id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-002110-pbb247lp	Chen, Chin-Pei	Membrane protein assembly: two cytoplasmic phosphorylated serine sites of Vpu from HIV-1 affect oligomerization	2016-06-29		.txt	text/plain	5987	327	60	title: Membrane protein assembly: two cytoplasmic phosphorylated serine sites of Vpu from HIV-1 affect oligomerization Coarse-grained molecular dynamic simulations with models of wild-type and mutant Vpu in a hydrated lipid bilayer supported the experimental data in demonstrating that, in addition to a previously known role in downregulation of host factors, the phosphorylation sites of Vpu also modulate oligomerization. Coarse grained molecular dynamics (CGMD) simulations of Vpu proteins embedded in a planar lipid bilayer model were chosen to evaluate the oligomeric assembly under likely in vivo conditions such as an abundance of Vpu proteins in a large lipid patch and simulated over a long time period. The dynamics data was plotted as area of the peak of the higher oligomer (A P1 ), divided by the total area of A P1 and the peak area of the dimer (A P2 ), A P1 /(A P1 + A P2 ), over time for Vpu-WT with a double logarithmic growth curve (Fig. 4b , black and Table 2 ). Three-dimensional structure of the channel-forming trans-membrane domain of virus protein "u" (Vpu) from HIV-1	./cache/cord-002110-pbb247lp.txt	./txt/cord-002110-pbb247lp.txt