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Regulation of Ferroptotic Cancer Cell Death by GPX4
Open accessAbstract
Ferroptosis is a form of nonapoptotic cell death for which key regulators remain unknown. We sought a common mediator for the lethality of 12 ferroptosis-inducing small molecules. We used targeted metabolomic profiling to discover that depletion of glutathione causes inactivation of glutathione peroxidases (GPXs) in response to one class of compounds and a chemoproteomics strategy to discover that GPX4 is directly inhibited by a second class of compounds. GPX4 overexpression and knockdown modulated the lethality of 12 ferroptosis inducers, but not of 11 compounds with other lethal mechanisms. In addition, two representative ferroptosis inducers prevented tumor growth in xenograft mouse tumor models. Sensitivity profiling in 177 cancer cell lines revealed that diffuse large B cell lymphomas and renal cell carcinomas are particularly susceptible to GPX4-regulated ferroptosis. Thus, GPX4 is an essential regulator of ferroptotic cancer cell death.
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In the citing paper
“the reduced glutathione (GSH)-dependent enzyme glutathione peroxidase 4 (GPX4)—which is directly targeted by RSL3—has emerged as the main endogenous inhibitor of ferroptosis by virtue of its ability to limit lipid peroxidation by catalyzing the GSH-dependent reduction of lipid hydroperoxides to lipid alcohols [547–550].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [548]
In the citing paper
“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 [548]
In the citing paper
“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 [548]
In the citing paper
“Among these genes, we identified known regulators of apoptosis, such as TP53, IKBIP, and factors specifically of neuronal survival, such as XIAP17–20, GDPGP121 and MAP3K123,22–24, as well as genes not previously implicated in neuronal survival, such as IGF2BP1 and IGF2BP3.”
From Genome-wide CRISPRi/a screens in human neurons link lysosomal failure to ferroptosis (2021) · cites this paper as [19]
In the citing paper
“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 Yang et al., 2014
In the citing paper
“Moreover, glutathione is not depleted during RSL3-induced cell death [24], supporting the presence of an alternative ferroptosis-initiating mechanism for RSL3.”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [24]
In the citing paper
“Analysis of mass spectrometry-based proteomic data from an affinity pulldown experiment ranked GPX4 (glutathione peroxidase 4, PHGPx) as the top protein target for (1S,3R)-RSL3 [24]; western blotting further confirmed binding between (1S,3R)-RSL3 and GPX4.”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [24]
In the citing paper
“Glutathione depletion causes loss of cellular antioxidant capacity, as well as inhibition of glutathione-dependent enzymes, such as glutathione peroxidases [24, 25].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [24]
In the citing paper
“Moreover, knockdown of GPX4 expression generates lipid ROS and induces ferroptosis, supporting the hypothesis that (1S, 3R)-RSL3 induces ferroptosis through inhibition of GPX4 [24].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [24]
In the citing paper
“This glutathione depletion is sufficient for erastin-dependent cell death, as glutathione depletion by another reagent, buthionine sulfoxamine (BSO), also initiated ferroptosis [24].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [24]
In the citing paper
“Cell lysates prepared from (1S, 3R)-RSL3-treated cells could not reduce phosphatidylcholine hydroperoxides into the corresponding alcohols, demonstrating that RSL3 inhibits GPX4 enzyme activity [24].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [24]
In the citing paper
“The screening assay in which erastin and RSL3 were identified later revealed ten additional compounds that induce ferroptosis [24, 26]. All but one compound (DPI2) inhibited GPX4 directly, similar to RSL3. In contrast, DPI2 depleted GSH, like erastin [24].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [24]
In the citing paper
“Overexpression of GPX4 suppressed cell death induced by these compounds [24], but not other lethal agents, indicating that GPX4 is a specific and robust central regulator of ferroptotic cell death, akin to BCL-2 in apoptosis.”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [24]
In the citing paper
“Indeed, a metabolite profiling assay revealed that glutathione was the most decreased cellular metabolite during erastin-induced ferroptosis [24].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [24]
In the citing paper
“Although erastin displayed selective lethality in engineered cells overexpressing HRASG12V , there was no consistent difference in erastin sensitivity between wild-type and mutated RAS cells.”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [24]
In the citing paper
“Tubular cells in the kidney are also particularly susceptible to ferroptosis induction by Gpx4 deletion in vivo [15], which is intriguing in light of the enhanced sensitivity of renal cell carcinoma cell lines in culture to erastin [24].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [24]
In the citing paper
“Moreover, RCC was found to be particularly susceptible to erastin-induced ferroptosis compared to other tissues in the NCI-60 panel, a panel of cancer cell lines derived from eight different tissues [24].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [24]
In the citing paper
“In addition, the depletion of GPX4 can promote the accumulation of lipid peroxide and lipid free radicals, causing ferroptosis (Yang et al., 2014).”
