id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-002808-84np9brx	Campos, Samuel K.	Subcellular Trafficking of the Papillomavirus Genome during Initial Infection: The Remarkable Abilities of Minor Capsid Protein L2	2017-12-03		.txt	text/plain	9673	460	43	How does L2, the minor capsid protein from a non-enveloped virus, complexed with the vDNA within the lumen of intracellular vesicular compartments, interact with a variety of cytosolic sorting molecules to direct its own transport to the TGN? Given the requirement for furin in TGN localization of L2/vDNA, it is very likely that cleavage triggers a structural change that enables L2 to insert and protrude into the local membrane via the TMD to recruit cytosolic SNXs and retromer. Regardless of the precise mechanisms of L2 translocation, the minor capsid protein eventually leaves vesicular compartments and is seen along with vDNA within interphase nuclei of infected cells, localized to punctate nuclear foci called promyelocytic leukemia (PML) nuclear domains, also known as PML oncogenic domains (PODS), or ND10 bodies [108] . The L2 minor capsid protein of low-risk human papillomavirus type 11 interacts with host nuclear import receptors and viral DNA Direct binding of retromer to human papillomavirus type 16 minor capsid protein L2 mediates endosome exit during viral infection	./cache/cord-002808-84np9brx.txt	./txt/cord-002808-84np9brx.txt