Ferrostatins Inhibit Oxidative Lipid Damage and Cell Death in Diverse Disease Models
Open accessAbstract
Ferrostatin-1 (Fer-1) inhibits ferroptosis, a form of regulated, oxidative, nonapoptotic cell death. We found that Fer-1 inhibited cell death in cellular models of Huntington’s disease (HD), periventricular leukomalacia (PVL), and kidney dysfunction; Fer-1 inhibited lipid peroxidation, but not mitochondrial reactive oxygen species formation or lysosomal membrane permeability. We developed a mechanistic model to explain the activity of Fer-1, which guided the development of ferrostatins with improved properties. These studies suggest numerous therapeutic uses for ferrostatins, and that lipid peroxidation mediates diverse disease phenotypes.
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A similar protective effect is observed in GPX4-independent models of renal ischemic or toxic injury, Parkinson disease, and other human pathologies.
“A similar protective effect is observed in GPX4-independent models of renal ischemic or toxic injury [540, 592], Parkinson disease [593], and other human pathologies [594].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [594]
Ferrostatin-1 and its analogs protect oligodendrocytes from glutathione depletion-induced death, suggesting ferroptosis is involved in this brain injury.
“Ferrostaton-1 and its analogs also protected OLs from death by glutathione depletion, suggesting that the ferroptosis pathway is involved in this form of brain injury [57].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [57]
Ferrostatin-1 prevents neuronal death induced by pathogenic HTT exon 1 fragment (73Q) in rat corticostriatal brain slices.
“When ferrostatin-1 was added to rat corticostriatal brain slices, it prevented neuronal cell death induced by the gene delivery of HTT exon 1 fragment with a pathogenic repeat (73Q) [57].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [57]
In a model simulating rhabdomyolysis-induced acute kidney injury, ferrostatin-1 prevents kidney proximal tubule cell death, suggesting ferroptosis is necessary.
“Using this model, ferrostatin-1 prevented cell death in kidney proximal tubules, suggesting the necessity of ferroptosis for rhabdomyolysis-induced acute kidney injury [57].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [57]
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Ferroptosis: A Regulated Cell Death Nexus Linking Metabolism, Redox Biology, and Disease
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“, ferrostatin-1 and SRS 11–92) remarkably protect OLs from cystine deprivation.(22)”
BackgroundInfluentialFerroptosis: Death by Lipid Peroxidation
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“Ferrostaton-1 and its analogs also protected OLs from death by glutathione depletion, suggesting that the ferroptosis pathway is involved in this form of brain injury [57].”
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“, 2014), kidney injury (Friedmann Angeli et al., 2014; Skouta et al., 2014), and liver injury (Carlson et al.”
InfluentialSelf-citationAutophagy promotes ferroptosis by degradation of ferritin
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Peroxidation of polyunsaturated fatty acids by lipoxygenases drives ferroptosis
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“Inhibition of ferroptosis is protective in models of Huntington’s disease (8), periventricular leukomalacia (8–10), and kidney dysfunction (8, 11, 12).”
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“protect against ischemic injury in the brain, liver, kidney, and heart and reduce neurodegenerative phenotypes in a number of cell and animal models, as well as prevent excess iron-induced ferroptosis in cardiomyocytes [56,62,63].”
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“A role of ferroptosis in neurodegeneration has also been implicated (Chen et al., 2015; Do Van et al., 2016; Skouta et al., 2014).”
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“36,207).”
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BackgroundMethodInfluentialSelf-citationFerroptosis: Mechanisms and links with diseases
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GTP Cyclohydrolase 1/Tetrahydrobiopterin Counteract Ferroptosis through Lipid Remodeling
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Self-citationFerroptosis, necroptosis, and pyroptosis in anticancer immunity
Tang, R., Xu, J., Zhang, B., Liu, J., Liang, C., Hua, J., Meng, Q., Yu, X., & Shi, S. (2020) · Journal of Hematology & Oncology · doi:10.1186/s13045-020-00946-7 · Cited by 1,280 · see citing works
“In contrast, cells that undergo ferroptosis because of cysteine deprivation have approximately 10% the normal level of intracellular GSH [20].”
