Ferroptosis: An Iron-Dependent Form of Nonapoptotic Cell Death
Open accessAbstract
Nonapoptotic forms of cell death may facilitate the selective elimination of some tumor cells or be activated in specific pathological states. The oncogenic RAS-selective lethal small molecule erastin triggers a unique iron-dependent form of nonapoptotic cell death that we term ferroptosis. Ferroptosis is dependent upon intracellular iron, but not other metals, and is morphologically, biochemically, and genetically distinct from apoptosis, necrosis, and autophagy. We identify the small molecule ferrostatin-1 as a potent inhibitor of ferroptosis in cancer cells and glutamate-induced cell death in organotypic rat brain slices, suggesting similarities between these two processes. Indeed, erastin, like glutamate, inhibits cystine uptake by the cystine/glutamate antiporter (system x(c)(-)), creating a void in the antioxidant defenses of the cell and ultimately leading to iron-dependent, oxidative death. Thus, activation of ferroptosis results in the nonapoptotic destruction of certain cancer cells, whereas inhibition of this process may protect organisms from neurodegeneration.
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Loss of GPX4 in invasive cancer cells with a mesenchymal and drug-resistant phenotype causes accumulation of lipid hydroperoxides that trigger ferroptosis.
“At the same time, the loss of the lipid repair enzyme glutathione peroxidase 4 (GPX4) in invasive cancer cells with a mesenchymal and drug-resistant phenotype causes the accumulation of lipid hydroperoxides (lipid-ROS) triggering the iron-dependent cell death known as ferroptosis (7).”
From Secreted Apoe rewires melanoma cell state vulnerability to ferroptosis (2024) · cites this paper as [7]
The Discussion (page unavailable in our copy) describes ferroptosis in cancer cells as iron-dependent death involving lethal lipid ROS. It does not establish that loss of GPX4 causes this process in invasive, mesenchymal, drug-resistant cancer cells; its account instead discusses inhibition of cystine uptake and RSL3, whose target it describes as uncertain. (LLM, conf=0.88)
Experimental — accuracy not yet measuredDaily injection of ferrostatin markedly reduces oligodendrocyte death and 4-HNE accumulation at two days and two weeks of cuprizone consumption.
“Daily injection of ferrostatin—a lipid ROS scavenger [286]—markedly reduces oligodendrocyte death and 4-HNE accumulation at two days and two weeks of cuprizone consumption [101].”
From Oligodendrocyte death and myelin loss in the cuprizone model: an updated overview of the intrinsic and extrinsic causes of cuprizone demyelination (2022) · cites this paper as [286]
Eprenetapopt is the first compound to reach a phase 3 clinical trial where triggering ferroptosis is central to its anticancer efficacy.
“eprenetapopt is the first compound to reach a phase 3 clinical trial where triggering ferroptosis is central to its anticancer efficacy.”
From Eprenetapopt triggers ferroptosis, inhibits NFS1 cysteine desulfurase, and synergizes with serine and glycine dietary restriction (2022) · cites this paper as [21]
The Abstract and Discussion describe ferroptosis in cancer cells and discuss erastin, RSL3, and other experimental compounds. Searches for eprenetapopt and phase 3 clinical trials found no passage addressing that drug, its trial status, or its mechanism of anticancer efficacy; page numbers were not available in our copy. (LLM, conf=0.78)
Experimental — accuracy not yet measuredErastin triggers ferroptosis by indirectly affecting the catalytic cycle of GPX4 via inhibition of the cystine/glutamate antiporter system xc− and consequent decrease in intracellular cysteine and GSH.
“erastin triggers ferroptosis by (indirectly) affecting the catalytic cycle of GPX4 via a mechanism that involves the inhibition of the cystine/glutamate antiporter system xc− and consequent decrease in intracellular cysteine (which derives from cystine reduction in the cytoplasm) and GSH (which is synthesized from cysteine) [539, 548, 549, 551].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [539]
Ferroptosis occurs independently of caspases, necrosome components, CYPD, and the molecular machinery for autophagy.
“Ferroptosis occurs independently of caspases, necrosome components and CYPD, and the molecular machinery for autophagy [539]”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [539]
Iron depletion by chelators or PHKG2 knockdown inhibits ferroptosis.
