PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16788056-6	2006	The coenzyme specificity, broad substrate specificity and inhibitor sensitivity of the enzyme differed from those of rat NADPH-dependent 17beta-hydroxysteroid dehydrogenase type 5, which was cloned from the liver and characterized using the recombinant enzyme.	NADP	121-126	aldo-keto reductase family 1, member C12	Rattus norvegicus	137-172	
9882448-6	1999	TBE-R1 utilized NADH or NADPH equally as cofactor, and the Km values of NADH and NADPH for TBE with TBE-R1 were estimated to be 15 and 29 microM, respectively.	NADP	24-29	aldo-keto reductase family 1, member C12	Rattus norvegicus	0-6	
12005031-3	2001	Using NAD or NADP as the cofactor, 17beta-hydroxysteroid dehydrogenase (substrate: 5-androstene-3beta,17beta-diol) peaks were observed on pnd 16 for fetal Leydig cells and on pnd 19 and 37 for adult Leydig cells.	NADP	13-17	aldo-keto reductase family 1, member C12	Rattus norvegicus	35-70	
12005031-7	2001	To conclude: (1) Generally, a stronger reaction for 17beta-hydroxysteroid dehydrogenase is shown with NAD as cofactor than with NADP; using NADP, fetal Leydig cells show a stronger staining than adult Leydig cells.	NADP	128-132	aldo-keto reductase family 1, member C12	Rattus norvegicus	52-87	
9882448-6	1999	TBE-R1 utilized NADH or NADPH equally as cofactor, and the Km values of NADH and NADPH for TBE with TBE-R1 were estimated to be 15 and 29 microM, respectively.	NADP	81-86	aldo-keto reductase family 1, member C12	Rattus norvegicus	100-106	
6938086-6	1980	These findings may be explained by the observed decrease in 17 beta-hydroxysteroid dehydrogenase (17 beta-HSD) activity, due to an insufficient supply of NADPH, in the older vs. earlier stages of development.	NADP	154-159	aldo-keto reductase family 1, member C12	Rattus norvegicus	60-96