BackgroundSynchronized 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
“SRS15-72B was cleared rapidly with a half-life of t1/2 = 2 min (Table S1).”
BackgroundMethodResultInfluentialSelf-citationEnergy-stress-mediated AMPK activation inhibits ferroptosis
Lee, H., Zandkarimi, F., Zhang, Y., Meena, J. K., Kim, J., Zhuang, L., Tyagi, S., Ma, L., Westbrook, T. F., Steinberg, G. R., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0461-8 · Cited by 1,138 · see citing works
Self-citationFricker, M., Tolkovsky, A. M., Borutaitė, V., Coleman, M. P., & Brown, G. C. (2018) · Physiological Reviews · doi:10.1152/physrev.00011.2017 · Cited by 1,122 · see citing works
“Overexpression of huntingtin exon-1 fragment with an expanded pathogenic polyglutamine repeat (Q73) in corticostriatal brain slices resulted in death of medium spiny neurons by ferroptosis (634).”
GPX4 at the Crossroads of Lipid Homeostasis and Ferroptosis
Forcina, G. C., & Dixon, S. J. (2019) · PROTEOMICS · doi:10.1002/pmic.201800311 · Cited by 1,080 · 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
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Essential 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
“Remove 3 transition metal chelators (7)”
Self-citationThe chemical basis of ferroptosis
Conrad, M., & Pratt, D. A. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0408-1 · Cited by 1,027 · see citing works
Fundamental Mechanisms of Regulated Cell Death and Implications for Heart Disease
Re, D. P. D., Amgalan, D., Linkermann, A., Liu, Q., & Kitsis, R. N. (2019) · Physiological Reviews · doi:10.1152/physrev.00022.2018 · Cited by 979 · 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
“…prevents nuclear accumulation of DPP4 and then triggers membrane-associated DPP4-mediated lipid peroxidation, which finally results in ferroptosis. are sensitive to erastin (Friedmann Angeli et al., 2014; Jiang et al., 2015; Linkermann et al., 2014; Matsushita et al., 2015; Skouta et al., 2014).”
PEBP1 Wardens Ferroptosis by Enabling Lipoxygenase Generation of Lipid Death Signals
Wenzel, S. E., Tyurina, Y. Y., Zhao, J., Croix, C. M. S., Dar, H. H., Mao, G., Tyurin, V. A., Anthonymuthu, T. S., Kapralov, A. A., Amoscato, A. A., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.044 · Cited by 960 · see citing works
“Therefore, we employed a GPX4 inhibitor, RSL3 (that chemically inactivates the enzyme and suppresses its expression), to block the enzymatic reduction of 15-HpETE-PE (Kagan et al., 2017; Skouta et al., 2014).”
MethodThe development of the concept of ferroptosis
Hirschhorn, T., & Stockwell, B. R. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.043 · Cited by 1,052 · see citing works
“PUFA in cells undergoing ferroptosis [144,145].”
InfluentialSelf-citationInsight into the mechanism of ferroptosis inhibition by ferrostatin-1
Miotto, G., Rossetto, M., Paolo, M. L. D., Orian, L., Venerando, R., Roveri, A., Vučković, A., Bosello-Travain, V., Zaccarin, M., Zennaro, L., et al. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101328 · Cited by 908 · see citing works
Iron homeostasis and oxidative stress: An intimate relationship
Galaris, D., Barbouti, A., & Pantopoulos, K. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118535 · Cited by 922 · see citing works
Reactive oxygen species and cancer paradox: To promote or to suppress?
