PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20345925-7 2010 Treatment of cells with CYP2D6 inhibitors (quinidine, propanolol, metoprolol or timolol) at varying concentrations significantly increased the neurotoxicity caused by 1-methyl-4-phenylpyridinium (MPP+) at 10 and 25 microM by between 9 +/- 1 and 22 +/- 5% (P < 0.01). Propranolol 54-64 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 24-30 12728976-0 2003 Dose-response relationships of propranolol in Chinese subjects with different CYP2D6 genotypes. Propranolol 31-42 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 78-84 20372009-3 2010 Major metabolism of drugs was ascribed to CYP1A2 for theophylline and caffeine, and CYP1A2 and CYP2D6 for propranolol and mexiletine. Propranolol 106-117 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 95-101 19817501-25 2009 Since the contribution of CYP2D6 is greater for metoprolol than for carvedilol, propranolol and timolol, a stronger gene-dose effect is seen with this beta-blocker, while such an effect is lesser or marginal in other beta-blockers. Propranolol 80-91 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 26-32 18535530-7 2008 Co administration of venlafaxine and propranolol, 2 drugs with affinity for the same cytochrome P450 isoenzyme (CYP2D6), may have contributed to drug accumulation and pulmonary toxicity. Propranolol 37-48 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 112-118 17333164-1 2007 Detailed molecular dynamics (MD) simulations have been performed to reproduce and rationalize the experimental finding that the F483A mutant of CYP2D6 has lower affinity for R-propranolol than for S-propranolol. Propranolol 174-187 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 144-150 17333164-1 2007 Detailed molecular dynamics (MD) simulations have been performed to reproduce and rationalize the experimental finding that the F483A mutant of CYP2D6 has lower affinity for R-propranolol than for S-propranolol. Propranolol 197-210 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 144-150 17333164-5 2007 The approach that calculates the free energies of exchanging R-propranolol with S-propranolol in the F483A mutant relative to the exchange free energy in WT CYP2D6 accurately reproduced the experimental binding data. Propranolol 61-74 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 157-163 12728976-2 2003 Propranolol is metabolized by polymorphic CYP2D6. Propranolol 0-11 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 42-48 12728976-3 2003 We postulate that the lower propranolol dosage in Chinese is due to a slower CYP2D6 metabolism. Propranolol 28-39 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 77-83 12728976-5 2003 Chinese subjects of different CYP2D6*1/CYP2D6*10 genotypes have been shown to have different propranolol pharmacokinetic characteristics. Propranolol 93-104 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 30-36 12728976-5 2003 Chinese subjects of different CYP2D6*1/CYP2D6*10 genotypes have been shown to have different propranolol pharmacokinetic characteristics. Propranolol 93-104 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 39-45 12728976-6 2003 In this study, we compared the beta-blockade effects of propranolol in Chinese subjects of the two different CYP2D6 genotypes. Propranolol 56-67 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 109-115 12728976-12 2003 RESULTS: Despite therebeing higher S-propranolol plasma concentration in CYP2D6*10 subjects than in CYP2D6*1 subjects at 10- and 20-mg dosage, the dose-response relationship was not significantly different in these subjects. Propranolol 35-48 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 73-79 10903420-5 2000 Inhibition studies using antibodies and characterization of CYP2D6 enzymes expressed in insect cells or human lymphoblastoid cells indicated that the enantioselectivity of PL oxidation, especially the ring 4- and 5-hydroxylations reflected the properties of CYP2D6 in human liver microsomes. Propranolol 172-174 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 60-66 11602512-2 2001 A series of 1"-mono-, di-, and trifluorinated analogs of propranolol and related steric congeners was prepared, and their metabolism was examined in recombinant-expressed CYP2D6. Propranolol 57-68 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 171-177 10945865-5 2000 Significant correlations were noted between propranolol 4-hydroxylation and ethoxyresorufin-O-deethylation (marker of CYP1A2 activity), with marked improvement in the correlations when CYP2D6-mediated propranolol 