The DOI matches its Crossref record; 33 of the 35 references it cites were found in a registry or an index.
Synthetic lethal screening identifies compounds activating iron-dependent, nonapoptotic cell death in oncogenic-RAS-harboring cancer cells.
Open accessAbstract
We screened small molecules to identify two compounds, which we named RSL3 and RSL5, that have increased lethality in the presence of oncogenic RAS. Counter screening with biologically active compounds defined aspects of the mechanism of action for RSL3 and RSL5, such as a nonapoptotic, MEK-dependent, and iron-dependent oxidative cell death. Erastin, a previously reported compound with RAS-selective lethality, showed similar properties. RNA interference experiments targeting voltage-dependent anion channel 3 (VDAC3), a target of erastin, demonstrated that RSL5 is a scaffold that acts through VDACs to activate the observed pathway. RSL3 activated a similar death mechanism but in a VDAC-independent manner. We found that cells transformed with oncogenic RAS have increased iron content relative to their normal cell counterparts through upregulation of transferrin receptor 1 and downregulation of ferritin heavy chain 1 and ferritin light chain.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“Under normal circumstances, glutathione peroxidase (GPX) neutralizes lipid peroxide to lipid alcohols, but the depletion of intracellular glutathione (GSH, GPX substrate) reduces GPX functionality (Yang and Stockwell, 2008; Friedmann Angeli et al., 2014).”
From Toxic Concentrations of Glutamate Induce Ferroptosis without Affecting Mitochondrial Respiration in Rodent Brain Slice Cultures (2026) · cites this paper as Yang and Stockwell, 2008
Experimental — accuracy not yet measuredIn 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 [543]
In the citing paper
“The mode of cell death induced by these compounds was surprisingly found to be non-apoptotic, as cells treated with erastin and RSL3 died in the absence of apoptotic hallmarks [11, 12, 13], and in cells where the core apoptosis machinery – caspases, BAX, and BAK was suppressed [14].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [12]
In the citing paper
“The first ferroptosis-inducing compounds, erastin [11] and RSL3 [12], were discovered using high-throughout screening of small molecule libraries [11, 12].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [12]
In the citing paper
“Cell death induced by RSL3 shares common features with erastin-mediated ferroptosis, such as iron, MEK, and ROS dependencies [12].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [12]
In the citing paper
“Moreover, iron chelators were identified as inhibitors of cell death induction, after RSL3 treatment, revealing the requirement of cellular iron [12].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [12]
In the citing paper
“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 [66]
In the citing paper
“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 [66]
In the citing paper
“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 [66]
In the citing paper
“two structurally different inducers of ferroptosis that affect distinct pathways [66].”
From Iron accumulation in senescent cells is coupled with impaired ferritinophagy and inhibition of ferroptosis (2018) · cites this paper as [66]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Specific killing of BRCA2-deficient tumours with inhibitors of poly(ADP-ribose) polymerase
Bryant, H. E., Schultz, N., Thomas, H. D., Parker, K. M., Flower, D., Lopez, E., Kyle, S., Meuth, M., Curtin, N. J., & Helleday, T. (2005) · Nature · doi:10.1038/nature03443 · Cited by 5,198
The ferritins: molecular properties, iron storage function and cellular regulation
Harrison, P. M., & Arosio, P. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00022-9 · Cited by 2,667
Creation of human tumour cells with defined genetic elements
Hahn, W. C., Counter, C. M., Lundberg, A. S., Beijersbergen, R. L., Brooks, M. W., & Weinberg, R. A. (1999) · Nature · doi:10.1038/22780 · Cited by 2,345
