Inactivation of the ferroptosis regulator Gpx4 triggers acute renal failure in mice
Open accessAbstract
Ferroptosis is a non-apoptotic form of cell death induced by small molecules in specific tumour types, and in engineered cells overexpressing oncogenic RAS. Yet, its relevance in non-transformed cells and tissues is unexplored and remains enigmatic. Here, we provide direct genetic evidence that the knockout of glutathione peroxidase 4 (Gpx4) causes cell death in a pathologically relevant form of ferroptosis. Using inducible Gpx4(-/-) mice, we elucidate an essential role for the glutathione/Gpx4 axis in preventing lipid-oxidation-induced acute renal failure and associated death. We furthermore systematically evaluated a library of small molecules for possible ferroptosis inhibitors, leading to the discovery of a potent spiroquinoxalinamine derivative called Liproxstatin-1, which is able to suppress ferroptosis in cells, in Gpx4(-/-) mice, and in a pre-clinical model of ischaemia/reperfusion-induced hepatic damage. In sum, we demonstrate that ferroptosis is a pervasive and dynamic form of cell death, which, when impeded, promises substantial cytoprotection.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Depletion of intracellular glutathione reduces GPX functionality.
“Under normal circumstances, glutathione peroxidase (GPX) neutralizes lipid peroxide to lipid alcohols, but the depletion of intracellular glutathione (GSH, GPX substrate) reduces GPX functionality (Yang and Stockwell, 2008; Friedmann Angeli et al., 2014).”
From Toxic Concentrations of Glutamate Induce Ferroptosis without Affecting Mitochondrial Respiration in Rodent Brain Slice Cultures (2026) · cites this paper as Friedmann Angeli et al., 2014
Depleting GSH with BSO can induce ferroptotic RCD at least in some cases.
“depleting GSH with L-buthionine sulfoximine (BSO)—an inhibitor of the glutamate–cysteine ligase complex—can induce ferroptotic RCD (at least in some cases) [547].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [547]
GPX4 has emerged as the main endogenous inhibitor of ferroptosis by limiting lipid peroxidation through GSH-dependent reduction of lipid hydroperoxides to lipid alcohols.
“the reduced glutathione (GSH)-dependent enzyme glutathione peroxidase 4 (GPX4)—which is directly targeted by RSL3—has emerged as the main endogenous inhibitor of ferroptosis by virtue of its ability to limit lipid peroxidation by catalyzing the GSH-dependent reduction of lipid hydroperoxides to lipid alcohols [547–550].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [547]
Gpx4−/− mice display embryonic lethality with complete penetrance.
“Gpx4−/− mice display embryonic lethality with complete penetrance [547, 550, 587, 588].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [547]
Deletion of Alox15 fails to rescue the renal phenotype imposed by the Gpx4−/− genotype.
“the deletion of Alox15 fails to rescue the renal phenotype imposed by the Gpx4−/− genotype (see below) [547]”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [547]
Oxidized PUFAs accumulate upon GPX4 inactivation and can result in PUFA fragmentation and ferroptosis.
“oxidized PUFAs accumulate upon GPX4 inactivation and this can result in PUFA fragmentation and ferroptosis [539, 547].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [547]
Inducible or tissue-specific ablation of Gpx4 in mice provokes acute renal or hepatic injury, neurodegeneration, and defective immunity to infection, all preventable or mitigated by ferroptosis-inhibiting strategies.
“the inducible or tissue-specific ablation of Gpx4 in mice provokes a variety of pathological conditions, including acute renal or hepatic injury [547, 563, 589], neurodegeneration [550, 590, 591], and defective immunity to infection [567], all of which can be prevented or mitigated by ferroptosis-inhibiting strategies.”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [547]
Multiple LOXs are involved in PUFA peroxidation and consequent ferroptosis in some mouse tissues.
“suggesting that multiple LOXs are involved in PUFA peroxidation and consequent ferroptosis in some mouse tissues.”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [547]
Erastin-induced death still occurs when RIPK1/RIPK3 are knocked down or RIPK1 is inhibited, so it does not require known necroptosis components.
“Although non-apoptotic, erastin-induced cell death proceeds normally upon knockdown of RIPK1/RIPK3, or pharmacological inhibition of RIPK1 [10, 15, our unpublished data], known components of necroptosis [16].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [15]
Kidney tubular cells are especially susceptible to ferroptosis induction by Gpx4 deletion in vivo.
“Tubular cells in the kidney are also particularly susceptible to ferroptosis induction by Gpx4 deletion in vivo [15], which is intriguing in light of the enhanced sensitivity of renal cell carcinoma cell lines in culture to erastin [24].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [15]
In mice with inducible Gpx4 loss, liproxstatin-1 delays acute renal failure and extends survival compared with vehicle.
“When liprostatin-1 was administered to mice with inducible loss of Gpx4 protein, it delayed the acute renal failure caused by Gpx4 depletion, and extended survival of mice compared to a vehicle-treated group [15].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [15]
Ferroptosis-derived dead cells can release damage-associated molecular patterns (DAMPs) and lipid metabolites that can cause an elevation of inflammation.
“Ferroptosis-derived dead cells can release damage-associated molecular patterns (DAMPs) and lipid metabolites that can cause an elevation of inflammation [76,77].”
