PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21541746-4	2012	Evaluation of the active site residues of the CYP7B1 model and validation of the active site architecture were performed via molecular docking experiments: the docking of the substrates 25-hydroxycholesterol and 27-hydroxycholesterol and the inhibitor 3alpha-Adiol identified structurally and functionally important residues.	25-hydroxycholesterol	186-207	cytochrome P450 family 7 subfamily B member 1	Homo sapiens	46-52	
22999953-2	2012	7alpha,25-OHC is synthesized from cholesterol by the stepwise actions of two enzymes, CH25H and CYP7B1, and is metabolized to a 3-oxo derivative by HSD3B7.	25-hydroxycholesterol	7-13	cytochrome P450 family 7 subfamily B member 1	Homo sapiens	96-102	
31828178-2	2019	Lack of CYP7B1 leads to an accumulation of its oxysterol substrates, in particular 25-hydroxycholesterol and 27-hydroxycholesterol that are able to cross the blood-brain barrier and have neurotoxic properties.	25-hydroxycholesterol	83-104	cytochrome P450 family 7 subfamily B member 1	Homo sapiens	8-14	
28147280-3	2017	CH25H and CYP7B1 hydroxylate cholesterol to 7alpha,25-OHC.	25-hydroxycholesterol	51-57	cytochrome P450 family 7 subfamily B member 1	Homo sapiens	10-16	
29689289-1	2018	Dihydroxycholesterols such as 7alpha,25-dihydroxysterols (7alpha,25-OHC) and 7alpha,27-OHC are generated from cholesterol by the enzymes CH25H, CYP7B1 and CYP27A1 in steady state but also in the context of inflammation.	25-hydroxycholesterol	65-71	cytochrome P450 family 7 subfamily B member 1	Homo sapiens	144-150