Systematic Genetic Analysis with Ordered Arrays of Yeast Deletion Mutants
Tong, A. H. Y., Evangelista, M., Parsons, A. B., Xu, H., Bader, G. D., Pagé, N., Robinson, M., Raghibizadeh, S., Hogue, C. W. V., Bussey, H., et al. (2001) · Science · doi:10.1126/science.1065810 · Cited by 2,138
A Lentiviral RNAi Library for Human and Mouse Genes Applied to an Arrayed Viral High-Content Screen
Moffat, J., Grueneberg, D. A., Yang, X., Kim, S. Y., Kloepfer, A. M., Hinkle, G., Piqani, B., Eisenhaure, T., Luo, B., Grenier, J. K., et al. (2006) · Cell · doi:10.1016/j.cell.2006.01.040 · Cited by 1,804
Self-citationDiscovery and development of sorafenib: a multikinase inhibitor for treating cancer
Wilhelm, S., Carter, C. A., Lynch, M., Lowinger, T., Dumas, J., Smith, R., Schwartz, B., Simantov, R., & Kelley, S. (2006) · Nature reviews. Drug discovery · doi:10.1038/nrd2130 · Cited by 1,651
RAS–RAF–MEK-dependent oxidative cell death involving voltage-dependent anion channels
Yagoda, N., von Rechenberg, M., Zaganjor, E., Bauer, A. J., Yang, W. S., Fridman, D. J., Wolpaw, A. J., Smukste, I., Peltier, J. M., Boniface, J. J., et al. (2007) · Nature · doi:10.1038/nature05859 · Cited by 1,631
Self-citationDolma, S., Lessnick, S. L., Hahn, W. C., & Stockwell, B. R. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00050-3 · Cited by 1,446
Self-citationEnhanced sensitivity of PTEN-deficient tumors to inhibition of FRAP/mTOR
Neshat, M. S., Mellinghoff, I. K., Tran, C., Stiles, B. L., THOMAS, G. V., Petersen, R., Frost, P., Gibbons, J. J., Wu, H., & Sawyers, C. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171076798 · Cited by 971
Paull, K. D., Shoemaker, R. H., Hodes, L., Monks, A. P., Scudiero, D. A., Rubinstein, L., Plowman, J., & Boyd, M. R. (1989) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/81.14.1088 · Cited by 970
Flagged first, then by citations
2 of the 35 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 101–200 of 1,002
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
A delicate balance: Iron metabolism and diseases of the brain
Hare, D. J., Ayton, S., Bush, A. I., & Lei, P. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00034 · Cited by 459
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 441
Wnt/beta-catenin signaling confers ferroptosis resistance by targeting GPX4 in gastric cancer
Wang, Y., Zheng, L., Shang, W., Yang, Z., Li, T., Liu, F., Shao, W., Lv, L. L., Chai, L., Qu, L., et al. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01008-w · Cited by 439
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
Self-citationOxidative stress and regulated cell death in Parkinson’s disease
Dionísio, P. A., Amaral, J. D., & Rodrigues, C. M. P. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101263 · Cited by 443
The 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
The role of NCOA4-mediated ferritinophagy in health and disease
Santana-Codina, N., & Mancias, J. D. (2018) · Pharmaceuticals · doi:10.3390/ph11040114 · Cited by 410
Molecular 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
Regulatory Phenomena in the Glutathione Peroxidase Superfamily
Brigelius‐Flohé, R., & Flohé, L. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7905 · Cited by 410
Ma, H., Wang, X., Zhang, W., Li, H., Zhao, W., Sun, J., & Yang, M. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/9067610 · Cited by 396
The crosstalk between ferroptosis and mitochondrial dynamic regulatory networks
Li, J., Jia, Y., Ding, Y.-X., Bai, J., Cao, F., & Li, F. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.83348 · Cited by 417
NRF2 Promotes Tumor Maintenance by Modulating mRNA Translation in Pancreatic Cancer
Chio, I. I. C., Jafarnejad, S. M., Ponz-Sarvise, M., Park, Y., Rivera, K., Palm, W., Wilson, J., Sangar, V., Hao, Y., Öhlund, D., et al. (2016) · Cell · doi:10.1016/j.cell.2016.06.056 · Cited by 378
“This includes erastin (Yang and Stockwell, 2008), dehydroascorbic acid (oxidized vitamin C) (Yun et al., 2015), and platinumbased cytotoxics (Socinski, 2004).”