“the ferroptosis-inhibiting effect of iron depletion by either chelators [539, 543, 548] or phosphorylase kinase catalytic subunit gamma 2 (PHKG2) knockdown [566]”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [539]
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 [539]
Inhibitors of the cystine/glutamate transporter xCT deplete intracellular glutathione in cancer cells, resulting in iron-dependent ROS accumulation and ferroptosis.
“Inhibitors of this transporter have been found to deplete intracellular glutathione in cancer cells, resulting in iron-dependent accumulation of ROS and a form of cell death termed ferroptosis (Dixon et al., 2012; Dixon et al., 2014; Yang et al., 2014).”
From Targeting Metabolism for Cancer Therapy (2017) · cites this paper as Dixon et al., 2012
MEK inhibition in PDAC increases lysosome biosynthesis and ferritinophagy, which are necessary to support increased iron-sulfur cluster proteins for respiration.
“MEK-inhibition in PDAC increased both lysosome biosynthesis and ferritinophagy, necessary to support increased iron-sulfur cluster proteins for respiration217”
From Pancreatic cancer: Advances and challenges (2023) · cites this paper as [217]
Ferroptosis is a non-apoptotic, peroxidation-driven regulated death process that needs abundant accessible cellular iron.
“Ferroptosis is this non-apoptotic, peroxidation-driven form of regulated cell death that requires abundant and accessible cellular iron; the existence of this ancient form of cell death was unknown and only discovered recently using a pharmacological approach [10].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [10]
Erastin causes ROS production in sensitive cell lines, as detected with DCF.
“Indeed, analysis with dichlorofluorescein (DCF), a ROS-detecting dye, revealed that erastin causes the generation of ROS in sensitive cell lines [10, 13].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [10]
RSL3 does not block cystine import, indicating it does not inhibit system xc−.
“However, RSL3 treatment does not prevent the import of radiolabeled cystine, indicating that RSL3 does not inhibit system xc− [10].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [10]
The erastin/RSL3 death mode was proposed as a previously unrecognized form called ferroptosis, indicating a critical role for cellular iron.
“Taken together, the mode of cell death induced by erastin, RSL3 and related compounds was proposed to be a previously unrecognized form of cell death termed ferroptosis (ferro = “ferrous ion (Fe2+)”, ptosis = “fall”), suggesting a critical role for cellular iron in this regulated form of oxidative cell death [10].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [10]
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 [10]
Erastin treatment blocks radiolabeled cystine import, confirming that erastin inhibits system xc−.
“Indeed, erastin treatment abolished the import of radiolabeled cystine [10], a substrate for the system xc− antiporter, confirming that erastin inhibits system xc−.”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [10]
Erastin and sulfasalazine have similar modulatory profiles, suggesting erastin may inhibit system xc− to start ferroptosis.
“In addition, modulatory profiles of erastin and sulfasalazine (SAS), an inhibitor of system xc−, were similar to each other, suggesting that erastin might act as a system xc− inhibitor to initiate ferroptosis [10].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [10]
Ferrostatin-1 is a lipid ROS scavenger that prevents erastin- and RSL3-induced ferroptosis but not staurosporine- or hydrogen peroxide-induced death.
“Ferrostatin-1 acts as a lipid ROS scavenger and prevents ferroptosis induced by erastin and RSL3, but does not suppress cell death induced by staurosporine (an apoptosis inducer) or hydrogen peroxide (an oxidative necrosis inducer) [10].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [10]
In cell culture models, adding iron to culture media sensitizes cancer cells to ferroptosis.
“In cell culture models, the addition of iron to culture media sensitizes cancer cells to ferroptosis”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [10]
Cu2+ and Co2+ catalyze Fenton chemistry, but do not sensitize cells to ferroptosis, whereas iron does.
“copper (Cu2+) and cobalt (Co2+) are known to catalyze Fenton chemistry, but these metals do not sensitize cells to ferroptosis, whereas iron does [10].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [10]
Iron sensitization of cancer cells to ferroptosis probably occurs by lowering the threshold to initiate oxidative damage.
“probably by lowering the threshold to initiate oxidative damage [10].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [10]
Erastin induces ferroptosis by causing glutathione depletion through inhibition of the glutamate-cystine antiporter system Xc-, leading to GPX4 inactivation and accumulation of lipid peroxides.
