PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32804006-3 2021 In contrast, the selenium-containing enzyme GPX4 is currently recognized as a central repressor of ferroptosis, and its activity depends on glutathione produced from the activation of the cystine-glutamate antiporter SLC7A11. Glutathione 140-151 glutathione peroxidase 4 Homo sapiens 44-48 32578659-2 2020 However, glutathione (GSH)-dependent glutathione peroxidase 4 (GPx4) can reduce PL-PUFA-OOH and antagonize the ferroptosis inducing effect of ROS. Glutathione 9-20 glutathione peroxidase 4 Homo sapiens 37-61 32578659-2 2020 However, glutathione (GSH)-dependent glutathione peroxidase 4 (GPx4) can reduce PL-PUFA-OOH and antagonize the ferroptosis inducing effect of ROS. Glutathione 9-20 glutathione peroxidase 4 Homo sapiens 63-67 32578659-2 2020 However, glutathione (GSH)-dependent glutathione peroxidase 4 (GPx4) can reduce PL-PUFA-OOH and antagonize the ferroptosis inducing effect of ROS. Glutathione 22-25 glutathione peroxidase 4 Homo sapiens 37-61 32578659-2 2020 However, glutathione (GSH)-dependent glutathione peroxidase 4 (GPx4) can reduce PL-PUFA-OOH and antagonize the ferroptosis inducing effect of ROS. Glutathione 22-25 glutathione peroxidase 4 Homo sapiens 63-67 32578659-6 2020 The GSH-free environment inhibited the activity of GPx4 and enhanced the accumulation of PL-PUFA-OOH oxidized by OH. Glutathione 4-7 glutathione peroxidase 4 Homo sapiens 51-55 32577235-8 2020 The rise in membrane PUFA levels enhanced membrane fluidity and lipid peroxidation, causing hypersensitivity to glutathione peroxidase (GPX4) inhibition and ferroptosis. Glutathione 112-123 glutathione peroxidase 4 Homo sapiens 136-140 32372896-1 2020 Ferroptosis is a kind of regulated cell death (RCD) caused by the redox state disorder of intracellular microenvironment controlled by glutathione (GSH) peroxidase 4 (GPX4), which is inhibited by iron chelators and lipophilic antioxidants. Glutathione 135-146 glutathione peroxidase 4 Homo sapiens 167-171 32413317-5 2020 Glutathione peroxidase 4 (GPX4) uses glutathione to protect cells from ferroptosis by eliminating phospholipid peroxides. Glutathione 37-48 glutathione peroxidase 4 Homo sapiens 0-24 32413317-5 2020 Glutathione peroxidase 4 (GPX4) uses glutathione to protect cells from ferroptosis by eliminating phospholipid peroxides. Glutathione 37-48 glutathione peroxidase 4 Homo sapiens 26-30 32372896-1 2020 Ferroptosis is a kind of regulated cell death (RCD) caused by the redox state disorder of intracellular microenvironment controlled by glutathione (GSH) peroxidase 4 (GPX4), which is inhibited by iron chelators and lipophilic antioxidants. Glutathione 148-151 glutathione peroxidase 4 Homo sapiens 167-171 30289974-1 2019 Glutathione peroxidase 4 (GPx4) is the only enzyme capable of reducing toxic lipid hydroperoxides in biological membranes to the corresponding alcohols using glutathione as the electron donor. Glutathione 158-169 glutathione peroxidase 4 Homo sapiens 0-24 31958545-2 2020 Ferroptosis is characterized by iron-dependence and lipid hydroperoxides accumulation, and its primary mechanism involves the suppression of system Xc--GSH (glutathione)-GPX4 (glutathione peroxidase 4) axis. Glutathione 152-155 glutathione peroxidase 4 Homo sapiens 170-174 31958545-2 2020 Ferroptosis is characterized by iron-dependence and lipid hydroperoxides accumulation, and its primary mechanism involves the suppression of system Xc--GSH (glutathione)-GPX4 (glutathione peroxidase 4) axis. Glutathione 152-155 glutathione peroxidase 4 Homo sapiens 176-200 31958545-2 2020 Ferroptosis is characterized by iron-dependence and lipid hydroperoxides accumulation, and its primary mechanism involves the suppression of system Xc--GSH (glutathione)-GPX4 (glutathione peroxidase 4) axis. Glutathione 157-168 glutathione peroxidase 4 Homo sapiens 170-174 31958545-2 2020 Ferroptosis is characterized by iron-dependence and lipid hydroperoxides accumulation, and its primary mechanism involves the suppression of system Xc--GSH (glutathione)-GPX4 (glutathione peroxidase 4) axis. Glutathione 157-168 glutathione peroxidase 4 Homo sapiens 176-200 31373204-6 2019 Meanwhile, transcriptomics analysis suggested the four enzymes related to glutathione metabolism-CD13, GPX4, RRM2B, and OPLAH-as potential targets of cisplatin resistance in nonsmall cell lung cancer. Glutathione 74-85 glutathione peroxidase 4 Homo sapiens 103-107 31581313-0 2020 Inactivation of the glutathione peroxidase GPx4 by the ferroptosis-inducing molecule RSL3 requires the adaptor protein 14-3-3epsilon. Glutathione 20-31 glutathione peroxidase 4 Homo sapiens 43-47 31581313-1 2020 Ras-selective lethal small molecule 3 (RSL3), a drug candidate prototype for cancer chemotherapy, triggers ferroptosis by inactivating the glutathione peroxidase GPx4. Glutathione 139-150 glutathione peroxidase 4 Homo sapiens 162-166 31591388-6 2019 Mechanistically, mutant IDH1 reduces the protein level of the glutathione peroxidase 4 (GPX4), a key enzyme in removing lipid ROS and ferroptosis, and promotes depletion of glutathione. Glutathione 62-73 glutathione peroxidase 4 Homo sapiens 88-92 30289974-1 2019 Glutathione peroxidase 4 (GPx4) is the only enzyme capable of reducing toxic lipid hydroperoxides in biological membranes to the corresponding alcohols using glutathione as the electron donor. Glutathione 158-169 glutathione peroxidase 4 Homo sapiens 26-30 30289974-8 2019 In addition to GPx4, two other negative modulators of ferroptosis (gamma-glutamylcysteine ligase and cysteine/glutamate antiporter), which are critical to maintain physiological levels of glutathione, are diminished in EAE. Glutathione 188-199 glutathione peroxidase 4 Homo sapiens 15-19 28462584-2 2018 It is specifically prevented by glutathione peroxidase 4 (GPx4), the selenoenzyme that reduces PLOOH by glutathione (GSH). Glutathione 32-43 glutathione peroxidase 4 Homo sapiens 58-62 30082768-3 2019 Non-enzymatic and enzymatic lipoxygenase (LOX)-mediated lipid peroxidation of lipid bilayers is efficiently counteracted by the glutathione (GSH)/glutathione peroxidase 4 (GPX4) axis. Glutathione 128-139 glutathione peroxidase 4 Homo sapiens 146-170 30082768-3 2019 Non-enzymatic and enzymatic lipoxygenase (LOX)-mediated lipid peroxidation of lipid bilayers is efficiently counteracted by the glutathione (GSH)/glutathione peroxidase 4 (GPX4) axis. Glutathione 128-139 glutathione peroxidase 4 Homo sapiens 172-176 30082768-3 2019 Non-enzymatic and enzymatic lipoxygenase (LOX)-mediated lipid peroxidation of lipid bilayers is efficiently counteracted by the glutathione (GSH)/glutathione peroxidase 4 (GPX4) axis. Glutathione 141-144 glutathione peroxidase 4 Homo sapiens 146-170 30082768-3 2019 Non-enzymatic and enzymatic lipoxygenase (LOX)-mediated lipid peroxidation of lipid bilayers