id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-000479-u87eaaj8	Stolf, Beatriz S.	Protein Disulfide Isomerase and Host-Pathogen Interaction	2011-10-11		.txt	text/plain	5990	297	41	These especially affect (i) pathogen entry through protein redox switches and redox modification (i.e., intraand interdisulfide and cysteine oxidation) and (ii) phagocytic ROS production via Nox family NADPH oxidase enzyme and the control of phagolysosome function with key implications for antigen processing. Among the many redox sensitive proteins that are altered during the course of different infections, protein disulfide isomerase (PDI-) mediated redox switches have been associated with pathogen attachment-internalization, antigen processing in the ER/phagosome, and the regulation of ROS production by Nox family enzymes. PDI is thought to attach to lipids, glycans, and integral membrane proteins via electrostatic interactions at the cell plasma membrane [14, 15] , where its reductive activity mediates the infection of different pathogens ( Figure 2 , discussed later). Protein disulfide isomerase (PDI) associates with NADPH oxidase and is required for phagocytosis of Leishmania chagasi promastigotes by macrophages	./cache/cord-000479-u87eaaj8.txt	./txt/cord-000479-u87eaaj8.txt