PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20649470-4 2011 Reduction of lipid hydroperoxides is the domain of monomeric GPx4-type enzymes and of some Prxs. Lipid Peroxides 13-33 glutathione peroxidase 4 Homo sapiens 61-65 22446825-4 2012 An understudied, yet critical component of cellular antioxidant defense is phospholipid hydroperoxide glutathione peroxidase (PHGPx/GPx4), an isoform within the family of selenium-dependent glutathione peroxidase (GPx) enzymes that can directly reduce lipid peroxides and other membrane-bound complex hydroperoxides. Lipid Peroxides 252-267 glutathione peroxidase 4 Homo sapiens 132-136 22433871-7 2012 Glutathione peroxidase-4 (GPx4), which specifically metabolizes lipid hydroperoxides, fell in TNFalpha-stimulated cells prior to death. Lipid Peroxides 64-84 glutathione peroxidase 4 Homo sapiens 0-24 22433871-7 2012 Glutathione peroxidase-4 (GPx4), which specifically metabolizes lipid hydroperoxides, fell in TNFalpha-stimulated cells prior to death. Lipid Peroxides 64-84 glutathione peroxidase 4 Homo sapiens 26-30 22105228-7 2012 This inhibition was mediated by glutathione peroxidase 4 (GPx4), which preferentially degrades lipid peroxides. Lipid Peroxides 95-110 glutathione peroxidase 4 Homo sapiens 32-56 22105228-7 2012 This inhibition was mediated by glutathione peroxidase 4 (GPx4), which preferentially degrades lipid peroxides. Lipid Peroxides 95-110 glutathione peroxidase 4 Homo sapiens 58-62 17516241-1 2007 Phospholipid Hydroperoxide Glutathione Peroxidase (PHGPx) is the only known enzyme able to reduce lipid peroxides bound to cell membranes. Lipid Peroxides 98-113 glutathione peroxidase 4 Homo sapiens 0-49 20798033-4 2010 This study demonstrates that increases in cellular lipid peroxides, induced by disruption of glutathione peroxidase 4, induce cellular PTP oxidation and reduce the activity of PDGF receptor targeting PTPs. Lipid Peroxides 51-66 glutathione peroxidase 4 Homo sapiens 93-117 19376195-7 2009 Mammalian GPx-1 dominates H(2)O(2) metabolism, whereas the domain of GPx-4 is the reduction of lipid hydroperoxides with important consequences such as counteracting 12/15-lipoxygenase-induced apoptosis and regulation of inflammatory responses. Lipid Peroxides 95-115 glutathione peroxidase 4 Homo sapiens 69-74 17630701-2 2007 Among GPx-isoforms, GPx4 is unique because of its capability to reduce complex lipid hydroperoxides and its tendency toward polymerization, but the structural basis for these properties remained unclear. Lipid Peroxides 79-99 glutathione peroxidase 4 Homo sapiens 20-24 19769463-9 2010 These data suggest a role of GPx4 in neurodegenerative diseases through its function in removal of lipid hydroperoxides. Lipid Peroxides 99-119 glutathione peroxidase 4 Homo sapiens 29-33 19808099-1 2010 Phospholipid-hydroperoxide glutathione peroxidase (PHGPx or GPx4; EC 1.11.1.12) is an antioxidant enzyme that reduces lipid hydroperoxides in biomembranes. Lipid Peroxides 118-138 glutathione peroxidase 4 Homo sapiens 51-56 18723092-1 2008 Type 4 glutathione peroxidase (GPx4) is a widely expressed mammalian selenoenzyme known to play a vital role in cytoprotection against lipid hydroperoxide (LOOH)-mediated oxidative stress and regulation of oxidative signaling cascades. Lipid Peroxides 135-154 glutathione peroxidase 4 Homo sapiens 31-35 18723092-1 2008 Type 4 glutathione peroxidase (GPx4) is a widely expressed mammalian selenoenzyme known to play a vital role in cytoprotection against lipid hydroperoxide (LOOH)-mediated oxidative stress and regulation of oxidative signaling cascades. Lipid Peroxides 156-160 glutathione peroxidase 4 Homo sapiens 31-35 18723092-8 2008 The relatively straightforward isolation procedure described should prove valuable for further functional studies on GPx4, e.g. how its ability to catalyze LOOH reduction compares with that of other LOOH detoxifying enzymes. Lipid Peroxides 156-160 glutathione peroxidase 4 Homo sapiens 117-121 18723092-8 2008 The relatively straightforward isolation procedure described should prove valuable for further functional studies on GPx4, e.g. how its ability to catalyze LOOH reduction compares with that of other LOOH detoxifying enzymes. Lipid Peroxides 199-203 glutathione peroxidase 4 Homo sapiens 117-121 17516241-1 2007 Phospholipid