PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
26222439-5	2015	In contrast to AKR1B10, which strongly prefers all-trans-retinaldehyde, AKR1B15 exhibits superior catalytic efficiency with 9-cis-retinaldehyde, the best substrate found for this enzyme.	Retinaldehyde	47-70	aldo-keto reductase family 1 member B10	Homo sapiens	15-22	
31028727-4	2019	AKR1B10 and AKR1B15 share 92% sequence identity, as well as the capability of being active towards retinaldehyde.	Retinaldehyde	99-112	aldo-keto reductase family 1 member B10	Homo sapiens	0-7	
31028727-12	2019	In general, the AKR1B10 mutants mirrored well the specific functional features of AKR1B15, i.e., the different preferences towards the retinaldehyde isomers, the much higher activity with steroids and ketones, and the unique behavior with inhibitors.	Retinaldehyde	135-148	aldo-keto reductase family 1 member B10	Homo sapiens	16-23	
21277289-3	2011	Since the enzyme exhibits broad substrate specificities toward various xenobiotics such as anti-tumor drugs or various endogenous compounds such as retinaldehyde, AKR1B10 may play an important role in tumor progression or drug resistance.	Retinaldehyde	148-161	aldo-keto reductase family 1 member B10	Homo sapiens	163-170	
22529810-2	2012	Only AKR1B10 and 1B12, with all-trans-retinaldehyde, and AKR1C3, with 9-cis-retinaldehyde, display high catalytic efficiency.	Retinaldehyde	28-51	aldo-keto reductase family 1 member B10	Homo sapiens	5-12	
22529810-3	2012	Major structural determinants for retinaldehyde isomer specificity are located in the external loops (A and C for AKR1B10, and B for AKR1C3), as assessed by site-directed mutagenesis and molecular dynamics.	Retinaldehyde	34-47	aldo-keto reductase family 1 member B10	Homo sapiens	114-121	
23220004-12	2013	Consistent with its substrate specificity towards retinaldehyde, AKR1B10 was more effectively inhibited by synthetic retinoids than AKR1B1.	Retinaldehyde	50-63	aldo-keto reductase family 1 member B10	Homo sapiens	65-72	
21329680-5	2011	AKR1B1 (aldose reductase) is related to secondary diabetic complications, while AKR1B10 is induced in cancer cells and is highly active with all-trans-retinaldehyde.	Retinaldehyde	141-164	aldo-keto reductase family 1 member B10	Homo sapiens	80-87	
19014918-3	2009	With all-trans-retinaldehyde, AKR1B10 shows a much higher k(cat) value than AKR1B1 (18 min(-1)vs. 0.37 min(-1)) and a catalytic efficiency comparable to that of the best retinaldehyde reductases.	Retinaldehyde	5-28	aldo-keto reductase family 1 member B10	Homo sapiens	30-37	
19014918-6	2009	Overall it is suggested that the rate-limiting step in the reaction mechanism with retinaldehyde differs between AKR1B1 and AKR1B10.	Retinaldehyde	83-96	aldo-keto reductase family 1 member B10	Homo sapiens	124-131	
18087047-8	2007	Molecular dynamics models of AKR1B10 and AKR1B1 with retinaldehyde isomers and site-directed mutagenesis show that subtle differences at the entrance of the retinoid-binding site, especially at position 125, are determinant for the all-trans-retinaldehyde specificity of AKR1B10.	Retinaldehyde	53-66	aldo-keto reductase family 1 member B10	Homo sapiens	29-36	
16787387-2	2006	Enzymes of the MDR (medium-chain dehydrogenase/reductase), SDR (short-chain dehydrogenase/reductase) and AKR (aldo-keto reductase) superfamilies have been reported to catalyse the conversion between retinol and retinaldehyde.	Retinaldehyde	211-224	aldo-keto reductase family 1 member B10	Homo sapiens	105-108	
18087047-8	2007	Molecular dynamics models of AKR1B10 and AKR1B1 with retinaldehyde isomers and site-directed mutagenesis show that subtle differences at the entrance of the retinoid-binding site, especially at position 125, are determinant for the all-trans-retinaldehyde specificity of AKR1B10.	Retinaldehyde	242-255	aldo-keto reductase family 1 member B10	Homo sapiens	29-36	
18087047-8	2007	Molecular dynamics models of AKR1B10 and AKR1B1 with retinaldehyde isomers and site-directed mutagenesis show that subtle differences at the entrance of the retinoid-binding site, especially at position 125, are determinant for the all-trans-retinaldehyde specificity of AKR1B10.	Retinaldehyde	242-255	aldo-keto reductase family 1 member B10	Homo sapiens	271-278