Ferroptosis: A Regulated Cell Death Nexus Linking Metabolism, Redox Biology, and Disease
Open accessAbstract
Ferroptosis is a form of regulated cell death characterized by the iron-dependent accumulation of lipid hydroperoxides to lethal levels. Emerging evidence suggests that ferroptosis represents an ancient vulnerability caused by the incorporation of polyunsaturated fatty acids into cellular membranes, and cells have developed complex systems that exploit and defend against this vulnerability in different contexts. The sensitivity to ferroptosis is tightly linked to numerous biological processes, including amino acid, iron, and polyunsaturated fatty acid metabolism, and the biosynthesis of glutathione, phospholipids, NADPH, and coenzyme Q 10. Ferroptosis has been implicated in the pathological cell death associated with degenerative diseases (i.e., Alzheimer's, Huntington's, and Parkinson's diseases), carcinogenesis, stroke, intracerebral hemorrhage, traumatic brain injury, ischemia-reperfusion injury, and kidney degeneration in mammals and is also implicated in heat stress in plants. Ferroptosis may also have a tumor-suppressor function that could be harnessed for cancer therapy. This Primer reviews the mechanisms underlying ferroptosis, highlights connections to other areas of biology and medicine, and recommends tools and guidelines for studying this emerging form of regulated cell death.
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?
Ferroptosis is involved in crocidolite-induced macrophage necrosis.
“indicating the involvement of ferroptosis [32] in crocidolite-induced macrophage necrosis.”
From Asbestos conceives Fe(II)-dependent mutagenic stromal milieu through ceaseless macrophage ferroptosis and β-catenin induction in mesothelium (2020) · cites this paper as [32]
Crocidolite generates a catalytic Fe(II)-rich mutagenic environment for mesothelial cells by necrotizing macrophages with lysosomal cell death and ferroptosis.
“Thus, crocidolite generated catalytic Fe(II)-rich mutagenic environment for mesothelial cells by necrotizing macrophages with lysosomal cell death and ferroptosis.”
From Asbestos conceives Fe(II)-dependent mutagenic stromal milieu through ceaseless macrophage ferroptosis and β-catenin induction in mesothelium (2020) · cites this paper as [32]
The ‘Ferroptosis applications in neoplastic diseases’ section associates excess iron with carcinogenesis, and the ‘Iron metabolism’ section describes iron’s role in ferroptosis; neither addresses the claimed crocidolite mechanism. Searches for crocidolite, asbestos, mesothelial cells, macrophages, and lysosomal cell death found no passage describing macrophage necrosis creating a mutagenic Fe(II)-rich environment. (LLM, conf=0.76)
Experimental — accuracy not yet measuredFerroptosis is initiated by specific perturbations of the intracellular microenvironment, notably severe lipid peroxidation, and relies on ROS generation and iron availability.
“Ferroptosis is a form of RCD initiated by specific perturbations of the intracellular microenvironment, notably severe lipid peroxidation, which relies on ROS generation and iron availability [533–536].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [536]
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-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-citationInactivation of the ferroptosis regulator Gpx4 triggers acute renal failure in mice
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., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3064 · Cited by 3,732 · see citing works
Self-citationFerroptosis: 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
Self-citationFerroptosis as a p53-mediated activity during tumour suppression
Jiang, L., Kon, N., Li, T., Wang, S.-J., Su, T., Hibshoosh, H., Baer, R., & Gu, W. (2015) · Nature · doi:10.1038/nature14344 · Cited by 3,398 · 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-citationPore-forming activity and structural autoinhibition of the gasdermin family
Ding, J., Wang, K., Liu, W., She, Y., Sun, Q., Shi, J., Sun, H., Wang, D.-C., & Shao, F. (2016) · Nature · doi:10.1038/nature18590 · Cited by 2,771 · 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-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
Self-citationPeroxidation 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-citationDixon, S. J., Patel, D. N., Welsch, M., Skouta, R., Lee, E. D., Hayano, M., Thomas, A. G., Gleason, C. E., Tatonetti, N. P., Slusher, B. S., et al. (2014) · eLife · doi:10.7554/elife.02523 · Cited by 2,088 · see citing works
Self-citationQuantitative proteomics identifies NCOA4 as the cargo receptor mediating ferritinophagy
Mancias, J. D., Wang, X., Gygi, S. P., Harper, J. W., & Kimmelman, A. C. (2014) · Nature · doi:10.1038/nature13148 · Cited by 2,084 · 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
Self-citationSun, 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
Self-citationDependency of a therapy-resistant state of cancer cells on a lipid peroxidase pathway
Viswanathan, V. S., Ryan, M. J., Dhruv, H. D., Gill, S., Eichhoff, O. M., Seashore-Ludlow, B., Kaffenberger, S. D., Eaton, J. K., Shimada, K., Aguirre, A. J., et al. (2017) · Nature · doi:10.1038/nature23007 · Cited by 2,011 · see citing works
Self-citationFerroptosis 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
Self-citationYang, W. S., & Stockwell, B. R. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.02.010 · Cited by 1,876 · see citing works
Self-citationLipid peroxidation in cell death
Gaschler, M. M., & Stockwell, B. R. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.10.086 · Cited by 1,852 · see citing works
Self-citationRAS–RAF–MEK-dependent oxidative cell death involving voltage-dependent anion channels
Yagoda, N., von Rechenberg, M., Zaganjor, E., Bauer, A. J., Yang, W. S., Fridman, D. J., Wolpaw, A. J., Smukste, I., Peltier, J. M., Boniface, J. J., et al. (2007) · Nature · doi:10.1038/nature05859 · Cited by 1,631 · see citing works
Self-citationNutrition Needs of Mammalian Cells in Tissue Culture
Eagle, H. (1955) · Science · doi:10.1126/science.122.3168.501 · Cited by 1,619 · 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-citationDolma, S., Lessnick, S. L., Hahn, W. C., & Stockwell, B. R. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00050-3 · Cited by 1,446 · 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 · cited 3× · see citing works
“…have been shown to be sensitive to ferroptosis, including hippocampal postnatal rat brain slices treated with glutamate (Dixon et al., 2012), striatal rat brain slices with ectopic mutant huntingtin expression (Skouta et al., 2014), and freshly isolated renal tubules (Linkermann et al., 2014).”
