PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17084997-0	2006	Ethanol oxidation into acetaldehyde by 16 recombinant human cytochrome P450 isoforms: role of CYP2C isoforms in human liver microsomes.	Acetaldehyde	23-35	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	60-75	
6725272-2	1984	This laboratory has recently reported that, in a reconstituted enzyme system containing alcohol-induced isozyme 3a of liver microsomal cytochrome P-450, the sum of acetaldehyde generated by the monooxygenation of ethanol and of hydrogen peroxide produced by the NADPH oxidase activity is inadequate to account for the O2 and NADPH consumed.	Acetaldehyde	164-176	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	135-151	
16713055-6	2006	These observations suggest that NOS2 can behave similarly to cytochrome P-450 in the catalysis of acetaldehyde formation from ethanol via the generation of alpha-hydroxyethyl radical when L-arginine is present.	Acetaldehyde	98-110	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	61-77