional strategies to generate individual gene products from a single RNA genome, e.g., subgenomic RNAs or multiple ORFs. Proteolytic cleavage as a covalent modification of the precursors of viral structural proteins is even more common and occurs even in DNA viruses. The sequence of the residues which form the last turn of this helix is highly conserved throughout the picornaviral 3C genes (K/RR/KNL/I), It is interesting that the structural and functional details of the proteolytic active site of the 3C proteinases are not the most conserved part of the 3C structure (Gorbalenya et al., 1988) . While the details of the specific enzyme substrate interactions gleaned from the crystal structures of 3C proteinases provide valuable information for the design of effective inhibitors, there is little experimental evidence for the mechanism of the chymotrypsin-like cysteine proteinases.	./cache/cord-022290-p0l1kv6n.txt	./txt/cord-022290-p0l1kv6n.txt