id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-009261-97qegnlo	Rieux, Charlotte	Thiopurine Derivative-Induced Fpg/Nei DNA Glycosylase Inhibition: Structural, Dynamic and Functional Insights	2020-03-17		.txt	text/plain	11719	574	52	Among forty compounds, four TXn were better inhibitors than 2TX for Fpg. Unexpectedly, but very interestingly, two dithiolated derivatives more selectively and efficiently inhibit the zincless finger (ZnLF)-containing enzymes (human and mimivirus Neil1 DNA glycosylases hNeil1 and MvNei1, respectively). The crystal structure of LlFpg bound to 14-mer [8-oxoG:C] DNA duplex (which differs from that used in this study only by the damaged nature present in the duplex: an 8-oxoG lesion in place of THF) revealed that the second Fpg molecule can bind to the overhanging base positioned at the 5 end of the damaged strand ( Figure S5b ) [38] . Similar to the 2TX-containing crystal structure, the intramolecular disulfide bridge Cys245-S-S-Cys265 is also formed in the presence of TXn. Not observed previously, one 2TX molecule that is non-covalently bound to the enzyme is inserted at the protein-DNA interface in the vicinity of the ZnF loop and the H2TH motif (Figure 10a,b) , the two DNA binding domains that characterize the Fpg/Nei DNA glycosylase superfamily [29] .	./cache/cord-009261-97qegnlo.txt	./txt/cord-009261-97qegnlo.txt