PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10421620-7 1999 The enzyme activity was significantly (p <.01) and stereoselectively inhibited by CYP2D1 inhibitors quinine and quinidine (not by CYP2C or CYP3A inhibitors), and by anti-CYP2D6 peptide antiserum (not by anti-CYP2C, -CYP2B, or -CYP3A antibodies). Quinine 103-110 cytochrome P450, family 2, subfamily d, polypeptide 1 Rattus norvegicus 85-91 9721180-9 1998 The human CYP2D6-specific inhibitor quinidine and the rat CYP2D1-specific inhibitor quinine were both shown to be inhibitors of bufuralol 1"-hydroxylase activity for dog liver microsomes, CYP2D15 WT2, and the CYP2D15 V1 variant with nearly equal potency. Quinine 84-91 cytochrome P450, family 2, subfamily d, polypeptide 1 Rattus norvegicus 58-64 9067326-4 1997 In vivo, quinine (20 mg/kg) and budipine (10 mg/kg) produced a marked suppression in brain and plasma hydromorphone levels detected after the peripheral administration of hydrocodone, thus confirming that the doses used suppressed CYP2D1 activity. Quinine 9-16 cytochrome P450, family 2, subfamily d, polypeptide 1 Rattus norvegicus 231-237 7835220-7 1994 The main enzyme concerned in the 1- and 8-hydroxylation of both enantiomers is considered to be CYP2D1 from the following observation: the marked strain differences between Sprague-Dawley and Dark Agouti rats and competitive inhibition by quinine. Quinine 239-246 cytochrome P450, family 2, subfamily d, polypeptide 1 Rattus norvegicus 96-102 9413916-8 1997 Quinine (Ki = 0.06 microM) and quinidine (Ki = 2.0 microM), selective inhibitors of CYP2D1, competitively inhibited 8-hydroxycarteolol formation. Quinine 0-7 cytochrome P450, family 2, subfamily d, polypeptide 1 Rattus norvegicus 84-90 9833017-2 1997 To determine the impact of impaired AMP metabolism on its behavioural effects, AMP-induced hyperactivity, AMP discrimination and AMP self-administration were examined in male Wistar rats with or without pretreatment with the CYP2D1 inhibitors quinine and budipine. Quinine 243-250 cytochrome P450, family 2, subfamily d, polypeptide 1 Rattus norvegicus 225-231 9833017-3 1997 In vivo, quinine (20 mg/kg) and budipine (10 mg/kg) increased the plasma area under the curve of AMP 4-fold and 3.6-fold respectively, and decreased the plasma levels of 4-OH-AMP, 3-fold and 8.6-fold, confirming that the doses used suppressed CYP2D1 activity. Quinine 9-16 cytochrome P450, family 2, subfamily d, polypeptide 1 Rattus norvegicus 243-249 9105413-7 1997 The contribution of CYP2D1 to the O-dealkylation of EM/NEM and CD/NCD was further confirmed by use of the specific CYP2D1 inhibitors quinine and propafenone. Quinine 133-140 cytochrome P450, family 2, subfamily d, polypeptide 1 Rattus norvegicus 20-26 9105413-7 1997 The contribution of CYP2D1 to the O-dealkylation of EM/NEM and CD/NCD was further confirmed by use of the specific CYP2D1 inhibitors quinine and propafenone. Quinine 133-140 cytochrome P450, family 2, subfamily d, polypeptide 1 Rattus norvegicus 115-121 8586645-6 1995 Quinine and quinidine showed 400 and 80 times, respectively, higher affinity for MBP than for debrisoquine 4-hydroxylase. Quinine 0-7 cytochrome P450, family 2, subfamily d, polypeptide 1 Rattus norvegicus 94-120 8185638-7 1994 By using quinine as a specific inhibitor of the enzyme, CYP2D1 was identified as an intermediate affinity site in the Wistar strain and was shown to have impaired activity in the DA strain. Quinine 9-16 cytochrome P450, family 2, subfamily d, polypeptide 1 Rattus norvegicus 56-62