From MiR-378a-3p/ SLC7A11 regulate ferroptosis in nerve injury induced by lead exposure (2022) · cites this paper as Yang et al., 2014
In the citing paper
“Lipid peroxidation is an important characteristic of ferroptosis and is strongly regulated by GPX4 and GSH (Chen et al., 2015;Yang et al., 2014).”
From MiR-378a-3p/ SLC7A11 regulate ferroptosis in nerve injury induced by lead exposure (2022) · cites this paper as Yang et al., 2014
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Citations
Cites
Controlling the False Discovery Rate: A Practical and Powerful Approach to Multiple Testing
Benjamini, Y., & Hochberg, Y. (1995) · Journal of the Royal Statistical Society Series B: Statistical Methodology · doi:10.1111/j.2517-6161.1995.tb02031.x · Cited by 109,482
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
Self-citationChemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury
Degterev, A., Huang, Z., Boyce, M., Li, Y., Jagtap, P., Mizushima, N., Cuny, G. D., Mitchison, T. J., Moskowitz, M. A., & Yuan, J. (2005) · Nature Chemical Biology · doi:10.1038/nchembio711 · Cited by 3,068
Wendel, A. (1981) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(81)77046-0 · Cited by 3,032
Fatty acid synthase and the lipogenic phenotype in cancer pathogenesis
Menendez, J. A., & Lupu, R. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2222 · Cited by 2,941
The NCI60 human tumour cell line anticancer drug screen
Shoemaker, R. H. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1951 · Cited by 2,673
Production of large amounts of hydrogen peroxide by human tumor cells.
Szatrowski, T. P., & Nathan, C. (1991) · PubMed · Cited by 2,504
Galluzzi, L., Vitale, I., Abrams, J. M., Alnemri, E. S., Baehrecke, E. H., Blagosklonny, M. V., Dawson, T. M., Dawson, V. L., El-Deiry, W. S., Fulda, S., et al. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2011.96 · Cited by 2,421
Brigelius-Flohé, R., & Maiorino, M. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.11.020 · Cited by 1,904
Yang, W. S., & Stockwell, B. R. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.02.010 · Cited by 1,876
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Items 501–600 of 1,027
Distinct Types of Cell Death and the Implication in Diabetic Cardiomyopathy
Chen, Y., Hua, Y., Li, X., Arslan, I. M., Zhang, W., & Meng, G. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00042 · Cited by 225
Systematic Analysis of the Aberrances and Functional Implications of Ferroptosis in Cancer
Liu, Z., Zhao, Q., Zuo, Z.-X., Yu, K., Yu, K., Zhang, X.-L., Zhang, X., Sheng, H., Ju, H., Cheng, H., et al. (2020) · iScience · doi:10.1016/j.isci.2020.101302 · Cited by 224
Inhibition of keratinocyte ferroptosis suppresses psoriatic inflammation
Shou, Y., Yang, L., Yang, Y., & Xu, J. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04284-5 · Cited by 226
Chen, X., Tsvetkov, A. S., Shen, H., Isidoro, C., Ktistakis, N. T., Linkermann, A., Koopman, W. J. H., Simon, H., Galluzzi, L., Luo, S., et al. (2024) · Autophagy · doi:10.1080/15548627.2024.2319901 · Cited by 240
Self-citationFerroptosis is involved in acetaminophen induced cell death
Lőrincz, T., Jemnitz, K., Kardon, T., Mandl, J., & Szarka, A. (2015) · Pathology & Oncology Research · doi:10.1007/s12253-015-9946-3 · Cited by 219
Yan, N., Xu, Z., Qu, C., & Zhang, J. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.107844 · Cited by 219
Zhang, B., Chen, X., Ru, F., Gan, Y., Li, B., Xia, W., Dai, G., He, Y., & Chen, Z. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04137-1 · Cited by 221