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Ferroptosis: An Iron-Dependent Form of Nonapoptotic Cell Death
Dixon, S. J., Lemberg, K. M., Lamprecht, M. R., Skouta, R., Zaitsev, E. M., Gleason, C. E., Patel, D. N., Bauer, A. J., Cantley, A. M., Yang, W. S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.042 · Cited by 18,691 · see citing works
Self-citationRegulation of Ferroptotic Cancer Cell Death by GPX4
Yang, W. S., SriRamaratnam, R., Welsch, M. E., Shimada, K., Skouta, R., Viswanathan, V. S., Cheah, J. H., Clemons, P. A., Shamji, A. F., Clish, C. B., et al. (2014) · Cell · doi:10.1016/j.cell.2013.12.010 · Cited by 7,713 · see citing works
Self-citationTietze, F. (1969) · Analytical Biochemistry · doi:10.1016/0003-2697(69)90064-5 · Cited by 6,077 · see citing works
Rouser, G., Fleischer, S., & Yamamoto, A. (1970) · Lipids · doi:10.1007/bf02531316 · Cited by 3,280 · see citing works
Wendel, A. (1981) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(81)77046-0 · Cited by 3,011 · see citing works
Galluzzi, L., Vitale, I., Abrams, J. M., Alnemri, E. S., Baehrecke, E. H., Blagosklonny, M. V., Dawson, T. M., Dawson, V. L., El-Deiry, W. S., Fulda, S., et al. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2011.96 · Cited by 2,421 · see citing works
Molecular mechanisms of necroptosis: an ordered cellular explosion
Vandenabeele, P., Galluzzi, L., Vanden Berghe, T., & Kroemer, G. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2970 · Cited by 2,382 · see citing works
The role of iron and reactive oxygen species in cell death
Dixon, S. J., & Stockwell, B. R. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1416 · Cited by 2,381 · see citing works
Self-citationBrigelius-Flohé, R., & Maiorino, M. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.11.020 · Cited by 1,904 · see citing works
Regulated necrosis: the expanding network of non-apoptotic cell death pathways
Berghe, T. V., Linkermann, A., Jouan-Lanhouet, S., Walczak, H., & Vandenabeele, P. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3737 · Cited by 1,735 · see citing works
Seiler, A., Schneider, M., Förster, H., Roth, S., Wirth, E. K., Culmsee, C., Plesnila, N., Kremmer, E., Rådmark, O., Wurst, W., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.07.005 · Cited by 1,470 · see citing works
Self-citationCytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors
Kagan, V. E., Tyurin, V. A., Jiang, J., Tyurina, Y. Y., Ritov, V. B., Amoscato, A. A., Osipov, A. N., Belikova, N. A., Kapralov, A. A., Kini, V., et al. (2005) · Nature Chemical Biology · doi:10.1038/nchembio727 · Cited by 1,256 · see citing works
Self-citationFerrostatins Inhibit Oxidative Lipid Damage and Cell Death in Diverse Disease Models
Skouta, R., Dixon, S. J., Wang, J., Dunn, D. E., Orman, M., Shimada, K., Rosenberg, P. A., Lo, D. C., Weinberg, J. M., Linkermann, A., et al. (2014) · Journal of the American Chemical Society · doi:10.1021/ja411006a · Cited by 1,146 · see citing works
Self-citationOxygen sensitivity severely limits the replicative lifespan of murine fibroblasts
Parrinello, S., Samper, E., Krtolica, A., Goldstein, J., Melov, S., & Campisi, J. (2003) · Nature Cell Biology · doi:10.1038/ncb1024 · Cited by 1,116 · see citing works
Targeting IAP proteins for therapeutic intervention in cancer
Fulda, S., & Vucic, D. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3627 · Cited by 837 · see citing works
Yant, L. J., Ran, Q., Rao, L., Van Remmen, H., Shibatani, T., Belter, J. G., Motta, L., Richardson, A., & Prolla, T. A. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01360-6 · Cited by 797 · see citing works
Regulation of RIP1 kinase signalling at the crossroads of inflammation and cell death
Ofengeim, D., & Yuan, J. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3683 · Cited by 615 · see citing works
Conrad, M., & Sato, H. (2011) · Amino Acids · doi:10.1007/s00726-011-0867-5 · Cited by 607 · see citing works
Self-citationTwo independent pathways of regulated necrosis mediate ischemia–reperfusion injury
Linkermann, A., Bräsen, J. H., Darding, M., Jin, M. K., Sanz, A. B., Heller, J.-O., Zen, F. D., Weinlich, R., Ortíz, A., Walczak, H., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305538110 · Cited by 568 · see citing works
Takahashi, N., Duprez, L., Grootjans, S., Cauwels, A., Nerinckx, W., DuHadaway, J. B., Goossens, V, Roelandt, R., Van Hauwermeiren, F., Libert, C., et al. (2012) · Cell Death & Disease · doi:10.1038/cddis.2012.176 · Cited by 465 · see citing works
Nomura, K., Imai, H., Koumura, T., Kobayashi, T., & Nakagawa, Y. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3510183 · Cited by 373 · see citing works
Mitochondrial glutathione peroxidase 4 disruption causes male infertility
Schneider, M., Förster, H., Boersma, A., Seiler, A., Wehnes, H., Sinowatz, F., Neumüller, C., Deutsch, M. J., Walch, A. K., de Angelis, M. H., et al. (2009) · The FASEB Journal · doi:10.1096/fj.09-132795 · Cited by 328 · see citing works