4-hydroxylation was inhibited with quinidine. Propranolol 44-55 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 185-191 10945865-5 2000 Significant correlations were noted between propranolol 4-hydroxylation and ethoxyresorufin-O-deethylation (marker of CYP1A2 activity), with marked improvement in the correlations when CYP2D6-mediated propranolol 4-hydroxylation was inhibited with quinidine. Propranolol 201-212 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 185-191 10945865-8 2000 CYP1A2- and CYP2D6-mediated propranolol 4-hydroxylation was about 70 and 100% higher (P <.05 for both), respectively, in African-Americans compared with Caucasians. Propranolol 28-39 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 12-18 11038161-8 2000 Metoprolol and dextromethorphan were primarily CYP2D6 substrates and propranolol was metabolized by CYP2D6 (59%), CYP1A2 (26%), and CYP2C19 (15%). Propranolol 69-80 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 100-106 10903420-5 2000 Inhibition studies using antibodies and characterization of CYP2D6 enzymes expressed in insect cells or human lymphoblastoid cells indicated that the enantioselectivity of PL oxidation, especially the ring 4- and 5-hydroxylations reflected the properties of CYP2D6 in human liver microsomes. Propranolol 172-174 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 258-264 9256169-6 1997 The binding of [3H]GBR-12935 to CYP2D6 was decreased partially by substrates or inhibitors of CYP2D isoforms (quinine, quinidine, propranolol, bufuralol, imipramine, and desipramine). Propranolol 130-141 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 32-38 9399616-0 1997 Impact of CYP2D6 poor metabolizer phenotype on propranolol pharmacokinetics and response. Propranolol 47-58 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 10-16 9399616-1 1997 We conducted an open-label study to determine the impact of cytochrome P-4502D6 (CYP2D6) on propranolol pharmacokinetics and response in 12 healthy men with CYP2D6 extensive metabolizer (EM) phenotype and 3 healthy men with CYP2D6 poor metabolizer (PM) phenotype. Propranolol 92-103 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 60-79 9399616-1 1997 We conducted an open-label study to determine the impact of cytochrome P-4502D6 (CYP2D6) on propranolol pharmacokinetics and response in 12 healthy men with CYP2D6 extensive metabolizer (EM) phenotype and 3 healthy men with CYP2D6 poor metabolizer (PM) phenotype. Propranolol 92-103 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 81-87 9256169-6 1997 The binding of [3H]GBR-12935 to CYP2D6 was decreased partially by substrates or inhibitors of CYP2D isoforms (quinine, quinidine, propranolol, bufuralol, imipramine, and desipramine). Propranolol 130-141 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 32-37 7895609-8 1994 Quinidine, a specific inhibitor of CYP2D6, inhibited propranolol 4- and 5-hydroxylase activities selectively and in a concentration-dependent manner. Propranolol 53-64 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 35-41 8946477-3 1996 The promethazine hydroxylase in human liver microsomes was inhibited by SKF-525A, propranolol, sparteine, quinidine and anti-CYP2D6 serum suggesting involvement of a P450 related to CYP2D6. Propranolol 82-93 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 182-188 7554699-0 1995 Propranolol disposition in Chinese subjects of different CYP2D6 genotypes. Propranolol 0-11 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 57-63 7554699-1 1995 Propranolol pharmacokinetics among different genotypes of CYP2D6 was compared in this study. Propranolol 0-11 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 58-64 7554699-10 1995 This study shows a different propranolol disposition in Chinese subjects of different CYP2D6 genotypes. Propranolol 29-40 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 86-92 8877032-0 1996 Variable contribution of CYP2D6 to the N-dealkylation of S-(-)-propranolol by human liver microsomes. Propranolol 57-74 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 25-31 8877032-1 1996 Recombinant cDNA expression systems for CYP2D6 have been shown to have significant catalytic activity with respect to the N-dealkylation of propranolol. Propranolol 140-151 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 40-46 8877032-3 1996 We have re-evaluated the role of CYP2D6 in the dealkylation of S-(-)-propranolol using a bank of 10 human livers characterized for their specific CYP2D6 and CYP1A2 activities, the latter enzyme being known to be involved substantially in the formation of