Hydroperoxide Glutathione Peroxidase (PHGPx) is the only known enzyme able to reduce lipid peroxides bound to cell membranes. Lipid Peroxides 98-113 glutathione peroxidase 4 Homo sapiens 51-56 16181973-1 2005 Phospholipid hydroperoxide glutathione peroxidase (PHGPx) is a unique intracellular enzyme that directly reduces lipid hydroperoxides in membranes and has the ability to use protein thiol groups as donor substrates. Lipid Peroxides 113-133 glutathione peroxidase 4 Homo sapiens 0-49 17020817-1 2006 Seleno-glutathione peroxidases are an important family of antioxidant enzymes, that include the phospholipid hydroperoxide glutathione peroxidase (GPx-4), an enzyme that reduces lipid hydroperoxides in membranes. Lipid Peroxides 178-198 glutathione peroxidase 4 Homo sapiens 96-145 17020817-1 2006 Seleno-glutathione peroxidases are an important family of antioxidant enzymes, that include the phospholipid hydroperoxide glutathione peroxidase (GPx-4), an enzyme that reduces lipid hydroperoxides in membranes. Lipid Peroxides 178-198 glutathione peroxidase 4 Homo sapiens 147-152 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. Lipid Peroxides 52-72 glutathione peroxidase 4 Homo sapiens 0-35 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. Lipid Peroxides 52-72 glutathione peroxidase 4 Homo sapiens 37-42 16409129-11 2006 Because of the growthinhibitory effects of PhGPx, lipid hydroperoxides may play an important role in the growth of pancreatic cancer. Lipid Peroxides 50-70 glutathione peroxidase 4 Homo sapiens 43-48 17431126-2 2007 Whereas several enzymes influence the response of cells to oxidative stress, only one enzyme, phospholipid hydroperoxide glutathione peroxidase (GPx-4), directly reduces lipid hydroperoxides in mammalian cells. Lipid Peroxides 170-190 glutathione peroxidase 4 Homo sapiens 94-143 17431126-2 2007 Whereas several enzymes influence the response of cells to oxidative stress, only one enzyme, phospholipid hydroperoxide glutathione peroxidase (GPx-4), directly reduces lipid hydroperoxides in mammalian cells. Lipid Peroxides 170-190 glutathione peroxidase 4 Homo sapiens 145-150 16181973-1 2005 Phospholipid hydroperoxide glutathione peroxidase (PHGPx) is a unique intracellular enzyme that directly reduces lipid hydroperoxides in membranes and has the ability to use protein thiol groups as donor substrates. Lipid Peroxides 113-133 glutathione peroxidase 4 Homo sapiens 51-56 15577264-0 2004 [Biological significance of lipid hydroperoxide and its reducing enzyme, phospholipid hydroperoxide glutathione peroxidase, in mammalian cells]. Lipid Peroxides 28-47 glutathione peroxidase 4 Homo sapiens 73-122 15577264-6 2004 The phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) is a unique antioxidant enzyme and separately distributed to the mitochondria, nucleus, nucleoli, and cytosol, where it regulates phospholipid hydroperoxide and fatty acid hydroperoxide as signal molecules. Lipid Peroxides 229-253 glutathione peroxidase 4 Homo sapiens 4-53 15577264-6 2004 The phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) is a unique antioxidant enzyme and separately distributed to the mitochondria, nucleus, nucleoli, and cytosol, where it regulates phospholipid hydroperoxide and fatty acid hydroperoxide as signal molecules. Lipid Peroxides 229-253 glutathione peroxidase 4 Homo sapiens 55-60 15577264-6 2004 The phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) is a unique antioxidant enzyme and separately distributed to the mitochondria, nucleus, nucleoli, and cytosol, where it regulates phospholipid hydroperoxide and fatty acid hydroperoxide as signal molecules. Lipid Peroxides 229-253 glutathione peroxidase 4 Homo sapiens 62-66 15577264-9 2004 Transformant studies show that lipid hydroperoxide is an activator of lipoxygenase and cyclooxygenase and participates in inflammation, cardiolipin hydroperoxide is the signal molecule for the release of cytochrome c during apoptotic cell death, and PHGPx is a signal regulator in the IgE receptor-mediated signaling pathway. Lipid Peroxides 31-50 glutathione peroxidase 4 Homo sapiens 250-255 15256721-1 2004 Phospholipid hydroperoxide glutathione peroxidase (PHGPx) is a unique antioxidant enzyme that markedly reduces lipid hydroperoxide generated in biomembranes. Lipid