PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32488710-3 2020 Genetic polymorphisms in genes encoding PAH-metabolizing enzymes like glutathione S-transferases (GSTM1, GSTP1, GSTT1) which conjugate glutathione to PAHs for reduction of oxidative stress may affect an individual"s response to PAH exposure. Glutathione 70-81 glutathione S-transferase pi 1 Homo sapiens 105-110 33599104-10 2021 Kyoto Encyclopedia of Genes and Genomes (KEGG) analysis indicated the down-regulated expression of glutathione S-transferase P (GSTP1) in the glutathione metabolism signalling pathway in the POAG combined with cataract group. Glutathione 99-110 glutathione S-transferase pi 1 Homo sapiens 128-133 33215267-2 2020 Glutathione S-transferase Pi (GSTP1-1) catalyzes the conjugation of glutathione with anticancer drugs and therefore reduces their efficacy. Glutathione 0-11 glutathione S-transferase pi 1 Homo sapiens 30-37 33215267-2 2020 Glutathione S-transferase Pi (GSTP1-1) catalyzes the conjugation of glutathione with anticancer drugs and therefore reduces their efficacy. Glutathione 68-79 glutathione S-transferase pi 1 Homo sapiens 30-37 33006026-2 2020 Glutathione S-transferase Pi (GSTP1) is reported to detoxify the xenobiotic substrates by catalyzing their conjugation to reduced glutathione (GSH) and its over-expression was demonstrated in the early stages of HCC, while loss of GSTP1 has been suggested to increase the risk of deoxyribonucleic acid (DNA) damage and mutation. Glutathione 0-11 glutathione S-transferase pi 1 Homo sapiens 30-35 33006026-2 2020 Glutathione S-transferase Pi (GSTP1) is reported to detoxify the xenobiotic substrates by catalyzing their conjugation to reduced glutathione (GSH) and its over-expression was demonstrated in the early stages of HCC, while loss of GSTP1 has been suggested to increase the risk of deoxyribonucleic acid (DNA) damage and mutation. Glutathione 0-11 glutathione S-transferase pi 1 Homo sapiens 231-236 33006026-2 2020 Glutathione S-transferase Pi (GSTP1) is reported to detoxify the xenobiotic substrates by catalyzing their conjugation to reduced glutathione (GSH) and its over-expression was demonstrated in the early stages of HCC, while loss of GSTP1 has been suggested to increase the risk of deoxyribonucleic acid (DNA) damage and mutation. Glutathione 130-141 glutathione S-transferase pi 1 Homo sapiens 30-35 33006026-2 2020 Glutathione S-transferase Pi (GSTP1) is reported to detoxify the xenobiotic substrates by catalyzing their conjugation to reduced glutathione (GSH) and its over-expression was demonstrated in the early stages of HCC, while loss of GSTP1 has been suggested to increase the risk of deoxyribonucleic acid (DNA) damage and mutation. Glutathione 130-141 glutathione S-transferase pi 1 Homo sapiens 231-236 33006026-2 2020 Glutathione S-transferase Pi (GSTP1) is reported to detoxify the xenobiotic substrates by catalyzing their conjugation to reduced glutathione (GSH) and its over-expression was demonstrated in the early stages of HCC, while loss of GSTP1 has been suggested to increase the risk of deoxyribonucleic acid (DNA) damage and mutation. Glutathione 143-146 glutathione S-transferase pi 1 Homo sapiens 30-35 33006026-2 2020 Glutathione S-transferase Pi (GSTP1) is reported to detoxify the xenobiotic substrates by catalyzing their conjugation to reduced glutathione (GSH) and its over-expression was demonstrated in the early stages of HCC, while loss of GSTP1 has been suggested to increase the risk of deoxyribonucleic acid (DNA) damage and mutation. Glutathione 143-146 glutathione S-transferase pi 1 Homo sapiens 231-236 33539969-6 2021 GSTP1-1, which produces regioisomers in order 1,2-trans-DCVG > 2,2-cis-DCVG > 1,2-cis-DCVG, is likely to contribute to extrahepatic GSH-conjugation of TCE. Glutathione 132-135 glutathione S-transferase pi 1 Homo sapiens 0-7 33672092-6 2021 We summarize the association findings between drug hypersensitivity reactions and variants in the genes that encode the enzymes related to the redox system such as enzymes related to glutathione: Glutathione S-transferase (GSTM1, GSTP, GSTT1) and glutathione peroxidase (GPX1), thioredoxin reductase (TXNRD1 and TXNRD2), superoxide dismutase (SOD1, SOD2, and SOD3), catalase (CAT), aldo-keto reductase (AKR), and the peroxiredoxin system (PRDX1, PRDX2, PRDX3, PRDX4, PRDX5, PRDX6). Glutathione 183-194 glutathione S-transferase pi 1 Homo sapiens 230-234 32488710-3 2020 Genetic polymorphisms in genes encoding PAH-metabolizing enzymes like glutathione S-transferases (GSTM1, GSTP1, GSTT1) which conjugate glutathione to PAHs for reduction of oxidative stress may affect an individual"s response to PAH exposure. Glutathione 135-146 glutathione S-transferase pi 1 Homo sapiens 105-110 32713331-4 2020 METHODS: In the present work, the interaction of COL and its derivative 2,3-didemethylcolchicine (2,3-DDCOL) with human glutathione transferases (hGSTA1-1, hGSTP1-1, GSTM1-1) was investigated by inhibition analysis, molecular modelling and molecular dynamics simulations. Glutathione 120-131 glutathione S-transferase pi 1 Homo sapiens 156-164 32183092-1 2020 Background and Objectives: One of the most frequent genetic alterations reported to date in prostate cancer (PC) is aberrant methylation of glutathione transferase P1 (GSTP1). Glutathione 140-151 glutathione S-transferase pi 1 Homo sapiens 168-173 32183092-7 2020 Conclusion: Prostate cancer may be influenced by multiple glutathione transferase (GST) polymorphic genes, especially GSTP1, highlighting the role of gene-gene interactions in human susceptibility to this cancer. Glutathione 58-69 glutathione S-transferase pi 1 Homo sapiens 118-123 30153066-2 2018 The multifunctional GST pi-isoform (GSTP) catalyzes the conjugation of glutathione with acrolein and inhibits c-Jun NH2-terminal kinase (JNK) activation. Glutathione 71-82 glutathione S-transferase pi 1 Homo sapiens 36-40 31611630-2 2019 In this study, we propose a promising strategy for cancer treatment using modulation of oxidative stress by suppression of glutathione S-transferases (GSTs), a typical antioxidant enzyme. Glutathione 123-134 glutathione S-transferase pi 1 Homo sapiens 151-155 31575956-7 2019 Antioxidant enzymes transcriptionally regulated by Nrf2 and involved in GSH, NADPH, and NADH generation were significantly lower including PRX1 and PRX3, GPX4, GSTP1, GCLC, and MTHFD2. Glutathione 72-75 glutathione S-transferase pi 1 Homo sapiens 160-165 31221747-5 2019 Instead, GST P1-1 sequesters and inactivates cisplatin with the aid of 2 solvent-accessible cysteines, resulting in protein subunits cross-linking, while maintaining its GSH-conjugation activity. Glutathione 170-173 glutathione S-transferase pi 1 Homo sapiens 9-17 30548113-0 2019 A Covalent Inhibitor for Glutathione S-Transferase Pi (GSTP1-1 ) in Human Cells. Glutathione 25-36 glutathione S-transferase pi 1 Homo sapiens 55-62 30290218-2 2019 At the same time, these compounds can be used to modulate the expression and multiple activities of GSTs and other glutathione-dependent genes, that are important aspects in both the chemoprevention and therapy of drug-resistant cancers. Glutathione 115-126 glutathione S-transferase pi 1 Homo sapiens 100-104 30290218-4 2019 Besides promoting GSH-dependent detoxification of cellular electrophiles, GSTP physically interacts with a number of small molecules and cellular proteins producing regulatory effects across the main signal transduction and transcription pathways (identified as the "regulatory interactome of GSTP"). Glutathione 18-21 glutathione S-transferase pi 1 Homo sapiens 74-78 30290218-4 2019 Besides promoting GSH-dependent detoxification of cellular electrophiles, GSTP physically interacts with a number of small molecules and cellular proteins producing regulatory effects across the main signal transduction and transcription pathways (identified as the "regulatory interactome of GSTP"). Glutathione 18-21 glutathione S-transferase pi 1 Homo sapiens 293-297 29959055-1 2018 Glutathione S-transferases (GSTs) are phase II detoxifying enzymes involved in the maintenance of cell integrity, oxidative stress and protection against DNA damage by catalyzing the conjugation of glutathione to a wide variety of electrophilic substrates. Glutathione 198-209 glutathione S-transferase pi 1 Homo sapiens 28-32 29348462-7 2018 Instead, we demonstrated that glutathione S-transferase pi 1 (GSTP1), a GST family member that catalyzes the conjugation of GSH with electrophilic compounds to fulfill its detoxification function, is highly expressed in HNSCC tissues. Glutathione 124-127 glutathione S-transferase pi 1 Homo sapiens 30-60 29807309-2 2018 Glutathione S-transferases (GSTs; EC 2.5.1.18) catalyze the conjugation of reduced glutathione (GSH) to a variety of xenobiotics and are normally recognized as detoxification enzymes. Glutathione 83-94 glutathione S-transferase pi 1 Homo sapiens 28-32 29807309-2 2018 Glutathione S-transferases (GSTs; EC 2.5.1.18) catalyze the conjugation of reduced glutathione (GSH) to a variety of xenobiotics and are normally recognized as detoxification enzymes. Glutathione 96-99 glutathione S-transferase pi 1 Homo sapiens 28-32 29807309-3 2018 Here, we used a colorimetric assay based on the human placental GSTP1-1 (hpGSTP1-1)-catalyzed reaction between GSH and the model substrate 1-chloro-2,4-dinitrobenzene (CDNB) as well as molecular docking to investigate the mechanistic and structural aspects of hpGSTP1-1 inhibition by DEL. Glutathione 111-114 glutathione S-transferase pi 1 Homo sapiens 64-71 29348462-7 2018 Instead, we demonstrated that glutathione S-transferase pi 1 (GSTP1), a GST family member that catalyzes the conjugation of GSH with electrophilic compounds to fulfill its detoxification function, is highly expressed in HNSCC tissues. Glutathione 124-127 glutathione S-transferase pi 1 Homo sapiens 62-67 29348462-8 2018 Administration of PL and APR-246 significantly suppresses GSTP1 activity, resulting in the accumulation of ROS, depletion of GSH, elevation of GSSG, and DNA damage. Glutathione 125-128 glutathione S-transferase pi 1 Homo sapiens 58-63 29720942-2 2018 Glutathione conjugation protects against AQ-induced toxicity and GSTP1 is able to conjugate its quinoneimine metabolites AQ-QI and DEA-QI with glutathione. Glutathione 143-154 glutathione S-transferase pi 1 Homo sapiens 65-70 29720942-8 2018 Overexpression of GSTP1 resulted in a two-fold increase in GSH-conjugation of the QIs, attenuated QI-induced cytotoxicity especially under GSH-depletion condition, abolished QIs-induced apoptosis but did not significantly inhibit the activation of the ER stress response. Glutathione 59-62 glutathione S-transferase pi 1 Homo sapiens 18-23 29720942-8 2018 Overexpression of GSTP1 resulted in a two-fold increase in GSH-conjugation of the QIs, attenuated QI-induced cytotoxicity especially under GSH-depletion condition, abolished QIs-induced apoptosis but did not significantly inhibit the activation of the ER stress response. Glutathione 139-142 glutathione S-transferase pi 1 Homo sapiens 18-23 28438694-3 2017 Glutathione S-transferase P1 (GSTP1), which belongs to the family of phase II metabolic enzymes, has been reported to function in detoxifying several anti-cancer drugs by conjugating them with glutathione. Glutathione 193-204 glutathione S-transferase pi 1 Homo sapiens 0-28 29310316-6 2018 Among the FDA derivatives examined, FOMe-Ac, the acetyl ester of fluorescein O-methyl ether, was found to be a potential reporter for GSH-dependent GSTP1 activity as well as for carboxylesterase activity. Glutathione 134-137 glutathione S-transferase pi 1 Homo sapiens 148-153 31966884-1 2017 This study was undertaken to detect the incidence of variations in exon 5 of GSTP1, a member of the glutathione-S-transferase family, in gastric cancer in relation to histological parameters. Glutathione 100-111 glutathione S-transferase pi 1 Homo sapiens 77-82 28438694-3 2017 Glutathione S-transferase P1 (GSTP1), which belongs to the family of phase II metabolic enzymes, has been reported to function in