PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12818727-5 2003 Ethoxyresorufin, coumarin, benzoxyresorufin, chlorzoxazone, testosterone and lauric acid were used as selective substrates for CYP1A1, CYP1A2, CYP1B1, CYP2A6, CYP2B6, CYP2E1, CYP3A4 and CYP4A, respectively. ethoxyresorufin 0-15 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 143-149 12419016-3 2002 To quantify the inhibitory potency of tamoxifen and its major metabolites, the metabolism of three substrates of CYP3A, midazolam, diltiazem and testosterone, and 7-ethoxyresorufin as a substrate of CYP1B1 were examined in catalytic assays carried out using human liver microsomes and cDNA-expression systems. ethoxyresorufin 163-180 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 199-205 11714871-4 2001 trans-Resveratrol decreased 7-ethoxyresorufin O-dealkylation activity catalyzed by human recombinant CYP1B1, CYP1A1, and CYP1A2 in a concentration-dependent manner and by a mixed type of inhibition. ethoxyresorufin 28-45 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 101-107 11100935-2 2000 In vitro, trans-resveratrol decreased human recombinant CYP1B1-catalyzed 7-ethoxyresorufin O-dealkylation activity, with an IC50 value of 1.4 +/- 0.2 microM (mean +/- SEM). ethoxyresorufin 73-90 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 56-62 11719446-4 2001 TMS showed potent and selective inhibition of the ethoxyresorufin O-deethylation (EROD) activity of P450 1B1 with an IC(50) value of 6 nM. ethoxyresorufin 50-65 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 100-108 9152602-6 1997 The activity towards 7-ethoxyresorufin O-deethylation catalyzed by CYP1B1 was about one-tenth of that of CYP1A1, but the Km values were lower for CYP1B1 than those for CYP1A1 and CYP1A2. ethoxyresorufin 21-38 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 67-73 10871058-6 2000 No kinetic differences were seen of 17beta-estradiol hydroxylation activities between the two CYP1B1 variants and an only minor increase in the apparent Km for ethoxyresorufin was observed for CYP1B1.2. ethoxyresorufin 160-175 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 193-199 14577217-0 1998 Enzymatic analysis of cDNA-expressed human CYP1A1, CYP1A2, and CYP1B1 with 7-ethoxyresorufin as substrate. ethoxyresorufin 75-92 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 63-69 9152602-6 1997 The activity towards 7-ethoxyresorufin O-deethylation catalyzed by CYP1B1 was about one-tenth of that of CYP1A1, but the Km values were lower for CYP1B1 than those for CYP1A1 and CYP1A2. ethoxyresorufin 21-38 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 146-152 23886934-4 2013 These protoberberines inhibited CYP1A1.1- and CYP1B1.1-catalyzed 7-ethoxyresorufin O-deethylation (EROD) activities, whereas CYP1A2.1 activity was barely affected. ethoxyresorufin 65-82 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 46-52 30420405-5 2019 In the current study, we report that 19(S/R)-HETE enantioselectively inhibits human recombinant CYP1B1 activity measured by 7-ethoxyresorufin O-deethylation assay. ethoxyresorufin 124-141 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 96-102 27265259-4 2016 The aryl morpholino triazenes were then screened at 100muM for their ability to inhibit CYP1A1 and CYP1B1 using ethoxyresorufin as the substrate. ethoxyresorufin 112-127 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 99-105 24086543-7 2013 As CYP1B1 is the most abundant P450 in human skin, we further demonstrated that: (i) CYP1B1 interacts with 8-MOP (ii) metabolism of the CYP1B1 substrates 7-ethoxyresorufin and 17-beta-estradiol showed concentration-dependent inhibition by 8-MOP and (iii) inhibition of 7-ethoxyresorufin metabolism by 8-MOP was influenced by CYP1B1 genotype. ethoxyresorufin 154-171 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 3-9 24086543-7 2013 As CYP1B1 is the most abundant P450 in human skin, we further demonstrated that: (i) CYP1B1 interacts with 8-MOP (ii) metabolism of the CYP1B1 substrates 7-ethoxyresorufin and 17-beta-estradiol showed concentration-dependent inhibition by 8-MOP and (iii) inhibition of 7-ethoxyresorufin metabolism by 8-MOP was influenced by CYP1B1 genotype. ethoxyresorufin 154-171 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 85-91 24086543-7 2013 As CYP1B1 is the most abundant P450 in human skin, we further demonstrated that: (i) CYP1B1 interacts with 8-MOP (ii) metabolism of the CYP1B1 substrates 7-ethoxyresorufin and 17-beta-estradiol showed concentration-dependent inhibition by 8-MOP and (iii) inhibition of 7-ethoxyresorufin metabolism by 8-MOP was influenced by CYP1B1 genotype. ethoxyresorufin 154-171 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 85-91 24086543-7 2013 As CYP1B1 is the most abundant P450 in human skin, we further demonstrated that: (i) CYP1B1 interacts with 8-MOP (ii) metabolism of the CYP1B1 substrates 7-ethoxyresorufin