id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-321162-pgd34ewv	Holmes, Kathryn V.	Tunicamycin resistant glycosylation of a coronavirus glycoprotein: Demonstration of a novel type of viral glycoprotein	1981-12-31		.txt	text/plain	4822	239	47	Abstract Tunicamycin has different effects on the glycosylation of the two envelope glycoproteins of mouse hepatitis virus (MHV), a coronavirus. The coronavirus envelope envelope glycoprotein E1 appears to be a novel type of viral glycoprotein which is post-translationally glycosylated by a tunicamycin-resistant process that yields oligosaccharide side chains different from those of N-linked glycoproteins. of the synthesis, glycosylation, and intracellular transport of glycoproteins is essential to understanding the structure and function of cell membranes and the role of oligosaccharides in glycoprotein processing and secretion. Labeling with monospecific fluorescent antibody against isolated El or E2 (Sturman et cd, 1980) showed that El remains restricted to the perinuclear area of the cell while E2, like most other viral glycoproteins, migrates rapidly via intracellular membranes to the plasma membrane (Doller and Holmes, 1980) .	./cache/cord-321162-pgd34ewv.txt	./txt/cord-321162-pgd34ewv.txt