N-desisopropylpropranolol. Propranolol 63-80 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 33-39 7640150-4 1995 alpha-Naphthoflavone and 7-ethoxyresorufin (selective inhibitors of CYP1A1/2) inhibited the N-desisopropylation of R- and S-propranolol by human liver microsomes by 20 and 40%, respectively, while quinidine (a selective inhibitor of CYP2D6) abolished the 4-hydroxylation of both propranolol enantiomers almost completely. Propranolol 124-135 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 233-239 7640150-15 1995 Recombinant human CYP1A2 and CYP2D6 exhibited comparable catalytic activity with respect to the N-desisopropylation of both propranolol enantiomers; only expressed CYP2D6 exhibited a marked catalytic activity with respect to the 4-hydroxylation of both propranolol enantiomers. Propranolol 124-135 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 29-35 7640150-15 1995 Recombinant human CYP1A2 and CYP2D6 exhibited comparable catalytic activity with respect to the N-desisopropylation of both propranolol enantiomers; only expressed CYP2D6 exhibited a marked catalytic activity with respect to the 4-hydroxylation of both propranolol enantiomers. Propranolol 124-135 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 164-170 7640150-15 1995 Recombinant human CYP1A2 and CYP2D6 exhibited comparable catalytic activity with respect to the N-desisopropylation of both propranolol enantiomers; only expressed CYP2D6 exhibited a marked catalytic activity with respect to the 4-hydroxylation of both propranolol enantiomers. Propranolol 253-264 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 29-35 7640150-15 1995 Recombinant human CYP1A2 and CYP2D6 exhibited comparable catalytic activity with respect to the N-desisopropylation of both propranolol enantiomers; only expressed CYP2D6 exhibited a marked catalytic activity with respect to the 4-hydroxylation of both propranolol enantiomers. Propranolol 253-264 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 164-170 7895609-12 1994 These results indicate that propranolol 5-hydroxylation, as well as 4-hydroxylation, is mainly catalyzed by CYP2D6 in human liver microsomes. Propranolol 28-39 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 108-114 7946944-0 1994 Inhibition of CYP2D6 activity by treatment with propranolol and the role of 4-hydroxy propranolol. Propranolol 48-59 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 14-20 7946944-2 1994 The 4-hydroxylation of propranolol by rat and human liver microsomes is associated with formation of a chemically reactive species which binds irreversibly to cytochrome P4502D6 (CYP2D6) destroying its catalytic function. Propranolol 23-34 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 159-177 7946944-2 1994 The 4-hydroxylation of propranolol by rat and human liver microsomes is associated with formation of a chemically reactive species which binds irreversibly to cytochrome P4502D6 (CYP2D6) destroying its catalytic function. Propranolol 23-34 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 179-185 7946944-12 1994 We conclude that, although treatment with propranolol 80 mg twice daily significantly decreases the catalytic function of CYP2D6, the inhibition is insufficient to result in phenocopying. Propranolol 42-53 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 122-128 35586822-1 2022 Background and Purpose: This study was conducted to explore the plasma drug concentration of propranolol in Chinese Han patients with infantile haemangioma (IH) and the influencing factors, as well as the relationship among plasma drug concentrations of propranolol, beta1-AR mutation and CYP2D6 188C>T, efficacy, and safety. Propranolol 93-104 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 289-295 34581987-7 2021 Propranolol (a CYP2D mechanism-based inhibitor), versus vehicle pre-treatments, increased brain oxycodone, and decreased brain oxymorphone/oxycodone drug level ratios (an in vivo CYP2D activity phenotype in the brain) in males and females in estrus, but not in females in diestrus. Propranolol 0-11 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 15-20 34581987-7 2021 Propranolol (a CYP2D mechanism-based inhibitor), versus vehicle pre-treatments, increased brain oxycodone, and decreased brain oxymorphone/oxycodone drug level ratios (an in vivo CYP2D activity phenotype in the brain) in males and females in estrus, but not in females in diestrus. Propranolol 0-11 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 179-184 34287102-9 2022 This metabolic profile in a patient with normal CYP2D6-metabolizer