PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8589517-2	1995	The MPG gene plays a key role in the excision repair of methylated adenine residues and has been localized upstream of the alpha-globin gene cluster in human and mouse.	Adenine	67-74	N-methylpurine DNA glycosylase	Homo sapiens	4-7	
9708359-2	1998	The amount of AP sites in MMS-treated HeLa cells transiently increased at 3 h, then gradually decreased to 40% at 24 h. The presence of adenine, an inhibitor of AP endonucleases, in the repair incubation of MMS-treated cells induced moderate accumulation of AP sites, suggesting inhibition of the activities of MPG as well as AP endonucleases by adenine metabolites.	Adenine	136-143	N-methylpurine DNA glycosylase	Homo sapiens	311-314	
8895486-1	1996	N-Methylpurine-DNA glycosylase (MPG), a ubiquitous DNA repair protein, removes several N-alkylpurine adducts, hypoxanthine, cyclic ethenoadducts of adenine, guanine and cytosine and 8-oxoguanine from DNA.	Adenine	148-155	N-methylpurine DNA glycosylase	Homo sapiens	0-30	
8895486-1	1996	N-Methylpurine-DNA glycosylase (MPG), a ubiquitous DNA repair protein, removes several N-alkylpurine adducts, hypoxanthine, cyclic ethenoadducts of adenine, guanine and cytosine and 8-oxoguanine from DNA.	Adenine	148-155	N-methylpurine DNA glycosylase	Homo sapiens	32-35	
26719496-5	2016	The guanine-to-adenine change causes substitution of the normal glutamic acid codon (GAG) with a mutant lysine codon (AAG) at position 312 (E312 K mutation).	Adenine	15-22	N-methylpurine DNA glycosylase	Homo sapiens	118-121	
88735-3	1979	At the position corresponding to amino acid 17, replacement of an adenine by a uracil changes the triplet AAG, which codes for lysine in the normal beta chain, to an amber termination codon, UAG.	Adenine	66-73	N-methylpurine DNA glycosylase	Homo sapiens	106-109	
19449863-1	2009	Human alkyladenine DNA glycosylase (AAG) locates and excises a wide variety of damaged purine bases from DNA, including hypoxanthine that is formed by the oxidative deamination of adenine.	Adenine	11-18	N-methylpurine DNA glycosylase	Homo sapiens	36-39	
20840885-7	2010	Here, we show that binding to AAG is, in fact, dramatically more thermodynamically favorable for hypoxanthine, at least, a specific lesion, produced by oxidative deamination of adenine, than for undamaged adenine.	Adenine	177-184	N-methylpurine DNA glycosylase	Homo sapiens	30-33	
20840885-7	2010	Here, we show that binding to AAG is, in fact, dramatically more thermodynamically favorable for hypoxanthine, at least, a specific lesion, produced by oxidative deamination of adenine, than for undamaged adenine.	Adenine	205-212	N-methylpurine DNA glycosylase	Homo sapiens	30-33	
21877721-8	2011	Finally, our work shows that the natural base adenine (A) is further inserted into the AAG active site than the damaged substrates, which results in the loss of a hydrogen bond with Y127 and misaligns the general base (E125) and water nucleophile to lead to poor nucleophile activation.	Adenine	46-53	N-methylpurine DNA glycosylase	Homo sapiens	87-90	
14688248-4	2004	Comparisons of the rate enhancements for excision of normal and modified purine nucleobases provide evidence that AAG excludes the normal purines via steric clashes with the exocyclic amino groups of adenine and guanine.	Adenine	200-207	N-methylpurine DNA glycosylase	Homo sapiens	114-117	
17018265-3	2007	AAG removes primarily damaged adenine residues.	Adenine	30-37	N-methylpurine DNA glycosylase	Homo sapiens	0-3	
17655363-11	2007	We find that the N9-H of hypoxanthine is more acidic than that of adenine and guanine, pointing to a way that AAG could discriminate damaged bases from normal bases.	Adenine	66-73	N-methylpurine DNA glycosylase	Homo sapiens	110-113	
17655363-12	2007	We hypothesize that AAG may cleave certain damaged nucleobases as anions and that the active site may take advantage of a nonpolar environment to favor deprotonated hypoxanthine as a leaving group versus deprotonated adenine or guanine.	Adenine	217-224	N-methylpurine DNA glycosylase	Homo sapiens	20-23