Self-citationSynchronized renal tubular cell death involves ferroptosis
Linkermann, A., Skouta, R., Himmerkus, N., Mulay, S. R., Dewitz, C., De Zen, F., Prokai, A., Zuchtriegel, G., Krombach, F., Welz, P.-S., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1415518111 · Cited by 1,126 · 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 · cited 2× · see citing works
“Other proteins impacting iron metabolism in the cell (e.g., HSPB1 and CISD1) impact ferroptosis sensitivity (Sun et al., 2015; Yuan et al., 2016a).”
Self-citationZilka, O., Shah, R., Li, B., Angeli, J. P. F., Grießer, M., Conrad, M., & Pratt, D. A. (2017) · ACS Central Science · doi:10.1021/acscentsci.7b00028 · Cited by 1,052 · see citing works
Self-citationHuman 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-citationMurphy, T. H., Miyamoto, M., Sastre, A., Schnaar, R. L., & COYLE, J. T. (1989) · Neuron · doi:10.1016/0896-6273(89)90043-3 · Cited by 1,033 · see citing works
Global survey of cell death mechanisms reveals metabolic regulation of ferroptosis
Shimada, K., Skouta, R., Kaplan, A., Yang, W. S., Hayano, M., Dixon, S. J., Brown, L. M., Valenzuela, C. A., Wolpaw, A. J., & Stockwell, B. R. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2079 · Cited by 1,017 · see citing works
Self-citationEssential versus accessory aspects of cell death: recommendations of the NCCD 2015
Galluzzi, L., Bravo-San Pedro, J. M., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Alnemri, E. S., Altucci, L., Andrews, D., Annicchiarico-Petruzzelli, M., et al. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.137 · Cited by 1,002 · 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
Self-citationUrsini, F., Maiorino, M., Valente, M., Ferri, L., & Gregolin, C. (1982) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(82)90150-3 · Cited by 884 · 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
Self-citationSpreading of pathology in neurodegenerative diseases: a focus on human studies
Brettschneider, J., Tredici, K. D., Lee, V. M.-Y., & Trojanowski, J. Q. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3887 · Cited by 790 · see citing works
Ferroptosis: A Novel Anti-tumor Action for Cisplatin
Guo, J., Xu, B.-F., Han, Q., Zhou, H., Xia, Y. F., Gong, C., Dai, X., Li, Z., & Wu, G. (2017) · Cancer Research and Treatment · doi:10.4143/crt.2016.572 · Cited by 787 · see citing works
Activation of SAT1 engages polyamine metabolism with p53-mediated ferroptotic responses
Ou, Y., Wang, S.-J., Li, D., Chu, B., & Gu, W. J. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1607152113 · Cited by 775 · see citing works
Intramuscular desferrioxamine in patients with Alzheimer's disease
MCLACHLAN, D. (1991) · The Lancet · doi:10.1016/0140-6736(91)92978-b · Cited by 764 · see citing works
The Roles of NRF2 in Modulating Cellular Iron Homeostasis
Kerins, M. J., & Ooi, A. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7176 · Cited by 741 · see citing works
Metallothionein‐1G facilitates sorafenib resistance through inhibition of ferroptosis
Sun, X., Niu, X., Chen, R., He, W., Chen, D., Kang, R., & Tang, D. (2016) · Hepatology · doi:10.1002/hep.28574 · Cited by 707 · see citing works
Self-citationTau-mediated iron export prevents ferroptotic damage after ischemic stroke
Tuo, Q.-Z., Lei, P., Jackman, K. A., Li, X.-L., Xiong, H., Li, X.-L., Liuyang, Z.-Y., Roisman, L. C., Zhang, S.-T., Ayton, S., et al. (2017) · Molecular Psychiatry · doi:10.1038/mp.2017.171 · Cited by 706 · see citing works
Self-citationDo 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
ESCRT-III Acts Downstream of MLKL to Regulate Necroptotic Cell Death and Its Consequences
Gong, Y.-N., Guy, C., Olauson, H., Becker, J. U., Yang, M., Fitzgerald, P., Linkermann, A., & Green, D. R. (2017) · Cell · doi:10.1016/j.cell.2017.03.020 · Cited by 689 · see citing works
Self-citationInhibition of neuronal ferroptosis protects hemorrhagic brain
Li, Q., Han, X., Lan, X., Gao, Y., Wan, J., Durham, F., Cheng, T., Yang, J., Wang, Z., Jiang, C. Q., et al. (2017) · JCI Insight · doi:10.1172/jci.insight.90777 · Cited by 686 · see citing works
Self-citationHSPB1 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
Self-citationCharacterization of ferroptosis in murine models of hemochromatosis
Wang, H., An, P., Xie, E., Wu, Q., Fang, X., Gao, H., Zhang, Z., Li, Y., Wang, X., Zhang, J., et al. (2017) · Hepatology · doi:10.1002/hep.29117 · Cited by 656 · see citing works
Necroptosis, necrosis and secondary necrosis converge on similar cellular disintegration features
Berghe, T. V., Vanlangenakker, N., Parthoens, E., Deckers, W., Devos, M., Festjens, N., Guerin, C. J., Brunk, U. T., Declercq, W., & Vandenabeele, P. (2010) · Cell Death & Differentiation · doi:10.1038/cdd.2009.184 · Cited by 639 · see citing works
Regulated 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-citationMammalian lipoxygenases and their biological relevance
Kühn, H., Banthiya, S., & van Leyen, K. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.10.002 · Cited by 629 · see citing works
