PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22020119-9	2012	Quantitatively, CYP26B1 had a lower K(m) (19nM) and V(max) (0.8 pmol/min/pmol) than CYP26A1 (K(m)=50 nM and V(max)=10 pmol/min/pmol) for formation of 4-OH-RA.	4-oh-ra	150-157	cytochrome P450 family 26 subfamily B member 1	Homo sapiens	16-23	
22020119-10	2012	The major atRA metabolites 4-OH-RA, 18-OH-RA and 4-oxo-RA were all substrates of CYP26A1 and CYP26B1, and CYP26A1 had a 2-10-fold higher catalytic activity towards all substrates tested.	4-oh-ra	27-34	cytochrome P450 family 26 subfamily B member 1	Homo sapiens	93-100	
27416800-5	2016	Holo-CRABPs had higher affinity for CYP26B1 than free atRA, but both apo-CRABPs inhibited the formation of 4-OH-RA by CYP26B1.	4-oh-ra	107-114	cytochrome P450 family 26 subfamily B member 1	Homo sapiens	118-125	
31419517-2	2019	The three CYP26 family enzymes, CYP26A1, CYP26B1 and CYP26C1 have all been shown to metabolize all-trans-retinoic acid (atRA) it"s 9-cisRA and 13-cisRA isomers and primary metabolites 4-OH-RA and 4-oxo-RA with high efficiency.	4-oh-ra	184-191	cytochrome P450 family 26 subfamily B member 1	Homo sapiens	41-48