id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-001532-kz3b01wq	Gantt, Soren	Nelfinavir Impairs Glycosylation of Herpes Simplex Virus 1 Envelope Proteins and Blocks Virus Maturation	2015-01-29		.txt	text/plain	4362	235	48	Given the apparent absence of an aspartyl protease encoded by HHVs, we investigated the mechanism of action of NFV herpes simplex virus type 1 (HSV-1) in cultured cells. The mechanisms by which NFV acts on tumor cells are multifactorial and include inhibition of cellular proteases, Akt activation, and NF -B signaling, as well as induction of the endoplasmic reticulum (ER) stress, the unfolded protein response (UPR), and autophagy [11, 16, 17] . The Akt inhibitor LY294002 completely suppressed Akt phosphorylation in HSV-1 infected cells, but NFV did not reduce the levels of phosphorylated Akt even at drug concentrations that potently block virus production ( Figure 3 ). Interestingly, although endoplasmic reticulum (ER) stress, the unfolded protein response (UPR), and autophagy are well known effects of NFV [16, [26] [27] [28] [29] , neither ER dilation nor the abundance of double-membrane bound vesicles consistent with autophagosomes appeared consistently different between NVF-treated and untreated HSV-1-infected cells.	./cache/cord-001532-kz3b01wq.txt	./txt/cord-001532-kz3b01wq.txt