Galadari, S., Rahman, A. U., Pallichankandy, S., & Thayyullathil, F. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.01.004 · Cited by 895 · see citing works
Transferrin Receptor Is a Specific Ferroptosis Marker
Feng, H., Schorpp, K., Jin, J., Yozwiak, C. E., Hoffstrom, B. G., Decker, A., Rajbhandari, P., Stokes, M. E., Bender, H. G., Csuka, J. M., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.02.049 · Cited by 891 · see citing works
Self-citationOxidative Stress in Neurodegenerative Diseases: From Molecular Mechanisms to Clinical Applications
Liu, Z., Zhou, T., Ziegler, A. C., Dimitrion, P., & Zuo, L. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/2525967 · Cited by 810 · see citing works
“To counteract this, some small antioxidant molecules, such as ferrostatin-1 (Fer-1), have been developed, which show efficacy in attenuating neurodegenerative symptoms [27, 28].”
BackgroundSignaling pathways and defense mechanisms of ferroptosis
Liu, J., Kang, R., & Tang, D. (2021) · FEBS Journal · doi:10.1111/febs.16059 · Cited by 809 · 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
Unsolved mysteries: How does lipid peroxidation cause ferroptosis?
Feng, H., & Stockwell, B. R. (2018) · PLoS Biology · doi:10.1371/journal.pbio.2006203 · Cited by 757 · see citing works
Self-citationFINO2 initiates ferroptosis through GPX4 inactivation and iron oxidation
Gaschler, M. M., Andia, A. A., Liu, H., Csuka, J. M., Hurlocker, B., Vaiana, C. A., Heindel, D. W., Zuckerman, D. S., Bos, P. H., Reznik, E., et al. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0031-6 · Cited by 750 · see citing works
“3, 12 Using an in vitro colorimetric assay, we monitored the oxidation state of iron treated with oxidizing compounds (Figure 5A).”
Self-citationMetabolic determinants of cancer cell sensitivity to canonical ferroptosis inducers
Soula, M., Weber, R. A., Zilka, O., Alwaseem, H., La, K., Yen, F. S., Molina, H., García‐Bermúdez, J., Pratt, D. A., & Birsoy, K. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0613-y · Cited by 754 · see citing works
Mechanisms of neuronal cell death in ischemic stroke and their therapeutic implications
Tuo, Q., Zhang, S., & Lei, P. (2021) · Medicinal Research Reviews · doi:10.1002/med.21817 · Cited by 747 · see citing works
“PUFA oxidation is a critical step in ferroptosis during cellular response to diverse stimuli.(170,243) The oxidation of arachidonoyl (C20:4) fatty acyl chains in the context of PE PLs (i.”
BackgroundImidazole Ketone Erastin Induces Ferroptosis and Slows Tumor Growth in a Mouse Lymphoma Model
Zhang, Y., Tan, H., Daniels, J. D., Zandkarimi, F., Liu, H., Brown, L. M., Uchida, K., O’Connor, O. A., & Stockwell, B. R. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.01.008 · Cited by 729 · see citing works
“The decrease in the phospholipids PC and PE upon IKE treatment is consistent with the effects of piperazine-erastin treatment and erastin treatment on lipid composition in HT-1080 cells (Yang et al., 2016; Skouta et al., 2014).”
InfluentialSelf-citationIron 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
Ferroptosis, a new form of cell death, and its relationships with tumourous diseases
Yu, H., Guo, P., Xie, X., Wang, Y., & Chen, G. (2016) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13008 · Cited by 712 · see citing works
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“It is not at all known whether ferroptosis is involved in PD but it has been suggested that the inhibition of ferroptosis may be neuroprotective (Dixon et al., 2012; Skouta et al., 2014).”
GPx4, Lipid Peroxidation, and Cell Death: Discoveries, Rediscoveries, and Open Issues
Maiorino, M., Conrad, M., & Ursini, F. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7115 · Cited by 709 · see citing works
“Ferrostatin-1 was also identified as a potent inhibitor of fer-roptosis for which a free radical scavenging mechanism had been proposed (103).”