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 380
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 372
Ferroptosis in Cancer Cell Biology
Bebber, C. M., Müller, F., Clemente, L. P., Weber, J., & von Karstedt, S. (2020) · Cancers · doi:10.3390/cancers12010164 · Cited by 372
Hypoxia, oxidative stress, and the interplay of HIFs and NRF2 signaling in cancer
Bae, T., Hallis, S. P., & Kwak, M. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-024-01180-8 · Cited by 410
Necroptosis and ferroptosis are alternative cell death pathways that operate in acute kidney failure
Müller, T., Dewitz, C., Schmitz, J., Schröder, A. S., Bräsen, J. H., Stockwell, B. R., Murphy, J. M., Kunzendorf, U., & Krautwald, S. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2547-4 · Cited by 370
Self-citationMitochondrial rescue prevents glutathione peroxidase-dependent ferroptosis
Jelinek, A., Heyder, L., Daude, M., Plessner, M., Krippner, S., Grosse, R., Diederich, W. E., & Culmsee, C. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.01.019 · Cited by 364
JNK-signaling: A multiplexing hub in programmed cell death
Dhanasekaran, D. N., & Reddy, E. P. (2017) · Genes & Cancer · doi:10.18632/genesandcancer.155 · Cited by 369
An essential role for functional lysosomes in ferroptosis of cancer cells
Torii, S., Shintoku, R., Kubota, C., Yaegashi, M., Torii, R., Sasaki, M., Suzuki, T., Mori, M., Yoshimoto, Y., Takeuchi, T., et al. (2016) · Biochemical Journal · doi:10.1042/bj20150658 · Cited by 349
Ferroptosis in health and disease
Berndt, C., Alborzinia, H., Skafar, V., Ayton, S., Barayeu, U., Bartelt, A., Bayır, H., Bebber, C. M., Birsoy, K., Böttcher, J. P., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103211 · Cited by 372
Self-citationThe epigenetic regulators and metabolic changes in ferroptosis-associated cancer progression
Wu, Y., Zhang, S.-W., Gong, X., Tam, S., Xiao, D., Liu, S., & Tao, Y. (2020) · Molecular Cancer · doi:10.1186/s12943-020-01157-x · Cited by 343
Ferroptosis and cell death mechanisms in Parkinson's disease
Guiney, S. J., Adlard, P. A., Bush, A. I., Finkelstein, D. I., & Ayton, S. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.01.004 · Cited by 353
Cell death in pancreatic cancer: from pathogenesis to therapy
Chen, X., Zeh, H. J., Kang, R., Kroemer, G., & Tang, D. (2021) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-021-00486-6 · Cited by 344
Bayır, H., Dixon, S. J., Tyurina, Y. Y., Kellum, J. A., & Kagan, V. E. (2023) · Nature Reviews Nephrology · doi:10.1038/s41581-023-00689-x · Cited by 355
Recent progress in ferroptosis: inducers and inhibitors
Du, Y., & Guo, Z. (2022) · Cell Death Discovery · doi:10.1038/s41420-022-01297-7 · Cited by 342
The therapeutic potential of targeting regulated non-apoptotic cell death
Hadian, K., & Stockwell, B. R. (2023) · Nature Reviews Drug Discovery · doi:10.1038/s41573-023-00749-8 · Cited by 349
Self-citationCell Death Pathways in Ischemic Stroke and Targeted Pharmacotherapy
Datta, A., Sarmah, D., Mounica, L., Kaur, H., Kesharwani, R., Verma, G., Veeresh, P., Kotian, V., Kalia, K., Borah, A., et al. (2020) · Translational Stroke Research · doi:10.1007/s12975-020-00806-z · Cited by 336
Cell death pathways: intricate connections and disease implications
Kist, M., & Vucic, D. (2021) · The EMBO Journal · doi:10.15252/embj.2020106700 · Cited by 337
Unraveling the Potential Role of Glutathione in Multiple Forms of Cell Death in Cancer Therapy
Lv, H., Zhen, C., Liu, J., Yang, P., Hu, L., & Shang, P. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/3150145 · Cited by 320
