PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2844232-6	1988	This revealed that all ligands except NADPH and NADH, which were fully bound, showed differential binding between the adenine end and the nicotinamide end of the molecule: The adenine end always bound with a higher occupancy than the nicotinamide end.	Niacinamide	234-246	2,4-dienoyl-CoA reductase 1	Homo sapiens	38-43	
2844232-6	1988	This revealed that all ligands except NADPH and NADH, which were fully bound, showed differential binding between the adenine end and the nicotinamide end of the molecule: The adenine end always bound with a higher occupancy than the nicotinamide end.	Niacinamide	138-150	2,4-dienoyl-CoA reductase 1	Homo sapiens	38-43	
11796730-4	2002	In the ternary complexes, NADPH is bound in a catalytically competent fashion, with the nicotinamide ring in a position suitable for hydride transfer to FAD.	Niacinamide	88-100	2,4-dienoyl-CoA reductase 1	Homo sapiens	26-31	
19482524-5	2009	Identification of a fragmented mass of m/z 382.94 (nicotinamide+sugar+phosphate) from the NADPH-peptide conjugates supported the intactness of the nicotinamide moiety.	Niacinamide	51-63	2,4-dienoyl-CoA reductase 1	Homo sapiens	90-95	
19482524-5	2009	Identification of a fragmented mass of m/z 382.94 (nicotinamide+sugar+phosphate) from the NADPH-peptide conjugates supported the intactness of the nicotinamide moiety.	Niacinamide	147-159	2,4-dienoyl-CoA reductase 1	Homo sapiens	90-95	
11923299-2	2002	We show in the reductive half-reaction of pentaerythritol tetranitrate (PETN) reductase that NADPH binds to form an enzyme-NADPH charge transfer intermediate prior to hydride transfer from the nicotinamide coenzyme to FMN.	Niacinamide	193-205	2,4-dienoyl-CoA reductase 1	Homo sapiens	93-98	
11923299-2	2002	We show in the reductive half-reaction of pentaerythritol tetranitrate (PETN) reductase that NADPH binds to form an enzyme-NADPH charge transfer intermediate prior to hydride transfer from the nicotinamide coenzyme to FMN.	Niacinamide	193-205	2,4-dienoyl-CoA reductase 1	Homo sapiens	123-128	
10527939-5	1999	The oxidation of NADPH was characterized by a decrease in the A(339) of the reduced nicotinamide with the concomitant appearance of a new chromophore with absorbance maximum at 274 nm, characterized by isosbestic points at 300 and 238 nm.	Niacinamide	84-96	2,4-dienoyl-CoA reductase 1	Homo sapiens	17-22	
10527939-13	1999	A quantitative comparison of difference spectra obtained with NADPH and NMNH indicated that chlorination occurred on the nicotinamide part of the molecule.	Niacinamide	121-133	2,4-dienoyl-CoA reductase 1	Homo sapiens	62-67