Molecular mechanisms of cell death in neurological diseases
Moujalled, D., Strasser, A., & Liddell, J. R. (2021) · Cell Death & Differentiation · doi:10.1038/s41418-021-00814-y · Cited by 749 · see citing works
The tumor suppressor protein p53 and the ferroptosis network
Kang, R., Kroemer, G., & Tang, D. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.05.074 · Cited by 700 · 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
“, excitotoxic cell death, Huntington’s disease, periventricular leukomalacia, and renal injury) (6, 39), as well as the protective role of HSPB1 in these diseases (40), it will be important to elucidate the mechanisms underlying HSPB1-mediated ferroptosis resistance under various conditions.”
BackgroundLoss of ferroportin induces memory impairment by promoting ferroptosis in Alzheimer’s disease
Bao, W.-D., Pang, P., Zhou, X.-T., Hu, F., Xiong, W., Chen, K., Wang, J., Wang, F., Xie, D., Ya⁃zhuo, H. U., et al. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-020-00685-9 · Cited by 679 · see citing works
Self-citationRegulated necrosis: disease relevance and therapeutic opportunities
Conrad, M., Angeli, J. P. F., Vandenabeele, P., & Stockwell, B. R. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2015.6 · Cited by 630 · see citing works
Self-citationFerroptosis is induced following siramesine and lapatinib treatment of breast cancer cells
Ma, S., Henson, E. S., Chen, Y., & Gibson, S. B. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.208 · Cited by 627 · see citing works
“Cystine transport through the cystine/glutamate antiporter (system xc −) is involved in regulating ROS through activation of GSH.44–46 Glutathione depletion leads to the iron-dependent accumulation of ROS, especially lipid ROS.47,48 The cystine uptake inhibitor erastin has been shown to block GSH activation leading to…”
BackgroundInfluentialFrom 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
Nano-targeted induction of dual ferroptotic mechanisms eradicates high-risk neuroblastoma
Hassannia, B., Wiernicki, B., Ingold, I., Qu, F., Herck, S. V., Tyurina, Y. Y., Bayır, H., Abhari, B. A., Angeli, J. P. F., Choi, S. M., et al. (2018) · Journal of Clinical Investigation · doi:10.1172/jci99032 · Cited by 626 · see citing works
Lipid Peroxidation-Dependent Cell Death Regulated by GPx4 and Ferroptosis
Imai, H., Matsuoka, M., Kumagai, T., Sakamoto, T., & Koumura, T. (2016) · Current topics in microbiology and immunology · doi:10.1007/82_2016_508 · Cited by 629 · see citing works
Targeting ferroptosis opens new avenues for the development of novel therapeutics
Sun, S., Shen, J., Jiang, J., Wang, F., & Min, J. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01606-1 · Cited by 632 · see citing works
“By scavenging free radicals, Fer-1 reduces ferroptosis-induced tissue injury and prolongs survival in mouse models of disease.(3,47,64) However, Fer-1 has not been pursued in drug development, given its metabolic instability and poor pharmacokinetics.”
BackgroundQuercetin alleviates acute kidney injury by inhibiting ferroptosis
Wang, Y., Quan, F., Cao, Q., Lin, Y., Yue, C., Bi, R., Cui, X., Yang, H., Yang, Y., Birnbaumer, L., et al. (2020) · Journal of Advanced Research · doi:10.1016/j.jare.2020.07.007 · Cited by 597 · see citing works
“However, despite the overwhelming evidence highlighting the therapeutic uses of Fer-1, the translational aspect of Fer-1 application in the clinic is limited due to its instability in vivo [7,9].”
BackgroundDixon, S. J., & Stockwell, B. R. (2018) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-030518-055844 · Cited by 588 · see citing works
“PUFA oxidation is essential for the execution of ferroptosis in response to diverse stimuli and can be inhibited by feeding cells deuterated PUFAs that are less susceptible to oxidation (Skouta et al. 2014, Yang et al. 2016).”
