PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11135730-0	2001	Cytochrome P-450 2B6 is responsible for interindividual variability of propofol hydroxylation by human liver microsomes.	Propofol	71-79	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	0-20	
11135730-6	2001	RESULTS: Propofol hydroxylation by hepatic microsomes showed more than 19-fold variability and was most closely correlated to CYP2B6 protein content (r = 0.904), and the CYP2B6 marker activities, S-mephenytoin N-demethylation (r = 0.919) and bupropion hydroxylation (r = 0.854).	Propofol	9-17	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	126-132	
11135730-6	2001	RESULTS: Propofol hydroxylation by hepatic microsomes showed more than 19-fold variability and was most closely correlated to CYP2B6 protein content (r = 0.904), and the CYP2B6 marker activities, S-mephenytoin N-demethylation (r = 0.919) and bupropion hydroxylation (r = 0.854).	Propofol	9-17	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	170-176	
11135730-8	2001	All of the CYPs evaluated were capable of hydroxylating propofol; however, CYP2B6 and CYP2C9 were most active.	Propofol	56-64	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	75-81	
11135730-11	2001	CONCLUSIONS: Cytochrome P-450 2B6, and to a lesser extent CYP2C9, contribute to the oxidative metabolism of propofol.	Propofol	108-116	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	13-33