is efficiently counteracted by the glutathione (GSH)/glutathione peroxidase 4 (GPX4) axis. Glutathione 141-144 glutathione peroxidase 4 Homo sapiens 172-176 30495919-3 2018 Herein, we report a ferroptosis-inducing agent based on arginine-rich manganese silicate nanobubbles (AMSNs) that possess highly efficient glutathione (GSH) depletion ability and thereby induce ferroptosis by the inactivation of glutathione-dependent peroxidases 4 (GPX4). Glutathione 139-150 glutathione peroxidase 4 Homo sapiens 229-264 30495919-3 2018 Herein, we report a ferroptosis-inducing agent based on arginine-rich manganese silicate nanobubbles (AMSNs) that possess highly efficient glutathione (GSH) depletion ability and thereby induce ferroptosis by the inactivation of glutathione-dependent peroxidases 4 (GPX4). Glutathione 139-150 glutathione peroxidase 4 Homo sapiens 266-270 28462584-2 2018 It is specifically prevented by glutathione peroxidase 4 (GPx4), the selenoenzyme that reduces PLOOH by glutathione (GSH). Glutathione 117-120 glutathione peroxidase 4 Homo sapiens 32-56 28462584-2 2018 It is specifically prevented by glutathione peroxidase 4 (GPx4), the selenoenzyme that reduces PLOOH by glutathione (GSH). Glutathione 117-120 glutathione peroxidase 4 Homo sapiens 58-62 28595877-4 2017 We show that the glutathione (GSH) peroxidase 4 (GPX4) inhibitor RSL3 triggers lipid peroxidation, production of reactive oxygen species (ROS) and cell death in ALL cells. Glutathione 17-28 glutathione peroxidase 4 Homo sapiens 49-53 29802123-2 2018 Vitamin E and coenzyme Q10 react with peroxyl radicals to yield peroxides, and then these oxidized lipid species can be detoxified by glutathione and glutathione peroxidase 4 (GPX4) and other components of the cellular antioxidant defense network. Glutathione 134-145 glutathione peroxidase 4 Homo sapiens 176-180 23201771-4 2013 MAJOR CONCLUSIONS: GPxs are involved in balancing the H2O2 homeostasis in signalling cascades, e.g. in the insulin signalling pathway by GPx1; GPx2 plays a dual role in carcinogenesis depending on the mode of initiation and cancer stage; GPx3 is membrane associated possibly explaining a peroxidatic function despite low plasma concentrations of GSH; GPx4 has novel roles in the regulation of apoptosis and, together with GPx5, in male fertility. Glutathione 346-349 glutathione peroxidase 4 Homo sapiens 351-355 25315394-8 2014 SUCLA2 and PDHB are involved in the tricarboxylic acid cycle, whereas PHGPx and PRDX5 are involved in glutathione metabolism. Glutathione 102-113 glutathione peroxidase 4 Homo sapiens 70-75 19376195-8 2009 Beyond, the degenerate GSH specificity of GPx-4 allows selenylation and oxidation to disulfides of protein thiols. Glutathione 23-26 glutathione peroxidase 4 Homo sapiens 42-47 22446825-0 2012 Characterization of phospholipid hydroperoxide glutathione metabolizing peroxidase (gpx4) isoforms in Coho salmon olfactory and liver tissues and their modulation by cadmium. Glutathione 47-58 glutathione peroxidase 4 Homo sapiens 84-88 23268326-3 2012 We recently reported changes in expression of the selenoprotein, phospholipid hydroperoxide glutathione peroxidase GPX4 and its co-localization with neuromelanin in PD brain. Glutathione 92-103 glutathione peroxidase 4 Homo sapiens 115-119 19808099-4 2010 Recombinant Bi-PHGPx, expressed as a 19 kDa protein in baculovirus-infected insect cells, exhibited enzymatic activity against PLPC-OOH and H(2)O(2) using glutathione as an electron donor. Glutathione 155-166 glutathione peroxidase 4 Homo sapiens 15-20 15474074-10 2004 CONCLUSION(S): Intracellular sperm GSH system components GPX-4 and GSH are altered in infertile men, and these alterations seem to be linked to sperm morphology. Glutathione 35-38 glutathione peroxidase 4 Homo sapiens 57-62 17680760-2 2007 This review considers the peculiarity of functions of mitochondrial GSH and enzymes of its metabolism, especially glutathione peroxidase 4, glutaredoxin 2, and kappa-glutathione transferase. Glutathione 68-71 glutathione peroxidase 4 Homo sapiens 114-138 19356030-8 2007 A reserve of glutathione, together with GPx expression, is necessary to eliminate free radicals using GSH or GPx-4 like structural protein and seems to be essential for a good post thaw recovery. Glutathione 13-24 glutathione peroxidase 4 Homo sapiens 109-114 16409129-1 2006 Phospholipid glutathione peroxidase (PhGPx) reduces lipid hydroperoxides generated in biomembranes and also uses a wide range of reducing cofactors in addition to glutathione. Glutathione 13-24 glutathione peroxidase 4 Homo sapiens 37-42 15292110-5 2004 These effects are counteracted by various oxidative defense enzymes and anti-oxidants such as glutathione peroxidase isoforms GPx1 and GPx4, glutathione reductase (GR), and cellular glutathione (reduced) (GSH). Glutathione 94-105 glutathione peroxidase 4 Homo sapiens 135-139 10560610-4 1999 Reduction of 12(S)-hydroperoxyeicosatetraenoic acid to 12(S)-hydroxyeicosatetraenoic acid by PHGPx was observed in the presence of glutathione (GSH), and the inhibitory effect of PHGPx on 12-lipoxygenase-catalyzed arachidonate metabolism was reversed by the addition of exogenous lipid hydroperoxide. Glutathione 131-142 glutathione peroxidase 4 Homo sapiens 93-98 14576462-6 2003 Depletion of cellular glutathione in cells by diethyl maleate or by dibuthionine-sulfoximine results in an increase in enzyme activities of 12(S)-lipoxygenase and cyclooxygenase, suggesting that glutathione-depleting agents abolish the enzyme activity of PHGPx in cells. Glutathione 22-33 glutathione peroxidase 4 Homo sapiens 255-260 14576462-6 2003 Depletion of cellular glutathione in cells by diethyl maleate or by dibuthionine-sulfoximine results in an increase in enzyme activities of 12(S)-lipoxygenase and cyclooxygenase, suggesting that glutathione-depleting agents abolish the enzyme activity of PHGPx in cells. Glutathione 195-206 glutathione peroxidase 4 Homo sapiens 255-260 11981452-8 2002 Phospholipid hydroperoxide glutathione peroxidase (PHGPX) reduced PLG-OOH to its hydroxide in the presence of glutathione while the conventional cytosolic glutathione peroxidase did not. Glutathione 27-38 glutathione peroxidase 4 Homo sapiens 51-56 10882192-4 2000 In terms of the inhibitory effect on 12-lipoxygenase, PHGPx was more sensitive to GSH concentrations than GPx1. Glutathione 82-85 glutathione peroxidase 4 Homo sapiens 54-59 10560610-4 1999 Reduction of 12(S)-hydroperoxyeicosatetraenoic acid to 12(S)-hydroxyeicosatetraenoic acid by PHGPx was observed in the presence of glutathione (GSH), and the inhibitory effect of PHGPx on 12-lipoxygenase-catalyzed arachidonate metabolism was reversed by the addition of exogenous lipid hydroperoxide. Glutathione 131-142 glutathione peroxidase 4 Homo sapiens 179-184 10560610-4 1999 Reduction of 12(S)-hydroperoxyeicosatetraenoic