Dixon, S. J. (2017) · Immunological Reviews · doi:10.1111/imr.12533 · Cited by 314
Emerging mechanisms and targeted therapy of ferroptosis in cancer
Wang, H., Cheng, Y., Mao, C., Liu, S., Xiao, D., Huang, J. X., & Tao, Y. (2021) · Molecular Therapy · doi:10.1016/j.ymthe.2021.03.022 · Cited by 326
Ferroptosis Detection: From Approaches to Applications
Zeng, F., Nijiati, S., Tang, L., Ye, J., Zhou, Z., & Chen, X. S. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202300379 · Cited by 324
Updated mechanisms of MASLD pathogenesis
Li, Y., Yang, P., Ye, J., Xu, Q., Wu, J., & Wang, Y. (2024) · Lipids in Health and Disease · doi:10.1186/s12944-024-02108-x · Cited by 354
Ferroptosis Inducers Are a Novel Therapeutic Approach for Advanced Prostate Cancer
Ghoochani, A., Hsu, E., Aslan, M., Rice, M. A., Nguyen, H. M., Brooks, J. D., Corey, E., Paulmurugan, R., & Stoyanova, T. I. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-3477 · Cited by 324
The Role of NCOA4-Mediated Ferritinophagy in Ferroptosis
Santana-Codina, N., Gikandi, A., & Mancias, J. D. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-62026-4_4 · Cited by 329
Ferroptosis: principles and significance in health and disease
Chen, F., Kang, R., Tang, D., & Liu, J. (2024) · Journal of Hematology & Oncology · doi:10.1186/s13045-024-01564-3 · Cited by 341
Yang, J., Mo, J., Dai, J., Ye, C., Cen, W., Zheng, X., Jiang, L., & Ye, L. (2021) · Cell Death & Disease · doi:10.1038/s41419-021-04367-3 · Cited by 300
“RAS-selective lethal 3 (RSL3), a small molecule, can kill RAS mutant cancer cells [10] and activate irondependent, nonapoptotic cell death of RAS mutant cancer cells [11].”
BackgroundA guideline on the molecular ecosystem regulating ferroptosis
Dai, E., Chen, X., Linkermann, A., Jiang, X., Kang, R., Kagan, V. E., Bayır, H., Yang, W. S., García‐Sáez, A. J., Ioannou, M. S., et al. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01360-8 · Cited by 327
Self-citationSystematic Mapping of Genetic Interaction Networks
Dixon, S. J., Costanzo, M., Baryshnikova, A., Andrews, B., & Boone, C. M. (2008) · Annual Review of Genetics · doi:10.1146/annurev.genet.39.073003.114751 · Cited by 298
Kinome screen of ferroptosis reveals a novel role of ATM in regulating iron metabolism
Chen, P., Wu, J., Ding, C. C., Lin, C., Pan, S. M., Bossa, N., Xu, Y., Yang, W., Mathey-Prévôt, B., & Chi, J. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0393-7 · Cited by 290
Self-citationHeme Oxygenase-1 Signaling and Redox Homeostasis in Physiopathological Conditions
Consoli, V., Sorrenti, V., Grosso, S., & Vanella, L. (2021) · Biomolecules · doi:10.3390/biom11040589 · Cited by 298
Emerging Roles of Energy Metabolism in Ferroptosis Regulation of Tumor Cells
Yao, X., Li, W., Fang, D., Xiao, C., Wu, X. W., Li, M., & Luo, Z. Y. (2021) · Advanced Science · doi:10.1002/advs.202100997 · Cited by 292
Glutathione peroxidase 4: a new player in neurodegeneration?
Cardoso, B. R., Hare, D. J., Bush, A. I., & Roberts, B. R. (2016) · Molecular Psychiatry · doi:10.1038/mp.2016.196 · Cited by 287
Iron and Alzheimer’s Disease: An Update on Emerging Mechanisms
Lane, D. J. R., Ayton, S., & Bush, A. I. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-179944 · Cited by 287
LncRNA PVT1 regulates ferroptosis through miR-214-mediated TFR1 and p53
Lu, J., Xu, F., & Lu, H. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118305 · Cited by 279
Which cell death modality wins the contest for photodynamic therapy of cancer?