Dysken, M. W., Sano, M., Asthana, S., Vertrees, J. E., Pallaki, M., Llorente, M., Love, S., Schellenberg, G. D., McCarten, J. R., Malphurs, J., et al. (2014) · JAMA · doi:10.1001/jama.2013.282834 · Cited by 628 · see citing works
Targeting Chelatable Iron as a Therapeutic Modality in Parkinson's Disease
Devos, D., Moreau, C., Devedjian, J. C., Kluza, J., Pétrault, M., Laloux, C., Jonneaux, A., Ryckewaert, G., Garçon, G., Rouaix, N., et al. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5593 · Cited by 622 · 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-citationIron neurochemistry in Alzheimer's disease and Parkinson's disease: targets for therapeutics
Belaidi, A. A., & Bush, A. I. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13425 · Cited by 580 · 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
Self-citationFerroptosis 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-citationCramer, S. L., Saha, A., Liu, J., Tadi, S., Tiziani, S., Yan, W., Triplett, K., Lamb, C., Alters, S. E., Rowlinson, S. W., et al. (2016) · Nature Medicine · doi:10.1038/nm.4232 · Cited by 541 · see citing works
The preclinical phase of the pathological process underlying sporadic Alzheimer’s disease
Braak, H., & Del Tredici, K. (2015) · Brain · doi:10.1093/brain/awv236 · Cited by 540 · see citing works
Zille, M., Karuppagounder, S. S., Chen, Y., Gough, P. J., Bertin, J., Finger, J. N., Milner, T. A., Jonas, E. A., & Ratan, R. R. (2017) · Stroke · doi:10.1161/strokeaha.116.015609 · Cited by 530 · see citing works
Identification 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
CISD1 inhibits ferroptosis by protection against mitochondrial lipid peroxidation
Yuan, H., Li, X., Zhang, X., Kang, R., & Tang, D. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.08.034 · Cited by 507 · see citing works
Self-citationChen, L., Hambright, W. S., Na, R., & Ran, Q. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.680090 · Cited by 498 · see citing works
Self-citationHayano, M., Yang, W., Corn, C. K., Pagano, N. C., & Stockwell, B. R. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.93 · Cited by 462 · see citing works
Self-citationder Laan, E. V. D. B.-V., Killian, J. A., & KRUIJFF, B. D. (2004) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2004.06.010 · Cited by 461 · see citing works
Newton, K., Dugger, D. L., Maltzman, A., Greve, J. M., Hedehus, M., Martin-McNulty, B., Carano, R. A. D., Cao, T. C., van Bruggen, N., Bernstein, L., et al. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.46 · Cited by 442 · see citing works
Regional Membrane Phospholipid Alterations in Alzheimer's Disease
Prasad, M. R., Lovell, M. A., Yatin, M., Dhillon, H. S., & Markesbery, W. R. (1998) · Neurochemical Research · doi:10.1023/a:1022457605436 · Cited by 440 · see citing works
Redox imbalance in cystine/glutamate transporter-deficient mice
Sato, H., Shiiya, A., Kimata, M., Maebara, K., Tamba, M., Sakakura, Y., Makino, N., Sugiyama, F., Yagami, K.-I., Moriguchi, T., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506439200 · Cited by 422 · see citing works
Williams, T. I., Lynn, B. C., Markesbery, W. R., & Lovell, M. A. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.06.004 · Cited by 390 · see citing works
Jennis, M., Kung, C.-P., Basu, S., Budina-Kolomets, A., Leu, J. I.-J., Khaku, S., Scott, J. P., Cai, K. Q., Campbell, M. R., Porter, D. K., et al. (2016) · Genes & Development · doi:10.1101/gad.275891.115 · Cited by 355 · see citing works
Self-citationIdentification and Successful Negotiation of a Metabolic Checkpoint in Direct Neuronal Reprogramming
Gascón, S., Murenu, E., Masserdotti, G., Ortega, F., Russo, G. L., Petřík, D., Deshpande, A., Heinrich, C., Karow, M., Robertson, S. P., et al. (2015) · Cell stem cell · doi:10.1016/j.stem.2015.12.003 · Cited by 354 · see citing works
Self-citationBrain Glutathione Levels – A Novel Biomarker for Mild Cognitive Impairment and Alzheimer’s Disease
Mandal, P. K., Saharan, S., Tripathi, M., & Murari, G. (2015) · Biological Psychiatry · doi:10.1016/j.biopsych.2015.04.005 · Cited by 339 · see citing works
Ferroptosis and cell death mechanisms in Parkinson's disease
Guiney, S. J., Adlard, P. A., Bush, A. I., Finkelstein, D. I., & Ayton, S. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.01.004 · Cited by 337 · see citing works
Self-citationQuantification of F2-isoprostanes as a biomarker of oxidative stress
Milne, G. L., Sanchez, S. C., Musiek, E. S., & Morrow, J. D. (2007) · Nature Protocols · doi:10.1038/nprot.2006.375 · Cited by 333 · see citing works
Alterations in L-Glutamate Binding in Alzheimer's and Huntington's Diseases
Greenamyre, J. T., Penney, J. B., Young, A. B., D’Amato, C. J., Hicks, S. P., & Shoulson, I. (1985) · Science · doi:10.1126/science.2858129 · Cited by 333 · see citing works
Inhibiting the system xC−/glutathione axis selectively targets cancers with mutant-p53 accumulation
Liu, D. S., Duong, C. P., Haupt, S., Montgomery, K. G., House, C. M., Azar, W. J., Pearson, H. B., Fisher, O. M., Read, M., Guerra, G. R., et al. (2017) · Nature Communications · doi:10.1038/ncomms14844 · Cited by 321 · see citing works
The Protective Role of Mitochondrial Ferritin on Erastin-Induced Ferroptosis