acid to 12(S)-hydroxyeicosatetraenoic acid by PHGPx was observed in the presence of glutathione (GSH), and the inhibitory effect of PHGPx on 12-lipoxygenase-catalyzed arachidonate metabolism was reversed by the addition of exogenous lipid hydroperoxide. Glutathione 144-147 glutathione peroxidase 4 Homo sapiens 93-98 10560610-4 1999 Reduction of 12(S)-hydroperoxyeicosatetraenoic acid to 12(S)-hydroxyeicosatetraenoic acid by PHGPx was observed in the presence of glutathione (GSH), and the inhibitory effect of PHGPx on 12-lipoxygenase-catalyzed arachidonate metabolism was reversed by the addition of exogenous lipid hydroperoxide. Glutathione 144-147 glutathione peroxidase 4 Homo sapiens 179-184 9315326-6 1997 On the other hand, structural and kinetic data indicate that also the specificity of PHGPx for the donor substrate is not restricted to GSH and the recent observation the PHGPx binds to specific mitochondrial proteins, from which it is released by ionic strength and thiols, suggests a possible fole of this selenoenzyme in catalyzing the specific oxidation of protein thiols, thus modulating the activity of cellular regulatory elements. Glutathione 136-139 glutathione peroxidase 4 Homo sapiens 85-90 7851631-3 1994 PHGPx was isolated from human liver using ammonium sulphate fractionation, affinity chromatography on bromosulphophthalein-glutathione-agarose, gel filtration on Sephadex G-50, anion exchange chromatography on Mono Q resin and high resolution gel filtration on Superdex 75. Glutathione 123-134 glutathione peroxidase 4 Homo sapiens 0-5 8986633-6 1996 Furthermore, in agreement with kinetic and structural information, PHGPx-chromatin binding could suggest an hypothetical thiol oxidase activity toward specific thiol bearing proteins which could substitute for GSH as alternative donor substrates. Glutathione 210-213 glutathione peroxidase 4 Homo sapiens 67-72 8679629-4 1996 Apparent first-order rate constants for GSH/PHGPX-induced peroxide loss (or diol accumulation) in Triton X-100 micelles, unilamellar liposomes, or erythrocyte ghost membranes increased in the following order: 5 alpha-OOH < 6 alpha-OOH approximately equal to 7 alpha,7 beta-OOH < 6beta-OOH. Glutathione 40-43 glutathione peroxidase 4 Homo sapiens 44-49 34778741-6 2021 Systematic in vitro and in vivo experiments have demonstrated that synchronous consumption of GSH and increased reactive oxygen species (ROS) facilitated reduced expression of glutathione peroxidase 4 (GPX4), which further contributed to disruption of intracellular redox homeostasis and ultimately boosted ferroptosis. Glutathione 94-97 glutathione peroxidase 4 Homo sapiens 202-206 8135530-3 1994 Incubation of HDLox or LDLox in the presence of PHGPx/GSH or Ebselen/GSH resulted in rapid degradation of both classes of lipid hydroperoxides, with equimolar amounts of Ch18:2-OH formed from Ch18:2-OOH. Glutathione 54-57 glutathione peroxidase 4 Homo sapiens 48-53 8135530-4 1994 No pronounced differences were observed between PCOOH and Ch18:2-OOH in terms of substrate specificity, whereas HDLox-associated PCOOH and Ch18:2-OOH appeared to be slightly better substrates for PHGPx/GSH as compared to those in LDLox. Glutathione 202-205 glutathione peroxidase 4 Homo sapiens 196-201 8135530-6 1994 These in vitro findings indicate that the enzymatic PHGPx/GSH and the nonenzymatic Ebselen/GSH systems can efficiently reduce hydroperoxides of phospholipids and cholesterylesters associated with intact lipoproteins. Glutathione 58-61 glutathione peroxidase 4 Homo sapiens 52-57 34592546-6 2022 Alternatively, GSH depletion not only deactivates glutathione peroxidase 4 (GPX4) to trigger ferroptosis, but also leads to oxidative stress amplification. Glutathione 15-18 glutathione peroxidase 4 Homo sapiens 50-74 34592546-6 2022 Alternatively, GSH depletion not only deactivates glutathione peroxidase 4 (GPX4) to trigger ferroptosis, but also leads to oxidative stress amplification. Glutathione 15-18 glutathione peroxidase 4 Homo sapiens 76-80 34936351-6 2022 Furthermore, the same strategy was successfully applied to cell-type-specific gene editing through the delivery of a Cas9/sgRNA complex to knockdown the endogenous expression of glutathione peroxidase (GPX4), a key protein in ferroptosis. Glutathione 178-189 glutathione peroxidase 4 Homo sapiens 202-206 34905922-7 2022 Both in vitro and in vivo results suggest that, in addition to the cytotoxicity imposed by the raised ROS level due to the presence of Mn(II) species, the depletion of endogenous GSH leads indirectly to the inhibition of glutathione peroxidase 4 (GPX4), consequently raising the lipid peroxidation (LPO) level to cause ferroptosis. Glutathione 179-182 glutathione peroxidase 4 Homo sapiens 221-245 34905922-7 2022 Both in vitro and in vivo results suggest that, in addition to the cytotoxicity imposed by the raised ROS level due to the presence of Mn(II) species, the depletion of endogenous GSH leads indirectly to the inhibition of glutathione peroxidase 4 (GPX4), consequently raising the lipid peroxidation (LPO) level to cause ferroptosis. Glutathione 179-182 glutathione peroxidase 4 Homo sapiens 247-251 34775124-7 2022 The GSH consumption by disulfide, CA and Fe3+, downregulates GPX4 and generates OH, which accelerate lipid peroxides (LPO) accumulation and consequently enhances ferroptosis. Glutathione 4-7 glutathione peroxidase 4 Homo sapiens 61-65 34710950-5 2022 The nanoassemblies could be activated by the elevated ROS levels in tumor intracellular environment and readily release the incorporated therapeutic contents, afterwards DEM could directly conjugate to GSH to disrupt the glutathione peroxidase 4 (GPX4)-mediated antioxidant defense while siMCT4 could block the MCT4-mediated efflux of lactic acid and acidify the intracellular milieu, both of which could improve the ferrocene-catalyzed lipid peroxidation and induce pronounced ferroptotic damage. Glutathione 202-205 glutathione peroxidase 4 Homo sapiens 221-245 34710950-5 2022 The nanoassemblies could be activated by the elevated ROS levels in tumor intracellular environment and readily release the incorporated therapeutic contents, afterwards DEM could directly conjugate to GSH to disrupt the glutathione peroxidase 4 (GPX4)-mediated antioxidant defense while siMCT4 could block the MCT4-mediated efflux of lactic acid and acidify the intracellular milieu, both of which could improve the ferrocene-catalyzed lipid peroxidation and induce pronounced ferroptotic damage. Glutathione 202-205 glutathione peroxidase 4 Homo sapiens 247-251 34623415-3 2021 The major cellular protector against ferroptosis is glutathione peroxidase 4 (GPX4), a membrane-associated selenoenzyme that reduces deleterious phospholipid hydroperoxides to their corresponding benign phospholipid alcohols in a glutathione-dependent