@article {1332027,
	title = {N-terminal domain of human uracil DNA glycosylase (hUNG2) promotes targeting to uracil sites adjacent to ssDNA-dsDNA junctions},
	journal = {Nucleic Acids Res},
	volume = {46},
	number = {14},
	year = {2018},
	month = {2018 Aug 21},
	pages = {7169-7178},
	abstract = {The N-terminal domain (NTD) of nuclear human uracil DNA glycosylase (hUNG2) assists in targeting hUNG2 to replication forks through specific interactions with replication protein A (RPA). Here, we explored hUNG2 activity in the presence and absence of RPA using substrates with ssDNA-dsDNA junctions that mimic structural features of the replication fork and transcriptional R-loops. We find that when RPA is tightly bound to the ssDNA overhang of junction DNA substrates, base excision by hUNG2 is strongly biased toward uracils located 21 bp or less from the ssDNA-dsDNA junction. In the absence of RPA, hUNG2 still showed an 8-fold excision bias for uracil located ,
	issn = {1362-4962},
	doi = {10.1093/nar/gky525},
	author = {Weiser, Brian P and Rodriguez, Gaddiel and Cole, Philip A and Stivers, James T}
}