detoxifying several anti-cancer drugs by conjugating them with glutathione. Glutathione 193-204 glutathione S-transferase pi 1 Homo sapiens 30-35 27872191-3 2017 These data in tandem with other information led to the conclusion that PL inhibits GSTP1, which forms covalent bonds between GSH and various electrophilic compounds, through covalent adduct formation at the C7-C8 olefin of PL, whereas the C2-C3 olefin of PL was postulated to react with GSH. Glutathione 125-128 glutathione S-transferase pi 1 Homo sapiens 83-88 28254657-5 2017 Eighty % reduction of intracellular glutathione (GSH) by buthionine sulfoximine (BSO), largely enhanced the sensitivity of the GSTP1 expressing MDA-MB-231 cells to HYP-PDT, but not in MCF7 cells. Glutathione 36-47 glutathione S-transferase pi 1 Homo sapiens 127-132 28254657-5 2017 Eighty % reduction of intracellular glutathione (GSH) by buthionine sulfoximine (BSO), largely enhanced the sensitivity of the GSTP1 expressing MDA-MB-231 cells to HYP-PDT, but not in MCF7 cells. Glutathione 49-52 glutathione S-transferase pi 1 Homo sapiens 127-132 28254657-7 2017 HYP loading studies suggested that HYP can be a substrate of GSTP for GSH conjugation as BSO enhanced the cellular HYP accumulation by 20% in MDA-MB-231 cells, but not in MCF7 cells. Glutathione 70-73 glutathione S-transferase pi 1 Homo sapiens 61-65 28254657-9 2017 This means that the GSTP-lacking MCF7 may use L-cysteine for xenobiotic detoxification, especially during GSH synthesis inhibition, which leads to L-cysteine build-up. Glutathione 106-109 glutathione S-transferase pi 1 Homo sapiens 20-24 27863446-6 2017 In summary, GSTP1-1 can detoxify arsenic-based drugs by sequestration at the active site and at the dimer interface, in situations where there is a plentiful supply of GSH, and at the reactive cysteines in conditions of low GSH. Glutathione 168-171 glutathione S-transferase pi 1 Homo sapiens 12-19 27863446-6 2017 In summary, GSTP1-1 can detoxify arsenic-based drugs by sequestration at the active site and at the dimer interface, in situations where there is a plentiful supply of GSH, and at the reactive cysteines in conditions of low GSH. Glutathione 224-227 glutathione S-transferase pi 1 Homo sapiens 12-19 28478157-6 2017 The results showed that GSTP1-1, GSTA4-4, GSTM4-4, GSTM2-2 and GSTA2-2 (activity in decreasing order) were active isoforms in catalyzing GSH conjugation of reactive QIs of AQ and DEAQ. Glutathione 137-140 glutathione S-transferase pi 1 Homo sapiens 24-31 27348130-2 2017 Pi-class glutathione-S-transferase (GSTP1) plays a role in the removal of oxidative adducts by transferring them to glutathione. Glutathione 9-20 glutathione S-transferase pi 1 Homo sapiens 36-41 27872191-3 2017 These data in tandem with other information led to the conclusion that PL inhibits GSTP1, which forms covalent bonds between GSH and various electrophilic compounds, through covalent adduct formation at the C7-C8 olefin of PL, whereas the C2-C3 olefin of PL was postulated to react with GSH. Glutathione 287-290 glutathione S-transferase pi 1 Homo sapiens 83-88 27872191-5 2017 To investigate, we solved the X-ray crystal structure of GSTP1 bound to PL and GSH at 1.1 A resolution to rationalize previously reported structure activity relationship studies. Glutathione 79-82 glutathione S-transferase pi 1 Homo sapiens 57-62 27872191-6 2017 Surprisingly, the structure showed that a hydrolysis product of PL (hPL) was conjugated to glutathione at the C7-C8 olefin, and this complex was bound to the active site of GSTP1; no covalent bond formation between hPL and GSTP1 was observed. Glutathione 91-102 glutathione S-transferase pi 1 Homo sapiens 173-178 27872191-6 2017 Surprisingly, the structure showed that a hydrolysis product of PL (hPL) was conjugated to glutathione at the C7-C8 olefin, and this complex was bound to the active site of GSTP1; no covalent bond formation between hPL and GSTP1 was observed. Glutathione 91-102 glutathione S-transferase pi 1 Homo sapiens 223-228 27872191-10 2017 Altogether, our data suggest a model wherein PL is a prodrug whose intracellular hydrolysis initiates the formation of the hPL-GSH conjugate, which blocks the active site of and inhibits GSTP1 and thereby cancer cell proliferation. Glutathione 127-130 glutathione S-transferase pi 1 Homo sapiens 187-192 27989146-5 2016 The results show that GSTP1-1 is a highly active catalyst of GSH-conjugation of the oxidative metabolites of NVP, even at high GSH-concentration. Glutathione 61-64 glutathione S-transferase pi 1 Homo sapiens 22-29 28550240-10 2017 RESULTS: In patients with GSTP1 AA genotype we have found significance level reaching plasma concentration rise in SOD and MDA, and drop in GSH, SH. Glutathione 140-143 glutathione S-transferase pi 1 Homo sapiens 26-31 27989146-5 2016 The results show that GSTP1-1 is a highly active catalyst of GSH-conjugation of the oxidative metabolites of NVP, even at high GSH-concentration. Glutathione 127-130 glutathione S-transferase pi 1 Homo sapiens 22-29 25372302-9 2014 The highest increase of total GSH conjugation was observed with hGSTP1-1, followed by hepatic hGSTs hGSTA2-2 and hGSTM1-1. Glutathione 30-33 glutathione S-transferase pi 1 Homo sapiens 64-72 27684484-5 2016 Here, we report the crystal structures of hGSTP1 and hGSTA1 each in complex with the GSH adduct of PEITC. Glutathione 85-88 glutathione S-transferase pi 1 Homo sapiens 42-48 27358914-4 2016 S-glutathionylation, the conjugation of glutathione to reactive cysteines, is catalyzed in part by glutathione-S-transferase pi (GSTP). Glutathione 40-51 glutathione S-transferase pi 1 Homo sapiens 129-133 27193186-7 2016 Quantitative proteomics analysis indicated that six NRF2-targeted proteins, including NQO1, GSR, G6PD, GCLC, GCLM and GSTP1 involved in the glutathione metabolism pathway, were reduced in H19-knockdown cells. Glutathione 140-151 glutathione S-transferase pi 1 Homo sapiens 118-123 27197232-10 2016 Tumors exhibited increased antioxidant metabolites and upregulation of glutathione S-transferase pathway genes, including Gstp1 and Gstz1, which are associated with poor outcome in human neuroblastoma. Glutathione 71-82 glutathione S-transferase pi 1 Homo sapiens 122-127 26922696-1 2016 Glutathione S-transferase P (GSTP), and possibly other members of the subfamily of cytosolic GSTs, are increasingly proposed to have roles far beyond the classical GSH-dependent enzymatic detoxification of electrophilic metabolites and xenobiotics. Glutathione 164-167 glutathione S-transferase pi 1 Homo sapiens 0-27 26922696-1 2016 Glutathione S-transferase P (GSTP), and possibly other members of the subfamily of cytosolic GSTs, are increasingly proposed to have roles far beyond the classical GSH-dependent enzymatic detoxification of electrophilic metabolites and xenobiotics. Glutathione 164-167 glutathione S-transferase pi 1 Homo sapiens 29-33 26922696-1 2016 Glutathione S-transferase P (GSTP), and possibly other members of the subfamily of cytosolic GSTs, are increasingly proposed to have roles far beyond the classical GSH-dependent enzymatic detoxification of electrophilic metabolites and xenobiotics. Glutathione 164-167 glutathione S-transferase pi 1 Homo sapiens 93-97 26447830-10 2016 Restoration of GSTP1 expression resulted in changes in modified glutathione levels that correlated with GSTP1 protein levels in response to protracted LDR-induced oxidative stress. Glutathione 64-75 glutathione S-transferase pi 1 Homo sapiens 15-20 26554337-4 2015 Therefore, we incubated GSTA1, GSTT1, GSTM1, and GSTP1 with glutathione and BO and quantified the formation of S-phenylglutathione. Glutathione 60-71 glutathione S-transferase pi 1 Homo sapiens 49-54 26295386-0 2015 Genetic Polymorphisms of Glutathione-Related Enzymes (GSTM1, GSTT1, and GSTP1) and Schizophrenia Risk: A Meta-Analysis. Glutathione 25-36 glutathione S-transferase pi 1 Homo sapiens 72-77 26028097-1 2015 BACKGROUND: Previous studies showed that genetic polymorphisms of glutathione S-transferase P1 (GSTP1) were involved in glutathione metabolism and genetic polymorphisms of ribonucleotide reductase (RRM1) were correlated with DNA synthesis. Glutathione 66-77 glutathione S-transferase pi 1 Homo sapiens 96-101 27037874-5 2016 It is anticipated that when GSH analogues with selective inhibitory or catalytic binding, were conjugated to allozyme-selective inhibitors of hGSTP1-1, the derived leads would be useful for the designing of novel chimeric inhibitors against the MDR-involved hGSTP1-1 allozymes. Glutathione 28-31 glutathione S-transferase pi 1 Homo sapiens 142-150 27037874-5 2016 It is anticipated that when GSH analogues with selective inhibitory or catalytic binding, were conjugated to allozyme-selective inhibitors of hGSTP1-1, the derived leads would be useful for the designing of novel chimeric inhibitors against the MDR-involved hGSTP1-1 allozymes. Glutathione 28-31 glutathione S-transferase pi 1 Homo sapiens 258-266 26295823-0 2015 GSTP1 Polymorphisms and their Association with Glutathione Transferase and Peroxidase Activities in Patients with Motor Neuron Disease. Glutathione 47-58 glutathione S-transferase pi 1 Homo sapiens 0-5 24970398-1 2014 Glutathione S-transferase pi-1 (GSTP-1) is a member of the glutathione S-transferase enzyme superfamily, which catalyzes the conjugation of electrophiles to glutathione during the process of detoxification. Glutathione 59-70 glutathione S-transferase pi 1 Homo sapiens 0-30 25324722-7 2014 To identify and characterize the potential inhibitory activity of 8-MOP, we studied the enzyme kinetics of the conjugation of 1-chloro-2,4-dinitrobenzene (CDNB) with GSH catalyzed by hGST P1-1. Glutathione 166-169 glutathione S-transferase pi 1 Homo sapiens 183-192 24970398-1 2014 Glutathione S-transferase pi-1 (GSTP-1) is a member of the glutathione S-transferase enzyme superfamily, which catalyzes the conjugation of electrophiles to glutathione during the process of detoxification. Glutathione 59-70 glutathione S-transferase pi 1 Homo sapiens 32-38 24810314-9 2014 We demonstrate that increased glutathione (GSH) levels sensitize colon cancer cells to thiazolides, indicating that both GSTP1 enzymatic activity as well as GSH levels are critical factors in thiazolide-induced cell death. Glutathione 30-41 glutathione S-transferase pi 1 Homo sapiens 121-126 24810314-9 2014 We demonstrate that increased glutathione (GSH) levels sensitize colon cancer cells to thiazolides, indicating that both GSTP1 enzymatic activity as well as GSH levels are critical factors in thiazolide-induced cell death. Glutathione 43-46 glutathione S-transferase pi 1 Homo sapiens 121-126 25076909-1 2014 Glutathione S-transferases (GSTs) are phase II drug detoxifying enzymes that play an essential role in the maintenance of cell integrity and protection against DNA damage by catalyzing the conjugation of glutathione to a wide variety of exo- and endogenous electrophilic substrates. Glutathione 204-215 glutathione S-transferase pi 1 Homo sapiens 28-32 24521039-4 2014 The resulting prodrugs are activated by glutathione in a reaction accelerated by glutathione S-transferase P1 (GSTP1), an enzyme frequently overexpressed in cancers. Glutathione 40-51 glutathione S-transferase pi 1 Homo sapiens 81-109 24552538-6 2014 The GSH conjugation was strongly increased by adding human GSTP1-1 in a wide range of GSH concentrations. Glutathione 4-7 glutathione S-transferase pi 1 Homo sapiens 59-66 24552538-6 2014 The GSH conjugation was strongly increased by adding human GSTP1-1 in a wide range of GSH concentrations. Glutathione 86-89 glutathione S-transferase pi 1 Homo sapiens 59-66 24677708-8 2014 Molecular docking studies performed with CDocker revealed that the newly synthesized 2-substituted-5-(4-nitrophenylsulfonamido)benzoxazoles act as catalytic inhibitors of hGST P1-1 by binding to the H-site and generating conjugates with GSH to form S-(4-nitrophenyl)GSH (GS-BN complex) via nucleophilic aromatic substitution reaction. Glutathione 237-240 glutathione S-transferase pi 1 Homo sapiens 171-180 24521039-4 2014 The