PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6372998-1	1984	The concept that alcohol dehydrogenase (ADH) is involved in the metabolism of methylazoxymethanol (MAM) was examined in a model consisting of two strains of the deer mouse, Peromyscus maniculatus, one of which has a normal complement of the enzyme [ADH(+)], and the other, which completely lacks it [ADH(-)].	methylazoxymethanol	78-97	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	40-43	
9848112-0	1998	The role of alcohol dehydrogenase in the metabolism of the colon carcinogen methylazoxymethanol.	methylazoxymethanol	76-95	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	12-33	
9848112-1	1998	The aim of this study was to determine whether the cytosolic enzyme alcohol dehydrogenase (ADH) activates methylazoxymethanol (MAM) in the mouse colon and whether differential tumor susceptibility in the mouse is dependent, in part, on strain-related differences in MAM metabolism by ADH.	methylazoxymethanol	106-125	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	68-89	
9848112-1	1998	The aim of this study was to determine whether the cytosolic enzyme alcohol dehydrogenase (ADH) activates methylazoxymethanol (MAM) in the mouse colon and whether differential tumor susceptibility in the mouse is dependent, in part, on strain-related differences in MAM metabolism by ADH.	methylazoxymethanol	106-125	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	91-94	
6372998-0	1984	Non-alcohol dehydrogenase-mediated metabolism of methylazoxymethanol in the deer mouse, Peromyscus maniculatus.	methylazoxymethanol	49-68	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	4-25	
6372998-1	1984	The concept that alcohol dehydrogenase (ADH) is involved in the metabolism of methylazoxymethanol (MAM) was examined in a model consisting of two strains of the deer mouse, Peromyscus maniculatus, one of which has a normal complement of the enzyme [ADH(+)], and the other, which completely lacks it [ADH(-)].	methylazoxymethanol	78-97	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	17-38	
6372998-1	1984	The concept that alcohol dehydrogenase (ADH) is involved in the metabolism of methylazoxymethanol (MAM) was examined in a model consisting of two strains of the deer mouse, Peromyscus maniculatus, one of which has a normal complement of the enzyme [ADH(+)], and the other, which completely lacks it [ADH(-)].	methylazoxymethanol	99-102	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	17-38	
6372998-1	1984	The concept that alcohol dehydrogenase (ADH) is involved in the metabolism of methylazoxymethanol (MAM) was examined in a model consisting of two strains of the deer mouse, Peromyscus maniculatus, one of which has a normal complement of the enzyme [ADH(+)], and the other, which completely lacks it [ADH(-)].	methylazoxymethanol	99-102	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	40-43	
6372998-4	1984	Pyrazole, a potent inhibitor of ADH, inhibited MAM metabolism as well as liver DNA methylation in the ADH(+) strain; however similar inhibition of these processes also occurred in the ADH(-) strain.	methylazoxymethanol	47-50	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	32-35