Self-citationA chemoproteomic platform to quantitatively map targets of lipid-derived electrophiles
Wang, C., Weerapana, E., Blewett, M. M., & Cravatt, B. F. (2013) · Nature Methods · doi:10.1038/nmeth.2759 · Cited by 303 · see citing works
Disruption of 12/15-Lipoxygenase Expression in Peritoneal Macrophages
Sun, D., & Funk, C. D. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.39.24055 · Cited by 256 · see citing works
Nomura, K., Imai, H., Koumura, T., et al. (2000) · Biochemical Journal · doi:10.1042/bj3510183 · Cited by 255 · see citing works
Proximal tubule H-ferritin mediates iron trafficking in acute kidney injury
Zarjou, A., Bolisetty, S., Joseph, R., Traylor, A., Apostolov, E. O., Arosio, P., Balla, J., Verlander, J. W., Darshan, D., Kühn, L. C., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci67867 · Cited by 210 · see citing works
Hameyer, D., Loonstra, A., Eshkind, L. G., Schmitt, S., Antunes, C., Groen, A., Bindels, E. M., Jonkers, J., Krimpenfort, P., Meuwissen, R. L. J., et al. (2007) · Physiological Genomics · doi:10.1152/physiolgenomics.00019.2007 · Cited by 200 · see citing works
Liang, H., Yoo, S.-E., Na, R., Walter, C. A., Richardson, A., & Ran, Q. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.032839 · Cited by 191 · see citing works
RIPK1 is not essential for TNFR1-induced activation of NF-κB
Wong, W. W.-L., Gentle, I. E., Nachbur, U., Anderton, H., Vaux, D. L., & Silke, J. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.178 · Cited by 183 · see citing works
Wortmann, M., Schneider, M., Pircher, J., Hellfritsch, J., Aichler, M., Naidu, V. M., Kölle, P., Kuhlencordt, P. J., Walch, A. K., Pohl, U., et al. (2013) · Circulation Research · doi:10.1161/circresaha.113.279984 · Cited by 160 · see citing works
Self-citationA mitochondrial pathway for biosynthesis of lipid mediators
Tyurina, Y. Y., Poloyac, S. M., Tyurin, V. A., Kapralov, A. A., Jiang, J., Anthonymuthu, T. S., Kapralova, V. I., Vikulina, A. S., Jung, M.-Y., Epperly, M. W., et al. (2014) · Nature Chemistry · doi:10.1038/nchem.1924 · Cited by 159 · see citing works
Self-citationGilbert, N. C., Rui, Z., Neau, D. B., Waight, M. T., Bartlett, S. G., Boeglin, W. E., BRASH, A. R., & Newcomer, M. E. (2012) · The FASEB Journal · doi:10.1096/fj.12-205286 · Cited by 155 · see citing works
Mitochondrial targeting of quinones: Therapeutic implications
Cochemé, H. M., Kelso, G. F., James, A. M., Ross, M. F., Trnka, J., Mahendiran, T., Asin-Cayuela, J., Blaikie, F. H., Manas, A. B., Porteous, C. M., et al. (2007) · Mitochondrion · doi:10.1016/j.mito.2007.02.007 · Cited by 138 · see citing works
Conrad, M., Sandin, Å., Förster, H., Seiler, A., Frijhoff, J., Dagnell, M., Bornkamm, G. W., Rådmark, O., van Huijsduijnen, R. H., Aspenström, P., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1007909107 · Cited by 99 · see citing works
Self-citationOxidative lipidomics of γ-irradiation-induced intestinal injury
Tyurina, Y. Y., Tyurin, V. A., Epperly, M. W., Greenberger, J. S., & Kagan, V. E. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.08.021 · Cited by 86 · see citing works
Self-citationKiermayer, C., Conrad, M., Schneider, M., Schmidt, J., & Brielmeier, M. (2007) · genesis · doi:10.1002/dvg.20244 · Cited by 71 · see citing works
Self-citationHerbach, N., Schairer, I., Blutke, A., et al. (2009) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.90665.2008 · Cited by 69 · see citing works
Self-citationMcIntyre, T. M. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.03.004 · Cited by 65 · see citing works
Identification of mosquito sterol carrier protein-2 inhibitors
Kim, M.-S., Wessely, V., & Lan, Q. (2005) · Journal of Lipid Research · doi:10.1194/jlr.m400389-jlr200 · Cited by 52 · see citing works
Vila, A., Levchenko, V., Korytowski, W., et al. (2004) · Biochemistry · doi:10.1021/bi0491200 · Cited by 51 · see citing works
Mannes, A. M., Seiler, A., Bosello-Travain, V., Maiorino, M., & Conrad, M. (2011) · The FASEB Journal · doi:10.1096/fj.10-177147 · Cited by 51 · see citing works
Self-citationCharacterization of cardiolipins and their oxidation products by LC–MS analysis
Tyurina, Y. Y., Domingues, R. M., Tyurin, V. A., Maciel, E. A., Domingues, P. M., Amoscato, A. A., Bayır, H., & Kagan, V. E. (2013) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2013.12.003 · Cited by 49 · see citing works
Self-citationKriska, T., Pilat, A. K., Schmitt, J. C., & Girotti, A. W. (2010) · Journal of Lipid Research · doi:10.1194/jlr.m008342 · Cited by 30 · see citing works
Unconventional RORγt+ T Cells Drive Hepatic Ischemia Reperfusion Injury
Eggenhofer, E., Rovira, J., Sabet-Baktach, M., et al. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1202975 · Cited by 29 · see citing works
Self-citationMonolysocardiolipin: improved preparation with high yield
Kim, J. H., & Hoppel, C. L. (2010) · Journal of Lipid Research · doi:10.1194/jlr.d010587 · Cited by 14 · see citing works
