PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15159582-2	2004	Recently, NEIL1, a human homolog of Escherichia coli DNA glycosylase endonuclease VIII, has been identified and shown to exhibit broad substrate specificity for a variety of types of pyrimidine-base damage.	pyrimidine	183-193	nei like DNA glycosylase 1	Homo sapiens	10-15	
17432829-7	2007	The results of our investigations provide structural explanations for the ability of hNeil1 to excise a variety of oxidative lesions: they possess common chemical features, namely, a pyrimidine-like ring and shared hydrogen bond donor-acceptor properties, which allow the lesions to fit well in the binding pocket, which is somewhat flexible.	pyrimidine	183-193	nei like DNA glycosylase 1	Homo sapiens	85-91	
22858590-2	2012	The human endonuclease VIII homologue NEIL1 removes a broad spectrum of oxidized pyrimidine and purine lesions.	pyrimidine	81-91	nei like DNA glycosylase 1	Homo sapiens	10-27	
22858590-2	2012	The human endonuclease VIII homologue NEIL1 removes a broad spectrum of oxidized pyrimidine and purine lesions.	pyrimidine	81-91	nei like DNA glycosylase 1	Homo sapiens	38-43	
15056851-3	2004	In human cells, oxidative pyrimidine lesions are generally removed by hNTH1, hNEIL1, or hNEIL2, whereas oxidative purine lesions are removed by hOGG1.	pyrimidine	26-36	nei like DNA glycosylase 1	Homo sapiens	77-83	
14734554-1	2004	In human cells, oxidative pyrimidine lesions are restored by the base excision repair pathway initiated by homologues of Endo III (hNTH1) and Endo VIII (hNEIL1 and hNEIL2).	pyrimidine	26-36	nei like DNA glycosylase 1	Homo sapiens	153-159