PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7628466-11	1995	Replacement of Arg44 by Lys however affects NADPH binding, resulting in a low yield of the charge-transfer species between reduced flavin and NADP+.	4,6-dinitro-o-cresol	131-137	2,4-dienoyl-CoA reductase 1	Homo sapiens	44-49	
7881908-5	1994	Complexes of OYE with p-hydroxybenzaldehyde, beta-estradiol, and an NADPH analog show all three binding at a common site, stacked on the flavin.	4,6-dinitro-o-cresol	137-143	2,4-dienoyl-CoA reductase 1	Homo sapiens	68-73	
7737455-6	1995	The flavin ring structure moves substantially in the active site, probably to enable substrate and product exchange into this site and possibly to regulate the reduction of the flavin by NADPH.	4,6-dinitro-o-cresol	4-10	2,4-dienoyl-CoA reductase 1	Homo sapiens	187-192	
7737455-6	1995	The flavin ring structure moves substantially in the active site, probably to enable substrate and product exchange into this site and possibly to regulate the reduction of the flavin by NADPH.	4,6-dinitro-o-cresol	177-183	2,4-dienoyl-CoA reductase 1	Homo sapiens	187-192	
34095235-1	2021	The biliverdin reductase B (BLVRB) class of enzymes catalyze the NADPH-dependent reduction of multiple flavin substrates and are emerging as critical players in cellular redox regulation.	4,6-dinitro-o-cresol	103-109	2,4-dienoyl-CoA reductase 1	Homo sapiens	65-70	
16274228-15	2005	The lack of activity results from the failure of the mutants to readily form the out conformation required for flavin reduction by NADPH.	4,6-dinitro-o-cresol	111-117	2,4-dienoyl-CoA reductase 1	Homo sapiens	131-136