id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-286970-4pl95r0o	Mamipour, Mina	An overview on molecular chaperones enhancing solubility of expressed recombinant proteins with correct folding	2017-04-12		.txt	text/plain	4994	279	50	In this article, we attempted to review cytoplasmic chaperones such as Hsp families and periplasmic chaperones including; generic chaperones, specialized chaperones, PPIases, and proteins involved in disulfide bond formation. Numerous studies demonstrate positive effects of molecular chaperons on correct folding formation of recombinant protein and prevention of IBs formation in the cytoplasm and periplasm [17, 18] . In this review we focused on cytoplasmic and periplasmic chaperones category and their applications in recombinant protein expression with correct folding. The Hsp90 family are highly conserved and proteins, which exist in all organisms from bacteria to humans and their expressions rises in response to the stress conditions in prokaryotic and eukaryotic LolA (B,C,D,E) periplasm space, Inner membrane and Outer membrane rapid transfer of associated lipoproteins ATP (+) [108] PapD and its family periplasm space and Outer membrane biogenesis of pilus (−) [163] FimC periplasm space interacts with each pilus subunit (−) [164] cells.	./cache/cord-286970-4pl95r0o.txt	./txt/cord-286970-4pl95r0o.txt