id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-017854-ff3gm50j	Bromberg, Z.	Heat Shock Proteins in Inflammation	2007		.txt	text/plain	2408	152	43	Most HSPs are constitutively and ubiquitously expressed molecular chaperones that guide the normal folding, intracellular disposition, and proteolytic turnover of many of the key regulators of cell growth and survival [14] . Thus, the protective process involves the interaction of many different HSPs. For example, HSP90, which comprises 1-2% of total cellular protein in non-stress conditions [15] , supports meta-stable protein conformations and expresses a high affinity binding state to hormone receptors. Several in vitro models have proven that heat shock or elevated levels of HSP70 suppresses NF-κB activity and that this inhibition of NF-κB results in a general reduction in the inflammatory response [44, 46, 71, 73] . Major heat shock protein hsp70 protects tumor cells from tumor necrosis factor cytotoxicity Anti-inflammatory effect of heat shock protein induction is related to stabilization of I kappa B alpha through preventing I kappa B kinase activation in respiratory epithelial cells	./cache/cord-017854-ff3gm50j.txt	./txt/cord-017854-ff3gm50j.txt