manner. Glutathione 230-241 glutathione peroxidase 4 Homo sapiens 52-76 34623415-3 2021 The major cellular protector against ferroptosis is glutathione peroxidase 4 (GPX4), a membrane-associated selenoenzyme that reduces deleterious phospholipid hydroperoxides to their corresponding benign phospholipid alcohols in a glutathione-dependent manner. Glutathione 230-241 glutathione peroxidase 4 Homo sapiens 78-82 34934357-4 2021 Increasing reports imply statins can modulate ferroptosis through disrupting reactive oxygen species (ROS) and glutathione peroxidase enzyme (GPX4) levels. Glutathione 111-122 glutathione peroxidase 4 Homo sapiens 142-146 34948133-6 2021 The dominating mechanism was due to a regulation of the classic ferroptosis-repressed GSH-dependent GPX4 signaling pathway instead of other fractional regulating signal axes that regulated ferroptosis via impacting on the ROS, cellular iron levels, etc. Glutathione 86-89 glutathione peroxidase 4 Homo sapiens 100-104 34917232-5 2021 However, the glutathione (GSH)/glutathione peroxidase 4 (GPX4) pathways of the two CML cell lines were both blocked after cysteine depletion. Glutathione 13-24 glutathione peroxidase 4 Homo sapiens 31-55 34917232-5 2021 However, the glutathione (GSH)/glutathione peroxidase 4 (GPX4) pathways of the two CML cell lines were both blocked after cysteine depletion. Glutathione 13-24 glutathione peroxidase 4 Homo sapiens 57-61 34917232-5 2021 However, the glutathione (GSH)/glutathione peroxidase 4 (GPX4) pathways of the two CML cell lines were both blocked after cysteine depletion. Glutathione 26-29 glutathione peroxidase 4 Homo sapiens 31-55 34778741-6 2021 Systematic in vitro and in vivo experiments have demonstrated that synchronous consumption of GSH and increased reactive oxygen species (ROS) facilitated reduced expression of glutathione peroxidase 4 (GPX4), which further contributed to disruption of intracellular redox homeostasis and ultimately boosted ferroptosis. Glutathione 94-97 glutathione peroxidase 4 Homo sapiens 176-200 34727409-6 2022 Here we identified miR-15a-3p positively regulates ferroptosis via directly targeting glutathione peroxidase glutathione peroxidase 4 (GPX4) in CRC. Glutathione 86-97 glutathione peroxidase 4 Homo sapiens 135-139 34535975-7 2021 Meanwhile, SRF blocks glutathione synthesis to downregulate glutathione peroxidase 4 (GPX4) which can scavenge LPO as a different pathway from ferritinophagy to promote ferroptosis in tumor cells. Glutathione 22-33 glutathione peroxidase 4 Homo sapiens 60-84 34535975-7 2021 Meanwhile, SRF blocks glutathione synthesis to downregulate glutathione peroxidase 4 (GPX4) which can scavenge LPO as a different pathway from ferritinophagy to promote ferroptosis in tumor cells. Glutathione 22-33 glutathione peroxidase 4 Homo sapiens 86-90 34988167-9 2021 Results: FeSO4 of 100 microM significantly promoted the occurrence of cell ferroptosis, increased the levels of MDA and ROS, and decreased the ratio of glutathione (GSH) or glutathione disulfide (GSSG) and the expression level of glutathione peroxidase (GPX4). Glutathione 230-241 glutathione peroxidase 4 Homo sapiens 254-258 34729312-2 2021 Several ferroptosis therapy strategies based on nanotechnology have been reported by either increasing intracellular iron levels or by inhibition of glutathione (GSH)-dependent lipid hydroperoxidase glutathione peroxidase 4 (GPX4). Glutathione 149-160 glutathione peroxidase 4 Homo sapiens 225-229 34729312-2 2021 Several ferroptosis therapy strategies based on nanotechnology have been reported by either increasing intracellular iron levels or by inhibition of glutathione (GSH)-dependent lipid hydroperoxidase glutathione peroxidase 4 (GPX4). Glutathione 162-165 glutathione peroxidase 4 Homo sapiens 225-229 34729312-4 2021 Herein, novel tumor microenvironments (TME)-activated metal-organic frameworks involving Fe & Cu ions bridged by disulfide bonds with PEGylation (FCSP MOFs) were developed, which would be degraded specifically under the redox TME, simultaneously achieving GSH-depletion induced GPX4 inactivation and releasing Fe ions to produce ROS via Fenton reaction, therefore causing ferroptosis. Glutathione 256-259 glutathione peroxidase 4 Homo sapiens 278-282 34829548-4 2021 As a specific inducer of ferroptosis, erastin inhibits cystine-glutamate antiporter system Xc-, blocking transportation into the cytoplasm of cystine, a precursor of glutathione (GSH) in exchange with glutamate and the consequent malfunction of GPX4. Glutathione 166-177 glutathione peroxidase 4 Homo sapiens 245-249 34986533-3 2021 Recent studies have shown that natural medicinal ingredients can induce ferroptosis in tumor cells through glutathione (GSH)/glutathione peroxidase 4 (GPx4) pathway, iron metabolism, lipid metabolism or other mechanisms. Glutathione 107-118 glutathione peroxidase 4 Homo sapiens 125-149 34986533-3 2021 Recent studies have shown that natural medicinal ingredients can induce ferroptosis in tumor cells through glutathione (GSH)/glutathione peroxidase 4 (GPx4) pathway, iron metabolism, lipid metabolism or other mechanisms. Glutathione 107-118 glutathione peroxidase 4 Homo sapiens 151-155 34986533-3 2021 Recent studies have shown that natural medicinal ingredients can induce ferroptosis in tumor cells through glutathione (GSH)/glutathione peroxidase 4 (GPx4) pathway, iron metabolism, lipid metabolism or other mechanisms. Glutathione 120-123 glutathione peroxidase 4 Homo sapiens 125-149 34986533-3 2021 Recent studies have shown that natural medicinal ingredients can induce ferroptosis in tumor cells through glutathione (GSH)/glutathione peroxidase 4 (GPx4) pathway, iron metabolism, lipid metabolism or other mechanisms. Glutathione 120-123 glutathione peroxidase 4 Homo sapiens 151-155 34448349-5 2021 Furthermore, the expression of glutathione peroxidase 4 protein (GPX4) is down-regulated by consumption intracellular GSH content via converting GSH into glutathione oxidized (GSSG), which is named the classical mode. Glutathione 118-121 glutathione peroxidase 4 Homo sapiens 31-55 34448349-5 2021 Furthermore, the expression of glutathione peroxidase 4 protein (GPX4) is down-regulated by consumption intracellular GSH content via converting GSH into glutathione oxidized (GSSG), which is named the classical mode. Glutathione 118-121 glutathione peroxidase 4 Homo sapiens 65-69 34448349-5 2021 Furthermore, the expression of glutathione peroxidase 4 protein (GPX4) is down-regulated by consumption intracellular GSH content via converting GSH into glutathione oxidized (GSSG), which is named the classical mode. Glutathione 145-148 glutathione peroxidase 4 Homo sapiens 31-55 34448349-5 2021 Furthermore, the expression of glutathione peroxidase 4 protein (GPX4) is down-regulated by consumption intracellular GSH content via converting GSH into