id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-341129-eo0vjcmk	Kielian, Margaret	Virus membrane-fusion proteins: more than one way to make a hairpin	2006		.txt	text/plain	6986	333	45	Virus membrane-fusion proteins drive the fusion reaction by undergoing a major conformational change that is triggered by interactions with the target cell. The class I membrane-fusion reaction is mediated by the refolding of the fusion protein to a highly stable rod-like structure with a central trimeric α-helical coiled coil. In vitro studies using the ectodomains of both the alphavirus and flavivirus proteins showed that trimerization requires insertion of the fusion peptide into target membranes 64, 65 . However, H230A virus undergoes apparently normal conformational changes upon exposure to low pH, including heterodimer dissociation and fusion-loop exposure, cholesterol-dependent target-membrane insertion, and formation of the E1 homotrimer. Recent work indicates that exogenous domain III blocks class II membrane fusion and infection by binding to the fusion protein during the low-pH-induced conformational change 92 .	./cache/cord-341129-eo0vjcmk.txt	./txt/cord-341129-eo0vjcmk.txt