Peroxides 7-26 glutathione peroxidase 4 Homo sapiens 51-56 15280629-9 2004 Phospholipid Hydroperoxide Glutathione Peroxidase (PH-GPx) is an antioxidant enzyme that is able to directly reduce lipid peroxides even when they are bound to cellular membranes. Lipid Peroxides 116-131 glutathione peroxidase 4 Homo sapiens 0-49 15280629-9 2004 Phospholipid Hydroperoxide Glutathione Peroxidase (PH-GPx) is an antioxidant enzyme that is able to directly reduce lipid peroxides even when they are bound to cellular membranes. Lipid Peroxides 116-131 glutathione peroxidase 4 Homo sapiens 51-57 15256721-5 2004 From studies of the overexpression of PHGPx, the generation of hydrogen peroxide and lipid hydroperoxide in mitochondria might be important triggers of apoptosis. Lipid Peroxides 85-104 glutathione peroxidase 4 Homo sapiens 38-43 15256721-7 2004 c liberation from mitochondria in 2DG-induced apoptosis since lipid hydroperoxide is a primary substrate for PHGPx. Lipid Peroxides 75-94 glutathione peroxidase 4 Homo sapiens 122-127 12419471-6 2002 Experiments with a transfectant clone, 7G4, exhibiting approximately 85 times greater activity of the LOOH-detoxifying selenoenzyme GPX4 than parental cells, provided additional information about death mechanism. Lipid Peroxides 102-106 glutathione peroxidase 4 Homo sapiens 132-136 12521597-7 2003 Recently, molecular techniques have allowed overexpression of PHGPx in mammalian cell lines, from which it has become clear that lipid hydroperoxides also have an important function as activators of lipoxygenase and cyclooxygenase, participate in inflammation, and act as signal molecules for apoptotic cell death and receptor-mediated signal transduction at the cellular level. Lipid Peroxides 129-149 glutathione peroxidase 4 Homo sapiens 62-67 12958179-1 2003 Phospholipid hydroperoxide glutathione peroxidase (PHGPx), a selenium-dependent glutathione peroxidase, can interact with lipophilic substrates, including the phospholipid hydroperoxides, fatty-acid hydroperoxides, and cholesteryl ester hydroperoxides, and reduce them to hydroxide compounds. Lipid Peroxides 188-213 glutathione peroxidase 4 Homo sapiens 0-49 12958179-1 2003 Phospholipid hydroperoxide glutathione peroxidase (PHGPx), a selenium-dependent glutathione peroxidase, can interact with lipophilic substrates, including the phospholipid hydroperoxides, fatty-acid hydroperoxides, and cholesteryl ester hydroperoxides, and reduce them to hydroxide compounds. Lipid Peroxides 188-213 glutathione peroxidase 4 Homo sapiens 51-56 12958179-8 2003 Taken together, these results support the notion that the endogenous PHGPx plays a pivotal role in the regulation of 12(S)-lipoxygenase and cyclooxygenase 1 activities by reducing the level of intracellular lipid hydroperoxides in arachidonate metabolism in A431 cells. Lipid Peroxides 207-227 glutathione peroxidase 4 Homo sapiens 69-74 12419471-7 2002 Located predominantly in mitochondria of 7G4 cells, GPX4 strongly inhibited both LOOH accumulation and apoptosis under protocol-1 conditions, but had no significant effect under protocol-2 conditions. Lipid Peroxides 81-85 glutathione peroxidase 4 Homo sapiens 52-56 11295525-4 2001 Because singlet oxygen introduces lipid hydroperoxides into cell membranes, we hypothesized that PhGPx would provide protection against the oxidative stress of singlet oxygen and therefore could interfere with cancer treatment. Lipid Peroxides 34-54 glutathione peroxidase 4 Homo sapiens 97-102 11677038-9 2001 L-form GPX4"s antiperoxidant and cytoprotective effects could reflect its ability to detoxify ChOOHs as they enter cells and/or cell-derived lipid hydroperoxides arising from ChOOH one-electron turnover. Lipid Peroxides 141-161 glutathione peroxidase 4 Homo sapiens 7-11 11295525-1 2001 Phospholipid hydroperoxide glutathione peroxidase (PhGPx) is an important enzyme in the removal of lipid hydroperoxides (LOOHs) from cell membranes. Lipid Peroxides 99-119 glutathione peroxidase 4 Homo sapiens 0-49 11295525-1 2001 Phospholipid hydroperoxide glutathione peroxidase (PhGPx) is an important enzyme in the removal of lipid hydroperoxides (LOOHs) from cell membranes. Lipid Peroxides 99-119 glutathione peroxidase 4 Homo sapiens 51-56 11295525-1 2001 Phospholipid hydroperoxide glutathione peroxidase (PhGPx) is