Wang, Y., Chang, S.-Y., Wu, Q., Gou, Y.-J., Jia, L., Cui, Y.-M., Yu, P., Shi, Z.-H., Wu, W.-S., Gao, G., et al. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00308 · Cited by 309 · see citing works
Shimada, K., Hayano, M., Pagano, N. C., & Stockwell, B. R. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2015.11.016 · Cited by 300 · see citing works
Self-citationMacLeod, A. K., McMahon, M. J., Plummer, S. M., Higgins, L. G., Penning, T. M., Igarashi, K., & Hayes, J. D. (2009) · Carcinogenesis · doi:10.1093/carcin/bgp176 · Cited by 297 · see citing works
Revett, T. J., Baker, G. B., Jhamandas, J. H., & Kar, S. (2012) · Journal of Psychiatry and Neuroscience · doi:10.1503/jpn.110190 · Cited by 294 · see citing works
Molecular Basis of Vitamin E Action
Khanna, S., Roy, S., Ryu, H., Bahadduri, P. M., Swaan, P. W., Ratan, R. R., & Sen, C. K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307075200 · Cited by 285 · see citing works
Glutathione peroxidase 4: a new player in neurodegeneration?
Cardoso, B. R., Hare, D. J., Bush, A. I., & Roberts, B. R. (2016) · Molecular Psychiatry · doi:10.1038/mp.2016.196 · Cited by 281 · see citing works
Self-citationCerebral quantitative susceptibility mapping predicts amyloid-β-related cognitive decline
Ayton, S., Fazlollahi, A., Bourgeat, P., Raniga, P., Ng, A., Lim, Y. Y., Diouf, I., Farquharson, S., Fripp, J., Ames, D. J., et al. (2017) · Brain · doi:10.1093/brain/awx137 · Cited by 281 · see citing works
Self-citationRaven, E. P., Lu, P. H., Tishler, T. A., Heydari, P., & Bartzokis, G. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130209 · Cited by 270 · 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-citationDi Domenico, F., Tramutola, A., & Butterfield, D. A. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.10.490 · Cited by 253 · 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
Self-citationGpx4 ablation in adult mice results in a lethal phenotype accompanied by neuronal loss in brain
Yoo, S.-E., Chen, L., Na, R., Liu, Y., Rios, C. I., Remmen, H. V., Richardson, A. G., & Ran, Q. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.043 · Cited by 250 · see citing works
Self-citationIdentification of baicalein as a ferroptosis inhibitor by natural product library screening
Xie, Y., Song, X., Sun, X., Huang, J. L., Zhong, M., Lotze, M. T., Zeh, H. J., Kang, R., & Tang, D. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.03.052 · Cited by 246 · see citing works
Self-citationA Mitochondrial-Targeted Nitroxide Is a Potent Inhibitor of Ferroptosis
Krainz, T., Gaschler, M. M., Lim, C., Sacher, J. R., Stockwell, B. R., & Wipf, P. (2016) · ACS Central Science · doi:10.1021/acscentsci.6b00199 · Cited by 233 · see citing works
Self-citationOmega 3 fatty acid for the prevention of cognitive decline and dementia
Sydenham, E., Dangour, A. D., & Lim, W. S. (2012) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd005379.pub3 · Cited by 223 · see citing works
FANCD2 protects against bone marrow injury from ferroptosis
Song, X., Xie, Y., Kang, R., Hou, W., Sun, X., Epperly, M. W., Greenberger, J. S., & Tang, D. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.10.068 · Cited by 200 · see citing works
Self-citationFive-Membered Ring Peroxide Selectively Initiates Ferroptosis in Cancer Cells
Abrams, R. P. M., Carroll, W. L., & Woerpel, K. A. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b00900 · Cited by 189 · see citing works
Self-citationGreenshields, A. L., Shepherd, T. G., & Hoskin, D. W. (2016) · Molecular Carcinogenesis · doi:10.1002/mc.22474 · Cited by 189 · see citing works
Effect of pioglitazone medication on the incidence of dementia
Heneka, M. T., Fink, A., & Doblhammer, G. (2015) · Annals of Neurology · doi:10.1002/ana.24439 · Cited by 185 · see citing works
Chemical tools for detecting Fe ions
Hirayama, T., & Nagasawa, H. (2016) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.16-70 · Cited by 154 · see citing works
A reactivity-based probe of the intracellular labile ferrous iron pool
Spangler, B., Morgan, C. W., Fontaine, S. D., Wal, M. N. V., Chang, C. J., Wells, J. A., & Renslo, A. R. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2116 · Cited by 151 · see citing works
Effect of antioxidants on cultured human diploid fibroblasts exposed to cystine-free medium
Bannai, S., Tsukeda, H., & Okumura, H. (1977) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(77)90623-4 · Cited by 139 · see citing works
Modulatory profiling identifies mechanisms of small molecule-induced cell death
Wolpaw, A. J., Shimada, K., Skouta, R., Welsch, M. E., Akavia, U. D., Pe'er, D., Shaik, F., Bulinski, J. C., & Stockwell, B. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106149108 · Cited by 133 · see citing works
Self-citationMassie, A., Schallier, A., Kim, S. W., Fernando, R. N., Kobayashi, S., Beck, H., Bundel, D. D., Vermoesen, K., Bannai, S., Smolders, I. J., et al. (2010) · The FASEB Journal · doi:10.1096/fj.10-177212 · Cited by 124 · see citing works
Self-citationCenini, G., Sultana, R., Memo, M., & Butterfield, D. A. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00163.x · Cited by 117 · see citing works