Wang, Y., Hu, J., Wu, S., Fleishman, J. S., Li, Y., Xu, Y.-S., Zou, W., Wang, J., Feng, Y., Chen, J., et al. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01720-0 · Cited by 225
Triggered ferroptotic polymer micelles for reversing multidrug resistance to chemotherapy
Gao, M., Deng, J., Liu, F., Fan, A., Wang, Y., Wu, H., Ding, D., Kong, D., Wang, Z., Peer, D., et al. (2019) · Biomaterials · doi:10.1016/j.biomaterials.2019.119486 · Cited by 218
Rui, T., Wang, H., Li, Q., Cheng, Y., Gao, Y. Z., Fang, X., Ma, X., Chen, G., Gao, C. H., Gu, Z., et al. (2020) · Journal of Pineal Research · doi:10.1111/jpi.12704 · Cited by 217
Hong, S. H., Lee, D., Lee, Y., Jo, M. J., Jeong, Y. A., Kwon, W. T., Choudry, H. A., Bartlett, D. L., & Lee, Y. J. (2017) · Oncotarget · doi:10.18632/oncotarget.23046 · Cited by 216
Epigenetic regulation of ferroptosis by H2B monoubiquitination and p53
Wang, Y., Yang, L., Zhang, X., Cui, W., Liu, Y., Sun, Q., He, Q., Zhao, S., Zhang, G., Wang, Y., et al. (2019) · EMBO Reports · doi:10.15252/embr.201847563 · Cited by 215
Li, X., Duan, L., Yuan, S., Zhuang, X., Qiao, T., & He, J. (2019) · Journal of Inflammation · doi:10.1186/s12950-019-0216-0 · Cited by 217
Hu, Q., Zhang, Y., Lou, H., Ou, Z., Liu, J., Duan, W., Wang, H., Ge, Y., Min, J., Wang, F., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04008-9 · Cited by 219
Tan, M., Yin, Y., Ma, X., Zhang, J., Pan, W., Tan, M., Zhao, Y., Yang, T., Jiang, T., & Li, H. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05645-y · Cited by 221
Programmed death of macrophages in atherosclerosis: mechanisms and therapeutic targets
Meyer, G. R. Y. D., Zurek, M., Puylaert, P., & Martinet, W. (2024) · Nature Reviews Cardiology · doi:10.1038/s41569-023-00957-0 · Cited by 221
Iron imbalance in neurodegeneration
Levi, S., Ripamonti, M., Moro, A., & Cozzi, A. (2024) · Molecular Psychiatry · doi:10.1038/s41380-023-02399-z · Cited by 189
The Diverse Functions of Non-Essential Amino Acids in Cancer
Choi, B.-H., & Coloff, J. L. (2019) · Cancers · doi:10.3390/cancers11050675 · Cited by 213
miR-182-5p and miR-378a-3p regulate ferroptosis in I/R-induced renal injury
Ding, C., Ding, X., Zheng, J., Wang, B., Li, Y., Xiang, H., Dou, M., Qiao, Y., Tian, P., & Xue, W. (2020) · Cell Death & Disease · doi:10.1038/s41419-020-03135-z · Cited by 197
Mitochondrial ferritin attenuates cerebral ischaemia/reperfusion injury by inhibiting ferroptosis
Wang, P., Cui, Y., Ren, Q., Yan, B., Zhao, Y., Yu, P., Gao, G., Shi, H., Chang, S., & Chang, Y. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03725-5 · Cited by 216
Fan, F., Liu, P., Bao, R., Chen, J., Zhou, M., Mo, Z., Ma, Y., Liu, H., Zhou, Y., Cai, X., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-21-1547 · Cited by 215
RSL3 Drives Ferroptosis through NF‐κB Pathway Activation and GPX4 Depletion in Glioblastoma
Li, S., He, Y., Chen, K., Jiaojiao, S., Zhang, L., He, Y., Yu, H., & Li, Q. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/2915019 · Cited by 213
MYCN mediates cysteine addiction and sensitizes neuroblastoma to ferroptosis
Alborzinia, H., Flórez, A. F., Kreth, S., Brückner, L. M., Yildiz, U., Gartlgruber, M., Odoni, D. I., Poschet, G., Garbowicz, K., Shao, C., et al. (2022) · Nature Cancer · doi:10.1038/s43018-022-00355-4 · Cited by 217
Baicalin induces ferroptosis in osteosarcomas through a novel Nrf2/xCT/GPX4 regulatory axis
Wen, R., Dong, X., Zhuang, H., Pang, F.-X., Ding, S.-C., Li, N., Mai, Y., Zhou, S., Wang, J., & Zhang, J. (2023) · Phytomedicine · doi:10.1016/j.phymed.2023.154881 · Cited by 213
