id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-289274-3g67f8sw	Tosoni, Elena	Nucleolin stabilizes G-quadruplex structures folded by the LTR promoter and silences HIV-1 viral transcription	2015-10-15		.txt	text/plain	8066	389	51	The implementation of electrophorethic mobility shift assay and pull-down experiments coupled with mass spectrometric analysis revealed that the cellular protein nucleolin is able to specifically recognize G-quadruplex structures present in the LTR promoter. In this direction, the significance of these structures as focal points of interactions with host and viral factors is supported also by the observation that G4-folded sequences are specifically recognized by various viral proteins, such as the Epstein Barr Virus Nuclear Antigen 1 (34, 35) and the SARS coronavirus unique domain (SUD), which occurs exclusively in highly pathogenic strains (36) . The LTR-II+III+IV oligonucleotide was incubated with extracts of HIV-1 producing and non-producing 293T cells to test whether the presence of viral proteins affected in any detectable way the observed EMSA profiles ( Figure 1C ). Positive identification was also confirmed by performing EMSA analysis of samples that included the G4-folded wt and mutant LTR-II+III+IV sequences with either nuclear extracts or purified human NCL. (B) EMSA analysis of the binding of nuclear extract (NE) proteins and purified NCL to the wt and mutant LTR sequences.	./cache/cord-289274-3g67f8sw.txt	./txt/cord-289274-3g67f8sw.txt