Mishchenko, T. A., Balalaeva, I. V., Gorokhova, A. A., Vedunova, M. V., & Krysko, D. V. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04851-4 · Cited by 293
Multivalent Small-Molecule Pan-RAS Inhibitors
Welsch, M., Kaplan, A. R., Chambers, J. M., Stokes, M. E., Bos, P. H., Zask, A., Zhang, Y., Sánchez-Martín, M., Badgley, M. A., Huang, C., et al. (2017) · Cell · doi:10.1016/j.cell.2017.02.006 · Cited by 282
Self-citationLewerenz, J., Ates, G., Methner, A., Conrad, M., & Maher, P. A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00214 · Cited by 276
Erastin induces ferroptosis via ferroportin-mediated iron accumulation in endometriosis
Li, Y., Zeng, X., Lu, D., Yin, M., Shan, M., & Gao, Y. (2020) · Human Reproduction · doi:10.1093/humrep/deaa363 · Cited by 286
Poursaitidis, I., Wang, X., Crighton, T., Labuschagne, C. F., Mason, D. Y., Cramer, S. L., Triplett, K., Roy, R., Pardo, O. E., Seckl, M. J., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.02.054 · Cited by 273
Ferroptosis and Its Potential Role in Human Diseases
Han, C., Liu, Y., Dai, R., Ismail, N., Su, W., & Li, B. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00239 · Cited by 283
Activation of lysosomal iron triggers ferroptosis in cancer
Cañeque, T., Baron, L., Müller, S., Carmona, A., Colombeau, L., Versini, A., Solier, S., Gaillet, C., Sindikubwabo, F., Sampaio, J. L., et al. (2025) · Nature · doi:10.1038/s41586-025-08974-4 · Cited by 287
Self-citationAron, A. T., Loehr, M. O., Bogena, J., & Chang, C. J. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b08016 · Cited by 270
FBW7-NRA41-SCD1 axis synchronously regulates apoptosis and ferroptosis in pancreatic cancer cells
Zeng, Y., Zhuo, Q., Hu, Q., Xu, X., Liu, M., Zhang, Z., Xu, W., Liu, W., Fan, G., Qin, Y., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101807 · Cited by 271
Weaver, K., & Skouta, R. (2022) · Biomedicines · doi:10.3390/biomedicines10040891 · Cited by 288
Mechanism of Ferroptosis and Its Role in Type 2 Diabetes Mellitus
Sha, W., Hu, F., Yang, X., Chu, Y., & Bu, S. (2021) · Journal of Diabetes Research · doi:10.1155/2021/9999612 · Cited by 276
Heat stress induces ferroptosis-like cell death in plants
Distéfano, A. M., Martin, M. V., Córdoba, J. P., Bellido, A. M., D’Ippólito, S., Colman, S. L., Soto, D., Roldán, J. A., Bartoli, C. G., Zabaleta, E. J., et al. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201605110 · Cited by 268
Self-citationGuerrero‐Hue, M., García‐Caballero, C., Palomino‐Antolín, A., Rubio‐Navarro, A., Vázquez‐Carballo, C., Herencia, C., Martín‐Sánchez, D., Farré‐Alins, V., Egea, J., Cannata, P., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201900077r · Cited by 267
Persister cancer cells: Iron addiction and vulnerability to ferroptosis
Rodriguez, R., Schreiber, S. L., & Conrad, M. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.12.001 · Cited by 280
Emerging roles for lipids in non-apoptotic cell death
Magtanong, L., Ko, P., & Dixon, S. J. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.25 · Cited by 267
Ferroptosis: when metabolism meets cell death
Zheng, J., & Conrad, M. (2024) · Physiological Reviews · doi:10.1152/physrev.00031.2024 · Cited by 286
The emerging role of ferroptosis in intestinal disease
Xu, S., He, Y., Lin, L., Chen, P., Chen, M., & Zhang, S. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03559-1 · Cited by 265
Molecular mechanisms of regulated necrosis