glutathione oxidized (GSSG), which is named the classical mode. Glutathione 145-148 glutathione peroxidase 4 Homo sapiens 65-69 34448349-5 2021 Furthermore, the expression of glutathione peroxidase 4 protein (GPX4) is down-regulated by consumption intracellular GSH content via converting GSH into glutathione oxidized (GSSG), which is named the classical mode. Glutathione 154-165 glutathione peroxidase 4 Homo sapiens 31-55 34448349-5 2021 Furthermore, the expression of glutathione peroxidase 4 protein (GPX4) is down-regulated by consumption intracellular GSH content via converting GSH into glutathione oxidized (GSSG), which is named the classical mode. Glutathione 154-165 glutathione peroxidase 4 Homo sapiens 65-69 35605092-4 2022 Moreover, it is shown that GPX4 elicits diverse biological functions by suppressing phospholipid hydroperoxide at the expense of decreased glutathione (GSH), including loss of neurons, autophagy, cell repair, inflammation, ferroptosis, apoptosis, and oxidative stress. Glutathione 139-150 glutathione peroxidase 4 Homo sapiens 27-31 34586745-0 2021 Glutathione peroxidase 4-dependent glutathione high-consumption drives acquired platinum chemoresistance in lung cancer-derived brain metastasis. Glutathione 35-46 glutathione peroxidase 4 Homo sapiens 0-24 34586745-4 2021 High consumption of glutathione (GSH) and two associated upregulated proteins (GPX4 and GSTM1) in BM were identified by integrated metabolomics and proteomics in cell lines and verified by clinical serum sample. Glutathione 20-31 glutathione peroxidase 4 Homo sapiens 79-83 34586745-4 2021 High consumption of glutathione (GSH) and two associated upregulated proteins (GPX4 and GSTM1) in BM were identified by integrated metabolomics and proteomics in cell lines and verified by clinical serum sample. Glutathione 33-36 glutathione peroxidase 4 Homo sapiens 79-83 34586745-9 2021 Radically altered profiles of BM metabolism and protein expression compared with primary lung cancer cells were described and GPX4 and GSTM1 were identified as being responsible for the high consumption of GSH, leading to decreased chemosensitivity by negatively regulating ferroptosis. Glutathione 206-209 glutathione peroxidase 4 Homo sapiens 126-130 34586745-11 2021 CONCLUSIONS: Collectively, our findings demonstrated that Wnt/NR2F2/GPX4 promoted acquired chemoresistance by suppressing ferroptosis with high consumption of GSH. Glutathione 159-162 glutathione peroxidase 4 Homo sapiens 68-72 34102574-3 2021 Reduced glutathione (GSH) is a central player in ferroptosis that is required for glutathione peroxidase 4 to eliminate oxidized phospholipids. Glutathione 8-19 glutathione peroxidase 4 Homo sapiens 82-106 34102574-3 2021 Reduced glutathione (GSH) is a central player in ferroptosis that is required for glutathione peroxidase 4 to eliminate oxidized phospholipids. Glutathione 21-24 glutathione peroxidase 4 Homo sapiens 82-106 34350694-3 2021 In response to the reducing microenvironment of tumor tissue, the S S bond can be disintegrated by intracellular glutathione to block the synthesis of lipid repair enzyme-glutathione peroxidase 4 for ferroptosis therapy. Glutathione 113-124 glutathione peroxidase 4 Homo sapiens 171-195 34360557-1 2021 Among the eight human glutathione peroxidase isoforms, glutathione peroxidase 4 (GPX4) is the only enzyme capable of reducing complex lipid peroxides to the corresponding alcohols. Glutathione 22-33 glutathione peroxidase 4 Homo sapiens 55-79 34360557-1 2021 Among the eight human glutathione peroxidase isoforms, glutathione peroxidase 4 (GPX4) is the only enzyme capable of reducing complex lipid peroxides to the corresponding alcohols. Glutathione 22-33 glutathione peroxidase 4 Homo sapiens 81-85 34238297-6 2021 Meanwhile, besides PDT effects, it was found that BCFe@SRF mediated treatment upon laser irradiation in hypoxic environment not only could accelerate lipid peroxidation (LPO) generation but also could deplete intracellular glutathione (GSH) and decrease glutathione peroxidase (GPX4) expression, which was believed as three symbolic events during ferroptosis. Glutathione 223-234 glutathione peroxidase 4 Homo sapiens 278-282 34238297-6 2021 Meanwhile, besides PDT effects, it was found that BCFe@SRF mediated treatment upon laser irradiation in hypoxic environment not only could accelerate lipid peroxidation (LPO) generation but also could deplete intracellular glutathione (GSH) and decrease glutathione peroxidase (GPX4) expression, which was believed as three symbolic events during ferroptosis. Glutathione 254-265 glutathione peroxidase 4 Homo sapiens 278-282 34169392-6 2021 From the perspective of ROS clearance, Vitamin E enhanced GPX4 function to consume L-glutathione and eliminated excess intracellular ROS. Glutathione 83-96 glutathione peroxidase 4 Homo sapiens 58-62 34127539-6 2021 GPX4, an antioxidant protein that uses reduced glutathione as a cofactor, directly catalyzes the reduction of hydrogen peroxide, organic hydroperoxides, and lipid peroxides. Glutathione 47-58 glutathione peroxidase 4 Homo sapiens 0-4 34167028-2 2021 Though GSH/Gpx4 is the predominant system detoxifying phospholipid hydroperoxides (PLOOH) in mammalian cells, recently Gpx4-independent regulators of ferroptosis like ferroptosis suppressor protein 1 (FSP1) in resistant cancer lines and iNOS/NO in M1 macrophages have been discovered. Glutathione 7-10 glutathione peroxidase 4 Homo sapiens 11-15 34167028-5 2021 In response, the host stimulates the iNOS/NO -driven anti-ferroptotic mechanism to stymie lipid peroxidation and protect GPx4/GSH-deficient cells. Glutathione 126-129 glutathione peroxidase 4 Homo sapiens 121-125 34092035-5 2021 In contrast, system xc--glutathione-GPX4 axis plays a central role in limiting lipid peroxidation, although other antioxidants (such as coenzyme Q10 and tetrahydrobiopterin) can also inhibit ferroptosis. Glutathione 24-35 glutathione peroxidase 4 Homo sapiens 36-40 35605092-4 2022 Moreover, it is shown that GPX4 elicits diverse biological functions by suppressing phospholipid hydroperoxide at the expense of decreased glutathione (GSH), including loss of neurons, autophagy, cell repair, inflammation, ferroptosis, apoptosis, and oxidative stress. Glutathione 152-155 glutathione peroxidase 4 Homo sapiens 27-31 35585057-0 2022 Involvement of FSP1-CoQ10-NADH and GSH-GPx-4 pathways in retinal pigment epithelium ferroptosis. Glutathione 35-38 glutathione peroxidase 4 Homo sapiens 39-44 35581292-10 2022 APOC1 also induced ferroptosis resistance by increasing cystathionine beta-synthase (CBS) expression, which promoted trans-sulfuration and increased GSH synthesis, ultimately leading to an increase in glutathione peroxidase-4 (GPX4). Glutathione 149-152 glutathione peroxidase 4 Homo sapiens 201-225 35489546-6 2022 More importantly, ferroptosis was