Tanaka, R., Hatate, H., Ito, M., et al. (2006) · Fisheries Science · doi:10.1111/j.1444-2906.2006.01197.x · Cited by 9 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Ferroptosis: A Regulated Cell Death Nexus Linking Metabolism, Redox Biology, and Disease
Stockwell, B. R., Friedmann Angeli, J. P., Bayir, H., Bush, A. I., Conrad, M., Dixon, S. J., Fulda, S., Gascón, S., Hatzios, S. K., Kagan, V. E., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.021 · Cited by 7,695 · see citing works
Self-citationGalluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works
Self-citationACSL4 dictates ferroptosis sensitivity by shaping cellular lipid composition
Doll, S., Proneth, B., Tyurina, Y. Y., Panzilius, E., Kobayashi, S., Ingold, I., Irmler, M., Beckers, J., Aichler, M., Walch, A., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2239 · Cited by 4,293 · see citing works
Self-citationFerroptosis: past, present and future
Li, J., Cao, F., Yin, H.-L., Huang, Z.-J., Lin, Z.-T., Mao, N., Sun, B., & Wang, G. (2020) · Cell Death & Disease · doi:10.1038/s41419-020-2298-2 · Cited by 4,171 · see citing works
Ferroptosis: process and function
Xie, Y., Hou, W., Song, X., Yu, Y., Huang, J., Sun, X., Kang, R., & Tang, D. (2016) · Cell Death & Differentiation · doi:10.1038/cdd.2015.158 · Cited by 3,727 · see citing works
Ferroptosis: Death by Lipid Peroxidation
Yang, W. S., & Stockwell, B. R. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.10.014 · Cited by 3,088 · see citing works
Self-citationOxidized arachidonic and adrenic PEs navigate cells to ferroptosis
Kagan, V. E., Mao, G., Qu, F., Angeli, J. P. F., Doll, S., Croix, C. S., Dar, H. H., Liu, B., Tyurin, V. A., Ritov, V. B., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2238 · Cited by 3,029 · see citing works
Self-citationAutophagy promotes ferroptosis by degradation of ferritin
Hou, W., Xie, Y., Song, X., Sun, X., Lotze, M. T., Zeh, H. J., Kang, R., & Tang, D. (2016) · Autophagy · doi:10.1080/15548627.2016.1187366 · Cited by 2,332 · see citing works
Peroxidation of polyunsaturated fatty acids by lipoxygenases drives ferroptosis
Yang, W. S., Kim, K. J., Gaschler, M. M., Patel, M., Shchepinov, M. S., & Stockwell, B. R. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1603244113 · Cited by 2,329 · see citing works
Self-citationTargeting Ferroptosis as a Vulnerability in Cancer
Lei, G., Zhuang, L., & Gan, B. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-022-00459-0 · Cited by 2,252 · see citing works
Reactive Oxygen Species-Induced Lipid Peroxidation in Apoptosis, Autophagy, and Ferroptosis
Su, L.-J., Zhang, J.-H., Gomez, H., Murugan, R., Hong, X., Xu, D., Jiang, F., & Peng, Z.-Y. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/5080843 · Cited by 2,166 · see citing works
Glutaminolysis and transferrin regulate ferroptosis
Gao, M., Monian, P., Quadri, N., Ramasamy, R., & Jiang, X. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.06.011 · Cited by 2,069 · see citing works
Sun, X., Ou, Z., Chen, R., Niu, X., Chen, D., Kang, R., & Tang, D. (2016) · Hepatology · doi:10.1002/hep.28251 · Cited by 2,012 · see citing works
Kastenhuber, E. R., & Lowe, S. W. (2017) · Cell · doi:10.1016/j.cell.2017.08.028 · Cited by 1,906 · see citing works
Lipid peroxidation and ferroptosis: The role of GSH and GPx4
Ursini, F., & Maiorino, M. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.02.027 · Cited by 1,954 · see citing works
Ferroptosis is an autophagic cell death process
Gao, M., Monian, P., Pan, Q., Zhang, W., Xiang, J., & Jiang, X. (2016) · Cell Research · doi:10.1038/cr.2016.95 · Cited by 1,899 · see citing works
Drug-tolerant persister cancer cells are vulnerable to GPX4 inhibition
Hangauer, M. J., Viswanathan, V. S., Ryan, M. J., Bole, D., Eaton, J. K., Matov, A., Galeas, J., Dhruv, H. D., Berens, M. E., Schreiber, S. L., et al. (2017) · Nature · doi:10.1038/nature24297 · Cited by 1,799 · see citing works
Role of GPX4 in ferroptosis and its pharmacological implication
Seibt, T. M., Proneth, B., & Conrad, M. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.014 · Cited by 1,520 · see citing works
Self-citationCao, J. Y., & Dixon, S. J. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2194-1 · Cited by 1,515 · see citing works
Ferroptosis: Mechanisms and links with diseases
Yan, H.-F., Zou, T., Tuo, Q.-Z., Xu, S., Li, H., Belaidi, A. A., & Lei, P. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00428-9 · Cited by 1,471 · see citing works
Jomova, K., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2024) · Archives of Toxicology · doi:10.1007/s00204-024-03696-4 · Cited by 1,445 · see citing works
Cysteine depletion induces pancreatic tumor ferroptosis in mice
Badgley, M. A., Kremer, D. M., Maurer, H. C., DelGiorno, K. E., Lee, H.-J., Purohit, V., Sagalovskiy, I. R., Ma, A., Kapilian, J., Firl, C. E. M., et al. (2020) · Science · doi:10.1126/science.aaw9872 · Cited by 1,294 · see citing works
