PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25458686-2 2014 The stereo specific metabolic activity of human CYP-2B6 (cytochrome P450) on endosulfan has been well demonstrated. Endosulfan 77-87 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 48-55 25458686-4 2014 The functional similarity was studied at organism level by batch-scale studies and it was proved that B. megaterium could metabolize endosulfan to endosulfan sulfate, as CYP-2B6 does in human system. Endosulfan 133-143 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 170-177 24832206-0 2014 Interactions of endosulfan and methoxychlor involving CYP3A4 and CYP2B6 in human HepaRG cells. Endosulfan 16-26 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 65-71 24832206-3 2014 In the present work, we searched for interactions between endosulfan and methoxychlor, two organochlorine pesticides whose major routes of metabolism involve CAR- and PXR-regulated CYP3A4 and CYP2B6, and whose mechanisms of action in humans remain poorly understood. Endosulfan 58-68 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 192-198 16855053-7 2006 This study shows that endosulfan-alpha is metabolized by HLMs to a single metabolite, endosulfan sulfate, and that it has potential use, in combination with inhibitors, as an in vitro probe for CYP2B6 and 3A4 catalytic activities. Endosulfan 22-32 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 194-200 20361990-0 2010 Endosulfan induces CYP2B6 and CYP3A4 by activating the pregnane X receptor. Endosulfan 0-10 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 19-25 20361990-11 2010 These data support the role of endosulfan-alpha as a strong activator of PXR and inducer of CYP2B6 and CYP3A4, which may impact metabolism of CYP2B6 or CYP3A4 substrates. Endosulfan 31-47 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 92-98 20361990-11 2010 These data support the role of endosulfan-alpha as a strong activator of PXR and inducer of CYP2B6 and CYP3A4, which may impact metabolism of CYP2B6 or CYP3A4 substrates. Endosulfan 31-47 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 142-148 16581944-5 2006 Correlation analysis between the known P450 enzyme activities and the rate of the formation of endosulfan sulfate in the 14 human liver microsomes showed that alpha-endosulfan metabolism is significantly correlated with CYP2B6-mediated bupropion hydroxylation and CYP3A-mediated midazolam hydroxylation, and that beta-endosulfan metabolism is correlated with CYP3A activity. Endosulfan 159-175 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 220-226 16581944-6 2006 The P450 isoform-selective inhibition study in human liver microsomes and the incubation study of cDNA-expressed enzymes also demonstrated that the stereoselective sulfonation of alpha-endosulfan is mediated by CYP2B6, CYP3A4, and CYP3A5, and that that of beta-endosulfan is transformed by CYP3A4 and CYP3A5. Endosulfan 256-271 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 211-217 16581944-8 2006 CYP2B6 enantioselectively metabolizes alpha-endosulfan, but not beta-endosulfan. Endosulfan 38-54 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 0-6 16581944-9 2006 These findings suggest that the CYP2B6 and CYP3A enzymes are major enzymes contributing to the stereoselective disposition of endosulfan. Endosulfan 126-136 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 32-38 16581944-5 2006 Correlation analysis between the known P450 enzyme activities and the rate of the formation of endosulfan sulfate in the 14 human liver microsomes showed that alpha-endosulfan metabolism is significantly correlated with CYP2B6-mediated bupropion hydroxylation and CYP3A-mediated midazolam hydroxylation, and that beta-endosulfan metabolism is correlated with CYP3A activity. Endosulfan 313-328 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 220-226 16581944-6 2006 The P450 isoform-selective inhibition study in human liver microsomes and the incubation study of cDNA-expressed enzymes also demonstrated that the stereoselective sulfonation of alpha-endosulfan is mediated by CYP2B6, CYP3A4, and CYP3A5, and that that of beta-endosulfan is transformed by CYP3A4 and CYP3A5. Endosulfan 179-195 cytochrome P450 family 2 subfamily B member 6 Homo sapiens 211-217