PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
30448017-6	2019	Here, we hypothesized that NEIL1 could excise NM-Fapy-dG and that NEIL3, a closely related DNA glycosylase, could excise both NM-Fapy-dG and AFB1-Fapy-dG.	nm-fapy-dg	46-56	nei endonuclease VIII-like 1 (E. coli)	Mus musculus	27-32
30448017-7	2019	Product formation from the reaction of human NEIL1 with ds oligodeoxynucleotides containing a unique NM-Fapy-dG followed a bi-component exponential function under single turnover conditions.	nm-fapy-dg	101-111	nei like DNA glycosylase 1	Homo sapiens	45-50
30448017-6	2019	Here, we hypothesized that NEIL1 could excise NM-Fapy-dG and that NEIL3, a closely related DNA glycosylase, could excise both NM-Fapy-dG and AFB1-Fapy-dG.	nm-fapy-dg	126-136	nei like 3 (E. coli)	Mus musculus	66-71
30448017-11	2019	Mus musculus NEIL3 (MmuNEIL3Delta324) excised NM-Fapy-dG from single-stranded (ss) DNA (turnover rate of ~0.4 min-1), but not from ds DNA.	nm-fapy-dg	46-56	nei like 3 (E. coli)	Mus musculus	13-18
30448017-14	2019	Overall, the data suggest that both NEIL1 and NEIL3 may protect cells against cytotoxic and mutagenic effects of NM-Fapy-dG, but NEIL1 may have a unique role in initiation of base excision repair of AFB1-Fapy-dG.	nm-fapy-dg	113-123	nei endonuclease VIII-like 1 (E. coli)	Mus musculus	36-41
30448017-14	2019	Overall, the data suggest that both NEIL1 and NEIL3 may protect cells against cytotoxic and mutagenic effects of NM-Fapy-dG, but NEIL1 may have a unique role in initiation of base excision repair of AFB1-Fapy-dG.	nm-fapy-dg	113-123	nei like 3 (E. coli)	Mus musculus	46-51