an important enzyme in the removal of lipid hydroperoxides (LOOHs) from cell membranes. Lipid Peroxides 121-126 glutathione peroxidase 4 Homo sapiens 0-49 11295525-1 2001 Phospholipid hydroperoxide glutathione peroxidase (PhGPx) is an important enzyme in the removal of lipid hydroperoxides (LOOHs) from cell membranes. Lipid Peroxides 121-126 glutathione peroxidase 4 Homo sapiens 51-56 12218361-1 2002 Phospholipid hydroperoxide glutathione peroxidase (PHGPx), a selenium-dependent glutathione peroxidase, can interact with lipophilic substrates, including phospholipid hydroperoxides, fatty acid hydroperoxides and cholesterol hydroperoxides, and can reduce them to hydroxide compounds. Lipid Peroxides 184-209 glutathione peroxidase 4 Homo sapiens 0-49 12218361-1 2002 Phospholipid hydroperoxide glutathione peroxidase (PHGPx), a selenium-dependent glutathione peroxidase, can interact with lipophilic substrates, including phospholipid hydroperoxides, fatty acid hydroperoxides and cholesterol hydroperoxides, and can reduce them to hydroxide compounds. Lipid Peroxides 184-209 glutathione peroxidase 4 Homo sapiens 51-56 11295525-8 2001 Cellular PhGPx activity had a remarkable inverse linear correlation to the removal of lipid hydroperoxides in living cells (r = -0.85), and correlated positively with cell survival after singlet oxygen exposure (r = 0.94). Lipid Peroxides 86-106 glutathione peroxidase 4 Homo sapiens 9-14 11295525-9 2001 These data demonstrate that PhGPx provides significant protection against singlet oxygen-generated lipid peroxidation via removal of LOOH and suggest that LOOHs are major mediators in this cell injury process. Lipid Peroxides 133-137 glutathione peroxidase 4 Homo sapiens 28-33 11295525-9 2001 These data demonstrate that PhGPx provides significant protection against singlet oxygen-generated lipid peroxidation via removal of LOOH and suggest that LOOHs are major mediators in this cell injury process. Lipid Peroxides 155-160 glutathione peroxidase 4 Homo sapiens 28-33 9285063-12 1997 These results clearly support our previous conclusion that expression of PHGPx is responsible for the protection of host cells from lipid hydroperoxide-mediated injury. Lipid Peroxides 132-151 glutathione peroxidase 4 Homo sapiens 73-78 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. Lipid Peroxides 280-299 glutathione peroxidase 4 Homo sapiens 93-98 10560610-5 1999 The results indicate that PHGPx directly reduced lipid hydroperoxides and then down-regulated the activity of arachidonate oxygenases. Lipid Peroxides 49-69 glutathione peroxidase 4 Homo sapiens 26-31 9359853-4 1997 By overexpressing phospholipid hydroperoxide glutathione peroxidase (PHGPx), which characteristically reacts with lipophilic hydroperoxides, the roles of H2O2 and lipid hydroperoxides were assessed. Lipid Peroxides 163-183 glutathione peroxidase 4 Homo sapiens 69-74 9359853-12 1997 These results show that overexpressed PHGPx is sufficient to inhibit NF kappa B activation, and suggests that NF kappa B activation by IL-1 is mediated by a preferential substrate of PHGPx, such as a fatty acid hydroperoxide, rather than by H2O2, the preferred substrate of the more abundant cytosolic GPx. Lipid Peroxides 200-224 glutathione peroxidase 4 Homo sapiens 38-43 9359853-12 1997 These results show that overexpressed PHGPx is sufficient to inhibit NF kappa B activation, and suggests that NF kappa B activation by IL-1 is mediated by a preferential substrate of PHGPx, such as a fatty acid hydroperoxide, rather than by H2O2, the preferred substrate of the more abundant cytosolic GPx. Lipid Peroxides 200-224 glutathione peroxidase 4 Homo sapiens 183-188 2294113-2 1990 The general reactivity of membrane lipid hydroperoxides (LOOHs) with the selenoenzyme phospholipid hydroperoxide glutathione peroxidase (PHGPX) has been investigated. Lipid Peroxides 57-62 glutathione peroxidase 4 Homo sapiens 137-142 2386798-8 1990 An important role of PHGPX in cellular detoxification of a wide variety of LOOHs in membranes and internalized lipoproteins is suggested from these findings. Lipid Peroxides 75-80 glutathione peroxidase 4 Homo sapiens 21-26 8679629-1 1996 Phospholipid hydroperoxide glutathione peroxidase (PHGPX) is a selenoenzyme that can catalyze the direct reduction of various membrane