PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17432829-4	2007	To elucidate structural properties determining hNeil1"s substrate specificities, we have investigated it in complex with two pairs of representative well-repaired substrates: the R- and S-spiroiminodihydantoin (Sp) stereoisomers, nonplanar further oxidation products of guanine, and the 5R,6S- and 5S,6R-thymine glycol (Tg) stereoisomers, the most prevalent oxidative lesions of thymine.	spiroiminodihydantoin	211-213	nei like DNA glycosylase 1	Homo sapiens	47-53	
32302101-7	2020	The primary factor that recognizes DNA lesions is the DNA damage-sensing factor XPC-RAD23B (XPC), while the glycosylase NEIL1 is known to remove Gh and Sp lesions from double-stranded DNA.	spiroiminodihydantoin	152-154	nei like DNA glycosylase 1	Homo sapiens	120-125	
32302101-12	2020	These slow kinetics are attributed to the dissociation of XPC-DNA complexes that allow for the rebinding of NEIL1 to the temporarily exposed Gh or Sp lesions, and the incisions observed under these steady-state conditions.	spiroiminodihydantoin	147-149	nei like DNA glycosylase 1	Homo sapiens	108-113	
27880870-8	2017	This review focuses on initiation of BER by the mammalian Nei-like1-3 (NEIL1-3) glycosylases for removal of 2Ih, Sp, and Gh.	spiroiminodihydantoin	113-115	nei like DNA glycosylase 1	Homo sapiens	71-76	
23926102-5	2013	Although Sp and Gh in quadruplex DNA were good substrates for mNeil3 and NEIL1, none of the glycosylases had activity on quadruplex DNA containing 8-oxoG.	spiroiminodihydantoin	9-11	nei like DNA glycosylase 1	Homo sapiens	73-78	
20099873-1	2010	Human DNA glycosylase NEIL1 exhibits a superior ability to remove oxidized guanine lesions guanidinohydantoin (Gh) and spiroiminodihydantoin (Sp) from duplex DNA in comparison to other substrates.	spiroiminodihydantoin	119-140	nei like DNA glycosylase 1	Homo sapiens	22-27	
20099873-1	2010	Human DNA glycosylase NEIL1 exhibits a superior ability to remove oxidized guanine lesions guanidinohydantoin (Gh) and spiroiminodihydantoin (Sp) from duplex DNA in comparison to other substrates.	spiroiminodihydantoin	142-144	nei like DNA glycosylase 1	Homo sapiens	22-27	
20099873-2	2010	In this work, Gh and Sp lesions in bubble, bulge, and single-stranded DNA were found to be good substrates for NEIL1 but were typically excised at much slower rates than from canonical duplex substrates.	spiroiminodihydantoin	21-23	nei like DNA glycosylase 1	Homo sapiens	111-116	
15533836-0	2005	Recognition of the oxidized lesions spiroiminodihydantoin and guanidinohydantoin in DNA by the mammalian base excision repair glycosylases NEIL1 and NEIL2.	spiroiminodihydantoin	36-57	nei like DNA glycosylase 1	Homo sapiens	139-144	
15533836-7	2005	Herein we report that two recently identified mammalian glycosylases, NEIL1 and NEIL2, showed a high affinity for recognition and cleavage of DNA containing Gh/Ia and Sp lesions.	spiroiminodihydantoin	167-169	nei like DNA glycosylase 1	Homo sapiens	70-75	
15533836-10	2005	NEIL1 was able to excise the Sp lesion opposite the four natural bases in double-stranded DNA, however, NEIL2 showed little cleavage activity against the Sp lesion in duplex DNA although DNA trapping studies show recognition and binding of NEIL2 to this lesion.	spiroiminodihydantoin	29-31	nei like DNA glycosylase 1	Homo sapiens	0-5	
34060590-1	2021	The oxidatively generated genotoxic spiroiminodihydantoin (Sp) lesions are well-known substrates of base excision repair (BER) pathway initiated by the bifunctional DNA glycosylase NEIL1.	spiroiminodihydantoin	36-57	nei like DNA glycosylase 1	Homo sapiens	181-186	
34060590-1	2021	The oxidatively generated genotoxic spiroiminodihydantoin (Sp) lesions are well-known substrates of base excision repair (BER) pathway initiated by the bifunctional DNA glycosylase NEIL1.	spiroiminodihydantoin	59-61	nei like DNA glycosylase 1	Homo sapiens	181-186	
34060590-2	2021	In this work we reported that the excision kinetics of the single Sp lesions site-specifically embedded in the covalently closed circular DNA plasmids (contour length 2686 base pairs) by NEIL1 are biphasic under single-turnover conditions ((NEIL1)>>(SpDNApl)) in contrast to monophasic excision kinetics of the same lesions embedded in147-mer Sp-modified DNA duplexes.	spiroiminodihydantoin	66-68	nei like DNA glycosylase 1	Homo sapiens	187-192	
34060590-2	2021	In this work we reported that the excision kinetics of the single Sp lesions site-specifically embedded in the covalently closed circular DNA plasmids (contour length 2686 base pairs) by NEIL1 are biphasic under single-turnover conditions ((NEIL1)>>(SpDNApl)) in contrast to monophasic excision kinetics of the same lesions embedded in147-mer Sp-modified DNA duplexes.	spiroiminodihydantoin	66-68	nei like DNA glycosylase 1	Homo sapiens	241-246