Self-citationIdentification of ACSL4 as a biomarker and contributor of ferroptosis
Yuan, H., Li, X., Zhang, X., Kang, R., & Tang, D. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.08.124 · Cited by 1,071 · see citing works
Human Haploid Cell Genetics Reveals Roles for Lipid Metabolism Genes in Nonapoptotic Cell Death
Dixon, S. J., Winter, G. E., Musavi, L. S., Lee, E. D., Snijder, B., Rebsamen, M., Superti-Furga, G., & Stockwell, B. R. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00245 · Cited by 1,043 · see citing works
Self-citationThe Tumor Suppressor p53 Limits Ferroptosis by Blocking DPP4 Activity
Xie, Y., Zhu, S., Song, X., Sun, X., Fan, Y., Liu, J., Zhong, M., Yuan, H., Zhang, L., Billiar, T. R., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.07.055 · Cited by 952 · see citing works
Ferroptosis: Role of lipid peroxidation, iron and ferritinophagy
Latunde-Dada, G. O. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.05.019 · Cited by 892 · see citing works
Zou, Y., Palte, M. J., Deik, A. A., Li, H., Eaton, J. K., Wang, W., Tseng, Y.-Y., Deasy, R., Kost-Alimova, M., Dančík, V., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09277-9 · Cited by 887 · see citing works
Hambright, W. S., Fonseca, R. S., Chen, L., Na, R., & Ran, Q. (2017) · Redox Biology · doi:10.1016/j.redox.2017.01.021 · Cited by 851 · see citing works
Resolving the Role of Lipoxygenases in the Initiation and Execution of Ferroptosis
Shah, R., Shchepinov, M. S., & Pratt, D. A. (2018) · ACS Central Science · doi:10.1021/acscentsci.7b00589 · Cited by 782 · see citing works
The emerging role of ferroptosis in inflammation
Sun, Y., Chen, P., Zhai, B., Zhang, M., Xiang, Y., Fang, J., Xu, S., Gao, Y., Chen, X., Sui, X., et al. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110108 · Cited by 739 · see citing works
RSL3 Drives Ferroptosis Through GPX4 Inactivation and ROS Production in Colorectal Cancer
Sui, X., Zhang, R., Liu, S., Duan, T., Zhai, L., Zhang, M., Han, X., Xiang, Y., Huang, X., Lin, H., et al. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01371 · Cited by 703 · see citing works
Do Van, B., Gouel, F., Jonneaux, A., Timmerman, K., Gelé, P., Pétrault, M., Bastide, M., Laloux, C., Moreau, C., Bordet, R., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.05.011 · Cited by 689 · see citing works
HSPB1 as a novel regulator of ferroptotic cancer cell death
Sun, X., Ou, Z., Xie, M., Kang, R., Fan, Y., Niu, X., Wang, H., Cao, L., & Tang, D. (2015) · Oncogene · doi:10.1038/onc.2015.32 · Cited by 666 · see citing works
Park, M. W., Cha, H. W., Kim, J., Kim, J. H., Yang, H., Yoon, S., Boonpraman, N., Yi, S. S., Yoo, I. D., & Moon, J.-S. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101947 · Cited by 683 · see citing works
Kim, S. E., Zhang, L., Ma, K., Riegman, M., Chen, F., Ingold, I., Conrad, M., Turker, M. Z., Gao, M., Jiang, X., et al. (2016) · Nature Nanotechnology · doi:10.1038/nnano.2016.164 · Cited by 622 · see citing works
Self-citationRegulated necrosis: disease relevance and therapeutic opportunities
Conrad, M., Angeli, J. P. F., Vandenabeele, P., & Stockwell, B. R. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2015.6 · Cited by 630 · see citing works
Self-citationHSPA5 Regulates Ferroptotic Cell Death in Cancer Cells
Zhu, S., Zhang, Q., Sun, X., Zeh, H. J., Lotze, M. T., Kang, R., & Tang, D. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-1979 · Cited by 576 · see citing works
Ferroptosis Inhibition: Mechanisms and Opportunities
Angeli, J. P. F., Shah, R., Pratt, D. A., & Conrad, M. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.02.005 · Cited by 563 · see citing works
Self-citationApoptosis and necroptosis in the liver: a matter of life and death
Schwabe, R. F., & Luedde, T. (2018) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-018-0065-y · Cited by 582 · see citing works
Involvement of cigarette smoke-induced epithelial cell ferroptosis in COPD pathogenesis
Yoshida, M., Minagawa, S., Araya, J., Sakamoto, T., Hara, H., Tsubouchi, K., Hosaka, Y., Ichikawa, A., Saito, N., Kadota, T., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10991-7 · Cited by 572 · see citing works
Ferroptosis, but Not Necroptosis, Is Important in Nephrotoxic Folic Acid–Induced AKI
Martin-Sanchez, D., Ruiz-Andres, O., Poveda, J., Carrasco, S., Cannata-Ortiz, P., Sanchez-Niño, M. D., Ruiz Ortega, M., Egido, J., Linkermann, A., Ortiz, A., et al. (2017) · Journal of the American Society of Nephrology · doi:10.1681/asn.2015121376 · Cited by 564 · see citing works
Iron and cancer: recent insights
Manz, D. H., Blanchette, N. L., Paul, B. T., Torti, F. M., & Torti, S. V. (2016) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.13008 · Cited by 507 · see citing works
Regulation of lipid peroxidation and ferroptosis in diverse species