lipid hydroperoxides and by so doing could play a vital role in cytoprotection against peroxidative damage. Lipid Peroxides 135-155 glutathione peroxidase 4 Homo sapiens 0-49 8679629-1 1996 Phospholipid hydroperoxide glutathione peroxidase (PHGPX) is a selenoenzyme that can catalyze the direct reduction of various membrane lipid hydroperoxides and by so doing could play a vital role in cytoprotection against peroxidative damage. Lipid Peroxides 135-155 glutathione peroxidase 4 Homo sapiens 51-56 2071029-1 1991 A comparative study has been carried out on the general reactivity of lipid hydroperoxides in liposomes, biological membranes and lipoproteins with two Se-dependent peroxidases: Glutathione Peroxidase (GPX) and Phospholipid Hydroperoxide Glutathione Peroxidase (PHGPX). Lipid Peroxides 70-90 glutathione peroxidase 4 Homo sapiens 211-260 2071029-1 1991 A comparative study has been carried out on the general reactivity of lipid hydroperoxides in liposomes, biological membranes and lipoproteins with two Se-dependent peroxidases: Glutathione Peroxidase (GPX) and Phospholipid Hydroperoxide Glutathione Peroxidase (PHGPX). Lipid Peroxides 70-90 glutathione peroxidase 4 Homo sapiens 262-267 2386798-1 1990 Lipid hydroperoxides (LOOHs) in various lipid assemblies are shown to be efficiently reduced and deactivated by phospholipid hydroperoxide glutathione peroxidase (PHGPX), the second selenoperoxidase to be identified and characterized. Lipid Peroxides 0-20 glutathione peroxidase 4 Homo sapiens 112-161 2386798-1 1990 Lipid hydroperoxides (LOOHs) in various lipid assemblies are shown to be efficiently reduced and deactivated by phospholipid hydroperoxide glutathione peroxidase (PHGPX), the second selenoperoxidase to be identified and characterized. Lipid Peroxides 0-20 glutathione peroxidase 4 Homo sapiens 163-168 2386798-1 1990 Lipid hydroperoxides (LOOHs) in various lipid assemblies are shown to be efficiently reduced and deactivated by phospholipid hydroperoxide glutathione peroxidase (PHGPX), the second selenoperoxidase to be identified and characterized. Lipid Peroxides 22-27 glutathione peroxidase 4 Homo sapiens 112-161 2386798-1 1990 Lipid hydroperoxides (LOOHs) in various lipid assemblies are shown to be efficiently reduced and deactivated by phospholipid hydroperoxide glutathione peroxidase (PHGPX), the second selenoperoxidase to be identified and characterized. Lipid Peroxides 22-27 glutathione peroxidase 4 Homo sapiens 163-168 2386798-2 1990 Coupled spectrophotometric analyses in the presence of NADPH, glutathione (GSH), glutathione reductase and Triton X-100 indicated that photochemically generated LOOHs in small unilamellar liposomes are substrates for PHGPX, but not for the classical glutathione peroxidase (GPX). Lipid Peroxides 161-166 glutathione peroxidase 4 Homo sapiens 217-222 2386798-4 1990 Kinetic iodometric analyses during GSH/PHGPX treatment of photoperoxidized liposomes indicated a rapid decay of total LOOH to a residual level of 35-40%; addition of Triton X-100 allowed the reaction to go to completion. Lipid Peroxides 118-122 glutathione peroxidase 4 Homo sapiens 39-44 2294113-6 1990 Thin layer chromatographic analyses revealed that the GPX-resistant (but PHGPX-reactive) LOOH was cholesterol hydroperoxide (ChOOH) consisting mainly of the 5 alpha (singlet oxygen-derived) product. Lipid Peroxides 89-93 glutathione peroxidase 4 Homo sapiens 73-78 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. Lipid Peroxides 102-117 glutathione peroxidase 4 Homo sapiens 61-65 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. Lipid Peroxides 119-122 glutathione peroxidase 4 Homo sapiens 61-65 34800783-3 2022 The metabolic disorder of intracellular LOOH catalyzed by iron causes the inactivity of GPX4, disrupts the redox balance, and triggers cell death. Lipid Peroxides 40-44 glutathione peroxidase 4 Homo sapiens 88-92 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. Lipid Peroxides 111-114 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. Lipid Peroxides 111-114 glutathione peroxidase 4 Homo sapiens 86-90 35614872-2 2022 It was found to manipulate oncogenes and resistant mutations of cancer cells via lipid metabolism pathways converging on phospholipid glutathione peroxidase (GPX4) that squanders lipid peroxides (L-OOH) to block the iron-mediated reactions of peroxides, thus rendering resistant cancer cells vulnerable to ferroptotic cell death. Lipid Peroxides 179-194 glutathione peroxidase 4 Homo sapiens 158-162 34492183-1 2021 Glutathione peroxidase 4 (GPx4) serves as the only enzyme that protects membranes through the reduction of lipid hydroperoxides, preventing membrane oxidative damage and cell death through ferroptosis. Lipid Peroxides 107-127 glutathione peroxidase 4 Homo sapiens 0-24 34492183-1 2021 Glutathione peroxidase 4 (GPx4) serves as the only enzyme that protects membranes through the reduction of lipid hydroperoxides, preventing membrane oxidative damage and cell death through ferroptosis. Lipid Peroxides 107-127 glutathione peroxidase 4 Homo sapiens 26-30 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. Lipid Peroxides 157-172 glutathione peroxidase 4 Homo sapiens 0-4 34127539-7 2021 GPX4 suppresses lipid peroxide accumulation, thus plays a key role in protecting cells from oxidative damage. Lipid Peroxides 16-30 glutathione peroxidase 4 Homo sapiens 0-4 35637349-1 2022 The selenoprotein glutathione peroxidase 4 (GPX4) prevents ferroptosis by converting lipid peroxides into nontoxic lipid alcohols. Lipid Peroxides 85-100 glutathione peroxidase 4 Homo sapiens 44-48 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. Lipid Peroxides 134-149 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. Lipid Peroxides 134-149 glutathione peroxidase 4 Homo sapiens 81-85 34133924-4 2021 Loss of Gpx4 results in excessive accumulation of lipid peroxides and ferroptosis of Treg cells upon T cell receptor (TCR)/CD28 co-stimulation. Lipid Peroxides 50-65 glutathione peroxidase 4 Homo sapiens 8-12 34133924-5 2021 Neutralization of lipid peroxides and blockade of iron availability rescue ferroptosis of Gpx4-deficient Treg cells. Lipid Peroxides 18-33 glutathione peroxidase 4 Homo sapiens 90-94 35551311-2 2022 Tf-DHA-ASO-MnO2 shows an effective targeted cancer therapy ability through the ferroptosis caused by the production of excessive lipid peroxides resulting from the combined effect of glutathione exhaustion, reactive oxygen species generation and down-regulation of glutathione peroxidase 4. Lipid Peroxides 129-144 glutathione peroxidase 4 Homo sapiens 265-289 35614872-2 2022 It was found to manipulate oncogenes and resistant mutations of cancer cells via lipid metabolism pathways converging on phospholipid glutathione peroxidase (GPX4) that squanders lipid peroxides (L-OOH) to block the iron-mediated reactions of peroxides, thus rendering resistant cancer cells vulnerable to ferroptotic cell death. Lipid Peroxides 196-201 glutathione peroxidase 4 Homo sapiens 158-162 35568865-6 2022 Meanwhile, ROS production introduced ferroptosis by depleting glutathione (GSH), inactivating glutathione peroxidase 4 (GPX4), leading to lipid peroxide (LPO) accumulation. Lipid Peroxides 138-152 glutathione peroxidase 4 Homo sapiens 94-118 35568865-6 2022 Meanwhile, ROS production introduced ferroptosis by depleting glutathione (GSH), inactivating glutathione peroxidase 4 (GPX4), leading to lipid peroxide (LPO) accumulation. Lipid Peroxides 138-152 glutathione peroxidase 4 Homo sapiens 120-124 35568865-6 2022 Meanwhile, ROS production introduced ferroptosis by depleting glutathione (GSH), inactivating glutathione peroxidase 4 (GPX4), leading to lipid peroxide (LPO) accumulation. Lipid Peroxides 154-157 glutathione peroxidase 4 Homo sapiens 94-118 35568865-6 2022 Meanwhile, ROS production introduced ferroptosis by depleting glutathione (GSH), inactivating glutathione peroxidase 4 (GPX4), leading to lipid peroxide (LPO) accumulation. Lipid Peroxides 154-157 glutathione peroxidase 4 Homo sapiens 120-124 35523770-2 2022 Lipid hydroperoxides are neutralized in cells by glutathione peroxidase 4 (GPX4) and inhibitors of GPX4 are potent ferroptosis inducers with therapeutic potential in cancer. Lipid Peroxides 0-20 glutathione peroxidase 4 Homo sapiens 49-73 35523770-2 2022 Lipid hydroperoxides are neutralized in cells by glutathione peroxidase 4 (GPX4) and inhibitors of GPX4 are potent ferroptosis inducers with therapeutic potential in cancer. Lipid Peroxides 0-20 glutathione peroxidase 4 Homo sapiens 75-79 35523770-2 2022 Lipid hydroperoxides are neutralized in