PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33105932-5	2020	Decreased AKR1B10 activity was detected by reduced coenzyme II (NADPH) absorbance at 340 nm.	NADP	43-62	aldo-keto reductase family 1 member B10	Homo sapiens	10-17	
27595938-4	2016	Using the differential scanning fluorimetry and the circular dichroism varying the urea concentration and temperature, we found that when the coenzyme NADP+ was absent, inhibitors such as isolithocholic acid stabilized the aldo-keto reductase AKR1A1 upon binding, which showed actually the three-state folding, but destabilized AKR1B10.	NADP	151-156	aldo-keto reductase family 1 member B10	Homo sapiens	328-335	
27595938-5	2016	In contrast, in the presence of NADP+ , they destabilized AKR1A1 and stabilized AKR1B10.	NADP	32-37	aldo-keto reductase family 1 member B10	Homo sapiens	80-87	
22319498-1	2012	The human aldo-keto reductase AKR1B10, originally identified as an aldose reductase-like protein and human small intestine aldose reductase, is a cytosolic NADPH-dependent reductase that metabolizes a variety of endogenous compounds, such as aromatic and aliphatic aldehydes and dicarbonyl compounds, and some drug ketones.	NADP	156-161	aldo-keto reductase family 1 member B10	Homo sapiens	30-37	
25376835-7	2015	Sequence alignments identified the NADPH-dependent AKR3G1 having 41.5 and 40% identity with the human enzymes AKR1B1 and AKR1B10, respectively.	NADP	35-40	aldo-keto reductase family 1 member B10	Homo sapiens	121-128	
24598757-6	2014	Moreover, the combination of surface lysine methylation and the introduction of K125R and V301L mutations enabled the determination of the X-ray crystallographic structure of the corresponding AKR1B10-NADP(+)-JF0064 complex.	NADP	201-205	aldo-keto reductase family 1 member B10	Homo sapiens	193-200	
23295227-1	2013	Only one crystal structure is currently available for tumor marker AKR1B10, complexed with NADP(+) and tolrestat, which is an aldose reductase inhibitor (ARI) of the carboxylic acid type.	NADP	91-95	aldo-keto reductase family 1 member B10	Homo sapiens	67-74	
19013440-8	2009	AKR1B10 catalyzed 4-MP reduction with a 30-fold increase in activity using NADPH as cofactor compared with NADH.	NADP	75-80	aldo-keto reductase family 1 member B10	Homo sapiens	0-7	
19706287-6	2009	Molecular docking studies of the curcuminoids in the AKR1B10-NADP(+) complex and site-directed mutagenesis of the putative binding residues suggest that Gln114, Val301 and Gln303 are important for determining the inhibitory potency and selectivity of the curcuminoids.	NADP	61-68	aldo-keto reductase family 1 member B10	Homo sapiens	53-60	
19028477-9	2009	Similarly, kinetic parameters K(m) and k(cat) (NADPH, DL-glyceraldehyde) for the reduction of dl-glyceraldehyde by wild-type AKR1B10 are 2.2+/-0.2 mM and 0.71+/-0.05 sec(-1), respectively.	NADP	47-52	aldo-keto reductase family 1 member B10	Homo sapiens	125-132	
19028477-11	2009	For dl-glyceraldehyde reduction that is catalyzed by the Cys299Ser mutant AKR1B10, K(m) is 15.8+/-1.0mM and k(cat) (NADPH, DL-glyceraldehyde) is 2.8+/-0.2 sec(-1).	NADP	116-121	aldo-keto reductase family 1 member B10	Homo sapiens	74-81	
20460771-6	2010	Molecular docking studies of mefenamic acid and glycyrrhetic acid in the AKR1B10-nicotinamide adenine dinucleotide phosphate (NADP(+)) complex and site-directed mutagenesis of the putative binding residues suggest that the side chain of Val301 and a hydrogen-bonding network among residues Val301, Gln114 and Ser304 are important for determining the inhibitory potency and selectivity of the non-steroidal antiinflammatory drugs.	NADP	81-124	aldo-keto reductase family 1 member B10	Homo sapiens	73-80	
20460771-6	2010	Molecular docking studies of mefenamic acid and glycyrrhetic acid in the AKR1B10-nicotinamide adenine dinucleotide phosphate (NADP(+)) complex and site-directed mutagenesis of the putative binding residues suggest that the side chain of Val301 and a hydrogen-bonding network among residues Val301, Gln114 and Ser304 are important for determining the inhibitory potency and selectivity of the non-steroidal antiinflammatory drugs.	NADP	126-133	aldo-keto reductase family 1 member B10	Homo sapiens	73-80	
19013440-9	2009	As was observed for aldose reductase (AKR1B1) 4-ONE rapidly inactivates AKR1B10, while this inactivation is not observed when the enzyme is pre-incubated with NADPH.	NADP	159-164	aldo-keto reductase family 1 member B10	Homo sapiens	72-79	
19013440-13	2009	However, it is still inactivated by 4-ONE in the absence of NADPH.While the best substrates for AKR1B10 are retinals, the high catalytic efficiency together with the protection from inactivation by NADPH suggests a role of AKR1B10 in the detoxification of biogenic aldehydes.	NADP	60-65	aldo-keto reductase family 1 member B10	Homo sapiens	96-103	
19013440-13	2009	However, it is still inactivated by 4-ONE in the absence of NADPH.While the best substrates for AKR1B10 are retinals, the high catalytic efficiency together with the protection from inactivation by NADPH suggests a role of AKR1B10 in the detoxification of biogenic aldehydes.	NADP	198-203	aldo-keto reductase family 1 member B10	Homo sapiens	96-103	
19013440-13	2009	However, it is still inactivated by 4-ONE in the absence of NADPH.While the best substrates for AKR1B10 are retinals, the high catalytic efficiency together with the protection from inactivation by NADPH suggests a role of AKR1B10 in the detoxification of biogenic aldehydes.	NADP	198-203	aldo-keto reductase family 1 member B10	Homo sapiens	223-230	
18087047-7	2007	The crystal structure of the ternary complex AKR1B10-NADP(+)-tolrestat was determined at 1.25-A resolution.	NADP	53-60	aldo-keto reductase family 1 member B10	Homo sapiens	45-52	
16381663-9	2006	In addition to its reducing activity, AKR1B10 catalyzed the NADP+-dependent oxidation of the secondary alcohol (S)-1-indanol to 1-indanone with high enzymatic efficiency (kcat/Km=112 mM-1 min-1).	NADP	60-65	aldo-keto reductase family 1 member B10	Homo sapiens	38-45