resulting prodrugs are activated by glutathione in a reaction accelerated by glutathione S-transferase P1 (GSTP1), an enzyme frequently overexpressed in cancers. Glutathione 40-51 glutathione S-transferase pi 1 Homo sapiens 111-116 25606397-1 2014 Glutathione S-transferases (GSTs) belong to a super family of phase II detoxification enzymes, which play an important role in protecting cells from damage caused by endogenous and exogenous compounds by conjugating reactive intermediates with glutathione to produce less reactive water-soluble compounds. Glutathione 244-255 glutathione S-transferase pi 1 Homo sapiens 28-32 24457959-2 2014 The dissociation constant of the heterocomplex is K(d)=0.3 muM; however the binding affinity strongly decreases when the active site of GSTP1-1 is occupied by the substrate GSH (K(d)>=2.6 muM) or is inactivated by oxidation (Kd=1.7 muM). Glutathione 173-176 glutathione S-transferase pi 1 Homo sapiens 136-143 24457959-3 2014 This indicates that GSTP1-1"s TRAF2-binding region involves the GSH-binding site. Glutathione 64-67 glutathione S-transferase pi 1 Homo sapiens 20-27 24457959-4 2014 The GSTP1-1 inhibitor NBDHEX further decreases the complex"s binding affinity, as compared with when GSH is the only ligand; this suggests that the hydrophobic portion of the GSTP1-1 active site also contributes to the interaction. Glutathione 101-104 glutathione S-transferase pi 1 Homo sapiens 4-11 24457959-4 2014 The GSTP1-1 inhibitor NBDHEX further decreases the complex"s binding affinity, as compared with when GSH is the only ligand; this suggests that the hydrophobic portion of the GSTP1-1 active site also contributes to the interaction. Glutathione 101-104 glutathione S-transferase pi 1 Homo sapiens 175-182 24457959-10 2014 Moreover, GSH"s intracellular content was so high that it always saturated GSTP1-1. Glutathione 10-13 glutathione S-transferase pi 1 Homo sapiens 75-82 24185126-0 2014 Effect of human glutathione S-transferase hGSTP1-1 polymorphism on the detoxification of reactive metabolites of clozapine, diclofenac and acetaminophen. Glutathione 16-27 glutathione S-transferase pi 1 Homo sapiens 42-48 24185126-8 2014 The different hGSTP1-1 mutants showed slightly altered regioselectivities in formation of individual GSH conjugates of clozapine which suggests that the binding orientation of the reactive nitrenium ion of clozapine is affected by the mutations. Glutathione 101-104 glutathione S-transferase pi 1 Homo sapiens 14-22 24185126-9 2014 For diclofenac, a significant decrease in activity in GSH-conjugation of diclofenac 1",4"-quinone imine was observed for variants hGSTP1-1*B (Val105/Ala114) and hGSTP1-1*C (Val105/Val114). Glutathione 54-57 glutathione S-transferase pi 1 Homo sapiens 130-136 24185126-9 2014 For diclofenac, a significant decrease in activity in GSH-conjugation of diclofenac 1",4"-quinone imine was observed for variants hGSTP1-1*B (Val105/Ala114) and hGSTP1-1*C (Val105/Val114). Glutathione 54-57 glutathione S-transferase pi 1 Homo sapiens 130-138 24696865-1 2014 This study aims to evaluate the effects of polymorphisms in glutathione (GSH-) related genes (GSTM1, GSTT1, GSTP1, GCLM, and GCLC) in the distribution of Hg in the blood compartments in humans exposed to methylmercury (MeHg). Glutathione 60-71 glutathione S-transferase pi 1 Homo sapiens 108-113 24696865-1 2014 This study aims to evaluate the effects of polymorphisms in glutathione (GSH-) related genes (GSTM1, GSTT1, GSTP1, GCLM, and GCLC) in the distribution of Hg in the blood compartments in humans exposed to methylmercury (MeHg). Glutathione 73-76 glutathione S-transferase pi 1 Homo sapiens 108-113 23569432-10 2013 GSTP1 expression level was correlated with plasma levels of MDA (P<0.01), XOD (P = 0.01) and GSH (P< 0.01), GST (P< 0.01). Glutathione 96-99 glutathione S-transferase pi 1 Homo sapiens 0-5 24066958-1 2013 Canfosfamide (TLK286, TELCYTA) is a prodrug that upon activation by glutathione transferase P1-1 (GST P1-1) yields an anticancer alkylating agent and a glutathione derivative. Glutathione 68-79 glutathione S-transferase pi 1 Homo sapiens 98-106 23804706-12 2013 These data suggest that the methylene group plays an important role in the downregulation of c-FLIP and Mcl-1 proteins and apoptosis induction, which is inactivated by GSTP1-1 by forming GSH conjugates. Glutathione 187-190 glutathione S-transferase pi 1 Homo sapiens 168-175 24083800-5 2013 The strongest increase of total GSH-conjugation was observed by adding hGSTP1-1, whereas hGSTM1-1 and hGSTA1-1 showed lower activity. Glutathione 32-35 glutathione S-transferase pi 1 Homo sapiens 71-79 24083800-7 2013 When considering the effects of hGSTs on GSH-conjugation of the different quinoneimines of diclofenac, it was found that hGSTP1-1 showed the highest activity in GSH-conjugation of the quinoneimine derived from 5-hydroxydiclofenac (5-OH-DF). Glutathione 41-44 glutathione S-transferase pi 1 Homo sapiens 121-129 24083800-7 2013 When considering the effects of hGSTs on GSH-conjugation of the different quinoneimines of diclofenac, it was found that hGSTP1-1 showed the highest activity in GSH-conjugation of the quinoneimine derived from 5-hydroxydiclofenac (5-OH-DF). Glutathione 161-164 glutathione S-transferase pi 1 Homo sapiens 121-129 24083800-11 2013 hGSTP1-1 showed the highest activity for the formation of these minor GSH-conjugates. Glutathione 70-73 glutathione S-transferase pi 1 Homo sapiens 0-8 23769903-7 2013 In distinction from the other inhibitors, which showed conventional inhibition patterns, the competitive inhibitor ethacrynic acid elicited strong kinetic cooperativity in the glutathione saturation of GST P1-1. Glutathione 176-187 glutathione S-transferase pi 1 Homo sapiens 202-210 23254386-12 2013 In addition, since glutathione S-transferase-pi (GSTP1) was re-expressed or its protein levels were increased after treatment with non-toxic azacitidine doses and since GSTP1 can easily be measured in patient sera, the monitoring of this protein may aide in the evaluation of therapy in future clinical trials. Glutathione 19-30 glutathione S-transferase pi 1 Homo sapiens 49-54 23142420-9 2013 The affinities for Prdx6 binding to GSH-loaded GSTP1-1"s either mirrored their observed peroxidase activities (using phospholipid hydroperoxide as a substrate), GSTP1-1A>GSTP1-1C (K(D)=51.0 vs 57.0 nM), or corresponded to inactivation, GSTP1-1B (GSTP1-1D) (K(D)=101.0 (94.0) nM). Glutathione 36-39 glutathione S-transferase pi 1 Homo sapiens 47-54 23142420-9 2013 The affinities for Prdx6 binding to GSH-loaded GSTP1-1"s either mirrored their observed peroxidase activities (using phospholipid hydroperoxide as a substrate), GSTP1-1A>GSTP1-1C (K(D)=51.0 vs 57.0 nM), or corresponded to inactivation, GSTP1-1B (GSTP1-1D) (K(D)=101.0 (94.0) nM). Glutathione 36-39 glutathione S-transferase pi 1 Homo sapiens 47-52 23142420-9 2013 The affinities for Prdx6 binding to GSH-loaded GSTP1-1"s either mirrored their observed peroxidase activities (using phospholipid hydroperoxide as a substrate), GSTP1-1A>GSTP1-1C (K(D)=51.0 vs 57.0 nM), or corresponded to inactivation, GSTP1-1B (GSTP1-1D) (K(D)=101.0 (94.0) nM). Glutathione 36-39 glutathione S-transferase pi 1 Homo sapiens 161-166 23142420-9 2013 The affinities for Prdx6 binding to GSH-loaded GSTP1-1"s either mirrored their observed peroxidase activities (using phospholipid hydroperoxide as a substrate), GSTP1-1A>GSTP1-1C (K(D)=51.0 vs 57.0 nM), or corresponded to inactivation, GSTP1-1B (GSTP1-1D) (K(D)=101.0 (94.0) nM). Glutathione 36-39 glutathione S-transferase pi 1 Homo sapiens 161-166 23142420-9 2013 The affinities for Prdx6 binding to GSH-loaded GSTP1-1"s either mirrored their observed peroxidase activities (using phospholipid hydroperoxide as a substrate), GSTP1-1A>GSTP1-1C (K(D)=51.0 vs 57.0 nM), or corresponded to inactivation, GSTP1-1B (GSTP1-1D) (K(D)=101.0 (94.0) nM). Glutathione 36-39 glutathione S-transferase pi 1 Homo sapiens 161-166 22920299-6 2012 Unexpectedly, glutathione (GSH) exerted a negative effect on the affinity of GSTP1-1 for JNK1alpha2, suggesting that the intracellular levels of this thiol may allow a fine-tuning of the MAPK signaling pathway. Glutathione 14-25 glutathione S-transferase pi 1 Homo sapiens 77-84 23072868-3 2012 Voltammetric measurements showed a strong decrease of the peak current intensity and an increase of the oxidation potential upon binding of ferrocene-glutathione conjugates to GST P1-1 showing that both conjugates can be used as dual electrochemical sensors for GST P1-1. Glutathione 150-161 glutathione S-transferase pi 1 Homo sapiens 176-184 23072868-3 2012 Voltammetric measurements showed a strong decrease of the peak current intensity and an increase of the oxidation potential upon binding of ferrocene-glutathione conjugates to GST P1-1 showing that both conjugates can be used as dual electrochemical sensors for GST P1-1. Glutathione 150-161 glutathione S-transferase pi 1 Homo sapiens 262-270 22390478-0 2012 Response of glutathione S-transferase Pi (GSTP1) to neoadjuvant therapy in rectal adenocarcinoma. Glutathione 12-23 glutathione S-transferase pi 1 Homo sapiens 42-47 22998212-12 2012 A corresponding GSH-conjugate with a similar mass increment was only observed if incubations of DF with P450 and GSH were supplemented by human GST P1-1. Glutathione 16-19 glutathione S-transferase pi 1 Homo sapiens 144-152 22920299-6 2012 Unexpectedly, glutathione (GSH) exerted a negative effect on the affinity of GSTP1-1 for JNK1alpha2, suggesting that the intracellular levels of this thiol may allow a fine-tuning of the MAPK signaling pathway. Glutathione 27-30 glutathione S-transferase pi 1 Homo sapiens 77-84 22920299-7 2012 Moreover, we found that the adduct formed by GSH and the strong GSTP1-1 inhibitor NBDHEX abolishes the interaction between GSTP1-1 and JNK1alpha2. Glutathione 45-48 glutathione S-transferase pi 1 Homo sapiens 64-71 22920299-7 2012 Moreover, we found that the adduct formed by GSH and the strong GSTP1-1 inhibitor NBDHEX abolishes the interaction between GSTP1-1 and JNK1alpha2. Glutathione 45-48 glutathione S-transferase pi 1 Homo sapiens 123-130 22175791-0 2012 The role of the glutathione S-transferase genes GSTT1, GSTM1, and GSTP1 in acetaminophen-poisoned patients. Glutathione 16-27 glutathione S-transferase pi 1 Homo sapiens 66-71 21887679-1 2012 BACKGROUND: Ezatiostat is a glutathione analog prodrug glutathione S-transferase P1-1 (GSTP1-1) inhibitor. Glutathione 28-39 glutathione S-transferase pi 1 Homo sapiens 87-94 22158036-2 2012 GSTP1 is a phase II detoxification enzyme and conjugates the tripeptide glutathione to endogenous metabolites and xenobiotics, thereby limiting the efficacy of antitumor chemotherapeutic treatments. Glutathione 72-83 glutathione S-transferase pi 1 Homo sapiens 0-5 22799388-1 2012 In the present case control study mRNA expression of the GSTP1 gene, encoding a phase II enzyme that detoxifies via glutathione conjugation, was investigated using semiquantitative PCR followed by SSCP for 49 confirmed head and neck (HN) cancer and 49 control samples. Glutathione 116-127 glutathione S-transferase pi 1 Homo sapiens 57-62 20654585-3 2010 Using two malignant glioma cell lines, MGR1 and MGR3, the ability of PKCalpha-phosphorylated GSTP1 to catalyze the conjugation of cisplatin to glutathione was assessed and correlated with cisplatin sensitivity and cisplatin-induced DNA interstrand cross-links and apoptosis of the cells. Glutathione 143-154 glutathione S-transferase pi 1 Homo sapiens 93-98 21914835-6 2011 Addition of human recombinant GSTA1, GSTA2, GSTM1, or GSTP1 protein to the incubation mixture further increased the GSH conjugates. Glutathione 116-119 glutathione S-transferase pi 1 Homo sapiens 54-59 21460233-1 2011 GSH transferases (GSTs) are a superfamily of proteins best known for detoxifying harmful electrophilic compounds by catalyzing their conjugation with GSH. Glutathione 0-3 glutathione S-transferase pi 1 Homo sapiens 18-22 21342130-5 2011 An aim of this review is to summarise recent knowledge on GSTP"s complementary functions