PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30890751-6 2019 These various outcomes could also be attenuated by silencing of glutathione S-transferase P1 (GSTP1), a mediator of metabolic alterations and drug resistance in various cancers, and a regulator of cysteine oxidation. Cysteine 197-205 glutathione S-transferase pi 1 Homo sapiens 64-92 30890751-6 2019 These various outcomes could also be attenuated by silencing of glutathione S-transferase P1 (GSTP1), a mediator of metabolic alterations and drug resistance in various cancers, and a regulator of cysteine oxidation. Cysteine 197-205 glutathione S-transferase pi 1 Homo sapiens 94-99 30890751-7 2019 Collectively, our findings indicate DUOX1 deficiency in lung cancers promotes dysregulated EGFR signaling and enhanced GSTP1-mediated turnover of EGFR cysteine oxidation, which result in enhanced nuclear EGFR localization and tumorigenic properties. Cysteine 151-159 glutathione S-transferase pi 1 Homo sapiens 119-124 28254657-8 2017 Studies in solutions showed that L-cysteine can bind the GSTP substrate CDNB in the absence of GSTP. Cysteine 33-43 glutathione S-transferase pi 1 Homo sapiens 57-61 30290218-5 2019 An emerging molecular mechanism behind such regulatory function is the activity of GSTP as a redox chaperonine responsible for the selective glutathionylation of protein Cys residues in the different subcellular compartments. Cysteine 170-173 glutathione S-transferase pi 1 Homo sapiens 83-87 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. Cysteine 46-56 glutathione S-transferase pi 1 Homo sapiens 20-24 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. Cysteine 147-157 glutathione S-transferase pi 1 Homo sapiens 20-24 23183361-6 2013 Interestingly, the inhibition of GST P1-1 and its cysteine mutants by the gold(I) compound is essentially the same, suggesting that probably the cysteine residues are not so essential for enzyme inactivation in contrast to other reported inhibitors. Cysteine 145-153 glutathione S-transferase pi 1 Homo sapiens 33-41 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. Cysteine 193-202 glutathione S-transferase pi 1 Homo sapiens 12-19 27358914-4 2016 S-glutathionylation, the conjugation of glutathione to reactive cysteines, is catalyzed in part by glutathione-S-transferase pi (GSTP). Cysteine 64-73 glutathione S-transferase pi 1 Homo sapiens 129-133 24571427-7 2014 Only a cysteine adduct and a putative cross-linking adduct were detected on glutathione S-transferase Pi (GSTP). Cysteine 7-15 glutathione S-transferase pi 1 Homo sapiens 76-104 24571427-7 2014 Only a cysteine adduct and a putative cross-linking adduct were detected on glutathione S-transferase Pi (GSTP). Cysteine 7-15 glutathione S-transferase pi 1 Homo sapiens 106-110 24397869-4 2014 Modifications of cysteine residues of (i) human glutathione-S-transferase P1-1 (GSTP1) and (ii) the schistosomiasis drug target thioredoxin glutathione reductase (TGR) were studied. Cysteine 17-25 glutathione S-transferase pi 1 Homo sapiens 80-85 23596995-2 2013 Active GSTP1-1 is a homodimer with cysteine residues close to the active site that can undergo oligomerization in response to stress, a process that affects enzyme activity and interactions with signaling and redox-active proteins. Cysteine 35-43 glutathione S-transferase pi 1 Homo sapiens 7-14 23572520-4 2013 Cys(47) of GSTP1-1 is S-nitrosated in two steps, with the chemical step limited by a pre-equilibrium between the open and closed conformations of helix alpha2 at the active site. Cysteine 0-3 glutathione S-transferase pi 1 Homo sapiens 11-18 16787314-12 2005 To probe the role of Cys-47 in the inactivation of GSTP1 by compound 1, we prepared mutant C47A GSTP1. Cysteine 21-24 glutathione S-transferase pi 1 Homo sapiens 51-56 22608530-8 2012 The method successfully revealed that RMs of both drugs adducted to Cys-47 of hGSTP and the mass shifts corresponded to modification by the N-acetyl-p-benzoquinone imine form of APAP and diquinone methide form of raloxifene, respectively. Cysteine 68-71 glutathione S-transferase pi 1 Homo sapiens 78-83 20232108-1 2011 PABA/NO is a diazeniumdiolate selectively activated by glutathione S-transferase P (GSTP) to release nitric oxide (NO) and is a potent inducer of protein S-glutathionylation, a redox-sensitive post-translational modification of cysteine residues. Cysteine 228-236 glutathione S-transferase pi 1 Homo sapiens 55-82 20232108-1 2011 PABA/NO is a diazeniumdiolate selectively activated by glutathione S-transferase P (GSTP) to release nitric