id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-265887-g5zhoyo9	Mukherjee, Shruti	Host-membrane interacting interface of the SARS coronavirus envelope protein: Immense functional potential of C-terminal domain	2020-08-11		.txt	text/plain	9085	538	41	(56) Apart from these highly conserved sequences throughout the genus, there are distinct potent glycosylation sites along the stretch that can serve as chaperone interacting motifs to help in the protein folding and/or aid in J o u r n a l P r e -p r o o f Journal Pre-proof trafficking along with the cellular machinery.(57) Glycosylation of particular asparagine residues (Asn 45, Asn 48, Asn 64, and Asn 68) in the SARS-CoV has been shown to be crucial in maintaining the proteinoligomerization events associated with the host membranes. (41) The formation of a disulfide bond may also play a crucial role in the oligomerization of the E protein, forming stable dimers, trimers, and pentamers depending on its functional requirement.(105) Thus even though the TMD spans the lipid bilayer, the CxxC motif could serve as an essential key to defining the membrane-associated oligomerization events-providing newer targets for preemptive therapeutic intervention.	./cache/cord-265887-g5zhoyo9.txt	./txt/cord-265887-g5zhoyo9.txt