Lipid unsaturation and organelle dynamics
Barelli, H., & Antonny, B. (2016) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2016.03.012 · Cited by 112 · see citing works
The in vivo evidence for regulated necrosis
Tonnus, W., & Linkermann, A. (2017) · Immunological Reviews · doi:10.1111/imr.12551 · Cited by 109 · see citing works
Self-citationWan, C., Li, S., Li, W., et al. (2006) · Plant Cell Reports · doi:10.1007/s00299-006-0234-2 · Cited by 99 · see citing works
Antiferroptotic activity of non-oxidative dopamine
Wang, D., Peng, Y., Xie, Y., Zhou, B., Sun, X., Kang, R., & Tang, D. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.10.099 · Cited by 88 · see citing works
Self-citationMeco, A. D., Li, J.-G., Blass, B. E., Abou-Gharbia, M. A., Lauretti, E., & Praticò, D. (2016) · Biological Psychiatry · doi:10.1016/j.biopsych.2016.05.023 · Cited by 80 · see citing works
Erratum: Pore-forming activity and structural autoinhibition of the gasdermin family
Ding, J., Wang, K., Liu, W., et al. (2016) · Nature · doi:10.1038/nature20106 · Cited by 66 · see citing works
Chiang, G. C.-Y., Mao, X., Kang, G., Chang, E., Pandya, S., Vallabhajosula, S., Isaacson, R., Ravdin, L., Initiative, A. D. N., & Shungu, D. C. (2017) · American Journal of Neuroradiology · doi:10.3174/ajnr.a5143 · Cited by 62 · see citing works
Correction: Corrigendum: Design of a hyperstable 60-subunit protein icosahedron
Hsia, Y., Bale, J. B., Gonen, S., et al. (2016) · Nature · doi:10.1038/nature20108 · Cited by 58 · see citing works
Mammalian Trit1 is a tRNA[Ser]Sec-isopentenyl transferase required for full selenoprotein expression
Fradejas‐Villar, N., Carlson, B. A., Rijntjes, E., Becker, N., Tobe, R., & Schweizer, U. (2013) · Biochemical Journal · doi:10.1042/bj20121713 · Cited by 52 · see citing works
Impact of PUFA on early immune and fetal development
Enke, U., Seyfarth, L., Schleußner, E., & Markert, U. R. (2008) · British Journal Of Nutrition · doi:10.1017/s000711450801413x · Cited by 52 · see citing works
Buijs, M., Doan, N. T., van Rooden, S., Versluis, M. J., van Lew, B., Milles, J., van der Grond, J., & van Buchem, M. A. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.09.005 · Cited by 50 · see citing works
Behavioral characterization of system xc- mutant mice
McCullagh, E. A., & Featherstone, D. E. (2014) · Behavioural Brain Research · doi:10.1016/j.bbr.2014.02.010 · Cited by 41 · see citing works
Haas, U., Raschperger, E., Hámberg, M., Samuelsson, B. O., Tryggvason, K., & Haeggström, J. Z. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1117094108 · Cited by 33 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Galluzzi, 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-citationThe CoQ oxidoreductase FSP1 acts parallel to GPX4 to inhibit ferroptosis
Bersuker, K., Hendricks, J. M., Li, Z., Magtanong, L., Ford, B., Tang, P. H., Roberts, M. A., Tong, B., Maimone, T. J., Zoncu, R., et al. (2019) · Nature · doi:10.1038/s41586-019-1705-2 · Cited by 3,703 · see citing works
Self-citationPore-forming activity and structural autoinhibition of the gasdermin family
Ding, J., Wang, K., Liu, W., She, Y., Sun, Q., Shi, J., Sun, H., Wang, D.-C., & Shao, F. (2016) · Nature · doi:10.1038/nature18590 · Cited by 2,771 · see citing works
Hayes, J. D., Dinkova-Kostova, A. T., & Tew, K. D. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.06.001 · Cited by 2,654 · see citing works
Targeting 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
NRF2 and the Hallmarks of Cancer
Rojo de la Vega, M., Chapman, E., & Zhang, D. D. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.03.022 · Cited by 1,672 · see citing works
Self-citationRole 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-citationFerroptosis: 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
13 reasons why the brain is susceptible to oxidative stress
Cobley, J. N., Fiorello, M. L., & Bailey, D. M. (2018) · Redox Biology · doi:10.1016/j.redox.2018.01.008 · Cited by 1,215 · see citing works
Intercellular interaction dictates cancer cell ferroptosis via NF2–YAP signalling
Wu, J., Minikes, A. M., Gao, M., Bian, H., Li, Y., Stockwell, B. R., Chen, Z.-N., & Jiang, X. (2019) · Nature · doi:10.1038/s41586-019-1426-6 · Cited by 1,110 · see citing works
Self-citationZou, 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
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
Inflammation in Parkinson’s Disease: Mechanisms and Therapeutic Implications
Pajares, M., I. Rojo, A., Manda, G., Boscá, L., & Cuadrado, A. (2020) · Cells · doi:10.3390/cells9071687 · Cited by 779 · 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
Iron Homeostasis and Ferroptosis in Human Diseases: Mechanisms and Therapeutic Prospects
Ru, Q., Li, Y., Chen, L., Wu, Y., Min, J., & Wang, F. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01969-z · Cited by 724 · 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
“Ferroptosis is a type of programmed cell death that is dependent on iron and the accumulation of lipid peroxides, mainly lipid hydroperoxides, which cause damage to the lipid bilayer of the plasma membrane through accelerated oxidation of membrane lipids [32,33].”