cells by glutathione peroxidase 4 (GPX4) and inhibitors of GPX4 are potent ferroptosis inducers with therapeutic potential in cancer. Lipid Peroxides 0-20 glutathione peroxidase 4 Homo sapiens 99-103 35484753-7 2022 Additionally, RSL3 directly inhibits glutathione peroxidase 4 (GPX4) to detoxify L-OOH, and ferrous ions further catalyze the irreversible conversion of highly reactive lipid alkoxyl radicals (L-O ) from L-OOH to triggering waterfall-like cascade ferroptosis. Lipid Peroxides 81-86 glutathione peroxidase 4 Homo sapiens 37-61 35453406-2 2022 Glutathione peroxidase-4 (GPx4) is a vital selenoenzyme responsible for neutralizing lipid peroxides, mediators of oxidative stress known to contribute to postoperative arrhythmogenesis. Lipid Peroxides 85-100 glutathione peroxidase 4 Homo sapiens 0-24 35453406-2 2022 Glutathione peroxidase-4 (GPx4) is a vital selenoenzyme responsible for neutralizing lipid peroxides, mediators of oxidative stress known to contribute to postoperative arrhythmogenesis. Lipid Peroxides 85-100 glutathione peroxidase 4 Homo sapiens 26-30 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. Lipid Peroxides 100-115 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. Lipid Peroxides 100-115 glutathione peroxidase 4 Homo sapiens 26-30 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. Lipid Peroxides 156-176 glutathione peroxidase 4 Homo sapiens 75-99 35484753-7 2022 Additionally, RSL3 directly inhibits glutathione peroxidase 4 (GPX4) to detoxify L-OOH, and ferrous ions further catalyze the irreversible conversion of highly reactive lipid alkoxyl radicals (L-O ) from L-OOH to triggering waterfall-like cascade ferroptosis. Lipid Peroxides 81-86 glutathione peroxidase 4 Homo sapiens 63-67 35484753-7 2022 Additionally, RSL3 directly inhibits glutathione peroxidase 4 (GPX4) to detoxify L-OOH, and ferrous ions further catalyze the irreversible conversion of highly reactive lipid alkoxyl radicals (L-O ) from L-OOH to triggering waterfall-like cascade ferroptosis. Lipid Peroxides 204-209 glutathione peroxidase 4 Homo sapiens 37-61 35484753-7 2022 Additionally, RSL3 directly inhibits glutathione peroxidase 4 (GPX4) to detoxify L-OOH, and ferrous ions further catalyze the irreversible conversion of highly reactive lipid alkoxyl radicals (L-O ) from L-OOH to triggering waterfall-like cascade ferroptosis. Lipid Peroxides 204-209 glutathione peroxidase 4 Homo sapiens 63-67 32945131-8 2020 The mechanism of action is attributed to GSH depletion and GPX4 inactivation, accumulating lipid hydroperoxides, which in turn leads to ferroptosis. Lipid Peroxides 91-111 glutathione peroxidase 4 Homo sapiens 59-63 34007410-3 2021 Ferroptosis is defined by three hallmarks, defined as the loss of lipid peroxide repair capacity by GPX4, the bioavailability of redox-active iron, and oxidation of polyunsaturated fatty acid- (PUFA-) containing phospholipids. Lipid Peroxides 66-80 glutathione peroxidase 4 Homo sapiens 100-104 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. Lipid Peroxides 161-176 glutathione peroxidase 4 Homo sapiens 55-79 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. Lipid Peroxides 161-176 glutathione peroxidase 4 Homo sapiens 81-85 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. Lipid Peroxides 109-129 glutathione peroxidase 4 Homo sapiens 49-53 32165281-6 2020 Converging evidence on both mechanism of LPO and GPx4 enzymology indicates that LPO is initiated by alkoxyl radicals produced by ferrous iron from the hydroperoxide derivatives of lipids (LOOH), traces of which are the unavoidable drawback of aerobic metabolism. Lipid Peroxides 188-192 glutathione peroxidase 4 Homo sapiens 49-53 31065106-8 2020 Thus, blocking the host SLC7a11-GPX4 pathway serves to selectively elevate lipid peroxides in infected cells, which localize within the parasite and lead to the elimination of liver stage parasites. Lipid Peroxides 75-90 glutathione peroxidase 4 Homo sapiens 32-36 32061663-7 2020 Ferroptosis is the result of the loss of glutathione peroxidase 4 (GPX4) activity that transforms iron-dependent lipid hydroperoxides to lipid alcohols, which are inert in the biological environment. Lipid Peroxides 113-133 glutathione peroxidase 4 Homo sapiens 41-65 32061663-7 2020 Ferroptosis is the result of the loss of