participated in the process of PBmB-induced therapy via glutathione (GSH)-depletion mediated GPX4 inactivation, together with Mn ions induced chemodynamic therapy (Fenton-like reaction), which made additional contributions to increase the therapeutic efficacy. Glutathione 90-101 glutathione peroxidase 4 Homo sapiens 127-131 35489546-6 2022 More importantly, ferroptosis was participated in the process of PBmB-induced therapy via glutathione (GSH)-depletion mediated GPX4 inactivation, together with Mn ions induced chemodynamic therapy (Fenton-like reaction), which made additional contributions to increase the therapeutic efficacy. Glutathione 103-106 glutathione peroxidase 4 Homo sapiens 127-131 35585057-5 2022 Here, we report that both FSP1-CoQ10-NADH and GSH-GPx-4 pathways inhibit retinal ferroptosis in sodium iodate (SIO)-induced retinal degeneration pathologies in human primary RPE cells (HRPEpiC), ARPE-19 cell line, and mice. Glutathione 46-49 glutathione peroxidase 4 Homo sapiens 50-55 35107212-4 2022 NRF2 and BACH1 inhibit and promote ferroptosis, respectively, by activating or suppressing the expression of genes in the major regulatory pathways of ferroptosis: intracellular labile iron metabolism, the GSH (glutathione) -GPX4 (glutathione peroxidase 4) pathway, and the FSP1 (ferroptosis suppressor protein 1)-CoQ (coenzyme Q) pathway. Glutathione 206-209 glutathione peroxidase 4 Homo sapiens 225-229 35337799-9 2022 In this study, solute carrier family 7 member 11 (SLC7A11) and GPX4 are involved in GSH synthesis decreased upon dissociation as a target of Nrf2. Glutathione 84-87 glutathione peroxidase 4 Homo sapiens 63-67 35306372-6 2022 Our results point to oxidation of GSH through the redox relay initiated by glutathione peroxidase 4, directly by ISOPOOH or indirectly by ISOPOOH-generated lipid hydroperoxides. Glutathione 34-37 glutathione peroxidase 4 Homo sapiens 75-99 35434035-3 2022 Over the past few years, extensive research has revealed that the essence of ferroptosis is iron-dependent accumulation of lipid hydroperoxides induced by oxidative stress, and the System Xc-glutathione (GSH)-glutathione peroxidase 4 (GPX4) pathway is the main ferroptosis prevention system. Glutathione 191-202 glutathione peroxidase 4 Homo sapiens 209-233 35434035-3 2022 Over the past few years, extensive research has revealed that the essence of ferroptosis is iron-dependent accumulation of lipid hydroperoxides induced by oxidative stress, and the System Xc-glutathione (GSH)-glutathione peroxidase 4 (GPX4) pathway is the main ferroptosis prevention system. Glutathione 191-202 glutathione peroxidase 4 Homo sapiens 235-239 35434035-3 2022 Over the past few years, extensive research has revealed that the essence of ferroptosis is iron-dependent accumulation of lipid hydroperoxides induced by oxidative stress, and the System Xc-glutathione (GSH)-glutathione peroxidase 4 (GPX4) pathway is the main ferroptosis prevention system. Glutathione 204-207 glutathione peroxidase 4 Homo sapiens 209-233 35434035-3 2022 Over the past few years, extensive research has revealed that the essence of ferroptosis is iron-dependent accumulation of lipid hydroperoxides induced by oxidative stress, and the System Xc-glutathione (GSH)-glutathione peroxidase 4 (GPX4) pathway is the main ferroptosis prevention system. Glutathione 204-207 glutathione peroxidase 4 Homo sapiens 235-239 35148992-2 2022 Lipid peroxidation is normally suppressed by glutathione peroxidase 4, which requires reduced glutathione. Glutathione 94-105 glutathione peroxidase 4 Homo sapiens 45-69 35128925-1 2022 Glutathione peroxidase 4 (GPX4) is an intracellular enzyme that oxidizes glutathione while reducing lipid peroxides and is a promising target for cancer therapy. Glutathione 73-84 glutathione peroxidase 4 Homo sapiens 0-24 35128925-1 2022 Glutathione peroxidase 4 (GPX4) is an intracellular enzyme that oxidizes glutathione while reducing lipid peroxides and is a promising target for cancer therapy. Glutathione 73-84 glutathione peroxidase 4 Homo sapiens 26-30 35275790-3 2022 We found that stages of EBV transformation generate lipid reactive oxygen species (ROS) byproducts to varying degrees, and that a Burkitt-like phase of B cell outgrowth requires lipid ROS detoxification by glutathione peroxidase 4 and its cofactor glutathione. Glutathione 248-259 glutathione peroxidase 4 Homo sapiens 206-230 35107212-4 2022 NRF2 and BACH1 inhibit and promote ferroptosis, respectively, by activating or suppressing the expression of genes in the major regulatory pathways of ferroptosis: intracellular labile iron metabolism, the GSH (glutathione) -GPX4 (glutathione peroxidase 4) pathway, and the FSP1 (ferroptosis suppressor protein 1)-CoQ (coenzyme Q) pathway. Glutathione 206-209 glutathione peroxidase 4 Homo sapiens 231-255 35107212-4 2022 NRF2 and BACH1 inhibit and promote ferroptosis, respectively, by activating or suppressing the expression of genes in the major regulatory pathways of ferroptosis: intracellular labile iron metabolism, the GSH (glutathione) -GPX4 (glutathione peroxidase 4) pathway, and the FSP1 (ferroptosis suppressor protein 1)-CoQ (coenzyme Q) pathway. Glutathione 211-222 glutathione peroxidase 4 Homo sapiens 225-229 35107212-4 2022 NRF2 and BACH1 inhibit and promote ferroptosis, respectively, by activating or suppressing the expression of genes in the major regulatory pathways of ferroptosis: intracellular labile iron metabolism, the GSH (glutathione) -GPX4 (glutathione peroxidase 4) pathway, and the FSP1 (ferroptosis suppressor protein 1)-CoQ (coenzyme Q) pathway. Glutathione 211-222 glutathione peroxidase 4 Homo sapiens 231-255 35062064-0 2022 Association of genetic variants in the GPX1 and GPX4 genes with the activities of glutathione-dependent enzymes, their interaction with smoking and the risk of acute pancreatitis. Glutathione 82-93 glutathione peroxidase 4 Homo sapiens 48-52 35104766-12 2022 Additionally, ponicidin could covalently bind to GSH in SW1990 cells to form a conjugate Pon-GSH, which further reduced the content of free GSH and GPX4 activity in cells. Glutathione 49-52 glutathione peroxidase 4 Homo sapiens 148-152 35102454-14 2022 Conversely, the GSH/GPX4 pathway, as well as CoQ10, Fer-1, and Lip-1, inhibits lipid peroxidation and, thus, alleviates ferroptosis. Glutathione 16-19 glutathione peroxidase 4 Homo sapiens 20-24 35050181-3 2022 The regulation of ferroptosis includes different molecular mechanisms and multiple cellular metabolic pathways, including glutathione/glutathione peroxidase 4(GPX4) signaling pathways, which are involved in the amino acid metabolism and the activation of GPX4; iron metabolic signaling pathways, which are involved in the regulation of iron import/export and the storage/release of intracellular iron through iron-regulatory proteins (IRPs), and lipid