Conrad, M., Kagan, V. E., Bayir, H., Pagnussat, G. C., Head, B., Traber, M. G., & Stockwell, B. R. (2018) · Genes & Development · doi:10.1101/gad.314674.118 · Cited by 544 · see citing works
Self-citationIdentification of artesunate as a specific activator of ferroptosis in pancreatic cancer cells
Eling, N., Reuter, L., Hazin, J., Hamacher-Brady, A., & Brady, N. R. (2015) · Oncoscience · doi:10.18632/oncoscience.160 · Cited by 524 · see citing works
The multifaceted role of reactive oxygen species in tumorigenesis
Kirtonia, A., Sethi, G., & Garg, M. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03536-5 · Cited by 452 · see citing works
The Role of Ferroptosis in Cancer Development and Treatment Response
Lu, B., Chen, X. B., Ying, M. D., He, Q. J., Cao, J., & Yang, B. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00992 · Cited by 444 · see citing works
ATF4 promotes angiogenesis and neuronal cell death and confers ferroptosis in a xCT-dependent manner
Chen, D., Fan, Z., Rauh, M., Buchfelder, M., Eyupoglu, I. Y., & Savaskan, N. (2017) · Oncogene · doi:10.1038/onc.2017.146 · Cited by 421 · see citing works
The chemistry and biology of ferroptosis
Stockwell, B. R., & Jiang, X. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.03.013 · Cited by 429 · see citing works
Self-citationThe application of Ferroptosis in diseases
Qiu, Y., Cao, Y., Cao, W., Jia, Y., & Lu, N. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104919 · Cited by 415 · see citing works
Phototherapy in cancer treatment: strategies and challenges
Cai, Y., Chai, T., Nguyen, W., Liu, J., Xiao, E., Ran, X., Ran, Y., Du, D., Chen, W., & Chen, X. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02140-y · Cited by 453 · see citing works
Lipid Metabolism and Ferroptosis
Lee, J.-Y., Kim, W. K., Bae, K.-H., Lee, S. C., & Lee, E.-W. (2021) · Biology · doi:10.3390/biology10030184 · Cited by 374 · see citing works
Targeting iron metabolism in drug discovery and delivery
Crielaard, B. J., Lammers, T., & Rivella, S. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.248 · Cited by 352 · see citing works
An essential role for functional lysosomes in ferroptosis of cancer cells
Torii, S., Shintoku, R., Kubota, C., Yaegashi, M., Torii, R., Sasaki, M., Suzuki, T., Mori, M., Yoshimoto, Y., Takeuchi, T., et al. (2016) · Biochemical Journal · doi:10.1042/bj20150658 · Cited by 349 · see citing works
iPLA2β-mediated lipid detoxification controls p53-driven ferroptosis independent of GPX4
Chen, D., Chu, B., Yang, X., Liu, Z., Jin, Y., Kon, N., Rabadan, R., Jiang, X., Stockwell, B. R., & Gu, W. (2021) · Nature Communications · doi:10.1038/s41467-021-23902-6 · Cited by 348 · see citing works
Self-citationQi, J., Kim, J.-W., Zhou, Z., Lim, C.-W., & Kim, B. (2020) · The American Journal of Pathology · doi:10.1016/j.ajpath.2019.09.011 · Cited by 338 · see citing works
Unraveling the Potential Role of Glutathione in Multiple Forms of Cell Death in Cancer Therapy
Lv, H., Zhen, C., Liu, J., Yang, P., Hu, L., & Shang, P. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/3150145 · Cited by 320 · see citing works
Dixon, S. J. (2017) · Immunological Reviews · doi:10.1111/imr.12533 · Cited by 314 · see citing works
Glutathione peroxidase 4 and vitamin E cooperatively prevent hepatocellular degeneration
Carlson, B. A., Tobe, R., Yefremova, E., Tsuji, P. A., Hoffmann, V. J., Schweizer, U., Gladyshev, V. N., Hatfield, D. L., & Conrad, M. (2016) · Redox Biology · doi:10.1016/j.redox.2016.05.003 · Cited by 316 · see citing works
Self-citationDietary lipids fuel GPX4-restricted enteritis resembling Crohn’s disease
Mayr, L., Grabherr, F., Schwärzler, J., Reitmeier, I., Sommer, F., Gehmacher, T., Niederreiter, L., He, G.-W., Ruder, B., Kunz, K. T. R., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15646-6 · Cited by 292 · see citing works
Heat stress induces ferroptosis-like cell death in plants
Distéfano, A. M., Martin, M. V., Córdoba, J. P., Bellido, A. M., D’Ippólito, S., Colman, S. L., Soto, D., Roldán, J. A., Bartoli, C. G., Zabaleta, E. J., et al. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201605110 · Cited by 268 · see citing works
Self-citationTumor cell plasticity in targeted therapy-induced resistance: Mechanisms and new strategies
Shi, Z.-D., Pang, K., Wu, Z.-X., Dong, Y., Hao, L., Qin, J.-X., Wang, W., Chen, Z.-S., & Han, C.-H. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01383-x · Cited by 256 · see citing works
Iron and thiol redox signaling in cancer: an exquisite balance to escape ferroptosis
Toyokuni, S., Ito, F., Yamashita, K., Okazaki, Y., & Akatsuka, S. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.04.024 · Cited by 252 · see citing works
Dar, H. H., Tyurina, Y. Y., Mikulska-Ruminska, K., Shrivastava, I., Ting, H.-C., Tyurin, V. A., Krieger, J., St. Croix, C. M., Watkins, S., Bayir, E., et al. (2018) · Journal of Clinical Investigation · doi:10.1172/jci99490 · Cited by 251 · see citing works
Self-citationThirty years of NRF2: advances and therapeutic challenges.