BackgroundDeep Multilayer Brain Proteomics Identifies Molecular Networks in Alzheimer’s Disease Progression
Bai, B., Wang, X., Li, Y., Chen, P.-C., Yu, K., Dey, K. K., Yarbro, J. M., Han, X., Lutz, B. M., Rao, S., et al. (2020) · Neuron · doi:10.1016/j.neuron.2019.12.015 · Cited by 632 · see citing works
“This new form of programmed cell death has recently been termed ferroptosis, different from apoptosis, necrosis and necroptosis (Stockwell et al., 2017).”
BackgroundDai, E., Han, L., Liu, J., Xie, Y., Kroemer, G., Klionsky, D. J., Zeh, H. J., Kang, R., Wang, J., & Tang, D. (2020) · Autophagy · doi:10.1080/15548627.2020.1714209 · Cited by 613 · 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
p53 in ferroptosis regulation: The new weapon for the old guardian
Liu, Y., & Gu, W. (2022) · Cell Death & Differentiation · doi:10.1038/s41418-022-00943-y · Cited by 540 · 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-citationAmaral, E. P., Costa, D. L., Namasivayam, S., Riteau, N., Kamenyeva, O., Mittereder, L., Mayer-Barber, K. D., Andrade, B. B., & Sher, A. (2019) · Journal of Experimental Medicine · doi:10.1084/jem.20181776 · Cited by 464 · see citing works
Torti, S. V., Manz, D. H., Paul, B. T., Blanchette-Farra, N., & Torti, F. M. (2018) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-082117-051732 · Cited by 426 · see citing works
Genome-wide CRISPRi/a screens in human neurons link lysosomal failure to ferroptosis
Tian, R., Abarientos, A., Hong, J., Hashemi, S. H., Yan, R., Dräger, N., Leng, K., Nalls, M. A., Singleton, A. B., Xu, K., et al. (2021) · Nature Neuroscience · doi:10.1038/s41593-021-00862-0 · Cited by 414 · 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
The metabolic landscape of RAS-driven cancers from biology to therapy
Mukhopadhyay, S., Vander Heiden, M. G., & McCormick, F. (2021) · Nature Cancer · doi:10.1038/s43018-021-00184-x · Cited by 315 · see citing works
Mukhopadhyay, S., Goswami, D., Adiseshaiah, P. P., Burgan, W., Yi, M., Guerin, T. M., Kozlov, S. V., Nissley, D. V., & McCormick, F. (2020) · Cancer Research · doi:10.1158/0008-5472.can-19-1363 · Cited by 279 · see citing works
NUPR1 is a critical repressor of ferroptosis
Liu, J., Song, X., Kuang, F., Zhang, Q., Xie, Y., Kang, R., Kroemer, G., & Tang, D. (2021) · Nature Communications · doi:10.1038/s41467-021-20904-2 · Cited by 290 · see citing works
Self-citationAcetyl-CoA metabolism in cancer
Guertin, D. A., & Wellen, K. E. (2023) · Nature Reviews Cancer · doi:10.1038/s41568-022-00543-5 · Cited by 303 · see citing works
Dietary 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
Self-citationRecent Advances in Understanding of Pathogenesis of Alcohol-Associated Liver Disease
Wu, X., Fan, X., Miyata, T., Kim, A., Cajigas-Du Ross, C. K., Ray, S., Huang, E., Taiwo, M., Arya, R., Wu, J., et al. (2023) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-031521-030435 · Cited by 289 · see citing works
Feng, L., Zhao, K., Sun, L., Yin, X., Zhang, J., Liu, C., & Li, B. (2021) · Journal of Translational Medicine · doi:10.1186/s12967-021-03042-7 · Cited by 277 · see citing works
Role of Selenoproteins in Redox Regulation of Signaling and the Antioxidant System: A Review
Zhang, Y., Roh, Y. J., Han, S.-J., Park, I., Lee, H. M., Ok, Y. S., Lee, B. C., & Lee, S.-R. (2020) · Antioxidants · doi:10.3390/antiox9050383 · Cited by 267 · see citing works
NCOA4-Mediated Ferritinophagy: A Potential Link to Neurodegeneration
Quiles del Rey, M., & Mancias, J. D. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00238 · Cited by 227 · see citing works
HIF-2α activation potentiates oxidative cell death in colorectal cancers by increasing cellular iron
Singhal, R., Mitta, S. R., Das, N. K., Kerk, S. A., Sajjakulnukit, P., Solanki, S., Andren, A., Kumar, R., Olive, K. P., Banerjee, R., et al. (2021) · Journal of Clinical Investigation · doi:10.1172/jci143691 · Cited by 215 · see citing works
Nrf2 attenuates ferroptosis-mediated IIR-ALI by modulating TERT and SLC7A11
Dong, H., Xia, Y., Jin, S., Xue, C., Wang, Y., Hu, R., & Jiang, H. (2021) · Cell Death & Disease · doi:10.1038/s41419-021-04307-1 · Cited by 196 · 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
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
Trapecar, M., Wogram, E., Svoboda, D., Communal, C., Omer, A., Lungjangwa, T., Sphabmixay, P., Velazquez, J., Schneider, K., Wright, C. W., et al. (2021) · Science Advances · doi:10.1126/sciadv.abd1707 · Cited by 176 · see citing works
Iron and the pathophysiology of diabetes
Harrison, A. V., Lorenzo, F. R., & McClain, D. A. (2023) · Annual Review of Physiology · doi:10.1146/annurev-physiol-022522-102832 · Cited by 161 · see citing works
