PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33784377-2	2021	Tethering of UNG2 to proliferating cell nuclear antigen (PCNA) allows rapid post-replicative removal of misincorporated uracil, but potential "pre-replicative" removal of deaminated cytosines in ssDNA has been questioned since this could mediate mutagenic translesion synthesis and induction of double-strand breaks.	Uracil	120-126	proliferating cell nuclear antigen	Homo sapiens	21-55	
33784377-2	2021	Tethering of UNG2 to proliferating cell nuclear antigen (PCNA) allows rapid post-replicative removal of misincorporated uracil, but potential "pre-replicative" removal of deaminated cytosines in ssDNA has been questioned since this could mediate mutagenic translesion synthesis and induction of double-strand breaks.	Uracil	120-126	proliferating cell nuclear antigen	Homo sapiens	57-61	
22521144-11	2012	Modulation of PCNA- versus RPA-binding may thus constitute a functional switch for UNG2 in cells subsequent to genotoxic stress and potentially also during the processing of uracil at the immunoglobulin locus in antigen-stimulated B cells.	Uracil	174-180	proliferating cell nuclear antigen	Homo sapiens	14-18	
18761016-0	2008	Interplay between DNA polymerase and proliferating cell nuclear antigen switches off base excision repair of uracil and hypoxanthine during replication in archaea.	Uracil	109-115	proliferating cell nuclear antigen	Homo sapiens	37-71	
20466601-1	2010	Uracil-DNA glycosylase, UNG2, interacts with PCNA and initiates post-replicative base excision repair (BER) of uracil in DNA.	Uracil	111-117	proliferating cell nuclear antigen	Homo sapiens	45-49	
18761016-3	2008	Addition of the processivity factor proliferating cell nuclear antigen (PCNA) resulted in increased affinity of the polymerase for all primer-templates, producing extremely tight complexes when uracil (K(d)=16 pM) or hypoxanthine (K(d)=65 pM) was present.	Uracil	194-200	proliferating cell nuclear antigen	Homo sapiens	36-70	
18761016-3	2008	Addition of the processivity factor proliferating cell nuclear antigen (PCNA) resulted in increased affinity of the polymerase for all primer-templates, producing extremely tight complexes when uracil (K(d)=16 pM) or hypoxanthine (K(d)=65 pM) was present.	Uracil	194-200	proliferating cell nuclear antigen	Homo sapiens	72-76	
18761016-9	2008	Thus, when the PCNA-polymerase complex encounters uracil/hypoxanthine in DNA templates, base excision repair is switched off, protecting the complex from a repair pathway that is dangerous in the context of single-stranded DNA formed during replication.	Uracil	50-56	proliferating cell nuclear antigen	Homo sapiens	15-19	
16216562-8	2005	Addition of PCNA (30-810 pmol) to standard uracil-DNA glycosylase reactions containing linear [uracil-(3)H]DNA stimulated UNG2 catalytic activity up to 2.6-fold.	Uracil	43-49	proliferating cell nuclear antigen	Homo sapiens	12-16	
11927597-8	2002	Nevertheless, our results raise the possibility that Pa-UDGa may be a functional analog of hUNG2 for PCNA-dependent postreplicative removal of misincorporated uracil.	Uracil	159-165	proliferating cell nuclear antigen	Homo sapiens	101-105	
10393198-6	1999	These results demonstrate rapid post-replicative removal of incorporated uracil by UNG2 and indicate the formation of a BER complex that contains UNG2, RPA and PCNA close to the replication fork.	Uracil	73-79	proliferating cell nuclear antigen	Homo sapiens	160-164