“The term ferroptosis was introduced to describe cell death induced by the compound erastin, which causes glutathione depletion through the glutamate-cystine antiporter system Xc- inhibition and consequently glutathione peroxidase 4 (GPX4) inactivation leading to accumulation of lipid peroxides (Ursini et al., 1982; Dixon et al., 2012).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Dixon et al., 2012
Accumulation of iron-dependent lipid modifications promotes ferroptosis.
“Accumulation of iron-dependent lipid modifications promotes a specific form of cell death, known as ferroptosis [4].”
From Iron as a central player and promising target in cancer progression (2019) · cites this paper as [4]
When the capacity of red pulp macrophages and Kupffer cells is overwhelmed, the cells die, presumably by ferroptosis induced by iron-mediated oxidative stress and lipid peroxidation.
“However, when the capacity of red pulp macrophages (the iron-recycling macrophage population in the spleen, henceforward abbreviated as RPM) and KC is overwhelmed, the cells die, presumably by a specific form of cell death called ferroptosis that is induced by iron-mediated oxidative stress and lipid peroxidation [54].”
From “Pumping iron”—how macrophages handle iron at the systemic, microenvironmental, and cellular levels (2017) · cites this paper as [54]
Ferroptosis is characterized by iron-dependent radical formation via the Fenton reaction and subsequent membrane lipid peroxidation, and is morphologically, biochemically and genetically different from apoptosis, necroptosis and autophagy.
“It is characterized by iron-dependent radical formation via the Fenton reaction and subsequent membrane lipid peroxidation, and is morphologically, biochemically and genetically different from apoptosis, necroptosis and autophagy.”
From Iron in immune cell function and host defense (2021) · cites this paper as [104]
Ferroptosis describes a form of iron-dependent cell death induced by the small molecule erastin.
“Ferroptosis describes a form of iron dependent cell death induced by the small molecule erastin”
From Iron in immune cell function and host defense (2021) · cites this paper as [104]
Neurodegeneration that results from iron toxicity can lead to apoptosis and ferroptosis, an iron-specific form of non-apoptotic cell death.
“Neurodegeneration that results from iron toxicity can lead to apoptosis73 and ferroptosis, an iron-specific form of non-apoptotic cell death.74”
From The role of iron in brain ageing and neurodegenerative disorders (2014) · cites this paper as [74]
Cell death elicited by ferroptosis-inducing compounds (e.g., erastin and RSL3) can be mitigated through various iron chelators.
“Cell death elicited by ferroptosis-inducing compounds (FINs) (e.g. erastin and RSL3) can also be mitigated through various iron chelators (Dfo, 2,2-bipyridile or compound 311) [62], [66], [81].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [62]
Ferroptosis can be initiated through repression of SLC7A11, resulting in iron-dependent accumulation of ROS and glutathione depletion.
“Distinctly, ferroptosis can be initiated through repression of the p53 target, SLC7A11, which encodes a component of the cysteine/glutamate antiporter (system Xc-), resulting in iron-dependent accumulation of ROS and glutathione (antioxidant) depletion [62], [82].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [62]
Cells are desensitized to ferroptosis through genetic silencing of iron uptake (TfR1), metabolism (IRP2 and ISCU) and storage (ferritin) genes, or through depletion of transferrin in the extracellular environment.
“Cells are also desensitized to ferroptosis through genetic silencing of iron uptake (TfR1), metabolism (IRP2 and ISCU) and storage (ferritin) genes [62], [66], [82], or through depletion of transferrin in the extracellular environment [83].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [62]
Ferroptosis is a unique cell death pathway distinct from apoptosis, reliant on availability of iron liberated through ferritinophagy.
“Ferroptosis, a unique cell death pathway distinct from apoptosis [62], [66], [80], is reliant on the availability of iron [62], [66], [81] liberated through ferritinophagy [63].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [62]
Ferroptosis is an iron-dependent autophagic cell death program that can be inhibited in MEFs by genetically inactivating autophagy or ferritinophagy.