Torti, S. V., & Torti, F. M. (2020) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2020.100860 · Cited by 153 · 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
Self-citationFundamental mechanisms of the cell death caused by Nitrosative stress
Wang, F., Yuan, Q., Chen, F., Pang, J., Pan, C., Xu, F., & Chen, Y. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.742483 · Cited by 133 · see citing works
Ribosome stalling during selenoprotein translation exposes a ferroptosis vulnerability
Li, Z., Ferguson, L., Deol, K. K., Roberts, M. A., Magtanong, L., Hendricks, J. M., Mousa, G. A., Kilinc, S., Schaefer, K., Wells, J. A., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01033-3 · Cited by 134 · see citing works
Self-citationp53 as a hub in cellular redox regulation and therapeutic target in cancer
Eriksson, S. E., Ceder, S., Bykov, V. J. N., & Wiman, K. G. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz005 · Cited by 123 · see citing works
Iron and innate antimicrobial immunity-depriving the pathogen, defending the host
Nairz, M., Dichtl, S., Schroll, A., Haschka, D., Tymoszuk, P., Theurl, I., & Weiss, G. (2018) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2018.03.007 · Cited by 123 · 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
Mastio, J., Condamine, T., Dominguez, G., Kossenkov, A. V., Donthireddy, L., Veglia, F., Lin, C., Wang, F., Fu, S., Zhou, J., et al. (2019) · Journal of Experimental Medicine · doi:10.1084/jem.20181952 · Cited by 115 · see citing works
Wei, X.-B., Jiang, W.-Q., Zeng, J.-H., Huang, L.-Q., Ding, H.-G., Jing, Y.-W., Han, Y.-L., Li, Y.-C., & Chen, S.-L. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02738-1 · Cited by 123 · see citing works
Tong, B., Ba, Y., Li, Z., Yang, C., Su, K., Qi, H., Zhang, D., Liu, X., Wu, Y., Chen, Y., et al. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106505 · Cited by 117 · see citing works
Self-citationSun, H., Cai, H., Xu, C., Zhai, H., Lux, F., Xie, Y., Feng, L., Du, L., Liu, Y., Sun, X., et al. (2022) · Journal of Nanobiotechnology · doi:10.1186/s12951-022-01654-9 · Cited by 86 · see citing works
Han, W., Duan, X., Ni, K., Li, Y., Chan, C., & Lin, W. (2022) · Biomaterials · doi:10.1016/j.biomaterials.2021.121315 · Cited by 103 · see citing works
Toyokuni, S. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.401 · Cited by 102 · see citing works
Self-citationSelective 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
Self-citationWu, Y., Torabi, S.-F., Lake, R. J., Hong, S., Yu, Z., Wu, P., Yang, Z., Nelson, K., Guo, W., Pawel, G. T., et al. (2023) · Science Advances · doi:10.1126/sciadv.ade7622 · Cited by 91 · 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
Haddad, M., Hervé, V., Ben Khedher, M. R., Rabanel, J.-M., & Ramassamy, C. (2021) · Antioxidants & Redox Signaling · doi:10.1089/ars.2020.8129 · Cited by 68 · see citing works
Yue, M., Wei, J., Chen, W., Hong, D., Chen, T., & Fang, X. (2022) · Nutrients · doi:10.3390/nu14224886 · Cited by 62 · 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
The interplay of autophagy and non-apoptotic cell death pathways
(2020) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2019.12.004 · Cited by 50 · see citing works
Yu, X., Wang, Y., Tan, J., Li, Y., Yang, P., Liu, X., Lai, J., Zhang, Y., Cai, L., Gu, Y., et al. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-01800-2 · Cited by 48 · 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
Ito, F., Yanatori, I., Maeda, Y., Nimura, K., Ito, S., Hirayama, T., Nagasawa, H., Kohyama, N., Okazaki, Y., Akatsuka, S., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101616 · Cited by 45 · see citing works
Self-citationCheng, X., Zhao, F., Ke, B., Chen, D., & Liu, F. (2023) · Cancers · doi:10.3390/cancers15215209 · Cited by 44 · see citing works
RBM45 reprograms lipid metabolism promoting hepatocellular carcinoma via Rictor and ACSL1/ACSL4
Wang, C., Chen, Z., Yi, Y., Ding, Y., Xu, F., Kang, H., Lin, K., Shu, X., Zhong, Z., Zhang, Z., et al. (2024) · Oncogene · doi:10.1038/s41388-023-02902-4 · Cited by 42 · see citing works
Genome-wide CRISPRi/a screens in human neurons link lysosomal failure to ferroptosis
Tian, R., Abarientos, A., Hong, J., Hashemi, S. H., Yan, R., Dräger, N., Leng, K., Nalls, M. A., Singleton, A. B., Xu, K., et al. (2020) · doi:10.1101/2020.06.27.175679 · Cited by 414 · 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
Zhang, K., Long, M., Dong, W., Li, J., Wang, X., Liu, W., Huang, Q., Ping, Y., Zou, H., Song, R., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25020763 · Cited by 38 · see citing works
