id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-354726-b9xvycyk	nan	Envelope glycoprotein interactions in coronavirus assembly	1995-10-02		.txt	text/plain	8008	405	53	Using coimmunoprecipitation analysis we demonstrated that the M and S proteins of mouse hepatitis virus (MHV) interact specifically forming heteromultimeric complexes in infected cells. Yet, the self-association of the MHV envelope glycoproteins into higher order complexes is indicative of its role in the sorting of the viral membrane proteins and in driving the formation of the viral lipoprotein coat in virus assembly. Yet, the self-association of the MHV envelope glycoproteins into higher order complexes is indicative of its role in the sorting of the viral membrane proteins and in driving the formation of the viral lipoprotein coat in virus assembly. We have shown previously that neither of the envelope glycoproteins accumulates at the site of budding when expressed independently: the M protein alone localizes to the Golgi complex (Rottier and Rose, 1987; Krijnse Locker et al., 1992a; Klumperman et al., 1994) , whereas the S protein is transported to the plasma membrane (Vennema, H., and P.	./cache/cord-354726-b9xvycyk.txt	./txt/cord-354726-b9xvycyk.txt