id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-261388-d56ci0hl	Tibbles, K.W	Activity of a purified His-tagged 3C-like proteinase from the coronavirus infectious bronchitis virus	1999-05-28		.txt	text/plain	3906	173	51	Previous studies in vitro of the processing of cloned polyprotein fragments from the coronavirus infectious bronchitis virus (IBV) large open reading frame (ORF1), confirmed the activity of a predicted 3C-like proteinase (3CLP) domain and suggested that the proteinase is released autocatalytically from the polyprotein in the form of a 35 kDa protein, 3CLpro, capable of further cleavages in trans. The bacterial expression system described utilises the minimum processing unit identified in our previous studies which established that, in addition to the 3CLP domain, MP2 protein sequence between the Q/S 4 cleavage target and a point delimited by an NcoI restriction site (ntd position 10118) was that minimally required for processing. Identification of a 24-kDa polypeptide processed from the coronavirus infectious bronchitis virus 1a polyprotein by the 3C-like proteinase and determination of its cleavage sites	./cache/cord-261388-d56ci0hl.txt	./txt/cord-261388-d56ci0hl.txt