in crosstalking pathways of conventional glutathione transfer, nitric oxide and lipid metabolism and ASK1-dependent stress response. Glutathione 130-141 glutathione S-transferase pi 1 Homo sapiens 58-62 21890734-7 2011 The mutant containing Phe87 showed high activity and high selectivity for the bioactivation pathway and was used for the large-scale production of GST-dependent GSH conjugates by incubation in the presence of recombinant human GST P1-1. Glutathione 161-164 glutathione S-transferase pi 1 Homo sapiens 227-235 21890734-9 2011 This work shows that drug-metabolizing CYP102A1 mutants, in combination with GSTs, are very useful tools for the generation of GSH conjugates of reactive metabolites of drugs to enable their isolation and structural elucidation. Glutathione 127-130 glutathione S-transferase pi 1 Homo sapiens 77-81 22009704-2 2011 Genetic polymorphisms of GSTP1 and XRCC1 involved in glutathione metabolic and DNA repair pathways may explain inter individual differences in chemosensitivity and clinical outcome in NSCLC patients treated with platinum-based regimens. Glutathione 53-64 glutathione S-transferase pi 1 Homo sapiens 25-30 21489839-4 2011 We observed a significant difference for GSTP1 polymorphisms in SCA patients with the V/V genotype that showed higher glutathione (GSH) and Trolox equivalent antioxidant capacity (TEAC) (p=0.0445 and p=0.0360), respectively, compared with the I/I genotype. Glutathione 118-129 glutathione S-transferase pi 1 Homo sapiens 41-46 21489839-4 2011 We observed a significant difference for GSTP1 polymorphisms in SCA patients with the V/V genotype that showed higher glutathione (GSH) and Trolox equivalent antioxidant capacity (TEAC) (p=0.0445 and p=0.0360), respectively, compared with the I/I genotype. Glutathione 131-134 glutathione S-transferase pi 1 Homo sapiens 41-46 20853826-6 2010 In the present work, we have resorted to density functional theory (DFT) and to potential of mean force (PMF) calculations to determine the GSH activation mechanism of GSTP1-1 and GSTM1-1 isoenzymes. Glutathione 140-143 glutathione S-transferase pi 1 Homo sapiens 168-175 20853826-7 2010 For the GSTP1-1 enzyme, we have demonstrated that a water molecule, after an initial conformational rearrangement of GSH, can assist a proton transfer between the GSH cysteine thiol (GSH-SH) and the GSH glutamate alpha carboxylate (GSH-COO(-)) groups. Glutathione 117-120 glutathione S-transferase pi 1 Homo sapiens 8-15 20853826-7 2010 For the GSTP1-1 enzyme, we have demonstrated that a water molecule, after an initial conformational rearrangement of GSH, can assist a proton transfer between the GSH cysteine thiol (GSH-SH) and the GSH glutamate alpha carboxylate (GSH-COO(-)) groups. Glutathione 163-166 glutathione S-transferase pi 1 Homo sapiens 8-15 20853826-7 2010 For the GSTP1-1 enzyme, we have demonstrated that a water molecule, after an initial conformational rearrangement of GSH, can assist a proton transfer between the GSH cysteine thiol (GSH-SH) and the GSH glutamate alpha carboxylate (GSH-COO(-)) groups. Glutathione 163-166 glutathione S-transferase pi 1 Homo sapiens 8-15 20849150-6 2010 In the presence of three of the GSTs, hGST P1-1, hGST M1-1, and hGST A1-1, total GSH conjugation was strongly increased in all bioactivation systems tested. Glutathione 81-84 glutathione S-transferase pi 1 Homo sapiens 38-47 20849150-11 2010 Chlorine substitution of the clozapine nitrenium ion, which so far was only observed in in vivo studies, appeared to be the major pathway of hGST P1-1-catalyzed GSH conjugation, whereas hGST A1-1 and hGST M1-1 also showed significant activity. Glutathione 161-164 glutathione S-transferase pi 1 Homo sapiens 141-150 20849150-12 2010 The second GSH conjugate, previously also only found in in vivo studies, was also formed by hGST P1-1 and to a small extent by hGST A1-1. Glutathione 11-14 glutathione S-transferase pi 1 Homo sapiens 92-101 19195803-3 2010 Polymorphisms of genes involved in glutathione metabolism, e.g. GSTP1 and GSTM1 are reportedly associated with autistic disorder. Glutathione 35-46 glutathione S-transferase pi 1 Homo sapiens 64-69 20731849-3 2010 Changes in expression of glutathione S-transferases (GSTs) and other proteins interacting with glutathione (GSH) in model cell lines could be of particular interest. Glutathione 25-36 glutathione S-transferase pi 1 Homo sapiens 53-57 20731849-3 2010 Changes in expression of glutathione S-transferases (GSTs) and other proteins interacting with glutathione (GSH) in model cell lines could be of particular interest. Glutathione 108-111 glutathione S-transferase pi 1 Homo sapiens 53-57 19850963-12 2010 The risk was modified by a functional polymorphism in GSTP1, suggesting a mechanism involving the glutathione pathway. Glutathione 98-109 glutathione S-transferase pi 1 Homo sapiens 54-59 19084393-1 2009 PURPOSE: Oxaliplatin is detoxified by conjugation to glutathione via the enzyme Glutathione-S-transferase pi (GSTP1). Glutathione 53-64 glutathione S-transferase pi 1 Homo sapiens 110-115 19330882-8 2009 Depletion of GSH to 20% of control levels via pretreatment with the de novo GSH biosynthesis inhibitor buthionine sulfoximine reduced the protection against B[a]P cytotoxicity by hGSTP1 from 16-fold to 5-fold, indicating that catalysis of conjugation with GSH, rather than binding or other effects, is responsible for the resistance. Glutathione 13-16 glutathione S-transferase pi 1 Homo sapiens 179-185 19330882-8 2009 Depletion of GSH to 20% of control levels via pretreatment with the de novo GSH biosynthesis inhibitor buthionine sulfoximine reduced the protection against B[a]P cytotoxicity by hGSTP1 from 16-fold to 5-fold, indicating that catalysis of conjugation with GSH, rather than binding or other effects, is responsible for the resistance. Glutathione 76-79 glutathione S-transferase pi 1 Homo sapiens 179-185 19330882-8 2009 Depletion of GSH to 20% of control levels via pretreatment with the de novo GSH biosynthesis inhibitor buthionine sulfoximine reduced the protection against B[a]P cytotoxicity by hGSTP1 from 16-fold to 5-fold, indicating that catalysis of conjugation with GSH, rather than binding or other effects, is responsible for the resistance. Glutathione 76-79 glutathione S-transferase pi 1 Homo sapiens 179-185 19950984-3 2010 Moreover, we describe in detail the interaction of brostallicin with GSH in the presence of GSTP1-1 and GSTM2-2, the predominant GST isoenzymes found within tumor cells. Glutathione 69-72 glutathione S-transferase pi 1 Homo sapiens 92-99 19950984-5 2010 Direct evidence that both GSTP1-1 and GSTM2-2 isoenzymes catalyze the Michael addition reaction of GSH to brostallicin has been obtained both by an HPLC-MS technique and by a new fluorometric assay. Glutathione 99-102 glutathione S-transferase pi 1 Homo sapiens 26-33 19950984-8 2010 The kinetic behavior of the reaction between brostallicin and GSH, catalyzed by GSTP1-1, has been studied in detail, and a minimum kinetic scheme that suitably describes the experimental data is provided. Glutathione 62-65 glutathione S-transferase pi 1 Homo sapiens 80-87 19330882-1 2009 Polycyclic aromatic hydrocarbons (PAHs) are activated by cytochrome P450 (CYP) isozymes, and a subset of the reactive metabolites generated is detoxified via conjugation with glutathione (GSH) by specific glutathione S-transferases (GSTs). Glutathione 175-186 glutathione S-transferase pi 1 Homo sapiens 233-237 19842992-8 2009 Children with the GSTP1 Val105 allele had significantly lower concentrations of erythrocyte glutathione compared to GSTP1 ILE/ILE homozygotes (P=0.03). Glutathione 92-103 glutathione S-transferase pi 1 Homo sapiens 18-23 18825537-2 2009 The glutathione S-transferases (GSTs; EC 2.5.1.18) family is a widely distributed phase-II detoxifying enzymes and the GST P1-1 isoenzyme has been shown to catalyze the conjugation of GSH with some alkylating anti-cancer agents, suggesting that over-expression of GST P1-1 would result in tumor cell resistance. Glutathione 184-187 glutathione S-transferase pi 1 Homo sapiens 119-127 18825537-2 2009 The glutathione S-transferases (GSTs; EC 2.5.1.18) family is a widely distributed phase-II detoxifying enzymes and the GST P1-1 isoenzyme has been shown to catalyze the conjugation of GSH with some alkylating anti-cancer agents, suggesting that over-expression of GST P1-1 would result in tumor cell resistance. Glutathione 184-187 glutathione S-transferase pi 1 Homo sapiens 264-272 18449862-2 2009 In this study, we performed association studies between GSH-related genes (GSTM1, GSTP1, GSTO1, GSTT1, GSTT2, GPX1, and GCLM) and schizophrenia in a Japanese population. Glutathione 56-59 glutathione S-transferase pi 1 Homo sapiens 82-87 18511072-3 2008 The allelic variants of GST P1-1 are associated with differing susceptibilities to leukaemia and differ markedly in their efficiency in catalysing glutathione (GSH) conjugation reactions. Glutathione 147-158 glutathione S-transferase pi 1 Homo sapiens 24-32 18852128-4 2008 To understand the mechanism by which variants of GSTP1-1 confer resistance to cisplatin, their relative abilities to catalyze conjugation of cisplatin with glutathione were examined. Glutathione 156-167 glutathione S-transferase pi 1 Homo sapiens 49-56 18852128-6 2008 Although these data are consistent with the idea that very low level resistance to cisplatin may be conferred by GSTP1-1-mediated cisplatin/glutathione conjugation, two observations indicate that such catalysis plays a minor role in the protection from cisplatin toxicity. Glutathione 140-151 glutathione S-transferase pi 1 Homo sapiens 113-120 18636161-3 2008 Overexpression of GST P1-1 in HepG2 cells decreased both the Bcl-xL deamidation and caspase-3 activation induced by treatment with GSH-DXR. Glutathione 131-134 glutathione S-transferase pi 1 Homo sapiens 18-26 18511072-3 2008 The allelic variants of GST P1-1 are associated with differing susceptibilities to leukaemia and differ markedly in their efficiency in catalysing glutathione (GSH) conjugation reactions. Glutathione 160-163 glutathione S-transferase pi 1 Homo sapiens 24-32 18511072-6 2008 We show also that all variants exhibit the same temperature stability in the range 10 degrees C to 45 degrees C. We have determined the crystal structures of GST P1-1 in complex with chlorambucil and its GSH conjugate for two of these allelic variants that have different residues at positions 104 and 113. Glutathione 204-207 glutathione S-transferase pi 1 Homo sapiens 158-166 18511072-8 2008 This result suggests that under certain stress conditions where GSH levels are low, GST P1-1 can inactivate the drug by sequestering it from the surrounding medium. Glutathione 64-67 glutathione S-transferase pi 1 Homo sapiens 84-92 18204073-4 2008 Compared with parental cells, expression of GSTP1-1 alone enhanced the rate of intracellular accumulation of SFN and its glutathione conjugate, SFN-SG--an effect that was associated with increased ARE-containing reporter gene induction. Glutathione 121-132 glutathione S-transferase pi 1 Homo sapiens 44-51 18204073-7 2008 Depletion of GSH prior to SFN treatment or the substitution of tert-butylhydroquinone for SFN abolished the effects of MRP1/GSTP1-1 on ARE-containing gene induction-indicating that these effects are GSH dependent. Glutathione 13-16 glutathione S-transferase pi 1 Homo sapiens 124-131 18204073-7 2008 Depletion of GSH prior to SFN treatment or the substitution of tert-butylhydroquinone for SFN abolished the effects of MRP1/GSTP1-1 on ARE-containing gene induction-indicating that these effects are GSH dependent. Glutathione 199-202 glutathione S-transferase pi 1 Homo sapiens 124-131 17431793-0 2007 Conformational change in the active center region of GST P1-1, due to binding of a synthetic conjugate of DXR with GSH, enhanced JNK-mediated apoptosis. Glutathione 115-118 glutathione S-transferase pi 1 Homo sapiens 53-61 18203258-4 2008 Site-specific, dose-dependent modification of Cys47 in native and His-tagged GSTP was revealed by MS, and correlated with