PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22505406-0	2012	Structure of the His269Arg mutant of the rat aldose reductase-like protein AKR1B14 complexed with NADPH.	NADP	98-103	aldo-keto reductase family 1, member B7	Rattus norvegicus	45-82	
11716357-0	2001	Enzymes in pancreatic islets that use NADP(H) as a cofactor including evidence for a plasma membrane aldehyde reductase.	NADP	38-45	aldo-keto reductase family 1, member B7	Rattus norvegicus	101-119	
21586312-5	2011	The bile acid binding to AKR1B14 mainly accelerates the NADP(+) dissociation, the rate-limited step of the enzyme reaction.	NADP	56-63	aldo-keto reductase family 1, member B7	Rattus norvegicus	25-32	
21586312-8	2011	The results, together with the docking of the bile acid in the recently determined crystal structure of AKR1B14, identify the bile acid-binding site of which His269 plays a key role in significant activation through its electrostatic interaction with the carboxyl group of bile acid, facilitating the release of NADP(+).	NADP	312-316	aldo-keto reductase family 1, member B7	Rattus norvegicus	104-111	
21168333-2	2011	The crystal structure of the binary complex (AKR1B14-NADPH) was determined at 1.86A resolution, and showed that the adenine ring and the 2"-phosphate group of the coenzyme formed pi-stacking and electrostatic interactions with the imidazole ring and ND1 atom, respectively, of His269, which is not conserved in other aldose reductase-like proteins.	NADP	53-58	aldo-keto reductase family 1, member B7	Rattus norvegicus	45-52	
21048316-2	2010	AKR1B14 catalyzed the nicotinamide adenine dinucleotide phosphate reduced form (NADPH)-dependent reduction of carbonyl compounds (derived from lipid peroxidation and glycation), xenobiotic aromatic aldehydes and some aromatic ketones.	NADP	22-65	aldo-keto reductase family 1, member B7	Rattus norvegicus	0-7	
21048316-2	2010	AKR1B14 catalyzed the nicotinamide adenine dinucleotide phosphate reduced form (NADPH)-dependent reduction of carbonyl compounds (derived from lipid peroxidation and glycation), xenobiotic aromatic aldehydes and some aromatic ketones.	NADP	80-85	aldo-keto reductase family 1, member B7	Rattus norvegicus	0-7	
2768281-1	1989	The human promyelocytic leukemia cell line HL60 differentiates to monocyte/macrophage cells when incubated with NADPH-linked high-Km aldehyde reductase (EC 1.1.1.2) purified from the cytosol of rat kidney.	NADP	112-117	aldo-keto reductase family 1, member B7	Rattus norvegicus	133-151	
2117925-2	1990	All aldose reductase inhibitors examined inhibited aldehyde reductase to some extent both in the reductive reaction as determined with glyceraldehyde as substrate and NADPH as coenzyme, and in the oxidative reaction where L-gulonic acid was oxidized to D-glucuronic acid in the presence of NADP+.	NADP	167-172	aldo-keto reductase family 1, member B7	Rattus norvegicus	51-69	
2117925-2	1990	All aldose reductase inhibitors examined inhibited aldehyde reductase to some extent both in the reductive reaction as determined with glyceraldehyde as substrate and NADPH as coenzyme, and in the oxidative reaction where L-gulonic acid was oxidized to D-glucuronic acid in the presence of NADP+.	NADP	290-295	aldo-keto reductase family 1, member B7	Rattus norvegicus	51-69	
2119895-7	1990	Aldose reductase utilized both reduced nicotinamide adenine dinucleotide phosphate (NADPH) and reduced nicotinamide adenine dinucleotide (NADH) as coenzymes, whereas aldehyde reductase utilized only NADPH.	NADP	199-204	aldo-keto reductase family 1, member B7	Rattus norvegicus	166-184	
2500152-6	1989	Aldose reductase utilized both NADPH and NADH as coenzyme, whereas aldehyde reductase utilized only NADPH.	NADP	100-105	aldo-keto reductase family 1, member B7	Rattus norvegicus	67-85	
7119799-4	1982	Evidence is presented that the further metabolism of the aldehyde by aldehyde reductase and the removal of hydrogen peroxide by glutathione peroxidase both release the limitation of NADP+ availability for the pentose phosphate pathway by leading to the oxidation of NADPH.	NADP	182-187	aldo-keto reductase family 1, member B7	Rattus norvegicus	69-87	
7119799-4	1982	Evidence is presented that the further metabolism of the aldehyde by aldehyde reductase and the removal of hydrogen peroxide by glutathione peroxidase both release the limitation of NADP+ availability for the pentose phosphate pathway by leading to the oxidation of NADPH.	NADP	266-271	aldo-keto reductase family 1, member B7	Rattus norvegicus	69-87