PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6133718-0	1983	Characterization of cimetidine, ranitidine, and related structures" interaction with cytochrome P-450.	Ranitidine	32-42	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	85-101	
2568738-3	1989	We studied the effect of cimetidine, ranitidine and famotidine on the monoxygenase, the oxidase and the peroxidase action of cytochrome P-450.	Ranitidine	37-47	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	125-141	
2568738-5	1989	Ranitidine and famotidine (both pharmacodynamically more potent than cimetidine) only slightly affected cytochrome P-450 activities.	Ranitidine	0-10	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	104-120	
3992022-5	1985	Activities of hepatic cytochrome P-450-dependent metabolizing enzymes such as aminopyrine- and TMO N-demethylase and aniline hydroxylase activity were decreased by pretreatment of rats with cimetidine, whereas in the rats pretreated with ranitidine, these enzyme activities were not changed.	Ranitidine	238-248	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	22-38	
6089451-1	1984	Of four H2 blockers, cimetidine, tiotidine, oxmetidine and ranitidine, all except ranitidine showed ligand (type II) interactions with oxidized cytochrome P-450.	Ranitidine	59-69	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	144-160	
6089451-1	1984	Of four H2 blockers, cimetidine, tiotidine, oxmetidine and ranitidine, all except ranitidine showed ligand (type II) interactions with oxidized cytochrome P-450.	Ranitidine	82-92	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	144-160	
6089451-3	1984	All H2 blockers except for ranitidine (up to 400 microM) produced a concentration-dependent inhibitory effect of the metabolic intermediate (MI)-cytochrome P-450 complex formation which is displayed during metabolism of tofenacine in PB hepatic microsomes in vitro.	Ranitidine	27-37	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	145-161	
6124064-2	1982	Ranitidine interacts with liver microsomes from rats pretreated with different inducers of cytochrome P-450 to produce substrate difference optical spectra with a peak at 426-429 nm and a trough at 390-400 nm.	Ranitidine	0-10	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	91-107	
6124064-4	1982	Cytochrome P-450 reduced with dithionite in the presence of ranitidine produced substrate difference spectra with a peak at 447 nm.	Ranitidine	60-70	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	0-16	
6124064-6	1982	Ks values for the interaction of ranitidine with cytochrome P-450 (not reduced), calculated from double reciprocal plots, were in the range 1.4-2.8 mM.	Ranitidine	33-43	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	49-65	
6124064-14	1982	spectra of cytochrome P-450 from phenobarbital-pretreated rats, in the presence of ranitidine, reveal two types of interaction depending on the ranitidine concentration.	Ranitidine	83-93	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	11-27	
6124064-14	1982	spectra of cytochrome P-450 from phenobarbital-pretreated rats, in the presence of ranitidine, reveal two types of interaction depending on the ranitidine concentration.	Ranitidine	144-154	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	11-27	
1364175-2	1992	H2 antagonists, cimetidine, famotidine and ranitidine were used to inhibit cytochrome P-450 in rat liver.	Ranitidine	43-53	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	75-91