BackgroundSelf-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
Chaperone-mediated autophagy is involved in the execution of ferroptosis
Wu, Z., Geng, Y., Lu, X., Shi, Y., Wu, G., Zhang, M., Shan, B., Pan, H., & Yuan, J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1819728116 · Cited by 580 · see citing works
“We found that unlike other inhibitors of ferroptosis such as ferrostatin-1 (Fer-1), which is known to display a strong antioxidant effect with high free radical scavenging activity (33), CDDO did not demonstrate any antioxidant activity (SI Appendix, Fig.”
BackgroundLinkermann, A., Chen, G., Dong, G., Kunzendorf, U., Krautwald, S., & Dong, Z. (2014) · Journal of the American Society of Nephrology · doi:10.1681/asn.2014030262 · Cited by 564 · see citing works
Self-citationFerroptosis, 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
Self-citationFerroptosis and its potential role in the physiopathology of Parkinson’s Disease
Mahoney‐Sanchez, L., Bouchaoui, H., Ayton, S., Devos, D., Duce, J. A., & Devedjian, J.-C. (2020) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2020.101890 · Cited by 558 · 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
“Some oviparous species predispose their young to excretion of metals in both the egg shell and contents (Burger 1994; Skrivan et al. 2005).”
BackgroundSelf-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
“We therefore asked if Fer-1 might act via blocking of localized ROS production in ART-treated Panc-1 cells, as Fer-1 was shown to inhibit lipid peroxidation during ferroptotic cell death [28, 47, 48].”
BackgroundOxidative Damage and Antioxidant Defense in Ferroptosis
Kuang, F., Liu, J., Tang, D., & Kang, R. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.586578 · Cited by 539 · see citing works
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-citationInhibiting Ferroptosis through Disrupting the NCOA4–FTH1 Interaction: A New Mechanism of Action
Fang, Y., Chen, X., Tan, Q., Zhou, H., Xu, J., & Gu, Q. (2021) · ACS Central Science · doi:10.1021/acscentsci.0c01592 · Cited by 515 · see citing works
Li, Y., Cao, Y., Xiao, J., Shang, J., Tan, Q., Feng, P., Huang, W.-F., Wu, F., Zhang, H., & Zhang, X. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-0528-x · Cited by 512 · see citing works
“This finding is in line with results from previous studies suggesting that ferroptosis is involved in the pathogenesis of human diseases such as Huntington’s disease, periventricular leukomalacia, and kidney dysfunction [25], as well as I/R injury [13, 25] and infectious diseases [26].”
ResultSelective covalent targeting of GPX4 using masked nitrile-oxide electrophiles
Eaton, J. K., Furst, L., Ruberto, R. A., Moosmayer, D., Hilpmann, A., Ryan, M. J., Zimmermann, K. C., Cai, L. L., Niehues, M., Badock, V., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0501-5 · Cited by 510 · 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
Li, W., Feng, G., Gauthier, J. M., Lokshina, I., Higashikubo, R., Evans, S., Liu, X., Hassan, A., Tanaka, S., Cicka, M., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci126428 · Cited by 492 · see citing works
“Fer-1 treatment also reduced the abundance of docosanoids and oxidized linoleic acid species consistent with the described mechanism of action of Fer-1 as a scavenger of peroxidated lipids (17)(Supplemental Fig.”
BackgroundSelf-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
Polyunsaturated fatty acid biosynthesis pathway determines ferroptosis sensitivity in gastric cancer
Lee, J.-Y., Nam, M., Son, H. Y., Hyun, K., Jang, S. Y., Kim, J. W., Kim, M. W., Jung, Y., Jang, E., Yoon, S., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2006828117 · Cited by 475 · see citing works
Signaling pathways in Parkinson’s disease: molecular mechanisms and therapeutic interventions
Xu, D.-C., Yong, C., Xu, Y., Chen-Yu, S., & Peng, L. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01353-3 · Cited by 498 · see citing works
“By halting lipid peroxidation, glutathione (GSH), an antioxidant that the body produces from glutamate and cysteine, can suppress ferroptosis.(103,104) The rate-limiting substrate, cysteine, can either be produced from methionine via the transsulfuration route or taken up by the xCT antiporter as an oxidized cystine d…”
BackgroundIron and ferroptosis: A still ill‐defined liaison
Doll, S. G., & Conrad, M. (2017) · IUBMB Life · doi:10.1002/iub.1616 · Cited by 472 · see citing works
“Fer-1 was shown to ameliorate cell death in rat corticostriatal brain slices expressing mutant huntingtin, an ex vivo model for HD, in a cellular model of periventricular leukomalacia, as well as in a proximal tubule (mouse) damage assay (Fe(21) hydroxyquinoline) (38).”