oxide (NO) and is a potent inducer of protein S-glutathionylation, a redox-sensitive post-translational modification of cysteine residues. Cysteine 228-236 glutathione S-transferase pi 1 Homo sapiens 84-88 19469519-6 2009 PPD and 2,5-dimethyl-1,4-benzoquinonediamine were also found to selectively modify the reactive Cys 47 residue of GSTP, which has a pK(a) of 3.5-4.2 and therefore exists in a largely protonated form. Cysteine 96-99 glutathione S-transferase pi 1 Homo sapiens 114-118 17918761-2 2007 Enzyme kinetics and electrospray mass spectrometry experiments using GST P1-1 and its cysteine-modified mutant forms revealed that the complexes are effective enzyme inhibitors, but they also rapidly inactivate the enzyme by covalent binding at Cys 47 and, to a lesser extent, Cys 101. Cysteine 86-94 glutathione S-transferase pi 1 Homo sapiens 69-77 17918761-2 2007 Enzyme kinetics and electrospray mass spectrometry experiments using GST P1-1 and its cysteine-modified mutant forms revealed that the complexes are effective enzyme inhibitors, but they also rapidly inactivate the enzyme by covalent binding at Cys 47 and, to a lesser extent, Cys 101. Cysteine 245-248 glutathione S-transferase pi 1 Homo sapiens 69-77 17918761-2 2007 Enzyme kinetics and electrospray mass spectrometry experiments using GST P1-1 and its cysteine-modified mutant forms revealed that the complexes are effective enzyme inhibitors, but they also rapidly inactivate the enzyme by covalent binding at Cys 47 and, to a lesser extent, Cys 101. Cysteine 277-280 glutathione S-transferase pi 1 Homo sapiens 69-77 23035985-5 2012 LC-MS/MS analysis demonstrated efficient alkylation of Cys residues of proteins including glutathione-S-transferase-P1 (GST-P1) and Kelch-like ECH-associated protein 1 (Keap1). Cysteine 55-58 glutathione S-transferase pi 1 Homo sapiens 90-118 23035985-5 2012 LC-MS/MS analysis demonstrated efficient alkylation of Cys residues of proteins including glutathione-S-transferase-P1 (GST-P1) and Kelch-like ECH-associated protein 1 (Keap1). Cysteine 55-58 glutathione S-transferase pi 1 Homo sapiens 120-126 22998212-6 2012 In total, 10 different peptide adducts were observed which result from modifications of Cys-47 and Cys-14 of hGST P1-1. Cysteine 88-91 glutathione S-transferase pi 1 Homo sapiens 109-118 22998212-6 2012 In total, 10 different peptide adducts were observed which result from modifications of Cys-47 and Cys-14 of hGST P1-1. Cysteine 99-102 glutathione S-transferase pi 1 Homo sapiens 109-118 20631055-5 2010 Ethacrynic acid, a classic GSTP1-1 inhibitor, 4-hydroxy-nonenal, hydrogen peroxide, and diamide all induced reversible GSTP1-1 oligomerization in Jurkat leukemia cells through the formation of disulphide bonds involving Cys47 and/or Cys101, as suggested by reducing and nonreducing SDS-polyacrylamide gel electrophoresis analysis of cysteine to serine mutants. Cysteine 333-341 glutathione S-transferase pi 1 Homo sapiens 119-126 15323418-0 2004 [The effects of cysteines on the function of human glutathion S-transferase pi(GSTp) under cell oxidative stress]. Cysteine 16-25 glutathione S-transferase pi 1 Homo sapiens 79-83 15323418-1 2004 Site-directed mutagenesis was used to generate three cysteine mutants of GSTp, C(47/101), C(14/47/101) and C(14/47/101/169). Cysteine 53-61 glutathione S-transferase pi 1 Homo sapiens 73-77 15323418-3 2004 Data showed that each cysteine mutant inhibited endogenous GST catalyzatic activity and had remarkable dominant negative effect. Cysteine 22-30 glutathione S-transferase pi 1 Homo sapiens 59-62 15323418-6 2004 These results suggest that cysteine residues of GSTp play an important role in protecting cells against oxitative stress. Cysteine 27-35 glutathione S-transferase pi 1 Homo sapiens 48-52 12686490-5 2003 Inhibition studies with the GSTP1-1 mutants C47S, C101S and the double mutant C47S/C101S showed that cysteine 47 is the key residue in the interaction between quercetin and GSTP1-1. Cysteine 101-109 glutathione S-transferase pi 1 Homo sapiens 28-35 12686490-5 2003 Inhibition studies with the GSTP1-1 mutants C47S, C101S and the double mutant C47S/C101S showed that cysteine 47 is the key residue in the interaction between quercetin and GSTP1-1. Cysteine 101-109 glutathione S-transferase pi 1 Homo sapiens 173-180 12686490-8 2003 Nevertheless, the results of the present study indicate that quinone-type oxidation products of quercetin likely act as specific active site inhibitors of GSTP1-1 by binding to cysteine 47. Cysteine 177-185 glutathione S-transferase pi 1 Homo sapiens 