Zhang, D. D. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-025-01145-0 · Cited by 282 · see citing works
Glutathione peroxidase 4 prevents necroptosis in mouse erythroid precursors
Canli, Ö., Alankuş, Y. B., Grootjans, S., Vegi, N., Hültner, L., Hoppe, P. S., Schroeder, T., Vandenabeele, P., Bornkamm, G. W., & Greten, F. R. (2016) · Blood · doi:10.1182/blood-2015-06-654194 · Cited by 247 · see citing works
Self-citationFerroptosis is involved in acetaminophen induced cell death
Lőrincz, T., Jemnitz, K., Kardon, T., Mandl, J., & Szarka, A. (2015) · Pathology & Oncology Research · doi:10.1007/s12253-015-9946-3 · Cited by 219 · see citing works
Muri, J., Thut, H., Bornkamm, G. W., & Kopf, M. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.10.070 · Cited by 198 · see citing works
Miao, R., Fang, X., Zhang, Y., Wei, J., Zhang, Y., & Tian, J. (2023) · Cell Death & Disease · doi:10.1038/s41419-023-05708-0 · Cited by 192 · see citing works
Youssef, L. A., Rebbaa, A., Pampou, S., Weisberg, S. P., Stockwell, B. R., Hod, E. A., & Spitalnik, S. L. (2018) · Blood · doi:10.1182/blood-2017-12-822619 · Cited by 186 · see citing works
Self-citationChaudhary, N., Choudhary, B. S., Shah, S. G., Khapare, N., Dwivedi, N., Gaikwad, A., Joshi, N., Raichanna, J., Basu, S., Gurjar, M., et al. (2021) · International Journal of Cancer · doi:10.1002/ijc.33711 · Cited by 185 · see citing works
APR-246 induces early cell death by ferroptosis in acute myeloid leukemia
Birsen, R., Larrue, C., Decroocq, J., Johnson, N., Guiraud, N., Gotanegre, M., Cantero-Aguilar, L., Grignano, E., Huynh, T., Fontenay, M., et al. (2021) · Haematologica · doi:10.3324/haematol.2020.259531 · Cited by 182 · see citing works
Activation of Glutathione Peroxidase 4 as a Novel Anti-inflammatory Strategy
Li, C., Deng, X., Xie, X., Liu, Y., Friedmann Angeli, J. P., & Lai, L. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01120 · Cited by 183 · see citing works
Self-citationFerroptosis at the crossroads of infection, aging and cancer
Toyokuni, S., Yanatori, I., Kong, Y., Zheng, H., Motooka, Y., & Jiang, L. (2020) · Cancer Science · doi:10.1111/cas.14496 · Cited by 142 · see citing works
CREB stimulates GPX4 transcription to inhibit ferroptosis in lung adenocarcinoma
Wang, Z., Zhang, X., Tian, X., Yang, Y., Ma, L., Wang, J., & Yu, Y. (2021) · Oncology Reports · doi:10.3892/or.2021.8039 · Cited by 122 · see citing works
Toyokuni, S. (2016) · Pathology International · doi:10.1111/pin.12396 · Cited by 111 · see citing works
Selective ferroptosis vulnerability due to familial Alzheimer’s disease presenilin mutations
Greenough, M. A., Lane, D. J. R., Balez, R., Anastacio, H. T. D., Zeng, Z., Ganio, K., McDevitt, C. A., Acevedo, K., Belaidi, A. A., Koistinaho, J., et al. (2022) · Cell Death & Differentiation · doi:10.1038/s41418-022-01003-1 · Cited by 102 · see citing works
An Overview of Pathways of Regulated Necrosis in Acute Kidney Injury
Kers, J., Leemans, J. C., & Linkermann, A. (2016) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2016.03.002 · Cited by 80 · see citing works
RelB-activated GPX4 inhibits ferroptosis and confers tamoxifen resistance in breast cancer
Xu, Z., Wang, X., Sun, W., Xu, F., Kou, H., Hu, W., Zhang, Y., Jiang, Q., Tang, J., & Xu, Y. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102952 · Cited by 76 · see citing works
NUPR1 inhibitor ZZW-115 induces ferroptosis in a mitochondria-dependent manner
Huang, C., Santofimia-Castaño, P., Liu, X., Xia, Y., Peng, L., Gotorbe, C., Neira, J. L., Tang, D., Pouyssegur, J., & Iovanna, J. (2021) · Cell Death Discovery · doi:10.1038/s41420-021-00662-2 · Cited by 76 · see citing works
Metabolism and iron signaling in ferroptotic cell death
Gao, M., Monian, P., & Jiang, X. (2015) · Oncotarget · doi:10.18632/oncotarget.5671 · Cited by 71 · see citing works
Iron Pathophysiology in Alzheimer’s Diseases
Wang, T., Xu, S.-F., Fan, Y.-G., Li, L.-B., & Guo, C. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-9589-5_5 · Cited by 64 · see citing works
MiR-378a-3p/ SLC7A11 regulate ferroptosis in nerve injury induced by lead exposure
Wang, W., Shi, F., Cui, J., Pang, S., Zheng, G., & Zhang, Y. (2022) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2022.113639 · Cited by 47 · see citing works
Ma, X., Dong, X., Xu, Y., Ma, N., Wei, M., Xie, X., Lu, Y., Cao, W., Lu, G., & Li, W. (2022) · Antioxidants · doi:10.3390/antiox12010100 · Cited by 41 · see citing works