BackgroundFerroptosis and Its Role in Diverse Brain Diseases
Weiland, A., Wang, Y., Wu, W., Lan, X., Han, X., Li, Q., & Wang, J. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1403-3 · Cited by 469 · see citing works
Self-citationThe Role of Erastin in Ferroptosis and Its Prospects in Cancer Therapy
Zhao, Y., Li, Y., Zhang, R., Wang, F., Wang, T., & Jiao, Y. (2020) · OncoTargets and Therapy · doi:10.2147/ott.s254995 · Cited by 459 · see citing works
Hayano, 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
“in models of glutamate toxicity, raising the question of whether CARS knockdown could prevent glutamate toxicity.(4,12) To test whether CARS knockdown could prevent glutamate toxicity in a high-throughput format, we developed an assay”
BackgroundSelf-citationThe Hippo Pathway Effector TAZ Regulates Ferroptosis in Renal Cell Carcinoma
Yang, W., Ding, C. C., Sun, T., Rupprecht, G., Lin, C., Hsu, D. S., & Chi, J. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.07.107 · Cited by 457 · 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
“Lipoxygenases can drive ferroptosis, mediated by system Xc− inhibition, by catalyzing the dioxygenation of membrane lipid PUFAs to produce fatty acid hydroperoxides (Yang et al., 2016).”
BackgroundInfluentialQin, X., Zhang, J., Wang, B., Xu, G., Yang, X., Zou, Z., & Yu, C. (2021) · Autophagy · doi:10.1080/15548627.2021.1911016 · Cited by 436 · see citing works
“bitor of the erastin-induced ferroptosis in HT-1080 cells (EC50 = 60 nM) [10]; it inhibited lipid peroxidation but did not affect mitochondrial reactive oxygen species (ROS) formation or lysosomal membrane permeability [22].”
BackgroundACSL4 deficiency confers protection against ferroptosis-mediated acute kidney injury
Wang, Y., Zhang, M., Bi, R., Su, Y., Quan, F., Lin, Y., Yue, C., Cui, X., Zhao, Q., Liu, S., et al. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102262 · Cited by 440 · see citing works
Switching Apoptosis to Ferroptosis: Metal–Organic Network for High-Efficiency Anticancer Therapy
Zheng, D., Lei, Q., Zhu, J., Fan, J., Li, C., Li, C., Xu, Z., Cheng, S., & Zhang, X. (2016) · Nano Letters · doi:10.1021/acs.nanolett.6b04060 · Cited by 434 · see citing works
Ferroptosis-Induced Endoplasmic Reticulum Stress: Cross-talk between Ferroptosis and Apoptosis
Lee, Y., Lee, D.-H., Choudry, H. A., Bartlett, D. L., & Lee, Y. J. (2018) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-18-0055 · Cited by 434 · see citing works
Ferroptosis involves in intestinal epithelial cell death in ulcerative colitis
Xu, M., Tao, J., Yang, Y., Tan, S., Liu, H., Jiang, J., Zheng, F., & Wu, B. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2299-1 · Cited by 433 · see citing works
FTH1 Inhibits Ferroptosis Through Ferritinophagy in the 6-OHDA Model of Parkinson's Disease
Tian, Y., Lü, J., Hao, X., Li, H., Zhang, G., Liu, X., Li, X., Zhao, C., Kuang, W., Chen, D., et al. (2020) · Neurotherapeutics · doi:10.1007/s13311-020-00929-z · Cited by 425 · see citing works
Targeting Nrf2 to Suppress Ferroptosis and Mitochondrial Dysfunction in Neurodegeneration
Abdalkader, M., Lampinen, R., Kanninen, K. M., Malm, T., & Liddell, J. R. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00466 · Cited by 421 · 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
“, 2019), and by the finding that ferroptosis inhibitors such as iron chelators and the lipid-peroxidation inhibitor Ferrostatin-1 are neuroprotective in animal and cellular models of neurodegenerative diseases (Chen et al., 2013; Kaur et al., 2003; Kupershmidt et al., 2012; Skouta et al., 2014).”
