id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-271259-6kkzh1tp	Chen, Shuai	Liberation of SARS-CoV main protease from the viral polyprotein: N-terminal autocleavage does not depend on the mature dimerization mode	2010-01-01		.txt	text/plain	7826	352	56	Therefore, the N-terminal auto-processing of M(pro) appears to require only two "immature" monomers approaching one another to form an "intermediate" dimer structure and does not strictly depend on the active dimer conformation existing in mature protease. These results indicate that N-terminal autocleavage of SARS-CoV M pro from the polyproteins only requires two "immature" proteases approaching one another to form an "intermediate" dimer structure and does not depend on the active dimer conformation existing in the mature protease. Since mutation of either of these two residues were reported to completely abolish the dimer of mature M pro , our finding raises the intriguing question of how the E290R and R298E mutants can auto-process their N-terminal GST tags when they are unable to form the active dimer structure.	./cache/cord-271259-6kkzh1tp.txt	./txt/cord-271259-6kkzh1tp.txt