status based on genotyping supports CYP2D6 inhibition by paroxetine and propranolol, two strong mechanism-based inhibitors. Propranolol 139-150 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 48-54 34287102-9 2022 This metabolic profile in a patient with normal CYP2D6-metabolizer status based on genotyping supports CYP2D6 inhibition by paroxetine and propranolol, two strong mechanism-based inhibitors. Propranolol 139-150 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 103-109 34287102-11 2022 CONCLUSION: Marked and prolonged serotonin toxicity was attributed to increased M2 production due to paroxetine- and propranolol-related CYP2D6 inhibition of tramadol metabolism. Propranolol 117-128 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 137-143 32189192-9 2020 propranolol irreversibly inhibited human CYP2D6 in TG brain but not mouse CYP2D in TG and WT brain. Propranolol 0-11 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 41-47 32761352-8 2020 A 24-h ICV propranolol pretreatment, which selectively and irreversibly inhibits human CYP2D6 in TG brain, increased harmine-induced hypothermia. Propranolol 11-22 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 87-93 32219146-0 2020 Influence of Cytochrome P450 2D6 Polymorphisms on the Efficacy of Oral Propranolol in Treating Infantile Hemangioma. Propranolol 71-82 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 13-32 32219146-1 2020 Objective: The aim of this study is to evaluate the association of genetic polymorphisms in Cytochrome P450 2D6(CYP2D6) and the change in VEGF levels with the response to propranolol in patients with Infantile hemangiomas (IH). Propranolol 171-182 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 92-111 32219146-1 2020 Objective: The aim of this study is to evaluate the association of genetic polymorphisms in Cytochrome P450 2D6(CYP2D6) and the change in VEGF levels with the response to propranolol in patients with Infantile hemangiomas (IH). Propranolol 171-182 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 112-118 32219146-10 2020 Patients with CYP2D6 (rs1135840) G/G homozygote had the highest response rate to propranolol. Propranolol 81-92 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 14-20 32219146-13 2020 Conclusion: The response to propranolol treatment in IH patients was associated with the gene polymorphism of CYP2D6 (rs1135840). Propranolol 28-39 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 110-116 31648367-0 2020 Propranolol is a mechanism-based inhibitor of CYP2D and CYP2D6 in humanized CYP2D6-transgenic mice: effects on activity and drug response. Propranolol 0-11 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 56-62 31648367-0 2020 Propranolol is a mechanism-based inhibitor of CYP2D and CYP2D6 in humanized CYP2D6-transgenic mice: effects on activity and drug response. Propranolol 0-11 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 76-82 31648367-3 2020 Our purpose was to characterize propranolol as a CYP2D inhibitor in human and mouse, and to develop a method for in vivo manipulation of CYP2D6 enzyme activity which could be used to investigate the role of CYP2D6 in drug-induced behaviours. Propranolol 32-43 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 49-54 31648367-5 2020 We also examined the impact of 24 h propranolol pre-treatment on serum levels of the CYP2D6 substrate haloperidol and haloperidol-induced catalepsy. Propranolol 36-47 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 85-91 31648367-11 2020 Manipulation of CYP2D with propranolol in vivo in TG and WT mice alters drug response, which will be useful for future investigation of the impact of variation in CYP2D6 on drug interactions and drug responses. Propranolol 27-38 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 163-169 30604050-7 2020 The concomitant intake of CYP2D6 inhibitors, risperidone, metoprolol, or propranolol was found to increase aripiprazole concentrations in patients with at least one wild-type CYP2D6*1 allele. Propranolol 73-84 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 175-181 32286940-8 2020 Propranolol is a substrate of CYP2D6, CYP1A2 and CYP2C19, retaining potential pharmacokinetic interactions with co-administered drugs. Propranolol 0-11 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 30-36 24119207-1 2014 Propranolol, the substrate of cytochrome P450 (CYP) 1A2 and CYP2D6, has been reported to be in high concentrations in end-stage renal disease (ESRD) patients. Propranolol 0-11 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 60-66 26489037-0 