Metal-Based Photosensitizers as Inducers of Regulated Cell Death Mechanisms
Zhang, Y., Doan, B., & Gasser, G. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00161 · Cited by 215
Dangol, S., Chen, Y., Hwang, B. K., & Jwa, N. (2018) · The Plant Cell · doi:10.1105/tpc.18.00535 · Cited by 212
Ferroptosis as a mechanism of neurodegeneration in Alzheimer's disease
Jakaria, M., Belaidi, A. A., Bush, A. I., & Ayton, S. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15519 · Cited by 212
Ferroptosis: Opportunities and Challenges in Myocardial Ischemia‐Reperfusion Injury
Zhao, W., Zhou, Y., Xu, T., & Wu, Q. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/9929687 · Cited by 217
Bi, Y., Liu, S., Qin, X., Abudureyimu, M., Wang, L., Zou, R., Ajoolabady, A., Zhang, W., Hu, P. C., Ren, J. T., et al. (2023) · Journal of Advanced Research · doi:10.1016/j.jare.2023.02.012 · Cited by 218
Jiang, M., Jike, Y., Liu, K., Gan, F., Zhang, K., Xie, M., Zhang, J., Chen, C., Zou, X., Jiang, X., et al. (2023) · Molecular Cancer · doi:10.1186/s12943-023-01804-z · Cited by 212
Pseudolaric acid B triggers ferroptosis in glioma cells via activation of Nox4 and inhibition of xCT
Wang, Z., Ding, Y., Wang, X., Lu, S., Wang, C., He, C. H., Wang, L., Piao, M., Chi, G., Luo, Y., et al. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.04.021 · Cited by 211
Cao, Y., Li, Y., He, C., Yan, F., Li, J., Xu, H., Zhuang, J., Zhou, H., Peng, Y., Fu, X., et al. (2021) · Neuroscience Bulletin · doi:10.1007/s12264-020-00620-5 · Cited by 215
Ferroptosis‐Enhanced Cancer Immunity by a Ferrocene‐Appended Iridium(III) Diphosphine Complex
Wang, W., Ling, Y., Zhong, Y., Li, Z., Tan, C., & Mao, Z. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202115247 · Cited by 211
Yang, J., Griffin, A. S., Qiang, Z., & Ren, J. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01243-0 · Cited by 224
Ferroptosis: A flexible constellation of related biochemical mechanisms
Dixon, S. J., & Pratt, D. A. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.03.005 · Cited by 219
Wang, G., Xie, L., Li, B., Sang, W., Yan, J., Li, J., Tian, H., Li, W., Zhang, Z., Tian, Y., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25990-w · Cited by 211
Origin and Consequences of Necroinflammation
Sarhan, M., Land, W. G., Tonnus, W., Hugo, C., & Linkermann, A. (2018) · Physiological Reviews · doi:10.1152/physrev.00041.2016 · Cited by 217
Cao, J. Y., Poddar, A., Magtanong, L., Lumb, J. H., Mileur, T. R., Reid, M. A., Dovey, C. M., Wang, J., Locasale, J. W., Stone, E. M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.043 · Cited by 212
Kim, D. H., Kim, W. D., Kim, S. K., Moon, D. H., & Lee, S. J. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2618-6 · Cited by 211
Targeting Ferroptosis: Pathological Mechanism and Treatment of Ischemia‐Reperfusion Injury
Li, X., Ma, N., Xu, J., Zhang, Y., Yang, P., Su, X., Xing, Y., Yang, F., Yang, F., Zhang, L., et al. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/1587922 · Cited by 214
The role of Ca2+ in cell death caused by oxidative glutamate toxicity and ferroptosis
Maher, P. A., van Leyen, K., Dey, P. N., Honrath, B., Dolga, A. M., & Methner, A. (2017) · Cell Calcium · doi:10.1016/j.ceca.2017.05.007 · Cited by 208
Ketamine Induces Ferroptosis of Liver Cancer Cells by Targeting lncRNA PVT1/miR-214-3p/GPX4
He, G., Bao, N. T. Y., Wang, S., Xi, M., Zhang, T.-H., & Chen, F. (2021) · Drug Design Development and Therapy · doi:10.2147/dddt.s332847 · Cited by 209