inhibition of glutathione (GSH) conjugating activity. Glutathione 136-147 glutathione S-transferase pi 1 Homo sapiens 77-81 18203258-4 2008 Site-specific, dose-dependent modification of Cys47 in native and His-tagged GSTP was revealed by MS, and correlated with inhibition of glutathione (GSH) conjugating activity. Glutathione 149-152 glutathione S-transferase pi 1 Homo sapiens 77-81 18162130-9 2007 Hypothetically, absence of GST-M1 leaves more glutathione as substrate for the co-expressed GST-P1. Glutathione 46-57 glutathione S-transferase pi 1 Homo sapiens 92-98 18177897-0 2008 Modulating catalytic activity by unnatural amino acid residues in a GSH-binding loop of GST P1-1. Glutathione 68-71 glutathione S-transferase pi 1 Homo sapiens 88-96 17267100-7 2007 Expression of GSTP1 correlated significantly with GSH level and gamma-GCS and GR activities. Glutathione 50-53 glutathione S-transferase pi 1 Homo sapiens 14-19 17431793-3 2007 In the present experiment, binding of GSH-DXR to GST P1-1 allosterically led to the disappearance of its enzyme activity and activated the kinase activity of JNK without dissociation of the JNK-GST P1-1 complex. Glutathione 38-41 glutathione S-transferase pi 1 Homo sapiens 49-57 17431793-3 2007 In the present experiment, binding of GSH-DXR to GST P1-1 allosterically led to the disappearance of its enzyme activity and activated the kinase activity of JNK without dissociation of the JNK-GST P1-1 complex. Glutathione 38-41 glutathione S-transferase pi 1 Homo sapiens 49-55 17431793-8 2007 The findings suggested that allosteric inhibition of GST P1-1 activity by the binding of GSH-DXR following conformational change may activate JNK and induce apoptosis via the mitochondrial pathway in the cells. Glutathione 89-92 glutathione S-transferase pi 1 Homo sapiens 53-61 17016661-7 2006 The herbal treatments also increased glutathione S-transferase-pi (GSTP1) expression, albeit to a lesser extent than MGMT. Glutathione 37-48 glutathione S-transferase pi 1 Homo sapiens 67-72 16791478-1 2006 Glutathione S-transferase P1 (GSTP1) belongs to a family of phase II metabolic enzymes that can detoxify the carcinogens and cytotoxic drugs by conjugating them with glutathione. Glutathione 166-177 glutathione S-transferase pi 1 Homo sapiens 0-28 16791478-1 2006 Glutathione S-transferase P1 (GSTP1) belongs to a family of phase II metabolic enzymes that can detoxify the carcinogens and cytotoxic drugs by conjugating them with glutathione. Glutathione 166-177 glutathione S-transferase pi 1 Homo sapiens 30-35 16636664-9 2006 Moreover, the glutathione-conjugating activity of GSTP1-1 was not involved in the regulation of TRAF2 signaling. Glutathione 14-25 glutathione S-transferase pi 1 Homo sapiens 50-57 17088135-9 2006 Children with asthma with GSTP1 val/val genotype had higher malondialdehyde and lower glutathione levels compared with other genotypes (P = .023 and P = .014, respectively). Glutathione 86-97 glutathione S-transferase pi 1 Homo sapiens 26-31 16819303-7 2006 The glutathione-conjugating activity of GSTP1 was essential for the above effects. Glutathione 4-15 glutathione S-transferase pi 1 Homo sapiens 40-45 16195232-7 2005 Electron paramagnetic resonance spectroscopy studies on intact Escherichia coli cells expressing the recombinant GST P1-1 enzyme indicate that bacterial cells, in response to NO treatment, are able to form the dinitrosyl diglutathionyl iron complex using intracellular iron and GSH. Glutathione 278-281 glutathione S-transferase pi 1 Homo sapiens 113-121 16317430-7 2006 Patients possessing the glutathione S-transferase P1-105 Valine/Valine (GSTP1-105VV) genotype showed a response rate of 67% compared to 21% in patients harbouring at least one GSTP1-105 Isoleucine (GSTP1-105I) allele (P=0.038). Glutathione 24-35 glutathione S-transferase pi 1 Homo sapiens 72-77 16230413-1 2005 GSTP1 is a member of the glutathione S-transferase enzyme superfamily, which catalyzes the conjugation of electrophiles with glutathione in the process of detoxification. Glutathione 25-36 glutathione S-transferase pi 1 Homo sapiens 0-5 16220971-1 2005 Human glutathione (GSH) transferase (hGSTP1-1) catalyzes the conversion of antitumor 2-crotonyloxymethyl-2-cycloalkenones (COMCs) to highly reactive exocyclic enone alkylating agents. Glutathione 19-22 glutathione S-transferase pi 1 Homo sapiens 37-45 15999103-6 2005 Inhibitors of glutathione synthesis (BSO), GSTs (curcumin, ethacrynic acid), and also of MRPs (MK571, sulphinpyrazone) improved the sensitising effect of GSTP1 AS RNA. Glutathione 14-25 glutathione S-transferase pi 1 Homo sapiens 154-159 15500952-6 2004 These results suggest that GSTP1 has protective effects against camptothecin-induced necrosis in subset of human lung adenocarcinoma through glutathione conjugation. Glutathione 141-152 glutathione S-transferase pi 1 Homo sapiens 27-32 15500952-1 2004 Glutathione S-transferase P1 (GSTP1) is known as a xenobiotic enzyme through conjugation of glutathione and also as an inhibitor of Jun N-terminal kinase (JNK). Glutathione 92-103 glutathione S-transferase pi 1 Homo sapiens 0-28 15500952-1 2004 Glutathione S-transferase P1 (GSTP1) is known as a xenobiotic enzyme through conjugation of glutathione and also as an inhibitor of Jun N-terminal kinase (JNK). Glutathione 92-103 glutathione S-transferase pi 1 Homo sapiens 30-35 15829614-3 2005 This resistance was attributed to the induction of certain glutathione S-transferases (hGSTP1-1, hGSTM2-2, and hGSTA1-1) and also for the tripeptide glutathione (GSH) synthesizing enzymes. Glutathione 59-70 glutathione S-transferase pi 1 Homo sapiens 87-95 15231573-7 2005 Added exogenous H(2)O(2) was removed more rapidly, which correlated with a greater decrease in reduced glutathione level in Raji clones expressing GSTP1 than in those clones without GSTP1 expression. Glutathione 103-114 glutathione S-transferase pi 1 Homo sapiens 147-152 15638917-0 2005 Genetic polymorphism of glutathione S-transferase genes (GSTM1, GSTT1 and GSTP1) and susceptibility to prostate cancer in Northern India. Glutathione 24-35 glutathione S-transferase pi 1 Homo sapiens 74-79 15604283-2 2004 GSTP1 phosphorylation by PKA was glutathione (GSH)-dependent, whereas phosphorylation by PKC did not require but was significantly enhanced by GSH. Glutathione 33-44 glutathione S-transferase pi 1 Homo sapiens 0-5 15604283-2 2004 GSTP1 phosphorylation by PKA was glutathione (GSH)-dependent, whereas phosphorylation by PKC did not require but was significantly enhanced by GSH. Glutathione 46-49 glutathione S-transferase pi 1 Homo sapiens 0-5 15604283-3 2004 In the presence of GSH, the stoichiometry of phosphorylation was 0.4 +/- 0.03 and 0.53 +/- 0.02 mol incorporated phosphate per mole of dimeric GSTP1 protein. Glutathione 19-22 glutathione S-transferase pi 1 Homo sapiens 143-148 15604283-4 2004 The GSTP1 protein was phosphorylated, in the presence of GSH, by eight different PKC isoforms (alpha, betaIota, betaIotaIota, delta, epsilon, gamma, eta, and zeta), belonging to the three major PKC subclasses, albeit with various efficiencies. Glutathione 57-60 glutathione S-transferase pi 1 Homo sapiens 4-9 15604283-9 2004 The GSH-dependence of the phosphorylation suggests that under high intracellular GSH conditions, such as is present in most drug-resistant tumors, the GSTP1 protein will exist in a hyper-phosphorylated and enzymatically more active state. Glutathione 4-7 glutathione S-transferase pi 1 Homo sapiens 151-156 15604283-9 2004 The GSH-dependence of the phosphorylation suggests that under high intracellular GSH conditions, such as is present in most drug-resistant tumors, the GSTP1 protein will exist in a hyper-phosphorylated and enzymatically more active state. Glutathione 81-84 glutathione S-transferase pi 1 Homo sapiens 151-156 15234070-8 2004 While Th A showed competitive inhibition towards CDNB it exhibited non-competitive inhibition towards GSH of the human GST P1-1. Glutathione 102-105 glutathione S-transferase pi 1 Homo sapiens 119-127 16599007-8 2004 These findings indicate that GCLC polymorphisms that affect GSH production also affect methylmercury retention, and that GSTP1 may play a role in conjugating methylmercury with GSH. Glutathione 177-180 glutathione S-transferase pi 1 Homo sapiens 121-126 15313406-5 2004 Our results demonstrate the ability of selected chemopreventive agents to decrease GSTP1-1 gene expression mechanisms and could thus contribute to reduce the incidence of glutathione related drug resistance in human leukemia. Glutathione 171-182 glutathione S-transferase pi 1 Homo sapiens 83-90 14679015-8 2003 The production of GSH-estrogen conjugates was dependent on the concentrations of E(2) and GSTP1 but overall yielded only one-tenth of the catechol estrogen production. Glutathione 18-21 glutathione S-transferase pi 1 Homo sapiens 90-95 15161912-8 2004 Immunoblot analysis of H69AR vesicles revealed the unexpected membrane association of GSH S-transferase P1-1 (GSTP1-1). Glutathione 86-89 glutathione S-transferase pi 1 Homo sapiens 110-117 15161912-10 2004 The addition of exogenous GSTP1-1 to HeLa-MRP1 vesicles resulted in GSH-dependent As(III) transport. Glutathione 68-71 glutathione S-transferase pi 1 Homo sapiens 26-33 15215328-0 2004 Polymorphisms in glutathione S-transferases GSTM1, GSTT1 and GSTP1 and cytochromes P450 CYP2E1 and CYP1A1 and susceptibility to cirrhosis or pancreatitis in alcoholics. Glutathione 17-28 glutathione S-transferase pi 1 Homo sapiens 61-66 15041478-15 2004 Altogether, the present study reveals that a major site for flavonoid interaction with GSH-dependent toxicokinetics is the GS-X pump MRP1 rather than the conjugating GSTP1-1 activity itself. Glutathione 87-90 glutathione S-transferase pi 1 Homo sapiens 166-173 14701855-7 2004 LA was 40 times less active than GSH in the inhibition of ONOOH-induced DHR-123 oxidation, whereas LA was 20 times more active than GSH in preventing the inhibition of GST-P1-1 by ONOOH. Glutathione 132-135 glutathione S-transferase pi 1 Homo sapiens 168-176 14679015-2 2003 The potential of the quinones to induce mutagenic DNA lesions is expected to be decreased by their conjugation with glutathione (GSH) either nonenzymatically or catalyzed by glutathione S-transferase P1 (GSTP1), a Phase II enzyme. Glutathione 116-127 glutathione S-transferase pi 1 Homo sapiens 174-202 14679015-2 2003 The potential of the quinones to induce mutagenic DNA lesions is expected to be decreased by their conjugation with glutathione (GSH) either nonenzymatically or catalyzed by glutathione S-transferase P1 (GSTP1), a Phase II enzyme. Glutathione 116-127 glutathione S-transferase pi 1 Homo sapiens 204-209 14679015-2 2003 The potential of the quinones to induce mutagenic DNA lesions is expected to be decreased by their conjugation with glutathione (GSH) either nonenzymatically or catalyzed by glutathione S-transferase P1 (GSTP1), a Phase II enzyme. Glutathione 129-132 glutathione S-transferase pi 1 Homo sapiens 174-202 14679015-9 2003 The concentration gap between catechol estrogens and GSH-estrogen conjugates may result from nonenzymatic reaction of the labile quinones with other nucleophiles besides GSH or may reflect the lower efficiency of GSTP1 compared with CYP1B1. Glutathione 53-56 glutathione S-transferase pi 1 Homo sapiens 213-218 14679015-2 2003 The potential of the quinones to induce mutagenic DNA lesions is expected to be decreased by their conjugation with glutathione (GSH) either nonenzymatically or catalyzed by glutathione S-transferase P1 (GSTP1), a Phase II enzyme. Glutathione 129-132 glutathione S-transferase pi 1 Homo sapiens 204-209 12937133-1 2003 Somatic inactivation of the glutathione S-transferase-pi gene (GSTP1) via CpG island hypermethylation occurs early during prostate carcinogenesis, present in approximately 70% of high-grade prostatic intraepithelial neoplasia (high-grade PIN) lesions and more than 90% of adenocarcinomas. Glutathione 28-39 glutathione S-transferase pi 1 Homo sapiens 63-68 14623254-1 2003 Glutathione S-transferase P1-1 (GSTP1-1) conjugates glutathione