2016 Influence of CYP2D6 and beta2-adrenergic receptor gene polymorphisms on the hemodynamic response to propranolol in Chinese Han patients with cirrhosis. Propranolol 100-111 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 13-19 26489037-2 2016 This study is to evaluate the relationship between CYP2D6 and beta2-adrenergic receptor (beta2-AR) gene polymorphisms and the hemodynamic response to propranolol in Chinese Han patients. Propranolol 150-161 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 51-57 26489037-12 2016 The multivariate logistic regression analysis indicated that CYP2D6 (188C>T) genotype was an independent predicting factor for HVPG response to propranolol (P = 0.033). Propranolol 147-158 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 61-67 26489037-13 2016 CONCLUSIONS: CYP2D6 (188C>T) gene polymorphisms influence the hemodynamic response to propranolol in this population of Chinese Han patients with gastroesophageal varices. Propranolol 89-100 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 13-19 23287855-4 2013 In vitro analysis suggested that the purified CYP102A5 metabolizes typical substrates of human CYP2C9, CYP2D6, CYP2E1, and CYP3A4, such as coumarin, propranolol, aniline, chlorzoxazone, p-nitrophenol, and nifedipine. Propranolol 149-160 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 103-109 22764579-2 2012 In this study, the co-expression enzyme of human recombinant CYPOR, CYPb5 and CYP2D6.1 or CYP2D6.10 with the Bac-to-Bac system in baculovirus-infected insect cells was used to study the catalytical activity to imipramine metabolism and stereoselective metabolism of propranolol. Propranolol 266-277 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 78-84 22764579-2 2012 In this study, the co-expression enzyme of human recombinant CYPOR, CYPb5 and CYP2D6.1 or CYP2D6.10 with the Bac-to-Bac system in baculovirus-infected insect cells was used to study the catalytical activity to imipramine metabolism and stereoselective metabolism of propranolol. Propranolol 266-277 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 90-96 22764579-9 2012 Both of CYP2D6.1 and CYP2D6.10 produced more hydroxyl propranolol from the R-(+)-isomer than from the S-(-)-isomer while there was no obvious difference for N-desisopropylation propranolol production between R-(+)- and S-(-)- isomer. Propranolol 54-65 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 8-14 22764579-9 2012 Both of CYP2D6.1 and CYP2D6.10 produced more hydroxyl propranolol from the R-(+)-isomer than from the S-(-)-isomer while there was no obvious difference for N-desisopropylation propranolol production between R-(+)- and S-(-)- isomer. Propranolol 54-65 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 21-27 21184751-0 2011 Regio- and stereoselective oxidation of propranolol enantiomers by human CYP2D6, cynomolgus monkey CYP2D17 and marmoset CYP2D19. Propranolol 40-51 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 73-79 21184751-3 2011 The present study was performed to compare regio- and stereoselectivity in the oxidation of propranolol (PL), a chiral substrate, by cytochrome P450 2D (CYP2D) enzymes among humans, cynomolgus monkeys and marmosets. Propranolol 92-103 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 133-151 21184751-3 2011 The present study was performed to compare regio- and stereoselectivity in the oxidation of propranolol (PL), a chiral substrate, by cytochrome P450 2D (CYP2D) enzymes among humans, cynomolgus monkeys and marmosets. Propranolol 92-103 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 153-158 21184751-3 2011 The present study was performed to compare regio- and stereoselectivity in the oxidation of propranolol (PL), a chiral substrate, by cytochrome P450 2D (CYP2D) enzymes among humans, cynomolgus monkeys and marmosets. Propranolol 105-107 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 133-151 21184751-3 2011 The present study was performed to compare regio- and stereoselectivity in the oxidation of propranolol (PL), a chiral substrate, by cytochrome P450 2D (CYP2D) enzymes among humans, cynomolgus monkeys and marmosets. Propranolol 105-107 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 153-158 21110747-11 2011 NMR and mass spectroscopic data have been extensively used for the unambiguous characterization of 4- and 5-hydroxylated and glucuronidated derivatives, all of them corresponding to the major animal and human metabolites of propranolol, a typical substrate of CYP2D6. Propranolol 224-235 cytochrome P450 family 2 subfamily D member 6 Homo sapiens 260-266