PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23889309-6 2001 Exposed workers with GSTM1 null/GSTP1 variant alleles had fewer detectable adducts than those with the GSTM1 null/GSTP1*A wild-type allele, supporting for the first time the recent in vitro finding that GSTP1 variants may be more effective in the detoxification of BPDE than the wild-type allele. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 265-269 glutathione S-transferase pi 1 Homo sapiens 32-37 15298956-0 2004 Benzo(a)pyrene diolepoxide (BPDE)-DNA adduct levels in leukocytes of smokers in relation to polymorphism of CYP1A1, GSTM1, GSTP1, GSTT1, and mEH. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 0-26 glutathione S-transferase pi 1 Homo sapiens 123-128 15298956-8 2004 In conclusion, CYP1A1, GSTM1, and GSTP1 genotyping seems to be a risk predictor of BPDE-DNA adduct formation in leukocytes. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 83-87 glutathione S-transferase pi 1 Homo sapiens 34-39 11597790-7 2001 The polymorphic site within the exon 5 of GSTP1 results in a Ile-->Val substitution, and the isoleucine GSTpi isoform has been found in vitro to be less active than the valine isoform towards the conjugation of BPDE. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 214-218 glutathione S-transferase pi 1 Homo sapiens 42-47 23889309-0 2001 Benzo(a)pyrene diolepoxide adducts to albumin in workers exposed to polycyclic aromatic hydrocarbons: association with specific CYP1A1, GSTM1, GSTP1 and EHPX genotypes. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 0-26 glutathione S-transferase pi 1 Homo sapiens 143-148 9403173-12 1997 Further, modeling of the enantiomers of anti- and syn-BPDE in the active site of GSTP1-1 provides an explanation for the exclusive preference for the enantiomers with R-configuration at the benzylic oxirane carbon. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 54-58 glutathione S-transferase pi 1 Homo sapiens 81-88 9771942-7 1998 Even though the mechanism of the differences in the activities of hGSTP1-1 variants toward anti-5-MeCDE versus anti-BPDE remains to be elucidated, it seems that the molecular configuration of the diol epoxide is an important determinant of the activity of hGSTP1-1 isoforms toward polycyclic aromatic hydrocarbon diol epoxides. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 116-120 glutathione S-transferase pi 1 Homo sapiens 66-74 9687571-2 1998 The chemopreventive role of glutathione S-transferases (GSTs) in protecting against covalent modification of DNA and other cellular macromolecules by BPDE was modeled in human T47D and MCF-7 cell lines previously stably transfected with human GSTpi1 (hGSTP1). 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 150-154 glutathione S-transferase pi 1 Homo sapiens 56-60 9687571-5 1998 The lower level of hGSTP1-1 expression in the transfected MCF-7 cell line (91 milliunits/mg) provided only marginal protection against [3H]BPDE adduct formation and did not affect sensitivity to BPDE-induced cytotoxicity. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 139-143 glutathione S-transferase pi 1 Homo sapiens 19-25 9687571-8 1998 These results indicate that hGSTP1-1 protects effectively against DNA and RNA modification by BPDE, but moderate to high level expression may be required for strong protection against BPDE-induced genotoxicity and cytotoxicity. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 94-98 glutathione S-transferase pi 1 Homo sapiens 28-36 11027134-17 2000 The lack of mobility of helix alpha9 and/or the lack of electrostatic assistance from R216 may be responsible for the relatively lower activity of hGSTA1-1, mGSTA4-4, and hGSTP1-1 toward (+)-anti-BPDE. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 196-200 glutathione S-transferase pi 1 Homo sapiens 171-179 10344744-3 1999 Here, we have determined the protective effect of overexpression of allelic variants of hGSTP1-1, through stable transfection in HepG2 cells, against (+)-anti-BPDE-induced DNA modification. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 159-163 glutathione S-transferase pi 1 Homo sapiens 88-96 10344744-5 1999 The glutathione S-transferase activity toward (+)-anti-BPDE was significantly higher (approximately 3.0-3.6-fold) in cells transfected with hGSTP1(VA) [HepG2(VA)] and hGSTP1(VV) [HepG2(VV)] compared with hGSTP1(IA) transfectant [HepG2(IA)]. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 55-59 glutathione S-transferase pi 1 Homo sapiens 140-146 10344744-5 1999 The glutathione S-transferase activity toward (+)-anti-BPDE was significantly higher (approximately 3.0-3.6-fold) in cells transfected with hGSTP1(VA) [HepG2(VA)] and hGSTP1(VV) [HepG2(VV)] compared with hGSTP1(IA) transfectant [HepG2(IA)]. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 55-59 glutathione S-transferase pi 1 Homo sapiens 167-173 10344744-5 1999 The glutathione S-transferase activity toward (+)-anti-BPDE was significantly higher (approximately 3.0-3.6-fold) in cells transfected with hGSTP1(VA) [HepG2(VA)] and hGSTP1(VV) [HepG2(VV)] compared with hGSTP1(IA) transfectant [HepG2(IA)]. