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