metabolic signaling pathways, which are involved in the metabolism of unsaturated fatty acids in cell membranes. Glutathione 122-133 glutathione peroxidase 4 Homo sapiens 134-158 35050181-3 2022 The regulation of ferroptosis includes different molecular mechanisms and multiple cellular metabolic pathways, including glutathione/glutathione peroxidase 4(GPX4) signaling pathways, which are involved in the amino acid metabolism and the activation of GPX4; iron metabolic signaling pathways, which are involved in the regulation of iron import/export and the storage/release of intracellular iron through iron-regulatory proteins (IRPs), and lipid metabolic signaling pathways, which are involved in the metabolism of unsaturated fatty acids in cell membranes. Glutathione 122-133 glutathione peroxidase 4 Homo sapiens 159-163 35050181-3 2022 The regulation of ferroptosis includes different molecular mechanisms and multiple cellular metabolic pathways, including glutathione/glutathione peroxidase 4(GPX4) signaling pathways, which are involved in the amino acid metabolism and the activation of GPX4; iron metabolic signaling pathways, which are involved in the regulation of iron import/export and the storage/release of intracellular iron through iron-regulatory proteins (IRPs), and lipid metabolic signaling pathways, which are involved in the metabolism of unsaturated fatty acids in cell membranes. Glutathione 122-133 glutathione peroxidase 4 Homo sapiens 255-259 34762602-3 2022 Peroxidases, including glutathione peroxidase-4 (GPX4), metabolize hydroperoxy-phospholipids to hydroxy derivatives to prevent ferroptotic death, but consume reduced glutathione (GSH). Glutathione 166-177 glutathione peroxidase 4 Homo sapiens 49-53 34983546-8 2022 PSTK was associated with the suppression of chemotherapy-induced ferroptosis in HCC cells, and the depletion of PSTK resulted in the inactivation of glutathione peroxidative 4 (GPX4) and the disruption of glutathione (GSH) metabolism owing to the inhibition of selenocysteine and cysteine synthesis, thus enhancing the induction of ferroptosis upon targeted chemotherapeutic treatment. Glutathione 149-160 glutathione peroxidase 4 Homo sapiens 177-181 34762602-3 2022 Peroxidases, including glutathione peroxidase-4 (GPX4), metabolize hydroperoxy-phospholipids to hydroxy derivatives to prevent ferroptotic death, but consume reduced glutathione (GSH). Glutathione 179-182 glutathione peroxidase 4 Homo sapiens 23-47 34762602-3 2022 Peroxidases, including glutathione peroxidase-4 (GPX4), metabolize hydroperoxy-phospholipids to hydroxy derivatives to prevent ferroptotic death, but consume reduced glutathione (GSH). Glutathione 179-182 glutathione peroxidase 4 Homo sapiens 49-53 33711415-9 2021 In summary, this set of data is compatible with a scenario where the more electrophilic status produced by GSH depletion not only activates ferroptosis by preventing GPx4 activity, but also favors the formation of lipid hydroperoxides. Glutathione 107-110 glutathione peroxidase 4 Homo sapiens 166-170 34048148-6 2021 Moreover, Erastin repressed glutathione peroxidase 4 (GPX4) expression and the levels of glutathione and cysteine in primary spinal cord neurons. Glutathione 28-39 glutathione peroxidase 4 Homo sapiens 54-58 33421769-2 2021 Cancer cells increase cystine uptake for the synthesis of glutathione (GSH), which is used by glutathione peroxidase 4 to reduce lipid peroxides. Glutathione 58-69 glutathione peroxidase 4 Homo sapiens 94-118 33917880-5 2021 We demonstrate that CAP indeed enhances the cytotoxicity of TMZ by targeting the antioxidant specific glutathione (GSH)/glutathione peroxidase 4 (GPX4) signaling. Glutathione 102-113 glutathione peroxidase 4 Homo sapiens 120-144 33377232-2 2021 Glutathione (GSH) plays an essential role in scavenging ROS to maintain cell viability and acts as a cofactor of GSH peroxidase 4 (GPX4) that protects lipids from oxidation. Glutathione 0-11 glutathione peroxidase 4 Homo sapiens 131-135 33377232-2 2021 Glutathione (GSH) plays an essential role in scavenging ROS to maintain cell viability and acts as a cofactor of GSH peroxidase 4 (GPX4) that protects lipids from oxidation. Glutathione 0-11 glutathione peroxidase 4 Homo sapiens 113-129 33377232-2 2021 Glutathione (GSH) plays an essential role in scavenging ROS to maintain cell viability and acts as a cofactor of GSH peroxidase 4 (GPX4) that protects lipids from oxidation. Glutathione 13-16 glutathione peroxidase 4 Homo sapiens 113-129 33377232-2 2021 Glutathione (GSH) plays an essential role in scavenging ROS to maintain cell viability and acts as a cofactor of GSH peroxidase 4 (GPX4) that protects lipids from oxidation. Glutathione 13-16 glutathione peroxidase 4 Homo sapiens 131-135 33707434-1 2021 Glutathione peroxidase 4 (GPX4) utilizes glutathione (GSH) to detoxify lipid peroxidation and plays an essential role in inhibiting ferroptosis. Glutathione 41-52 glutathione peroxidase 4 Homo sapiens 0-24 33707434-1 2021 Glutathione peroxidase 4 (GPX4) utilizes glutathione (GSH) to detoxify lipid peroxidation and plays an essential role in inhibiting ferroptosis. Glutathione 41-52 glutathione peroxidase 4 Homo sapiens 26-30 33707434-1 2021 Glutathione peroxidase 4 (GPX4) utilizes glutathione (GSH) to detoxify lipid peroxidation and plays an essential role in inhibiting ferroptosis. Glutathione 54-57 glutathione peroxidase 4 Homo sapiens 0-24 33707434-1 2021 Glutathione peroxidase 4 (GPX4) utilizes glutathione (GSH) to detoxify lipid peroxidation and plays an essential role in inhibiting ferroptosis. Glutathione 54-57 glutathione peroxidase 4 Homo sapiens 26-30 33495834-3 2021 Ferroptosis is a novel type of cell death in hepatic IRI that involves small molecules that inhibit glutathione biosynthesis or glutathione peroxidase 4 (GPX4), which is a glutathione-dependent antioxidant enzyme, causing mitochondrial damage. Glutathione 128-139 glutathione peroxidase 4 Homo sapiens 154-158 33917880-10 2021 We attribute the anticancer properties to the release of intracellular reactive oxygen species, through inhibiting the GSH/GPX4 antioxidant machinery, which can lead to DNA damage. Glutathione 119-122 glutathione peroxidase 4 Homo sapiens 123-127 33462411-4 2021 Various antioxidant systems, especially the system xc--glutathione-GPX4 axis, play a significant role in preventing lipid peroxidation-mediated ferroptosis. Glutathione 55-66 glutathione peroxidase 4 Homo sapiens 67-71 33746607-7 2021 When the expression of GPX4 changes, its biological activities, such as the glutathione metabolic process, cellular biosynthetic process, cellular response to chemical stimulus, and antioxidant activity, change accordingly, thereby affecting the survival quality and physiological and biochemical activities of cells. Glutathione 76-87 glutathione peroxidase 4 Homo sapiens 