Elucidating the contribution of mitochondrial glutathione to ferroptosis in cardiomyocytes
Jang, S., Chapa‐Dubocq, X. R., Tyurina, Y. Y., Croix, C. M. S., Kapralov, A. A., Tyurin, V. A., Bayır, H., Kagan, V. E., & Javadov, S. A. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102021 · Cited by 210
Curcumenol triggered ferroptosis in lung cancer cells via lncRNA H19/miR-19b-3p/FTH1 axis
Zhang, R., Pan, T. S., Yu, X., Zhang, M., Xie, H., Liang, Z., Chen, B., Xu, C., Wang, J., Huang, X., et al. (2021) · Bioactive Materials · doi:10.1016/j.bioactmat.2021.11.013 · Cited by 208
Lin, F., Chen, W., Zhou, J., Zhu, J., Yao, Q., Feng, B., Feng, X., Shi, X., Pan, Q., Yu, J., et al. (2022) · Cell Death & Disease · doi:10.1038/s41419-022-04708-w · Cited by 206
Phagocytosis of Necrotic Debris at Sites of Injury and Inflammation
Westman, J., Grinstein, S., & Marques, P. E. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2019.03030 · Cited by 214
Cui, Y., Zhang, Z., Zhou, X., Zhao, Z., Zhao, R., Xu, X., Kong, X., Ren, J., Yao, X., Wen, Q., et al. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02231-x · Cited by 208
YAP1 alleviates sepsis-induced acute lung injury via inhibiting ferritinophagy-mediated ferroptosis
Zhang, J., Zheng, Y., Wang, Y., Wang, J., Sang, A., Song, X., & Li, X. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.884362 · Cited by 206
Fighting age-related orthopedic diseases: focusing on ferroptosis
Ru, Q., Li, Y., Xie, W., Ding, Y., Chen, L., Xu, G., Wu, Y., & Wang, F. (2023) · Bone Research · doi:10.1038/s41413-023-00247-y · Cited by 211
Resveratrol protects against myocardial ischemia-reperfusion injury via attenuating ferroptosis
Li, T., Tan, Y., Ouyang, S., He, J., & Liu, L. (2021) · Gene · doi:10.1016/j.gene.2021.145968 · Cited by 205
Interplay Between Lipid Metabolism and Autophagy
Xie, Y., Li, J., Kang, R., & Tang, D. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00431 · Cited by 205
Gupta, U., Ghosh, S., Wallace, C. T., Shang, P., Xin, Y., Nair, A. P., Yazdankhah, M., Strizhakova, A., Ross, M. A., Liu, H., et al. (2022) · Autophagy · doi:10.1080/15548627.2022.2062887 · Cited by 207
Molecular crosstalk between apoptosis, necroptosis, and survival signaling
Berghe, T. V., Kaiser, W. J., Bertrand, M. J. M., & Vandenabeele, P. (2015) · Molecular & Cellular Oncology · doi:10.4161/23723556.2014.975093 · Cited by 209
Daher, B., Parks, S. K., Durivault, J., Cormerais, Y., Baidarjad, H., Tambutté, É., Pouysségur, J., & Vučetić, M. (2019) · Cancer Research · doi:10.1158/0008-5472.can-18-3855 · Cited by 208
Stem Cell Plasticity and Dormancy in the Development of Cancer Therapy Resistance
Angelis, M. L. D., Francescangeli, F., Torre, F. L., & Zeuner, A. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00626 · Cited by 209
Targeting ferroptosis in breast cancer
Li, Z., Chen, L., Chen, C., Zhou, Y., Hu, D., Yang, J., Chen, Y., Zhuo, W., Mao, M., Zhang, X., et al. (2020) · Biomarker Research · doi:10.1186/s40364-020-00230-3 · Cited by 208
Ferroptosis: the potential value target in atherosclerosis
Ouyang, S., You, J., Zhi, C., Li, P., Lin, X., Tan, X., Ma, W., Li, L., & Xie, W. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04054-3 · Cited by 207
The pleiotropic functions of reactive oxygen species in cancer
Wu, K., Zowalaty, A. E. E., Sayin, V. I., & Papagiannakopoulos, T. Y. (2024) · Nature Cancer · doi:10.1038/s43018-024-00738-9 · Cited by 216
Selenium detoxification is required for cancer-cell survival