glutathione peroxidase 4 (GPX4) activity that transforms iron-dependent lipid hydroperoxides to lipid alcohols, which are inert in the biological environment. Lipid Peroxides 113-133 glutathione peroxidase 4 Homo sapiens 67-71 31574461-12 2020 In summary, GPx4 and fer-1 in the presence of ferrous iron, produces, by distinct mechanism, the most relevant anti-ferroptotic effect, i.e the disappearance of initiating lipid hydroperoxides. Lipid Peroxides 172-192 glutathione peroxidase 4 Homo sapiens 12-16 30888116-4 2019 The lipid hydroperoxidase glutathione peroxidase 4 (GPX4) converts lipid hydroperoxides to lipid alcohols, and this process prevents the iron (Fe2+ )-dependent formation of toxic lipid reactive oxygen species (ROS). Lipid Peroxides 67-87 glutathione peroxidase 4 Homo sapiens 26-50 30888116-4 2019 The lipid hydroperoxidase glutathione peroxidase 4 (GPX4) converts lipid hydroperoxides to lipid alcohols, and this process prevents the iron (Fe2+ )-dependent formation of toxic lipid reactive oxygen species (ROS). Lipid Peroxides 67-87 glutathione peroxidase 4 Homo sapiens 52-56 28678785-6 2017 This lipid metabolism creates a dependency on pathways converging on the phospholipid glutathione peroxidase (GPX4), a selenocysteine-containing enzyme that dissipates lipid peroxides and thereby prevents the iron-mediated reactions of peroxides that induce ferroptotic cell death. Lipid Peroxides 168-183 glutathione peroxidase 4 Homo sapiens 110-114 28972104-1 2017 Increases in lipid peroxidation can cause ferroptosis, a form of cell death triggered by inhibition of glutathione peroxidase 4 (GPX4), which catalyzes the reduction of lipid peroxides and is a target of ferroptosis inducers, such as erastin. Lipid Peroxides 169-184 glutathione peroxidase 4 Homo sapiens 103-127 28972104-1 2017 Increases in lipid peroxidation can cause ferroptosis, a form of cell death triggered by inhibition of glutathione peroxidase 4 (GPX4), which catalyzes the reduction of lipid peroxides and is a target of ferroptosis inducers, such as erastin. Lipid Peroxides 169-184 glutathione peroxidase 4 Homo sapiens 129-133 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. Lipid Peroxides 77-97 glutathione peroxidase 4 Homo sapiens 0-24 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. Lipid Peroxides 77-97 glutathione peroxidase 4 Homo sapiens 26-30 29515790-3 2018 Selenium-containing enzyme glutathione peroxidase 4 (GPx4) antagonizes this damage by reducing lipid hydroperoxides to respective hydroxides. Lipid Peroxides 95-115 glutathione peroxidase 4 Homo sapiens 27-51 29515790-3 2018 Selenium-containing enzyme glutathione peroxidase 4 (GPx4) antagonizes this damage by reducing lipid hydroperoxides to respective hydroxides. Lipid Peroxides 95-115 glutathione peroxidase 4 Homo sapiens 53-57 27506793-2 2016 Small molecules that inhibit glutathione peroxidase 4 (GPX4), a phospholipid peroxidase, cause lethal accumulation of lipid peroxides and induce ferroptotic cell death. Lipid Peroxides 118-133 glutathione peroxidase 4 Homo sapiens 29-53 27506793-2 2016 Small molecules that inhibit glutathione peroxidase 4 (GPX4), a phospholipid peroxidase, cause lethal accumulation of lipid peroxides and induce ferroptotic cell death. Lipid Peroxides 118-133 glutathione peroxidase 4 Homo sapiens 55-59 25516417-6 2016 The physiological role of GPx4 is the elimination of lipid peroxides from membranes or lipoproteins. Lipid Peroxides 53-68 glutathione peroxidase 4 Homo sapiens 26-30 27836545-1 2017 The phospholipid hydroperoxidase glutathione peroxidase (GPX4) is an enzyme that reduces lipid hydroperoxides in lipid membranes. Lipid Peroxides 89-109 glutathione peroxidase 4 Homo sapiens 57-61 26042203-2 2015 Glutathione peroxidase 4 (GPx4) is a selenoenzyme that selectively neutralizes lipid hydroperoxides, and human gpx4 gene variants have been associated with obesity and cardiovascular disease in epidemiological studies. Lipid Peroxides 79-99 glutathione peroxidase 4 Homo sapiens 0-24 26042203-2 2015 Glutathione peroxidase 4 (GPx4) is a selenoenzyme that selectively neutralizes lipid hydroperoxides, and human gpx4 gene variants have been associated with obesity and cardiovascular disease in epidemiological studies. Lipid Peroxides 79-99 glutathione peroxidase 4 Homo sapiens 26-30