to electrophilic compounds and its expression is correlated to chemotherapeutic drug resistance. Glutathione 52-63 glutathione S-transferase pi 1 Homo sapiens 32-39 12937169-1 2003 The thermodynamics of binding of both the substrate glutathione (GSH) and the competitive inhibitor S-hexylglutathione to the mutant Y49F of human glutathione S-transferase (hGST P1-1), a key residue at the dimer interface, has been investigated by isothermal titration calorimetry and fluorescence spectroscopy. Glutathione 52-63 glutathione S-transferase pi 1 Homo sapiens 174-183 12937169-1 2003 The thermodynamics of binding of both the substrate glutathione (GSH) and the competitive inhibitor S-hexylglutathione to the mutant Y49F of human glutathione S-transferase (hGST P1-1), a key residue at the dimer interface, has been investigated by isothermal titration calorimetry and fluorescence spectroscopy. Glutathione 65-68 glutathione S-transferase pi 1 Homo sapiens 174-183 13679171-3 2003 In order to further investigate the effect of the isosteric substitution on the binding abilities of the new GSH analogues 4, 5 and 9, the previously reported cysteinyl-containing analogue H-Glo(-Cys-Gly-OH)-OH has been also evaluated as a co-substrate for hGSTP1-1. Glutathione 109-112 glutathione S-transferase pi 1 Homo sapiens 257-265 12686490-3 2003 GSTP1-1 activity is completely inhibited upon 1 h incubation with 100 microM quercetin or 2 h incubation with 25 microM quercetin, whereas 1 and 10 microM quercetin inhibit GSTP1-1 activity to a significant extent reaching a maximum of 25 and 42% inhibition respectively after 2 h. Co-incubation with tyrosinase greatly enhances the rate of inactivation, whereas co-incubation with ascorbic acid or glutathione prevents this inhibition. Glutathione 399-410 glutathione S-transferase pi 1 Homo sapiens 0-7 12805482-2 2003 This study examines whether glutathione S-transferase-pi (GSTP1-1) is involved in resistance to anticancer drugs in cholangiocarcinoma and whether GSTP1-1-specific inhibitors can overcome this resistance. Glutathione 28-39 glutathione S-transferase pi 1 Homo sapiens 58-65 12686490-4 2003 Addition of glutathione upon complete inactivation of GSTP1-1 partially restores the activity. Glutathione 12-23 glutathione S-transferase pi 1 Homo sapiens 54-61 12660004-1 2003 Glutathione transferases (GSTs), a multiple gene family of phase II enzymes, catalyze detoxifying endogenous reactions with glutathione and protect cellular macromolecules from damage caused by cytotoxic and carcinogenic agents. Glutathione 124-135 glutathione S-transferase pi 1 Homo sapiens 26-30 12680784-7 2003 Thus, we conclude that an electrophilic quinone oxidation product that reacts with intracellular nucleophiles including protein thiol or GSH plays a major role in the GSTP1 gene expression. Glutathione 137-140 glutathione S-transferase pi 1 Homo sapiens 167-172 11757669-0 2001 Polymorphisms of glutathione S-transferase genes (GSTM1, GSTP1 and GSTT1) and bladder cancer susceptibility in the Turkish population. Glutathione 17-28 glutathione S-transferase pi 1 Homo sapiens 57-62 12440523-6 2002 This inhibition of GST P1-1 is noncompetitive with respect to both substrates CDNB and GSH. Glutathione 87-90 glutathione S-transferase pi 1 Homo sapiens 19-27 12119004-1 2002 Glutathione S-transferases (GSTs) are a family of detoxification isozymes that protect cells by conjugating GSH to a variety of toxic compounds, and they may also play a role in the regulation of both cellular proliferation and apoptosis. Glutathione 108-111 glutathione S-transferase pi 1 Homo sapiens 28-32 12119004-5 2002 We also showed that GSH partially protected the inactivation of GST P1-1 by 4-OHEN in vitro, and depletion of cellular GSH enhanced the 4-OHEN-induced inhibition of GST activity. Glutathione 20-23 glutathione S-transferase pi 1 Homo sapiens 64-70 11849043-4 2002 Relative to control cells, those expressing GSTA1-1 showed the highest rate (about 50-fold increase) to perform GSH-conjugation of (-)-anti-DBPDE (R-absolute configuration at the benzylic oxirane carbon in the fjord-region) followed by GSTM1-1 (25-fold increase) and GSTP1-1 (10-fold increase). Glutathione 112-115 glutathione S-transferase pi 1 Homo sapiens 267-274 11849043-9 2002 With (+)-anti-BPDE, GSTP1-1-expressing cells demonstrated a substantially higher rate of GSH-conjugate formation than cells with GSTA1-1 and GSTM1-1 cells (33- and 10-fold increase, respectively). Glutathione 89-92 glutathione S-transferase pi 1 Homo sapiens 20-27 12112003-5 2002 The data obtained from our etoposide-resistant clone and the possibility to reverse the sensitive phenotype to a resistant one by means of hexyl-glutathione preincubation, seem to suggest that cellular levels of glutathione have a key role in protecting GST P1-1 by oxidation and consequently the cell"s decision between life and death. Glutathione 212-223 glutathione S-transferase pi 1 Homo sapiens 254-262 11368548-9 2001 The inhibition of GSTP1-1 was completely reversible upon filtration and reconstitution in buffer containing 10 mM GSH. Glutathione 114-117 glutathione S-transferase pi 1 Homo sapiens 18-25 11433346-3 2001 Here we show that glutathione S-transferase P1-1 (GSTP1) interacts with FANCC, and that overexpression of both proteins in a myeloid progenitor cell line prevents apoptosis following factor deprivation. Glutathione 18-29 glutathione S-transferase pi 1 Homo sapiens 50-55 11159743-1 2001 The phase II glutathione S-transferases (GSTs) GSTT1, GSTM1 and GSTP1 catalyse glutathione-mediated reduction of exogenous and endogenous electrophiles. Glutathione 13-24 glutathione S-transferase pi 1 Homo sapiens 64-69 11295612-8 2001 GSTP1 is an enzyme that helps catalyze the conjugation reaction between potentially damaging electrophiles and glutathione. Glutathione 111-122 glutathione S-transferase pi 1 Homo sapiens 0-5 11113459-6 2000 The results of the present study clearly indicate that the location of the epoxide function determines specificity of the allelic variants of hGSTP1-1 in the GSH conjugation of activated diol epoxide isomers of B[c]C. Glutathione 158-161 glutathione S-transferase pi 1 Homo sapiens 142-150 11108808-10 2000 Indeed, their synthetic C(7)-aglycon-GSH conjugates exerted a strong inhibitory effect on GST P1-1, with K(i) at 25 degrees in the 1-2 microM range, scarcely dependent on their stereochemistry at C(7). Glutathione 37-40 glutathione S-transferase pi 1 Homo sapiens 90-98 11196146-11 2001 Bioactivation assays using LNCaP cytosols showed that enzymatic activation of N-OH-PhIP to a DNA binding species was dependent on ATP and could be inhibited by recombinant human GSTP1 in the presence of glutathione. Glutathione 203-214 glutathione S-transferase pi 1 Homo sapiens 178-183 11113459-2 2000 The Pi class human glutathione (GSH) transferase (hGSTP1-1), which is polymorphic in humans with respect to amino acid residues in positions 104 (isoleucine or valine) and/or 113 (alanine or valine), plays an important role in the detoxification of PAH-diol epoxides. Glutathione 19-30 glutathione S-transferase pi 1 Homo sapiens 50-58 10799737-1 2000 The catalytic efficiencies of the allelic variants of human glutathione (GSH) S-transferase Pi (hGSTP1-1), which differ in their primary structures by the amino acids in positions 104 (isoleucine or valine) and/or 113 (alanine or valine), in the GSH conjugation (detoxification) of acrolein and crotonaldehyde have been determined. Glutathione 60-71 glutathione S-transferase pi 1 Homo sapiens 96-104 11113459-2 2000 The Pi class human glutathione (GSH) transferase (hGSTP1-1), which is polymorphic in humans with respect to amino acid residues in positions 104 (isoleucine or valine) and/or 113 (alanine or valine), plays an important role in the detoxification of PAH-diol epoxides. Glutathione 32-35 glutathione S-transferase pi 1 Homo sapiens 50-58 11071881-2 2000 Increased glutathione (GSH) conjugation (inactivation) of alkylating anticancer drugs or their activated metabolites due to overexpression of the Pi class GSH S-transferase (hGSTP1-1) is believed to be an important mechanism in tumor cell resistance to alkylating agents. Glutathione 10-21 glutathione S-transferase pi 1 Homo sapiens 174-182 11071881-2 2000 Increased glutathione (GSH) conjugation (inactivation) of alkylating anticancer drugs or their activated metabolites due to overexpression of the Pi class GSH S-transferase (hGSTP1-1) is believed to be an important mechanism in tumor cell resistance to alkylating agents. Glutathione 23-26 glutathione S-transferase pi 1 Homo sapiens 174-182 11071881-4 2000 Here, we report that the allelic variants of hGSTP1-1 significantly differ in their efficiency in catalyzing the GSH conjugation of chlorambucil. Glutathione 113-116 glutathione S-transferase pi 1 Homo sapiens 45-51 10996298-5 2000 The presence of GSTP1-1 significantly accelerated the initial rate of GSH-mediated consumption of curcumin in 10 mM potassium phosphate, pH 7.0, and 1 mM GSH. Glutathione 70-73 glutathione S-transferase pi 1 Homo sapiens 16-23 11108662-6 2000 We conclude that MRP2-mediated efflux of the glutathione conjugate of 4NQO and/or another toxic derivative of 4NQO is required to support GSTP1-1-associated protection from 4NQO toxicities in HepG2 cells. Glutathione 45-56 glutathione S-transferase pi 1 Homo sapiens 138-145 10996298-5 2000 The presence of GSTP1-1 significantly accelerated the initial rate of GSH-mediated consumption of curcumin in 10 mM potassium phosphate, pH 7.0, and 1 mM GSH. Glutathione 154-157 glutathione S-transferase pi 1 Homo sapiens 16-23 10996298-7 2000 GSTP1-1 was also shown to catalyze the reverse reaction leading to the formation of curcumin from GSH adducts of FMK and FAL. Glutathione 98-101 glutathione S-transferase pi 1 Homo sapiens 0-7 10799737-1 2000 The catalytic efficiencies of the allelic variants of human glutathione (GSH) S-transferase Pi (hGSTP1-1), which differ in their primary structures by the amino acids in positions 104 (isoleucine or valine) and/or 113 (alanine or valine), in the GSH conjugation (detoxification) of acrolein and crotonaldehyde have been determined. Glutathione 73-76 glutathione S-transferase pi 1 Homo sapiens 96-104 10799737-1 2000 The catalytic efficiencies of the allelic variants of human glutathione (GSH) S-transferase Pi (hGSTP1-1), which differ in their primary structures by the amino acids in positions 104 (isoleucine or valine) and/or 113 (alanine or valine), in the GSH conjugation (detoxification) of acrolein and crotonaldehyde have been determined. Glutathione 246-249 glutathione S-transferase pi 1 Homo sapiens 96-104 10799737-3 2000 The catalytic efficiencies of the hGSTP1-1 variants IA, IV, and VA in the GSH conjugation of acrolein were statistically significantly higher (at P=0.05) compared with the VV isoform. Glutathione 74-77 glutathione S-transferase pi 1 Homo sapiens 34-42 10666194-0 2000 Polymorphisms within glutathione S-transferase genes (GSTM1, GSTT1, GSTP1) and risk of relapse in childhood B-cell precursor acute lymphoblastic leukemia: a case-control study. Glutathione 21-32 glutathione S-transferase pi 1 Homo sapiens 68-73 10692562-5 2000 The inhibition of class alpha GSTs was competitive towards GSH. Glutathione 59-62 glutathione S-transferase pi 1 Homo sapiens 30-34 10717233-2 2000 We report here that the pathogenesis of hepatocellular carcinoma (HCC), one of the most common cancers in the world, frequently involves an accumulation of somatic <CpG island> DNA methylation changes at GSTP1, the gene encoding the pi-class glutathione S-transferase. Glutathione 248-259 glutathione S-transferase pi 1 Homo sapiens 210-215 10692504-1 2000 gamma-L-Glutamyl-S-(benzyl)-L-cysteinyl-R-(-)-phenylglycine (TER 117) has previously been developed for selective inhibition of human glutathione S-transferase P1-1 (GST P1-1) based on the postulated contribution of this isoenzyme to the development of drug resistance in cancer cells. Glutathione 134-145 glutathione S-transferase pi 1 Homo sapiens 166-174 10350652-11 1999 GSH homeostasis