Carlisle, A. E., Lee, N., Matthew-Onabanjo, A. N., Spears, M. E., Park, S. J., Youkana, D., Doshi, M. B., Peppers, A., Li, R., Joseph, A. B., et al. (2020) · Nature Metabolism · doi:10.1038/s42255-020-0224-7 · Cited by 207
HMOX1 upregulation promotes ferroptosis in diabetic atherosclerosis
Meng, Z., Liang, H., Zhao, J., Gao, J., Liu, C., Ma, X., Liu, J., Liang, B., Jiao, X., Cao, J.-M., et al. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119935 · Cited by 205
Oxidative stress induces mitochondrial iron overload and ferroptotic cell death
Chen, Y., Guo, X., Zeng, Y., Mo, X., Hong, S., He, H., Li, J., Fatima, S., & Liu, Q. (2023) · Scientific Reports · doi:10.1038/s41598-023-42760-4 · Cited by 202
Ferroptosis as a mechanism to mediate p53 function in tumor radiosensitivity
Lei, G., Zhang, Y., Hong, T., Zhang, X., Liu, X., Mao, C., Yan, Y., Koppula, P., Cheng, W., Sood, A. K., et al. (2021) · Oncogene · doi:10.1038/s41388-021-01790-w · Cited by 206
Yin, K., Wang, D., Zhao, H., Wang, Y., Zhang, Y., Liu, Y., Li, B., & Xing, M. (2022) · Environmental Pollution · doi:10.1016/j.envpol.2022.119449 · Cited by 205
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 203
Ferroptosis as an emerging target in inflammatory diseases
Mao, H., Zhao, Y., Li, H., & Lei, L. (2020) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2020.04.001 · Cited by 203
MGST1 is a redox-sensitive repressor of ferroptosis in pancreatic cancer cells
Kuang, F., Liu, J., Xie, Y., Tang, D., & Kang, R. (2021) · Cell Chemical Biology · doi:10.1016/j.chembiol.2021.01.006 · Cited by 199
Ferrostatin-1 alleviates lipopolysaccharide-induced cardiac dysfunction
Xiao, Z., Kong, B., Fang, J., Qin, T., Dai, C., Shuai, W., & Huang, H. (2021) · Bioengineered · doi:10.1080/21655979.2021.2001913 · Cited by 199
Ferroptosis in Parkinson's disease: Molecular mechanisms and therapeutic potential
Ding, X.-S., Gao, L., Han, Z., Eleuteri, S., Shi, W., Shen, Y., Song, Z.-Y., Su, M., Yang, Q., Qu, Y., et al. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102077 · Cited by 211
Sorafenib fails to trigger ferroptosis across a wide range of cancer cell lines
Zheng, J., Sato, M., Mishima, E., Sato, H., Proneth, B., & Conrad, M. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03998-w · Cited by 198
PLA2G6 guards placental trophoblasts against ferroptotic injury
Beharier, O., Tyurin, V. A., Goff, J. P., Guerrero-Santoro, J., Kajiwara, K., Chu, T., Tyurina, Y. Y., St Croix, C. M., Wallace, C. T., Parry, S., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2009201117 · Cited by 198
The α6β4 integrin promotes resistance to ferroptosis
Brown, C. W., Amante, J. J., Goel, H. L., & Mercurio, A. M. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201701136 · Cited by 200
Dimethyl fumarate induces ferroptosis and impairs NF-κB/STAT3 signaling in DLBCL
Schmitt, A., Xu, W., Bucher, P., Grimm, M., Konantz, M., Horn, H., Zapukhlyak, M., Berning, P., Brändle, M., Jarboui, M. A., et al. (2021) · Blood · doi:10.1182/blood.2020009404 · Cited by 202
Zheng, X. W., Wang, Q., Zhou, Y., Zhang, D., Geng, Y., Hu, W., Wu, C., Shi, Y., & Jiang, J. (2022) · 癌症：英文版 · doi:10.1002/cac2.12363 · Cited by 196
Alves, F. M., Lane, D. J. R., Nguyen, T. P. M., Bush, A. I., & Ayton, S. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02088-5 · Cited by 212
Hu, S., Ma, J., Su, C., Chen, Y., Shu, Y., Qi, Z., Zhang, B., Shi, G., Zhang, Y., Zhang, Y., et al. (2021) · Acta Biomaterialia · doi:10.1016/j.actbio.2021.09.003 · Cited by 196