BackgroundMolecular mechanisms of ferroptosis and their involvement in brain diseases
Costa, I., Barbosa, D. J., Benfeito, S., Silva, V., Chavarria, D., Borges, F., Remião, F., & Silva, R. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108373 · Cited by 402 · see citing works
Xie, B., Wang, Y., Lin, Y., Mao, Q., Feng, J., Gao, G., & Jiang, J. (2018) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13069 · Cited by 394 · see citing works
Artemisinin derivatives induce iron-dependent cell death (ferroptosis) in tumor cells
Ooko, E., Saeed, M. E. M., Kadioglu, O., Sarvi, S., Colak, M., Elmasaoudi, K., Janah, R., Greten, H. J., & Efferth, T. (2015) · Phytomedicine · doi:10.1016/j.phymed.2015.08.002 · Cited by 387 · see citing works
Oxidative Stress: Signaling Pathways, Biological Functions, and Disease
Liu, S., Liu, J., Wang, Y., Deng, F., & Deng, Z. (2025) · MedComm · doi:10.1002/mco2.70268 · Cited by 435 · see citing works
Ferroptosis and necroinflammation, a yet poorly explored link
Proneth, B., & Conrad, M. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0173-9 · Cited by 378 · see citing works
Heme oxygenase-1 mitigates ferroptosis in renal proximal tubule cells
Adedoyin, O. O., Boddu, R., Traylor, A., Lever, J. M., Bolisetty, S., George, J. F., & Agarwal, A. (2017) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00044.2017 · Cited by 369 · see citing works
- Authors
- 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., & Stockwell, B. R.
- Affiliations
- Columbia University (US)
- Boston Children's Hospital (US)
- Duke University (US)
- University of Michigan (US)
- Christian-Albrechts-Universität zu Kiel (DE)
- Corresponding author
- Stockwell, Brent R.
- ORCID
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2014-03-04
- Volume
- 136
- Issue
- 12
- Pages
- 4551-4556
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- PMC
- PMC3985476
- OpenAlex
- W2074892323
- Cited by
- 1,146
- References
- 44
- Citations by year
- 2026: 115 · 2025: 120 · 2024: 172 · 2023: 144 · 2022: 142 · 2021: 107 · 2020: 108 · 2019: 75 · 2018: 59 · 2017: 39 · 2016: 35 · 2015: 24 · 2014: 6
- FWCI
- 27.82
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Journal of the American Chemical Society (publishedVersion, other-oa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
- Funders
- Howard Hughes Medical Institute (Stockwell)
- National Cancer Institute (CA161061, R01CA097061)
- National Institute of General Medical Sciences (R01GM085081)
- 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 › Biochemistry › Antioxidant Activity and Oxidative Stress
- Keywords
- ferroptosis, Fer-1, lipid peroxidation, oxidative lipid damage, cell death, Huntington's disease, periventricular leukomalacia, renal dysfunction, non-apoptotic cell death
- MeSH terms
- Cyclohexylamines, Huntington Disease, Kidney Diseases, Leukomalacia, Periventricular, Membrane Lipids, Oxidation-Reduction, Phenylenediamines, Lipid Peroxidation, Cell Death
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