thus appears to be maintained by an interaction between GSTP1 and GCS in human hepatic cells resistant to the GSH poison. Glutathione 0-3 glutathione S-transferase pi 1 Homo sapiens 72-77 10383436-4 1999 In fact, above 35 degrees C, glutathione (GSH) binding to GST P1-1 displays positive cooperativity, whereas negative cooperativity occurs below 25 degrees C. This binding mechanism minimizes changes of GSH affinity for GST P1-1 because of temperature fluctuation. Glutathione 29-40 glutathione S-transferase pi 1 Homo sapiens 58-66 10383436-4 1999 In fact, above 35 degrees C, glutathione (GSH) binding to GST P1-1 displays positive cooperativity, whereas negative cooperativity occurs below 25 degrees C. This binding mechanism minimizes changes of GSH affinity for GST P1-1 because of temperature fluctuation. Glutathione 29-40 glutathione S-transferase pi 1 Homo sapiens 219-227 10383436-4 1999 In fact, above 35 degrees C, glutathione (GSH) binding to GST P1-1 displays positive cooperativity, whereas negative cooperativity occurs below 25 degrees C. This binding mechanism minimizes changes of GSH affinity for GST P1-1 because of temperature fluctuation. Glutathione 42-45 glutathione S-transferase pi 1 Homo sapiens 58-66 10383436-4 1999 In fact, above 35 degrees C, glutathione (GSH) binding to GST P1-1 displays positive cooperativity, whereas negative cooperativity occurs below 25 degrees C. This binding mechanism minimizes changes of GSH affinity for GST P1-1 because of temperature fluctuation. Glutathione 42-45 glutathione S-transferase pi 1 Homo sapiens 219-227 10383436-4 1999 In fact, above 35 degrees C, glutathione (GSH) binding to GST P1-1 displays positive cooperativity, whereas negative cooperativity occurs below 25 degrees C. This binding mechanism minimizes changes of GSH affinity for GST P1-1 because of temperature fluctuation. Glutathione 202-205 glutathione S-transferase pi 1 Homo sapiens 58-66 10383436-4 1999 In fact, above 35 degrees C, glutathione (GSH) binding to GST P1-1 displays positive cooperativity, whereas negative cooperativity occurs below 25 degrees C. This binding mechanism minimizes changes of GSH affinity for GST P1-1 because of temperature fluctuation. Glutathione 202-205 glutathione S-transferase pi 1 Homo sapiens 219-227 10383436-6 1999 As a whole, GST P1-1 represents the first enzyme which displays a temperature-dependent homotropic regulation of substrate (e.g. GSH) binding. Glutathione 129-132 glutathione S-transferase pi 1 Homo sapiens 12-20 10441116-1 1999 Two variants of human class pi glutathione (GSH) S-transferase 1-1 with either isoleucine or valine in position 104 (hGSTP1-1[I104] and hGSTP1-1[V104]) have distinct activity toward (+)-anti-7, 8-dihydroxy-9,10-oxy-7,8,9,10-tetrahydrobenzo[a]pyrene [(+)-anti-BPDE]. Glutathione 44-47 glutathione S-transferase pi 1 Homo sapiens 117-123 10353259-2 1999 The glutathione-related metabolism of PGA2 was therefore investigated both with purified glutathione S-transferase P1-1 (GSTP1-1) and with IGR-39 human melanoma cells. Glutathione 4-15 glutathione S-transferase pi 1 Homo sapiens 121-128 10353259-10 1999 In conclusion, PGA2 modulates all three aspects of the glutathione-mediated biotransformation system, i.e. GSH levels, GSTP1-1 activity, and transport of GSH conjugates. Glutathione 55-66 glutathione S-transferase pi 1 Homo sapiens 119-126 10334868-3 1999 Increased glutathione (GSH) conjugation through catalysis by GSH S-transferases (GSTs) is believed to be an important mechanism in tumor cell resistance to alkylating agents. Glutathione 10-21 glutathione S-transferase pi 1 Homo sapiens 81-85 10334868-3 1999 Increased glutathione (GSH) conjugation through catalysis by GSH S-transferases (GSTs) is believed to be an important mechanism in tumor cell resistance to alkylating agents. Glutathione 23-26 glutathione S-transferase pi 1 Homo sapiens 81-85 10334868-4 1999 In the present study, we report that the allelic variants of human Pi class GST (hGSTP1-1), which differ in their primary structures at amino acids in positions 104 and/or 113, exhibit significant differences in their activity in the GSH conjugation of alkylating anticancer drug thiotepa. Glutathione 234-237 glutathione S-transferase pi 1 Homo sapiens 81-89 10334868-7 1999 The hGSTP1-1-catalyzed GSH conjugation of thiotepa was time and protein dependent and followed Michaelis-Menten kinetics. Glutathione 23-26 glutathione S-transferase pi 1 Homo sapiens 4-10 10350652-11 1999 GSH homeostasis thus appears to be maintained by an interaction between GSTP1 and GCS in human hepatic cells resistant to the GSH poison. Glutathione 126-129 glutathione S-transferase pi 1 Homo sapiens 72-77 9973324-7 1999 The tTG-catalyzed polymerization of GST P1-1 leads to its functional inactivation and is competitively inhibited by GSH. Glutathione 116-119 glutathione S-transferase pi 1 Homo sapiens 36-44 9882456-0 1999 Quantitative differences in the active-site hydrophobicity of five human glutathione S-transferase isoenzymes: water-soluble carcinogen-selective properties of the neoplastic GSTP1-1 species. Glutathione 73-84 glutathione S-transferase pi 1 Homo sapiens 175-182 9882456-1 1999 The active-site (the H-site) hydrophobicity of five human glutathione S-transferases (GSTs) was analyzed by application of linear free energy relationships (LFERs) with a series of S-alkylated glutathione inhibitors, GS(CH2)n - 1CH3 (n = 1-14). Glutathione 58-69 glutathione S-transferase pi 1 Homo sapiens 86-90 9788613-1 1998 In this study, the role of glutathione S-transferase (GST) P1-1, the cellular reduced glutathione (GSH) status, and ATP-dependent efflux pumps in the cellular glutathione-dependent biotransformation of thiotepa and transport of the main metabolite monoglutathionylthiotepa in relation to cytotoxicity was studied in control and GST-P1-1-transfected MCF-7 cell lines. Glutathione 27-38 glutathione S-transferase pi 1 Homo sapiens 328-334 9877184-0 1998 GSTP1-1 stereospecifically catalyzes glutathione conjugation of ethacrynic acid. Glutathione 37-48 glutathione S-transferase pi 1 Homo sapiens 0-7 9850062-1 1998 Four allelic variants of glutathione (GSH) S-transferase P1-1 (hGSTP1-1) that differ in their structures at amino acid(s) in position(s) 104 and/or 113 are known to exist in human populations. Glutathione 25-36 glutathione S-transferase pi 1 Homo sapiens 63-71 9850062-1 1998 Four allelic variants of glutathione (GSH) S-transferase P1-1 (hGSTP1-1) that differ in their structures at amino acid(s) in position(s) 104 and/or 113 are known to exist in human populations. Glutathione 38-41 glutathione S-transferase pi 1 Homo sapiens 63-71 9850062-3 1998 In this communication, we report that the I104,A113 allele of hGSTP1-1, which is most frequent in human populations, is also most efficient in the GSH conjugation of carcinogenic anti-diol epoxides of benzo[g]chrysene and benzo[c]phenanthrene (anti-BGCDE and anti-BCPDE, respectively). Glutathione 147-150 glutathione S-transferase pi 1 Homo sapiens 62-70 9776312-1 1998 We tested the hypothesis that combined increased expression of human glutathione S-transferase P1-1 (GSTP1-1), an enzyme that catalyzes the conjugation with glutathione of several toxic electrophiles, and the glutathione-conjugate efflux pump, multidrug resistance protein (MRP), confers high level resistance to the cytotoxicities of anticancer and other drugs. Glutathione 69-80 glutathione S-transferase pi 1 Homo sapiens 101-108 9776312-1 1998 We tested the hypothesis that combined increased expression of human glutathione S-transferase P1-1 (GSTP1-1), an enzyme that catalyzes the conjugation with glutathione of several toxic electrophiles, and the glutathione-conjugate efflux pump, multidrug resistance protein (MRP), confers high level resistance to the cytotoxicities of anticancer and other drugs. Glutathione 157-168 glutathione S-transferase pi 1 Homo sapiens 101-108 9776312-9 1998 These results establish that coordinated expression of MRP and GSTP1-1 can confer high level resistance to the cytotoxicities of some drugs, including ethacrynic acid, but that such resistance is variable and does not apply to all toxic drugs that can potentially form glutathione conjugates in either spontaneous or GSTP1-1-catalyzed reactions. Glutathione 269-280 glutathione S-transferase pi 1 Homo sapiens 63-70 9788613-10 1998 Only enhanced biotransformation and subsequent transport of the glutathione conjugate into the medium (which occurs with the GST-P1-1 transfectant) results in enhanced viability. Glutathione 64-75 glutathione S-transferase pi 1 Homo sapiens 125-133 9788613-1 1998 In this study, the role of glutathione S-transferase (GST) P1-1, the cellular reduced glutathione (GSH) status, and ATP-dependent efflux pumps in the cellular glutathione-dependent biotransformation of thiotepa and transport of the main metabolite monoglutathionylthiotepa in relation to cytotoxicity was studied in control and GST-P1-1-transfected MCF-7 cell lines. Glutathione 99-102 glutathione S-transferase pi 1 Homo sapiens 328-334 9771942-3 1998 All three variants of hGSTP1-1 were significantly more efficient than either hGSTA1-1 or hGSTM1-1 in GSH conjugation of (+)-anti-5-MeCDE. Glutathione 101-104 glutathione S-transferase pi 1 Homo sapiens 22-30 9525277-1 1998 Previous studies have identified allelic variants of the human glutathione transferase (GST) Pi gene and showed that the two different encoded proteins with isoleucine (GSTP1-1/I-105) or valine (GSTP1-1/V-105) at position 105, respectively, differ significantly in their catalytic activities with model substrates. Glutathione 63-74 glutathione S-transferase pi 1 Homo sapiens 169-176 9525277-1 1998 Previous studies have identified allelic variants of the human glutathione transferase (GST) Pi gene and showed that the two different encoded proteins with isoleucine (GSTP1-1/I-105) or valine (GSTP1-1/V-105) at position 105, respectively, differ significantly in their catalytic activities with model substrates. Glutathione 63-74 glutathione S-transferase pi 1 Homo sapiens 195-202 9568063-1 1998 BACKGROUND: The aim of the present study was to establish the risk of squamous cell carcinoma (SCC) of the larynx associated with the congenital absence of glutathione S-transferase M1 (GSTM1), and to describe the expression of the isoenzymes GSTA1/2, GSTP1-1, and GSTM1 and glutathione (GSH) content in healthy and tumoral larynx tissue. Glutathione 156-167 glutathione S-transferase pi 1 Homo sapiens 252-259 9281308-1 1997 The kinetics of the conjugation of glutathione (GSH) with anti-1, 2-dihydroxy-3,4-oxy-1,2,3,4-tetrahydrochrysene (anti-CDE), the activated form of the widespread environmental pollutant chrysene, catalyzed by two naturally occurring polymorphic forms of the pi class human GSH S-transferase (hGSTP1-1), has been investigated. Glutathione 35-46 glutathione S-transferase pi 1 Homo sapiens 292-300 9281308-7 1997 These studies revealed that the enantioselectivity of hGSTP1-1 for (+)-anti-CDE and the differential catalytic efficiencies of the V104 and I104 forms of hGSTP1-1 in the GSH conjugation of (+)-anti-CDE were due to the differences in the active-site architecture of the two proteins. Glutathione 170-173 glutathione S-transferase pi 1 Homo sapiens 154-162 9281308-1 1997 The kinetics of the conjugation of glutathione (GSH) with anti-1, 2-dihydroxy-3,4-oxy-1,2,3,4-tetrahydrochrysene (anti-CDE), the activated form of the widespread environmental pollutant chrysene, catalyzed by two naturally occurring polymorphic forms of the pi class human GSH S-transferase (hGSTP1-1), has been investigated. Glutathione 48-51 glutathione S-transferase pi 1 Homo sapiens 292-300 9281308-2 1997 The polymorphic forms of hGSTP1-1, which differ in their primary structure by a single amino acid in position 104, exhibited preference for the GSH conjugation of (+)-anti-CDE, which is a far more potent carcinogen than (-)-anti-CDE. Glutathione 144-147 glutathione S-transferase pi 1 Homo sapiens 25-33 9281308-3 1997 When concentration of anti-CDE was varied (5-200 microM and