Ke, L., Wei, F., Xie, L., Karges, J., Chen, Y., Ji, L., & Chao, H. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202205429 · Cited by 196
Palmitoylation-dependent regulation of GPX4 suppresses ferroptosis
Huang, B., Wang, H., Liu, S., Meng, H., Luo, D., Zhou, Y., Huang, Y., Nian, Y., Zhang, L., Chu, B., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-56344-5 · Cited by 199
Li, D., Liu, X., Pi, W., Zhang, Y., Yu, L., Cheng, X., Sun, Z., & Jiang, J. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.808480 · Cited by 194
Kinowaki, Y., Kurata, M., Ishibashi, S., Ikeda, M., Tatsuzawa, A., Yamamoto, M., Miura, O., Kitagawa, M., & Yamamoto, K. (2018) · Laboratory Investigation · doi:10.1038/s41374-017-0008-1 · Cited by 194
Induction of ferroptosis and mitochondrial dysfunction by oxidative stress in PC12 cells
Wu, C., Zhao, W., Yu, J. Z., Li, S., Lin, L., & Chen, X. (2018) · Scientific Reports · doi:10.1038/s41598-017-18935-1 · Cited by 195
Programmed Cell Death, from a Cancer Perspective: An Overview
Mishra, A. P., Salehi, B., Sharifi‐Rad, M., Pezzani, R., Kobarfard, F., Sharifi‐Rad, J., & Nigam, M. (2018) · Molecular Diagnosis & Therapy · doi:10.1007/s40291-018-0329-9 · Cited by 200
Zhang, P., Chen, L., Zhao, Q., Du, X., Bi, M., Li, Y. H., Jiao, Q., & Jiang, H. F. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.03.015 · Cited by 192
Ferroptosis mediates selective motor neuron death in amyotrophic lateral sclerosis
Wang, T., Tomas, D., Perera, N. D., Cuic, B., Luikinga, S. J., Viden, A., Barton, S. K., McLean, C., Samson, A. L., Southon, A. G., et al. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-021-00910-z · Cited by 193
Hu, Q., Wei, W., Wu, D., Huang, F., Li, M., Li, W., Yin, J., Peng, Y., Lu, Y., Zhao, Q., et al. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.810327 · Cited by 194
TMEM164 is a new determinant of autophagy-dependent ferroptosis
Liu, J., Liu, Y., Wang, Y., Li, C., Xie, Y., Klionsky, D. J., Kang, R., & Tang, D. (2022) · Autophagy · doi:10.1080/15548627.2022.2111635 · Cited by 195
Molecular Mechanisms of Ferroptosis and Relevance to Cardiovascular Disease
Xie, L., Fefelova, N., Pamarthi, S. H., & Gwathmey, J. K. (2022) · Cells · doi:10.3390/cells11172726 · Cited by 195
Mitochondrial permeability transition pore-dependent necrosis
Robichaux, D. J., Harata, M., Murphy, E., & Karch, J. M. (2022) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2022.11.003 · Cited by 197
Upadhyayula, P. S., Higgins, D. M. O., Mela, A., Banu, M. A., Dovas, A., Zandkarimi, F., Patel, P. R., Mahajan, A., Humala, N., Nguyen, T. T. T., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36630-w · Cited by 195
Self-citationOrganometallic anti-tumor agents: targeting from biomolecules to dynamic bioprocesses
Peng, K., Zheng, Y., Xia, W. T., & Mao, Z. (2023) · Chemical Society Reviews · doi:10.1039/d2cs00757f · Cited by 193
ACSL4 and polyunsaturated lipids support metastatic extravasation and colonization
Wang, Y., Hu, M., Cao, J., Wang, F., Han, J. R., Wu, T. W., Li, L., Yu, J., Fan, Y., Xie, G., et al. (2024) · Cell · doi:10.1016/j.cell.2024.10.047 · Cited by 197
Recommendations for robust and reproducible research on ferroptosis
Mishima, E., Nakamura, T., Doll, S. G., Proneth, B., Fedorova, M., Pratt, D. A., Angeli, J. P. F., Dixon, S. J., Wahida, A., & Conrad, M. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-025-00843-2 · Cited by 211
Searching for harmony in transition-metal signaling