Galluzzi, L., Kepp, O., Krautwald, S., Kroemer, G., & Linkermann, A. (2014) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2014.02.006 · Cited by 258
NRF2, a Superstar of Ferroptosis
Yan, R., Lin, B., Jin, W., Tang, L., Hu, S., & Cai, R. (2023) · Antioxidants · doi:10.3390/antiox12091739 · Cited by 292
Iron Metabolism, Ferroptosis, and the Links With Alzheimer’s Disease
Yan, N., & Zhang, J. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01443 · Cited by 256
PM2.5 induces ferroptosis in human endothelial cells through iron overload and redox imbalance
Wang, Y., & Tang, M. X. (2019) · Environmental Pollution · doi:10.1016/j.envpol.2019.07.105 · Cited by 263
Ferroptosis and its emerging roles in cardiovascular diseases
Li, N., Jiang, W., Wang, W., Xiong, R., Wu, X., & Geng, Q. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105466 · Cited by 256
Beyond ferrostatin-1: a comprehensive review of ferroptosis inhibitors
Scarpellini, C., Klejborowska, G., Lanthier, C., Hassannia, B., Berghe, T. V., & Augustyns, K. (2023) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2023.08.012 · Cited by 262
VDAC, a multi-functional mitochondrial protein as a pharmacological target
Shoshan‐Barmatz, V., & Ben-Hail, D. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.04.001 · Cited by 257
The mitochondrial voltage-dependent anion channel 1 in tumor cells
Shoshan‐Barmatz, V., Ben-Hail, D., Admoni, L., Krelin, Y., & Tripathi, S. S. (2014) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2014.10.040 · Cited by 255
The Regulation of Ferroptosis by Tumor Suppressor p53 and its Pathway
Liu, J., Zhang, C., Wang, J., Hu, W., & Feng, Z. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218387 · Cited by 255
Development of small-molecule probes that selectively kill cells induced to express mutant RAS
Weïwer, M., Bittker, J. A., Lewis, T. A., Shimada, K., Yang, W. S., MacPherson, L., Dandapani, S., Palmer, M., Stockwell, B. R., Schreiber, S. L., et al. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.09.047 · Cited by 237
Self-citationDouble-edge sword roles of iron in driving energy production versus instigating ferroptosis
Zhang, S., Xin, W., Anderson, G. J., Li, R., Gao, L., Chen, S., Zhao, J., & Liu, S. (2022) · Cell Death and Disease · doi:10.1038/s41419-021-04490-1 · Cited by 250
Torrence, M. E., MacArthur, M. R., Hosios, A. M., Valvezan, A. J., Asara, J. M., Mitchell, J. R., & Manning, B. D. (2021) · eLife · doi:10.7554/elife.63326 · Cited by 243
Liu, B., Zhao, C., Li, H., Chen, X., Ding, Y., & Xu, S. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.02.061 · Cited by 238
Metabolic networks in mutant KRAS-driven tumours: tissue specificities and the microenvironment
Kerk, S. A., Papagiannakopoulos, T. Y., Shah, Y. M., & Lyssiotis, C. A. (2021) · Nature reviews. Cancer · doi:10.1038/s41568-021-00375-9 · Cited by 246
Hong, X., Roh, W., Sullivan, R. J., Wong, K. H. K., Wittner, B. S., Guo, H., Dubash, T. D., Sade-Feldman, M., Wesley, B., Horwitz, E. P., et al. (2020) · Cancer Discovery · doi:10.1158/2159-8290.cd-19-1500 · Cited by 243
Mu, Y., Sun, J., Li, Z., Zhang, W., Liu, Z., Li, C., Peng, C., Cui, G., Shao, H., & Du, Z. (2021) · Chemosphere · doi:10.1016/j.chemosphere.2021.132944 · Cited by 243
Diverse compounds from pleuromutilin lead to a thioredoxin inhibitor and inducer of ferroptosis
Llabani, E., Hicklin, R. W., Lee, H. Y., Motika, S. E., Crawford, L. A., Weerapana, E., & Hergenrother, P. J. (2019) · Nature Chemistry · doi:10.1038/s41557-019-0261-6 · Cited by 234
Wang, