id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-317675-s1ac5vcx	de Marco, Ario	Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli	2009-05-14		.txt	text/plain	11534	524	31	The cytoplasmic accumulation of thioredoxin as a consequence of its recombinant overexpression in wild type bacteria was proposed for increasing the yields of coexpressed eukaryotic proteins without disulfide bonds in their native structure [191] . Fusions between recombinant scFvs and thioredoxin 1 expressed in trxB -, gorbacteria resulted in increased cytoplasmic yields [196] , correct folding of a scFv against the c-Met receptor [188] , and of the first domain of the multiple Kazal-type inhibitor LEKTI, a polypeptide that contains two disulfide bridges in its native structure [197] . In the case of a serpin domain, AD494 cells did not improve the total amount of soluble recombinant protein accumulated in the cytoplasm with respect to wild type bacteria, but it was correctly folded and active, whilst the protein expressed in the control cells did not form the essential disulfide bonds [210] .	./cache/cord-317675-s1ac5vcx.txt	./txt/cord-317675-s1ac5vcx.txt