155-162 11294649-9 2001 These results demonstrate that hGST P1-1 is inactivated by 4-OHEN through two possible mechanisms: (1) covalent modification of cysteine residues and (2) oxidative damage leading to proteins inactivated by disulfide bond formation. Cysteine 128-136 glutathione S-transferase pi 1 Homo sapiens 31-40 8620581-9 1996 Indications were found that human GST P1-1 may be inhibited via three mechanisms: in addition to the well documentated nucleophilic addition of quinones and oxidation of cysteine residues, a covalent subunit cross-linking was also observed. Cysteine 170-178 glutathione S-transferase pi 1 Homo sapiens 34-42 10353259-4 1999 PGA2 appeared to inhibit GSTP1-1 mainly by binding to the cysteine 47 moiety of the enzyme. Cysteine 58-66 glutathione S-transferase pi 1 Homo sapiens 25-32 9463521-10 1997 When [14C]EA was incubated with the GSTP1-1, modified by the alpha, beta-unsaturated carbonyl compounds, no [14C]EA was incorporated in the enzyme, indicating that in all cases this cysteine residue was one of the major targets. Cysteine 182-190 glutathione S-transferase pi 1 Homo sapiens 36-43 9463521-13 1997 The results indicate that alpha, beta-unsaturated carbonyl derivatives inhibit GSTP1-1 irreversibly mainly by binding to cysteine residues of GSTP1-1, especially Cys-47, This means that some of these compounds (e.g. CUR) might modify GST activity in vivo when GSH concentrations are low by covalent binding to the enzyme. Cysteine 121-129 glutathione S-transferase pi 1 Homo sapiens 79-86 9463521-13 1997 The results indicate that alpha, beta-unsaturated carbonyl derivatives inhibit GSTP1-1 irreversibly mainly by binding to cysteine residues of GSTP1-1, especially Cys-47, This means that some of these compounds (e.g. CUR) might modify GST activity in vivo when GSH concentrations are low by covalent binding to the enzyme. Cysteine 121-129 glutathione S-transferase pi 1 Homo sapiens 142-149 9463521-13 1997 The results indicate that alpha, beta-unsaturated carbonyl derivatives inhibit GSTP1-1 irreversibly mainly by binding to cysteine residues of GSTP1-1, especially Cys-47, This means that some of these compounds (e.g. CUR) might modify GST activity in vivo when GSH concentrations are low by covalent binding to the enzyme. Cysteine 162-165 glutathione S-transferase pi 1 Homo sapiens 79-86 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. Cysteine 157-160 glutathione S-transferase pi 1 Homo sapiens 16-25 8313381-4 1994 From the fact that preincubation of GST P1-1 with 1-chloro-2,4-dinitrobenzene reduced the incorporation of [14C]EA from 0.94 +/- 0.21 (SD) to 0.16 +/- 0.02 mol EA/mol subunit and from automated Edman degradation of the major radioactive peptide isolated after pepsin digestion of the [14C]EA-labeled enzyme, it was concluded that the reaction of EA takes place with cysteine 47 of GST P1-1. Cysteine 366-374 glutathione S-transferase pi 1 Homo sapiens 36-44 1417864-0 1992 Characterization of cysteine residues of glutathione S-transferase P: evidence for steric hindrance of substrate binding by a bulky adduct to cysteine 47. Cysteine 20-28 glutathione S-transferase pi 1 Homo sapiens 41-68 1417864-0 1992 Characterization of cysteine residues of glutathione S-transferase P: evidence for steric hindrance of substrate binding by a bulky adduct to cysteine 47. Cysteine 142-150 glutathione S-transferase pi 1 Homo sapiens 41-68 2310397-4 1990 Similar treatment with N-dimethyl-amino-3,5-dinitrophenyl maleimide, a colored analogue of NEM, followed by trypsin digestion, HPLC and amino acid sequence analysis revealed that one cysteine residue at the 47th position from the N-terminal of the GST P subunit was preferentially modified. Cysteine 183-191 glutathione S-transferase pi 1 Homo sapiens 248-253 2310397-5 1990 Subunits of GST P and GST pi are known to have 4 cysteine residues at the same corresponding positions. Cysteine 49-57 glutathione S-transferase pi 1 Homo sapiens 12-17 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. Cysteine 92-101 glutathione S-transferase pi 1 Homo sapiens 9-17 32176468-7 2020 Human liver microsomes and CYP1A2 supersomes showed the highest bioactivation rate for adduct formation, in which all four cysteines of hGSTP reacted with NAPQI. Cysteine 123-132 glutathione S-transferase pi 1 Homo sapiens 136-141 31457004-9 2019 Seven modified cysteine sites were confirmed, including Cys112 in GSTA1, Cys78 in GSTM1, Cys115 and 174 in GSTM2, as well as Cys15, 48, and 170 in GSTP1. Cysteine 15-23 glutathione S-transferase pi 1 Homo sapiens 147-152