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 55-59 glutathione S-transferase pi 1 Homo sapiens 167-173 10344744-7 1999 Maximum protection against (+)-anti-BPDE-induced DNA damage was afforded by the hGSTP1(VV) isoform. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 36-40 glutathione S-transferase pi 1 Homo sapiens 80-86 10344744-8 1999 The results of this study indicate that the allelic variants of hGSTP1-1 significantly differ in their ability to provide protection against (+)-anti-BPDE-induced DNA damage. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 150-154 glutathione S-transferase pi 1 Homo sapiens 64-72 16099480-2 2005 The protective effects were attributed to induction of glutathione-S-transferases (GSTs) and aim of the present human study was to find out if coffee causes induction of GSTs and protects against DNA-damage caused by (+/-)-anti-B[a]P-7,8-dihydrodiol-9,10-epoxide (BPDE), the DNA-reactive metabolite of benzo(a)pyrene. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 264-268 glutathione S-transferase pi 1 Homo sapiens 170-174 9199210-1 1997 In this study, we demonstrate that the active site architecture of the human glutathione (GSH) S-transferase Pi (GSTP1-1) accounts for its enantioselectivity in the GSH conjugation of 7beta,8alpha-dihydroxy-9alpha,10alpha-oxy-7,8,9, 10-tetrahydrobenzo(a) pyrene (anti-BPDE), the ultimate carcinogen of benzo(a)pyrene. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 268-272 glutathione S-transferase pi 1 Homo sapiens 113-120 9199210-2 1997 Furthermore, we report that the two polymorphic forms of human GSTP1-1, differing in their primary structure by a single amino acid in position 104, have disparate activity toward (+)-anti-BPDE, which can also be rationalized in terms of their active site structures. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 189-193 glutathione S-transferase pi 1 Homo sapiens 63-70 9199210-3 1997 When concentration of (+)-anti-BPDE, which among four BPDE isomers is the most potent carcinogen, was varied and GSH concentration was kept constant at 2 mM (saturating concentration), both forms of hGSTP1-1 [hGSTP1-1(V104) and hGSTP1-1(I104)] obeyed Michaelis-Menten kinetics. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 31-35 glutathione S-transferase pi 1 Homo sapiens 199-207 9199210-4 1997 The V(max) of GSH conjugation of (+)-anti-BPDE was approximately 3.4-fold higher for hGSTP1-1(V104) than for hGSTP1-1(I104). 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 42-46 glutathione S-transferase pi 1 Homo sapiens 85-98 9199210-4 1997 The V(max) of GSH conjugation of (+)-anti-BPDE was approximately 3.4-fold higher for hGSTP1-1(V104) than for hGSTP1-1(I104). 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 42-46 glutathione S-transferase pi 1 Homo sapiens 109-122 9199210-8 1997 The mechanism of differences in kinetic properties and enantioselectivity of hGSTP1-1 variants toward anti-BPDE was investigated by modeling of the two proteins with conjugation product molecules in their active sites. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 107-111 glutathione S-transferase pi 1 Homo sapiens 77-85 9199210-9 1997 Molecular modeling studies revealed that the differences in catalytic properties of hGSTP1-1 variants as well as the enantioselectivity of hGSTP1-1 in the GSH conjugation of anti-BPDE can be rationalized in terms of the architecture of their active sites. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 179-183 glutathione S-transferase pi 1 Homo sapiens 84-92 9199210-9 1997 Molecular modeling studies revealed that the differences in catalytic properties of hGSTP1-1 variants as well as the enantioselectivity of hGSTP1-1 in the GSH conjugation of anti-BPDE can be rationalized in terms of the architecture of their active sites. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 179-183 glutathione S-transferase pi 1 Homo sapiens 139-147 9199210-10 1997 Our results suggest that the population polymorphism of hGSTP1-1 variants with disparate enzyme activities may, at least in part, account for the differential susceptibility of individuals to carcinogens such as anti-BPDE and possibly other similar carcinogens. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 217-221 glutathione S-transferase pi 1 Homo sapiens 56-64 20843134-1 2010 The GSTP1 enzyme plays a key role in biotransformation and bioactivation of certain environmental pollutants such as benzo[a]pyrene-7, 8-diol-9,10-epoxide (BPDE) and other diol epoxides of polycyclic aromatic hydrocarbons. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 117-154 glutathione S-transferase pi 1 Homo sapiens 4-9 20843134-1 2010 The GSTP1 enzyme plays a key role in biotransformation and bioactivation of certain environmental pollutants such as benzo[a]pyrene-7, 8-diol-9,10-epoxide (BPDE) and other diol epoxides of polycyclic aromatic hydrocarbons. 7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide 156-160 glutathione S-transferase pi 1 Homo sapiens 4-9