and 17-beta-estradiol showed concentration-dependent inhibition by 8-MOP and (iii) inhibition of 7-ethoxyresorufin metabolism by 8-MOP was influenced by CYP1B1 genotype. ethoxyresorufin 154-171 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 85-91 24086543-7 2013 As CYP1B1 is the most abundant P450 in human skin, we further demonstrated that: (i) CYP1B1 interacts with 8-MOP (ii) metabolism of the CYP1B1 substrates 7-ethoxyresorufin and 17-beta-estradiol showed concentration-dependent inhibition by 8-MOP and (iii) inhibition of 7-ethoxyresorufin metabolism by 8-MOP was influenced by CYP1B1 genotype. ethoxyresorufin 269-286 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 3-9 24086543-7 2013 As CYP1B1 is the most abundant P450 in human skin, we further demonstrated that: (i) CYP1B1 interacts with 8-MOP (ii) metabolism of the CYP1B1 substrates 7-ethoxyresorufin and 17-beta-estradiol showed concentration-dependent inhibition by 8-MOP and (iii) inhibition of 7-ethoxyresorufin metabolism by 8-MOP was influenced by CYP1B1 genotype. ethoxyresorufin 269-286 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 85-91 24086543-7 2013 As CYP1B1 is the most abundant P450 in human skin, we further demonstrated that: (i) CYP1B1 interacts with 8-MOP (ii) metabolism of the CYP1B1 substrates 7-ethoxyresorufin and 17-beta-estradiol showed concentration-dependent inhibition by 8-MOP and (iii) inhibition of 7-ethoxyresorufin metabolism by 8-MOP was influenced by CYP1B1 genotype. ethoxyresorufin 269-286 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 85-91 24086543-7 2013 As CYP1B1 is the most abundant P450 in human skin, we further demonstrated that: (i) CYP1B1 interacts with 8-MOP (ii) metabolism of the CYP1B1 substrates 7-ethoxyresorufin and 17-beta-estradiol showed concentration-dependent inhibition by 8-MOP and (iii) inhibition of 7-ethoxyresorufin metabolism by 8-MOP was influenced by CYP1B1 genotype. ethoxyresorufin 269-286 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 85-91 34235626-4 2021 METHODS: The O-dealkylation rate of 7-ethoxyresorufin (EROD) by recombinant human CYP1A1 and CYP1B1, in addition to the O-dealkylation rate of 7-methoxyresorufin (MROD) by recombinant human CYP1A2, were measured in the absence and presence of varying concentrations (0-40 nM) of the synthetic analogues of 19(R)- and 19(S)-HETE. ethoxyresorufin 36-53 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 93-99 2875537-7 1986 Aryl hydrocarbon hydroxylase activity was measured with two different substrates, benzo(a)pyrene and 7-ethoxyresorufin. ethoxyresorufin 101-118 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 0-28 21053930-2 2010 Thirty-two of the 33 flavonoids tested produced reverse type I binding spectra with P450 1B1, and the potencies of binding were correlated with the abilities to inhibit 7-ethoxyresorufin O-deethylation activity. ethoxyresorufin 169-186 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 84-92 23218183-5 2013 CYP1B1 enzymatic activity was evaluated using an ethoxyresorufin O-deethylation assay in transfected HEK-293T cells. ethoxyresorufin 49-64 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 0-6 19548353-1 2008 Eleven polycyclic aromatic hydrocarbons (PAHs) and 14 acetylenic PAHs and biphenyls were used to analyze interactions with cytochrome P450 (P450) 1B1 in inhibiting catalytic activity, using 7-ethoxyresorufin O-deethylation (EROD) as a model reaction. ethoxyresorufin 190-207 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 123-149 19463925-4 2009 2,2",4,6"-TMS showed potent and selective inhibition of ethoxyresorufin O-deethylation (EROD) activity of CYP1B1 with IC(50) values of 2 nM. ethoxyresorufin 56-71 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 106-112 17060372-9 2007 The metabolizing activities of CYP1A1 and CYP1B1, as measured by the 7-ethoxyresorufin O-deethylation (EROD) assay, revealed that UDPM noncompetitively inhibited CYP1A1 and CYP1B1 EROD activity in a dose-dependent manner. ethoxyresorufin 69-86 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 42-48 16226778-2 2006 G. biloba extract of known abundance of terpene trilactones and flavonol glycosides inhibited 7-ethoxyresorufin O-dealkylation catalyzed by human recombinant CYP1B1, CYP1A1, and CYP1A2, and human liver microsomes, with apparent Ki values of 2 +/- 0.3, 5 +/- 0.5, 16 +/- 1.4, and 39 +/- 1.2 microg/ml (mean +/- SE), respectively. ethoxyresorufin 94-111 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 158-164 16719376-0 2006 Enzymatic analysis of cDNA-expressed human CYP1A1, CYP1A2, and CYP1B1 with 7-ethoxyresorufin as substrate. ethoxyresorufin 75-92 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 63-69 15280921-8 2004 The O-deethylation of ethoxyresorufin to resorufin was used to measure CYP1B1 activity in RCC. ethoxyresorufin 22-37 cytochrome P450 family 1 subfamily B member 1 Homo sapiens 71-77