Chang, C. J. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1913 · Cited by 190
Pharmacologic Screening Identifies Metabolic Vulnerabilities of CD8+ T Cells
Drijvers, J. M., Gillis, J. E., Muijlwijk, T., Nguyen, T. H., Gaudiano, E. F., Harris, I. S., LaFleur, M. W., Ringel, A. E., Yao, C.-H., Kurmi, K., et al. (2020) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-20-0384 · Cited by 191
Five-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 193
Lipid droplets and polyunsaturated fatty acid trafficking: Balancing life and death
Danielli, M., Perne, L., Jarc Jovičić, E., & Petan, T. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1104725 · Cited by 180
Targeting Programmed Cell Death Using Small‐Molecule Compounds to Improve Potential Cancer Therapy
Ke, B., Tian, M., Li, J., Liu, B., & He, G. (2016) · Medicinal Research Reviews · doi:10.1002/med.21398 · Cited by 190
NEET Proteins: A New Link Between Iron Metabolism, Reactive Oxygen Species, and Cancer
Mittler, R., Darash‐Yahana, M., Sohn, Y. S., Bai, F., Song, L., Cabantchik, I. Z., Jennings, P. A., Onuchic, J. N., & Nechushtai, R. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7502 · Cited by 189
Role of acyl-CoA synthetase ACSL4 in arachidonic acid metabolism
Kuwata, H., & Hara, S. (2019) · Prostaglandins & Other Lipid Mediators · doi:10.1016/j.prostaglandins.2019.106363 · Cited by 192
Tumor Microenvironment: A Metabolic Player that Shapes the Immune Response
Cassim, S., & Pouysségur, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms21010157 · Cited by 192
Guo, X., Liu, F., Deng, J., Dai, P., Qin, Y., Li, Z., Wang, B., Fan, A., Wang, Z., & Zhao, Y. (2020) · ACS Nano · doi:10.1021/acsnano.0c00764 · Cited by 190
Metadata
- Authors
- 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., Brown, L. M., Girotti, A. W., Cornish, V. W., Schreiber, S. L., & Stockwell, B. R.
- Affiliations
- Columbia University (US)
- Broad Institute (US)
- Medical College of Wisconsin (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Stockwell, Brent R.
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2014-01
- Volume
- 156
- Issue
- 1-2
- Pages
- 317-331
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC4076414
- OpenAlex
- W2002490399
- Cited by
- 7,713
- References
- 48
- Citations by year
- 2026: 1070 · 2025: 1226 · 2024: 1343 · 2023: 1164 · 2022: 1041 · 2021: 759 · 2020: 421 · 2019: 256 · 2018: 151 · 2017: 115 · 2016: 86 · 2015: 53 · 2014: 25
- FWCI
- 74.73
- 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 Science Foundation (CHE 0840451)
- New York State Stem Cell Science (C026715)
- Empire State Development's Division of Science, Technology and Innovation
- Arnold and Mabel Beckman Foundation
- National Institutes of Health (R01CA161061, 5R01CA097061, 5R01GM085081, 1S10RR025431-01A1)
- Broad Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Ferroptosis and cancer prognosis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Keywords
- ferroptosis, GPX4, glutathione peroxidase, glutathione depletion, ferroptosis inducers, non-apoptotic cell death, cancer cell death, chemoproteomics, targeted metabolomics, diffuse large B-cell lymphoma, renal cell carcinoma, tumor growth inhibition
- MeSH terms
- Phospholipid Hydroperoxide Glutathione Peroxidase, Animals, Carbolines, Carcinoma, Renal Cell, Glutathione, Glutathione Peroxidase, Humans, Neoplasm Transplantation, Neoplasms, Piperazines, Lymphoma, B-Cell, Cell Death, Cell Line, Tumor, Mice, Gene Knockdown Techniques, Heterografts
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