23-27 33421769-2 2021 Cancer cells increase cystine uptake for the synthesis of glutathione (GSH), which is used by glutathione peroxidase 4 to reduce lipid peroxides. Glutathione 71-74 glutathione peroxidase 4 Homo sapiens 94-118 33172933-7 2021 Overexpression of FZD7 activated the oncogenic factor Tp63, driving upregulation of glutathione metabolism pathways, including glutathione peroxidase 4 (GPX4), which protected cells from chemotherapy-induced oxidative stress. Glutathione 84-95 glutathione peroxidase 4 Homo sapiens 127-151 33603367-6 2021 MIL-101(Fe)@sor NPs significantly induced ferroptosis in HepG2 cells, increased the levels of lipid peroxidation and malondialdehyde, and reduced those of glutathione and glutathione peroxidase 4 (GPX-4). Glutathione 155-166 glutathione peroxidase 4 Homo sapiens 197-202 33172933-7 2021 Overexpression of FZD7 activated the oncogenic factor Tp63, driving upregulation of glutathione metabolism pathways, including glutathione peroxidase 4 (GPX4), which protected cells from chemotherapy-induced oxidative stress. Glutathione 84-95 glutathione peroxidase 4 Homo sapiens 153-157 33372514-7 2021 With the disulfide bond-mediated GSH depletion and DOX-mediated reactive oxygen species (ROS) production, treatment with DOX@PssP-Hh NPs prominently reduced glutathione peroxidase 4 (GPX4) level and would lead to enhanced oxidative stresses. Glutathione 33-36 glutathione peroxidase 4 Homo sapiens 157-181 33372514-7 2021 With the disulfide bond-mediated GSH depletion and DOX-mediated reactive oxygen species (ROS) production, treatment with DOX@PssP-Hh NPs prominently reduced glutathione peroxidase 4 (GPX4) level and would lead to enhanced oxidative stresses. Glutathione 33-36 glutathione peroxidase 4 Homo sapiens 183-187 33260096-10 2021 Furthermore, the glutathione-depletion inactivates the glutathione peroxidase 4 (GPX4, a critical regulatory target in ferroptosis), inhibiting the reduction of lipid peroxides and reinforcing the ferroptotic cell death. Glutathione 17-28 glutathione peroxidase 4 Homo sapiens 55-79 33393679-3 2022 Decreased glutathione (GSH) synthesis and low glutathione dependent antioxidant peroxidase 4(GPX4) activity are the major causes of ferroptosis. Glutathione 46-57 glutathione peroxidase 4 Homo sapiens 93-97 33260096-10 2021 Furthermore, the glutathione-depletion inactivates the glutathione peroxidase 4 (GPX4, a critical regulatory target in ferroptosis), inhibiting the reduction of lipid peroxides and reinforcing the ferroptotic cell death. Glutathione 17-28 glutathione peroxidase 4 Homo sapiens 81-85 33415100-5 2020 We identified the hyperactive glutathione (GSH) metabolism pathway with the overexpression of various GSH metabolism-related enzymes (GPX4, RRM2, GCLC, GPX1, GSTM4, GSTM1). Glutathione 30-41 glutathione peroxidase 4 Homo sapiens 134-138 33415100-5 2020 We identified the hyperactive glutathione (GSH) metabolism pathway with the overexpression of various GSH metabolism-related enzymes (GPX4, RRM2, GCLC, GPX1, GSTM4, GSTM1). Glutathione 43-46 glutathione peroxidase 4 Homo sapiens 134-138 33415100-5 2020 We identified the hyperactive glutathione (GSH) metabolism pathway with the overexpression of various GSH metabolism-related enzymes (GPX4, RRM2, GCLC, GPX1, GSTM4, GSTM1). Glutathione 102-105 glutathione peroxidase 4 Homo sapiens 134-138 32776663-9 2020 More importantly, the study finds that ACADSB negatively regulates expression of glutathione reductase (GSR) and glutathione peroxidase 4 (GPX4), the two main enzymes responsible for clearing glutathione (GSH) in CRC cells. Glutathione 81-92 glutathione peroxidase 4 Homo sapiens 139-143 33087576-2 2020 The selenium-dependent glutathione peroxidase 4 (GPX4) inhibits ferroptosis, converting unstable ferroptotic lipid hydroperoxides to nontoxic lipid alcohols in a tissue-specific manner. Glutathione 23-34 glutathione peroxidase 4 Homo sapiens 49-53 33294126-4 2020 At least three major pathways (the glutathione-GPX4, FSP1-coenzyme Q10 (CoQ10), and GTP cyclohydrolase-1- (GCH1-) tetrahydrobiopterin (BH4) pathways) have been identified to participate in ferroptosis regulation. Glutathione 35-46 glutathione peroxidase 4 Homo sapiens 47-51 32776663-9 2020 More importantly, the study finds that ACADSB negatively regulates expression of glutathione reductase (GSR) and glutathione peroxidase 4 (GPX4), the two main enzymes responsible for clearing glutathione (GSH) in CRC cells. Glutathione 205-208 glutathione peroxidase 4 Homo sapiens 113-137 32776663-9 2020 More importantly, the study finds that ACADSB negatively regulates expression of glutathione reductase (GSR) and glutathione peroxidase 4 (GPX4), the two main enzymes responsible for clearing glutathione (GSH) in CRC cells. Glutathione 205-208 glutathione peroxidase 4 Homo sapiens 139-143 32531676-14 2020 Taken together, these results demonstrate that solasonine promotes ferroptosis of HCC cells via GPX4-induced destruction of the glutathione redox system. Glutathione 128-139 glutathione peroxidase 4 Homo sapiens 96-100 32945131-1 2020 Ferroptotic cell death results from glutathione peroxidase 4 (GPX4) inactivation and/or glutathione (GSH) depletion. Glutathione 36-47 glutathione peroxidase 4 Homo sapiens 62-66 33096672-6 2020 In particular, by using in vivo and in vitro models of fasting, we found that typical Nrf2-dependent genes, including those controlling iron (e.g., Ho-1) and glutathione (GSH) metabolism (e.g., Gcl, Gsr) are induced along with increased levels of the glutathione peroxidase 4 (Gpx4), a GSH-dependent antioxidant enzyme. Glutathione 158-169 glutathione peroxidase 4 Homo sapiens 251-275 33096672-6 2020 In particular, by using in vivo and in vitro models of fasting, we found that typical Nrf2-dependent genes, including those controlling iron (e.g., Ho-1) and glutathione (GSH) metabolism (e.g., Gcl, Gsr) are induced along with increased levels of the glutathione peroxidase 4 (Gpx4), a GSH-dependent antioxidant enzyme. Glutathione 158-169 glutathione peroxidase 4 Homo sapiens 277-281 33096672-6 2020 In particular, by using in vivo and in vitro models of fasting, we found that typical Nrf2-dependent genes, including those controlling iron (e.g., Ho-1) and glutathione (GSH) metabolism (e.g., Gcl, Gsr) are induced along with increased levels of the glutathione peroxidase 4 (Gpx4), a GSH-dependent antioxidant enzyme. Glutathione 171-174 glutathione peroxidase 4 Homo sapiens 251-275 33096672-6 2020 In particular, by using in vivo and in vitro models of fasting, we found that typical Nrf2-dependent genes, including those controlling iron (e.g., Ho-1) and glutathione (GSH) metabolism (e.g., Gcl, Gsr) are induced along with increased levels of the glutathione peroxidase 4 (Gpx4), a GSH-dependent antioxidant enzyme. Glutathione 171-174 glutathione peroxidase 4 Homo sapiens 277-281