“an iron-dependent autophagic cell death program [62], [63], [64] that can be inhibited in MEFs by genetically inactivating autophagy or ferritinophagy [65].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [62]
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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-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-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
Ferroptosis: 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
Inactivation 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-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-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
Modulation of oxidative stress as an anticancer strategy
Gorrini, C., Harris, I. S., & Mak, T. W. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4002 · Cited by 3,579 · see citing works
Ferroptosis 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-citationCD8+ T cells regulate tumour ferroptosis during cancer immunotherapy
Wang, W., Green, M., Choi, J. E., Gijón, M., Kennedy, P. D., Johnson, J. K., Liao, P., Lang, X., Kryczek, I., Sell, A., et al. (2019) · Nature · doi:10.1038/s41586-019-1170-y · Cited by 2,880 · 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
Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,622 · 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
ROS in cancer therapy: the bright side of the moon
Perillo, B., Di Donato, M., Pezone, A., Di Zazzo, E., Giovannelli, P., Galasso, G., Castoria, G., & Migliaccio, A. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-0384-2 · Cited by 2,176 · see citing works
From Krebs to clinic: glutamine metabolism to cancer therapy
Altman, B. J., Stine, Z. E., & Dang, C. V. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.71 · Cited by 2,119 · 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
Dixon, 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-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-citationGlutaminolysis 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
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
The role of iron in brain ageing and neurodegenerative disorders
Ward, R. J., Zucca, F. A., Duyn, J. H., Crichton, R. R., & Zecca, L. (2014) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70117-6 · Cited by 1,819 · 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
NLRP3 inflammasome activation and cell death
Huang, Y., Xu, W., & Zhou, R. (2021) · Cellular & Molecular Immunology · doi:10.1038/s41423-021-00740-6 · Cited by 1,527 · 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
Cao, 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
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
How does p53 induce apoptosis and how does this relate to p53-mediated tumour suppression
Aubrey, B. J., Kelly, G. L., Janic, A., Herold, M. J., & Strasser, A. (2018) · Cell Death & Differentiation · doi:10.1038/cdd.2017.169 · Cited by 1,395 · see citing works
Pancreatic cancer: Advances and challenges
Halbrook, C. J., Lyssiotis, C. A., Pasca di Magliano, M., & Maitra, A. (2023) · Cell · doi:10.1016/j.cell.2023.02.014 · Cited by 1,321 · 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-citation13 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
Ferrostatins 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-citationNiu, B., Liao, K., Zhou, Y., Wen, T., Quan, G., Pan, X., & Wu, C. (2021) · Biomaterials · doi:10.1016/j.biomaterials.2021.121110 · Cited by 1,168 · see citing works
Synchronized 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 · see citing works
Linkermann, A., & Green, D. R. (2014) · New England Journal of Medicine · doi:10.1056/nejmra1310050 · Cited by 1,103 · 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-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-citationGlobal 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-citationTargeting Metabolism for Cancer Therapy
Luengo, A., Gui, D. Y., & Vander Heiden, M. G. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.08.028 · Cited by 971 · see citing works
Targeting p53 pathways: mechanisms, structures, and advances in therapy
Wang, H., Guo, M., Wei, H., & Chen, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01347-1 · Cited by 1,016 · see citing works
Beta Cell Dysfunction and Insulin Resistance
Cerf, M. E. (2013) · Frontiers in Endocrinology · doi:10.3389/fendo.2013.00037 · Cited by 964 · see citing works
The 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
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
Julien, O., & Wells, J. A. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.44 · Cited by 816 · see citing works
The role of cellular reactive oxygen species in cancer chemotherapy
Yang, H., Villani, R. M., Wang, H., Simpson, M. J., Roberts, M. S., Tang, M., & Liang, X. (2018) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-018-0909-x · Cited by 794 · 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
NFS1 undergoes positive selection in lung tumours and protects cells from ferroptosis
Alvarez, S. W., Sviderskiy, V. O., Terzi, E. M., Papagiannakopoulos, T., Moreira, A. L., Adams, S., Sabatini, D. M., Birsoy, K., & Possemato, R. (2017) · Nature · doi:10.1038/nature24637 · Cited by 787 · 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
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
The metabolic roots of senescence: mechanisms and opportunities for intervention
Wiley, C. D., & Campisi, J. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00483-8 · Cited by 691 · 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
T cell lipid peroxidation induces ferroptosis and prevents immunity to infection
Matsushita, M., Freigang, S., Schneider, C., Conrad, M., Bornkamm, G. W., & Kopf, M. (2015) · Journal of Experimental Medicine · doi:10.1084/jem.20140857 · Cited by 672 · see citing works
“Cystine in the extracellular space is transported exclusively by the xc and converted to cysteine, which facilitates the synthesis of intracellular glutathione (GSH), a major cellular antioxidant (Fahey and Sundquist, 1991).”