Ferrous iron–activatable drug conjugate achieves potent MAPK blockade in <i>KRAS</i> -driven tumors
Jiang, H., Muir, R. K., Gonciarz, R. L., Olshen, A. B., Yeh, I., Hann, B. C., Zhao, N., Wang, Y.-H., Behr, S. C., Korkola, J. E., et al. (2022) · Journal of Experimental Medicine · doi:10.1084/jem.20210739 · Cited by 33 · see citing works
Yamaguchi, H., Hayama, K., Sasagawa, I., Okada, Y., Kawase, T., Tsubokawa, N., & Tsuchimochi, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030908 · Cited by 30 · see citing works
Unveiling ferroptosis as a promising therapeutic avenue for colorectal cancer and colitis treatment
Kao, A. T., Cabanlong, C. V., Padilla, K., & Xue, X. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.05.025 · Cited by 30 · 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
Itraconazole Inhibits the Growth of Cutaneous Squamous Cell Carcinoma by Targeting HMGCS1/ACSL4 Axis
Xu, C., Zhuo, Y., Liu, Y., & Chen, H. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.828983 · Cited by 23 · see citing works
Schiera, G., Macajone, G., Volpes, S., Greco, L., Di Liegro, C. M., Serio, G., Caradonna, F., & Naselli, F. (2026) · Cells · doi:10.3390/cells15040366 · Cited by 8 · see citing works
Lai, L., Du, W., Wu, H., Liu, W., lv, K., Shangguan, P., Xie, L., Xu, J., & Lan, P. (2025) · Scientific Reports · doi:10.1038/s41598-025-10746-z · Cited by 4 · see citing works
Snake venom-induced tissue damage as a paradigm of redox imbalance, ferroptosis, and inflammaging
Dahiya, R., Singh, A. P., & Rawat, A. (2026) · Toxicology Letters · doi:10.1016/j.toxlet.2026.111894 · Cited by 3 · see citing works
- Authors
- 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., Noel, K., Jiang, X., Linkermann, A., Murphy, M. E., Overholtzer, M., Oyagi, A., Pagnussat, G. C., Park, J., Ran, Q., Rosenfeld, C. S., Salnikow, K., Tang, D., Torti, F. M., Torti, S. V., Toyokuni, S., Woerpel, K. A., & Zhang, D. D.
- Affiliations
- Columbia University (US)
- The University of Melbourne (AU)
- Helmholtz Munich (DE)
- Stanford University (US)
- Goethe University Frankfurt (DE)
- Yale University (US)
- University of Pittsburgh (US)
- Memorial Sloan Kettering Cancer Center (US)
- University Hospital Carl Gustav Carus (DE)
- The Wistar Institute (US)
- Consejo Nacional de Investigaciones Científicas y Técnicas (AR)
- Flagship Pioneering (United States) (US)
- The University of Texas at San Antonio Health Science Center (US)
- National Institutes of Health (US)
- UConn Health (US)
- Nagoya University (JP)
- New York University (US)
- University of Arizona (US)
- Corresponding author
- Stockwell, Brent R.
- ORCID
- Stockwell, Brent R.
- Bush, Ashley I.
- Conrad, Marcus
- Dixon, Scott J.
- Fulda, Simone
- Gascón, Sergio
- Hatzios, Stavroula K.
- Kagan, Valerian E.
- Noel, Kay
- Jiang, Xuejun
- Linkermann, Andreas
- Murphy, Maureen E.
- Overholtzer, Michael
- Pagnussat, Gabriela C.
- Park, Jason
- Ran, Qitao
- Tang, Daolin
- Torti, Frank M.
- Torti, Suzy V.
- Toyokuni, Shinya
- Woerpel, K.A.
- Zhang, Donna D.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2017-10
- Volume
- 171
- Issue
- 2
- Pages
- 273-285
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC5685180
- OpenAlex
- W2762087180
- Cited by
- 7,695
- References
- 113
- Citations by year
- 2026: 1160 · 2025: 1220 · 2024: 1219 · 2023: 1121 · 2022: 1179 · 2021: 851 · 2020: 500 · 2019: 296 · 2018: 130 · 2017: 4 · 2016: 4 · 2015: 1 · 2014: 1
- FWCI
- 46.48
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Minerva Access (University of Melbourne) (submittedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion, cc-by-nc-nd)
- Site cant be reached (submittedVersion)
- PuSH - Publication Server of Helmholtz Zentrum München (submittedVersion)
- Funders
- NIH (R35CA209896, P01 CA087497, 4R00CA166517, 1R01GM122923, R01CA171101, R01CA188025, CA102184, HL114453, U19AI068021, NS076511, NS061817, R01GM115366, 1R01GM118730, R01CA204232, P30CA008748, R01CA160417)
- JSPS KAKENHI (JP16K15257, JP17H04064)
- ACS (RSG-16-014-01-CDD)
- NNSFC (2016A030308011, 31671435)
- Geoffrey Beene Cancer Research Center
- HFSP (RGP 0013/14)
- Topics
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Ferroptosis and cancer prognosis
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- ferroptosis, regulated cell death, lipid peroxidation, iron metabolism, redox biology, degenerative diseases, neurodegenerative diseases, ischemia-reperfusion injury, traumatic brain injury, intracerebral hemorrhage, cancer therapy, tumor suppression
- MeSH terms
- Animals, Humans, Iron, Oxidation-Reduction, Cell Death, Apoptosis, Reactive Oxygen Species
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