the GSH concentration was kept constant at 2 mM, both hGSTP1-1(I104) and hGSTP1-1(V104) obeyed Michaelis-Menten kinetics. Glutathione 64-67 glutathione S-transferase pi 1 Homo sapiens 114-120 9281308-6 1997 The mechanism of the differences in the kinetic properties of hGSTP1-1 isoforms toward anti-CDE was investigated by molecular modeling of the two proteins with GSH conjugation products in their active sites. Glutathione 160-163 glutathione S-transferase pi 1 Homo sapiens 62-68 9092542-6 1997 The encoded proteins expressed in Escherichia coli and purified by GSH affinity chromatography showed a 3-fold lower Km (CDNB) and a 3-4-fold higher Kcat/Km for the hGSTP1*A encoded protein than the proteins encoded by hGSTP1*B and hGSTP1*C. Analysis of 75 cases showed the relative frequency of hGSTP1*C to be 4-fold higher in malignant gliomas than in normal tissues. Glutathione 67-70 glutathione S-transferase pi 1 Homo sapiens 165-171 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. Glutathione 77-88 glutathione S-transferase pi 1 Homo sapiens 113-120 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. Glutathione 90-93 glutathione S-transferase pi 1 Homo sapiens 113-120 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. Glutathione 165-168 glutathione S-transferase pi 1 Homo sapiens 113-120 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. Glutathione 113-116 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). Glutathione 14-17 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). Glutathione 14-17 glutathione S-transferase pi 1 Homo sapiens 109-122 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. Glutathione 155-158 glutathione S-transferase pi 1 Homo sapiens 139-147 9092542-6 1997 The encoded proteins expressed in Escherichia coli and purified by GSH affinity chromatography showed a 3-fold lower Km (CDNB) and a 3-4-fold higher Kcat/Km for the hGSTP1*A encoded protein than the proteins encoded by hGSTP1*B and hGSTP1*C. Analysis of 75 cases showed the relative frequency of hGSTP1*C to be 4-fold higher in malignant gliomas than in normal tissues. Glutathione 67-70 glutathione S-transferase pi 1 Homo sapiens 219-225 9092542-6 1997 The encoded proteins expressed in Escherichia coli and purified by GSH affinity chromatography showed a 3-fold lower Km (CDNB) and a 3-4-fold higher Kcat/Km for the hGSTP1*A encoded protein than the proteins encoded by hGSTP1*B and hGSTP1*C. Analysis of 75 cases showed the relative frequency of hGSTP1*C to be 4-fold higher in malignant gliomas than in normal tissues. Glutathione 67-70 glutathione S-transferase pi 1 Homo sapiens 219-225 9092542-6 1997 The encoded proteins expressed in Escherichia coli and purified by GSH affinity chromatography showed a 3-fold lower Km (CDNB) and a 3-4-fold higher Kcat/Km for the hGSTP1*A encoded protein than the proteins encoded by hGSTP1*B and hGSTP1*C. Analysis of 75 cases showed the relative frequency of hGSTP1*C to be 4-fold higher in malignant gliomas than in normal tissues. Glutathione 67-70 glutathione S-transferase pi 1 Homo sapiens 219-225 9084911-3 1997 In the present study, the role of the major human GSTs in the conjugation of PGA2 and PGJ2 with GSH was investigated with purified enzymes, i.e., the Alpha-class enzymes GST A1-1 and GST A2-2, the Mu-class enzyme GST M1a-1a, and the Pi-class enzyme GST P1-1. Glutathione 96-99 glutathione S-transferase pi 1 Homo sapiens 249-257 8555414-11 1995 When 2 mM ifosfamide mustard was incubated with 1 mM GSH in the presence of 40 microM GST P1-1, the formation of monoglutathionyl ifosfamide mustard was 2.3-fold increased above the spontaneous level. Glutathione 53-56 glutathione S-transferase pi 1 Homo sapiens 86-94 9020891-1 1997 Although the three-dimensional structure of human glutathione transferase (GST) P1-1 crystallized with a GSH analogue has been reported, its structure in the non-complexed form has not been determined. Glutathione 105-108 glutathione S-transferase pi 1 Homo sapiens 50-82 9020891-5 1997 When GST P1-1 and the antibody were incubated in the presence of 60 microM GSH, no inhibition of activity was found, whereas 1-chloro-2,4-dinitrobenzene had no effect at concentrations up to 10 microM. Glutathione 75-78 glutathione S-transferase pi 1 Homo sapiens 5-13 9020891-6 1997 The binding of GST P1-1 to antibody adsorbed to Protein A-Sepharose was also prevented by both 0.1 mM GSH and N-ethylmaleimide treatment. Glutathione 102-105 glutathione S-transferase pi 1 Homo sapiens 15-23 9084911-12 1997 GST P1-1 showed a clear selectivity with regard to the formation of the S-GSH conjugate of PGA2. Glutathione 74-77 glutathione S-transferase pi 1 Homo sapiens 0-8 7728969-2 1995 GSTP1-1 showed a broad substrate specificity with both low and high GSH (10 mM) concentrations at pH 7.0, and the inhibitor insensitivity was then prominent. Glutathione 68-71 glutathione S-transferase pi 1 Homo sapiens 0-7 7887912-3 1995 GSTs A1-1, A2-2, M1a-1a and P1-1 catalysed both the forward and reverse reactions with specific activities (mumol/min per mg at 30 microM isothiocyanate or GSH conjugate) ranging from 23.1 for the GSH conjugation of BITC by GST P1-1 to 0.03 for the dissociation of BITC-SG by GST A1-1. Glutathione 156-159 glutathione S-transferase pi 1 Homo sapiens 224-230 8313381-2 1994 When the glutathione conjugate of EA was incubated with a 5-fold molar excess of N-acetyl-L-cysteine or GST P1-1, a time-dependent transfer of EA to N-acetyl-L-cysteine or GST P1-1 was observed. Glutathione 9-20 glutathione S-transferase pi 1 Homo sapiens 104-112 8108434-8 1994 GST P1-1 added to the culture medium of HeLa cells augmented the protective effect of glutathione against the toxicity of adenine propenal and thymine propenal. Glutathione 86-97 glutathione S-transferase pi 1 Homo sapiens 0-8 8313381-2 1994 When the glutathione conjugate of EA was incubated with a 5-fold molar excess of N-acetyl-L-cysteine or GST P1-1, a time-dependent transfer of EA to N-acetyl-L-cysteine or GST P1-1 was observed. Glutathione 9-20 glutathione S-transferase pi 1 Homo sapiens 172-180 8313381-5 1994 When GST P1-1 was inactivated with a 5-fold molar excess of EA, adding an excess of glutathione resulted in full restoration of the catalytic activity in about 120 h. These findings may have several implications. Glutathione 84-95 glutathione S-transferase pi 1 Homo sapiens 5-13 8313381-6 1994 Under normal physiological conditions the inhibition of GST P1-1 by covalent binding of EA would be reversed by glutathione, leaving reversible inhibition by the glutathione conjugate of EA and by EA itself as the main mechanism of inhibition; however, when glutathione levels are low the covalent inhibition might be predominant, resulting in a completely different time course for the inhibition. Glutathione 112-123 glutathione S-transferase pi 1 Homo sapiens 56-64 8313381-6 1994 Under normal physiological conditions the inhibition of GST P1-1 by covalent binding of EA would be reversed by glutathione, leaving reversible inhibition by the glutathione conjugate of EA and by EA itself as the main mechanism of inhibition; however, when glutathione levels are low the covalent inhibition might be predominant, resulting in a completely different time course for the inhibition. Glutathione 162-173 glutathione S-transferase pi 1 Homo sapiens 56-64 8313381-6 1994 Under normal physiological conditions the inhibition of GST P1-1 by covalent binding of EA would be reversed by glutathione, leaving reversible inhibition by the glutathione conjugate of EA and by EA itself as the main mechanism of inhibition; however, when glutathione levels are low the covalent inhibition might be predominant, resulting in a completely different time course for the inhibition. Glutathione 162-173 glutathione S-transferase pi 1 Homo sapiens 56-64 34689350-1 2022 Over 50% prescribed drugs are metabolized by cytochrome P450 3A (CYP3A) and glutathione S-transferase pi (GSTP1) adds a glutathione to the oxidative products by CYP3A, which increases the hydrophilic property of metabolites and facilitates the excretion. Glutathione 76-87 glutathione S-transferase pi 1 Homo sapiens 106-111 8352805-1 1993 The pH-Vmax/KmGSH plot of glutathione S-transferase P (GST-P) showed a bell-shaped profile, indicating bifunctional catalysis for glutathione (GSH) conjugation. Glutathione 26-37 glutathione S-transferase pi 1 Homo sapiens 55-60 8352805-1 1993 The pH-Vmax/KmGSH plot of glutathione S-transferase P (GST-P) showed a bell-shaped profile, indicating bifunctional catalysis for glutathione (GSH) conjugation. Glutathione 14-17 glutathione S-transferase pi 1 Homo sapiens 26-53 8352805-1 1993 The pH-Vmax/KmGSH plot of glutathione S-transferase P (GST-P) showed a bell-shaped profile, indicating bifunctional catalysis for glutathione (GSH) conjugation. Glutathione 14-17 glutathione S-transferase pi 1 Homo sapiens 55-60 8343114-8 1993 The reaction of Tyr-7 of GSTP1-1 with DEPC was poorly inhibited by 1 mM GSH (14%) or 10 microM S-hexylglutathione (18%). Glutathione 72-75 glutathione S-transferase pi 1 Homo sapiens 25-32 8343115-11 1993 The GSH-binding determinants of GSTP1-1 are compared using sequence similarity with those of GSTs of Alpha, Mu and Theta classes. Glutathione 4-7 glutathione S-transferase pi 1 Homo sapiens 32-39 8343115-11 1993 The GSH-binding determinants of GSTP1-1 are compared using sequence similarity with those of GSTs of Alpha, Mu and Theta classes. Glutathione 4-7 glutathione S-transferase pi 1 Homo sapiens 93-97 2310397-2 1990 Inactivated GST P lost its S-hexyl-GSH-Sepharose column affinity. Glutathione 35-38 glutathione S-transferase pi 1 Homo sapiens 12-17 8340390-8 1993 The recombinant FAEES-III protein does not bind to a glutathione agarose affinity matrix, presumably because two of the substituted amino acids, Trp-39-->Cys and Gln-52-->Glu, are thought to contribute to the GST glutathione binding site. Glutathione 219-230 glutathione S-transferase pi 1 Homo sapiens 16-25 34689350-1 2022 Over 50% prescribed drugs are metabolized by cytochrome P450 3A (CYP3A) and glutathione S-transferase pi (GSTP1) adds a glutathione to the oxidative products by CYP3A, which increases the hydrophilic property of metabolites and facilitates the excretion. Glutathione 120-131 glutathione S-transferase pi 1 Homo sapiens 106-111 35344726-4 2022 To explore a possible link between these enzymes and bitter taste perception, we demonstrate that salivary glutathione transferases (GSTA1 and GSTP1) can metabolize bitter molecules. Glutathione 107-118 glutathione S-transferase pi 1 Homo sapiens 143-148 34988113-2 2021 The distribution of polymorphisms in cytosolic glutathione S-transferases GSTA1, GSTM1, GSTM3, GSTP1 (rs1695 and rs1138272), and GSTT1 were assessed in 207 COVID-19 patients and 252 matched healthy individuals, emphasizing their individual and cumulative effect in disease development and severity. Glutathione 47-58 glutathione S-transferase pi 1 Homo sapiens 95-100 34623592-1 2022 BACKGROUND: Glutathione S-transferase Pi (GSTP1) enzyme has a major antioxidant effect on the central nervous system (CNS), where it acts against oxidative damage, an established risk factor for amyotrophic lateral sclerosis (ALS). Glutathione 12-23 glutathione S-transferase pi 1 Homo sapiens 42-47 34430738-1 2021 RAPTA-EA1 is a promising glutathione transferase (GSTP-1) inhibitor that has previously been shown to inhibit the growth of various breast cancer cells. Glutathione 25-36 glutathione S-transferase pi 1 Homo sapiens 50-56 34191807-1 2021 GSTP1 is a member of the Glutathione-S-transferase (GST) family silenced by CpG island DNA hypermethylation in 90-95% of prostate cancers. Glutathione 25-36 glutathione S-transferase pi 1 Homo sapiens 0-5 35124341-0 2022 Impact of glutathione S transferases P1 (Ile105Val) variants on the risk of GSTp, phosphorylated c-Jun kinase, and P53 phenotypic expression and their implications on overall survival outcomes in non-small cell lung cancer patients treated with chemotherapy. Glutathione 10-21 glutathione S-transferase pi 1 Homo sapiens 76-80