BackgroundInteractions of iron, dopamine and neuromelanin pathways in brain aging and Parkinson's disease
Zucca, F. A., Segura-Aguilar, J., Ferrari, E., Muñoz, P., Paris, I., Sulzer, D., Sarna, T., Casella, L., & Zecca, L. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.09.012 · Cited by 659 · 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
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-citationHeme oxygenase-1 accelerates erastin-induced ferroptotic cell death
Kwon, M.-Y., Park, E., Lee, S.-J., & Chung, S. W. (2015) · Oncotarget · doi:10.18632/oncotarget.5162 · Cited by 612 · see citing works
From ancient herb to modern drug: Artemisia annua and artemisinin for cancer therapy
Efferth, T. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.02.009 · Cited by 632 · see citing works
Dai, 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
Parthanatos: mitochondrial‐linked mechanisms and therapeutic opportunities
Fatokun, A. A., Dawson, V. L., & Dawson, T. M. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12416 · Cited by 594 · see citing works
HSPA5 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
Initiation and execution mechanisms of necroptosis: an overview
Grootjans, S., Vanden Berghe, T., & Vandenabeele, P. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.65 · Cited by 566 · 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
ROS in Cancer: The Burning Question
Chio, I. I. C., & Tuveson, D. A. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.03.004 · Cited by 532 · 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
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
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Regulated cell death and inflammation: an auto-amplification loop causes organ failure
Linkermann, A., Stockwell, B. R., Krautwald, S., & Anders, H.-J. (2014) · Nature Reviews Immunology · doi:10.1038/nri3743 · Cited by 522 · 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
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
Masaldan, S., Clatworthy, S. A. S., Gamell, C., Meggyesy, P. M., Rigopoulos, A.-T., Haupt, S., Haupt, Y., Denoyer, D., Adlard, P. A., Bush, A. I., et al. (2018) · Redox Biology · doi:10.1016/j.redox.2017.08.015 · 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
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
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
Macrophages and Iron Metabolism
Soares, M. P., & Hamza, I. (2016) · Immunity · doi:10.1016/j.immuni.2016.02.016 · Cited by 401 · see citing works
Disease tolerance and immunity in host protection against infection
Soares, M. P., Teixeira, L., & Moita, L. F. (2017) · Nature reviews. Immunology · doi:10.1038/nri.2016.136 · Cited by 376 · see citing works
Artemisinin derivatives induce iron-dependent cell death (ferroptosis) in tumor cells
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Self-citation
- Authors
- 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., Morrison, B., & Stockwell, B. R.
- Affiliations
- Columbia University (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Stockwell, Brent R.
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2012-05
- Volume
- 149
- Issue
- 5
- Pages
- 1060-1072
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC3367386
- OpenAlex
- W1997183854
- Cited by
- 18,691
- References
- 48
- Citations by year
- 2026: 2902 · 2025: 3499 · 2024: 3393 · 2023: 2809 · 2022: 2342 · 2021: 1539 · 2020: 828 · 2019: 500 · 2018: 294 · 2017: 209 · 2016: 160 · 2015: 92 · 2014: 61 · 2013: 29 · 2012: 14
- FWCI
- 50.51
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (5R01CA097061, 5R01GM085081, R01CA161061)
- Arnold and Mabel Beckman Foundation
- Columbia University
- Empire State Development's Division of Science, Technology and Innovation
- Canadian Institutes of Health Research
- National Science Foundation (CHE-0840451)
- 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, non-apoptotic cell death, iron-dependent cell death, erastin, ferrostatin-1, SLC7A11, system xc-, cystine uptake, glutamate-induced cell death, neurodegeneration, cancer cell death, oxidative stress, antioxidant defense
- MeSH terms
- Animals, Cyclohexylamines, Fibroblasts, Hippocampus, Humans, Iron, Neoplasms, Phenylenediamines, Piperazines, Cell Death, Reactive Oxygen Species, Glutamic Acid, Lipid Metabolism, Rats, In Vitro Techniques
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