Tan, X., Huang, X., Niu, B., Guo, X., Lei, X., & Qu, B. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1102158 · Cited by 40 · see citing works
Dihydroxy‐Metabolites of Dihomo‐γ‐linolenic acid drive ferroptosis‐mediated neurodegeneration
Sarparast, M., Pourmand, E., Hinman, J., Vonarx, D., Reason, T., Zhang, F., Paithankar, S., Chen, B., Borhan, B., Watts, J. L., et al. (2023) · ACS Central Science · doi:10.1021/acscentsci.3c00052 · Cited by 33 · see citing works
A Class of Disulfide Compounds Suppresses Ferroptosis by Stabilizing GPX4
Liu, J.-P., Cen, S.-Y., Xue, Z., Wang, T.-X., Gao, Y., Zheng, J., Zhang, C., Hu, J., Nie, S., Xiong, Y., et al. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.2c00445 · Cited by 29 · see citing works
Anti-cancer effects of fenbendazole on 5-fluorouracil-resistant colorectal cancer cells
Park, D., Lee, J.-H., & Yoon, S.-P. (2022) · The Korean Journal of Physiology & Pharmacology · doi:10.4196/kjpp.2022.26.5.377 · Cited by 23 · see citing works
Multi-platform-based characterization of ferroptosis in human colorectal cancer
Zhong, Y., Zhang, W., Yu, H., Lin, L., Gao, X., He, J., Li, D., Chen, Y., Zeng, Z., Xu, Y., et al. (2022) · iScience · doi:10.1016/j.isci.2022.104750 · Cited by 14 · see citing works
AP-1 inhibitor induces ferroptosis via the PI3K/AKT pathway in multiple myeloma cells
Tang, S., Liu, J., Li, F., Yan, Y., Long, X., & Fu, Y. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e34397 · Cited by 13 · see citing works
Richards, S. E. V., Yang, M., Deik, A. A., & Ricq, E. L. (2025) · Neurochemical Research · doi:10.1007/s11064-025-04463-2 · Cited by 3 · see citing works
Vaglio-Garro, A., Theuermann, M., Sweis, K. E., Zavadskis, S., Kokas, M., Környei, Z., Karas, M., Tretter, L., Komlódi, T., Weidinger, A., et al. (2026) · eneuro · doi:10.1523/eneuro.0439-25.2026
- Authors
- Friedmann Angeli, J. P., Schneider, M., Proneth, B., Tyurina, Y. Y., Tyurin, V. A., Hammond, V. J., Herbach, N., Aichler, M., Walch, A., Eggenhofer, E., Basavarajappa, D., Rådmark, O., Kobayashi, S., Seibt, T., Beck, H., Neff, F., Esposito, I., Wanke, R., Förster, H., Yefremova, O., Heinrichmeyer, M., Bornkamm, G. W., Geissler, E. K., Thomas, S. B., Stockwell, B. R., O’Donnell, V. B., Kagan, V. E., Schick, J. A., & Conrad, M.
- Affiliations
- LMU Klinikum (DE)
- Helmholtz Munich (DE)
- University of Pittsburgh (US)
- Cardiff University (GB)
- Ludwig-Maximilians-Universität München (DE)
- University Hospital Regensburg (DE)
- Karolinska Institutet (SE)
- Yamagata University (JP)
- Institut für Chirurgische Forschung (DE)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Conrad, Marcus
- ORCID
- Schneider, Manuela
- Proneth, Bettina
- Tyurina, Yulia Y.
- Tyurin, Vladimir A.
- Herbach, Nadja
- Walch, Axel
- Eggenhofer, Elke
- Basavarajappa, Devaraj
- Rådmark, Olof
- Kobayashi, Sho
- Seibt, Tobias
- Beck, Heike
- Wanke, Rüdiger
- Geissler, Edward K.
- Stockwell, Brent R.
- O’Donnell, Valerie B.
- Kagan, Valerian E.
- Schick, Joel A.
- Conrad, Marcus
- Venue
- Nature Cell Biology
- Published
- 2014-11-17
- Volume
- 16
- Issue
- 12
- Pages
- 1180-1191
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC4894846
- OpenAlex
- W2035898183
- Cited by
- 3,732
- References
- 46
- Citations by year
- 2026: 425 · 2025: 505 · 2024: 615 · 2023: 571 · 2022: 526 · 2021: 389 · 2020: 243 · 2019: 169 · 2018: 103 · 2017: 82 · 2016: 63 · 2015: 36 · 2014: 1
- FWCI
- 48.68
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- University of Regensburg Publication Server (University of Regensburg) (submittedVersion)
- ORCA Online Research @Cardiff (Cardiff University) (submittedVersion)
- Funders
- National Heart, Lung, and Blood Institute (P01HL114453)
- Topics
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Ferroptosis and cancer prognosis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Keywords
- ferroptosis, GPX4, acute kidney injury, lipid peroxidation, glutathione, ferroptosis inhibitors, liproxstatin-1, ischemia-reperfusion injury, liver injury, non-apoptotic cell death
- MeSH terms
- Phospholipid Hydroperoxide Glutathione Peroxidase, Animals, Arachidonate 12-Lipoxygenase, Arachidonate 15-Lipoxygenase, Cardiolipins, Cell Line, Glutathione Peroxidase, Humans, Imidazoles, Indoles, Kidney, Male, Mice, Inbred C57BL, Mitochondria, Peroxidases, Phosphatidylcholines, Phosphatidylethanolamines, Quinoxalines, Spiro Compounds, Lipid Peroxidation, Reperfusion Injury, Apoptosis, Mice, Knockout, In Situ Nick-End Labeling, Mice, Acute Kidney Injury
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review