PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15865448-7	2005	As a result, the widely expressed CRBPI, which binds all-trans-retinol with much higher affinity than all-trans-retinaldehyde, restricts the oxidation of all-trans-retinol by RDH12, but has little effect on the reduction of all-trans-retinaldehyde, and CRALBP inhibits the reduction of 11-cis-retinal stronger than the oxidation of 11-cis-retinol, in accord with its higher affinity for 11-cis-retinal.	Retinaldehyde	102-125	retinol binding protein 1	Homo sapiens	34-39	
23220004-7	2013	The relative contribution of each enzyme type in retinoid metabolism is discussed in terms of the different subcellular localization, topology of membrane-bound enzymes, kinetic constants, binding affinity of CRBP for retinol and retinaldehyde, and partition of retinoid pools between membranes and cytoplasm.	Retinaldehyde	230-243	retinol binding protein 1	Homo sapiens	209-213	
18569334-6	2008	is capable to oxidize all-trans-retinol bound to CRBP (holo-CRBP) to all-trans-retinaldehyde and then to all-trans-retinoic acid.	Retinaldehyde	69-92	retinol binding protein 1	Homo sapiens	49-53	
18569334-6	2008	is capable to oxidize all-trans-retinol bound to CRBP (holo-CRBP) to all-trans-retinaldehyde and then to all-trans-retinoic acid.	Retinaldehyde	69-92	retinol binding protein 1	Homo sapiens	60-64	
15865448-7	2005	As a result, the widely expressed CRBPI, which binds all-trans-retinol with much higher affinity than all-trans-retinaldehyde, restricts the oxidation of all-trans-retinol by RDH12, but has little effect on the reduction of all-trans-retinaldehyde, and CRALBP inhibits the reduction of 11-cis-retinal stronger than the oxidation of 11-cis-retinol, in accord with its higher affinity for 11-cis-retinal.	Retinaldehyde	224-247	retinol binding protein 1	Homo sapiens	34-39	
15865448-7	2005	As a result, the widely expressed CRBPI, which binds all-trans-retinol with much higher affinity than all-trans-retinaldehyde, restricts the oxidation of all-trans-retinol by RDH12, but has little effect on the reduction of all-trans-retinaldehyde, and CRALBP inhibits the reduction of 11-cis-retinal stronger than the oxidation of 11-cis-retinol, in accord with its higher affinity for 11-cis-retinal.	Retinaldehyde	286-300	retinol binding protein 1	Homo sapiens	34-39	
15865448-7	2005	As a result, the widely expressed CRBPI, which binds all-trans-retinol with much higher affinity than all-trans-retinaldehyde, restricts the oxidation of all-trans-retinol by RDH12, but has little effect on the reduction of all-trans-retinaldehyde, and CRALBP inhibits the reduction of 11-cis-retinal stronger than the oxidation of 11-cis-retinol, in accord with its higher affinity for 11-cis-retinal.	Retinaldehyde	387-401	retinol binding protein 1	Homo sapiens	34-39	
10329026-6	1999	Several retinol dehydrogenase (RDH) enzymes, members of the short-chain dehydrogenase/reductase (SDR) gene superfamily, catalyze the first and rate-limiting step that generates retinaldehyde from retinol bound to cellular retinol-binding protein (holo-CRBP).	Retinaldehyde	177-190	retinol binding protein 1	Homo sapiens	252-256	
10559215-6	1999	Employing cellular retinoid-binding protein (CRBP), purified from human liver, demonstrated that E1 isozyme (but not E2 isozyme) could utilize CRBP-bound retinaldehyde as substrate, a feature thought to be specific to retinaldehyde dehydrogenases.	Retinaldehyde	154-167	retinol binding protein 1	Homo sapiens	10-43	
10559215-6	1999	Employing cellular retinoid-binding protein (CRBP), purified from human liver, demonstrated that E1 isozyme (but not E2 isozyme) could utilize CRBP-bound retinaldehyde as substrate, a feature thought to be specific to retinaldehyde dehydrogenases.	Retinaldehyde	154-167	retinol binding protein 1	Homo sapiens	45-49	
10559215-6	1999	Employing cellular retinoid-binding protein (CRBP), purified from human liver, demonstrated that E1 isozyme (but not E2 isozyme) could utilize CRBP-bound retinaldehyde as substrate, a feature thought to be specific to retinaldehyde dehydrogenases.	Retinaldehyde	154-167	retinol binding protein 1	Homo sapiens	143-147	
8440409-7	1993	For example, the cellular retinol-binding protein, CRBP, has been implicated in retinol uptake, retinol esterification, mobilization of retinyl esters, and the initial oxidation of retinol to retinaldehyde.	Retinaldehyde	192-205	retinol binding protein 1	Homo sapiens	51-55	
1542003-5	1992	The ability of pure hCRBP(II) to bind all-trans-retinol, retinal and retinoic acid was examined by competitive binding assay and compared with the binding specificity of pure human cellular retinol-binding protein (hCRBP).	Retinaldehyde	57-64	retinol binding protein 1	Homo sapiens	20-25	
34480899-10	2021	These results suggest that P450 27C1 directly accepts all-trans retinol and retinaldehyde from CRBP-1 and all-trans retinoic acid from CRABP-2, but not from CRABP-1.	Retinaldehyde	76-89	retinol binding protein 1	Homo sapiens	95-101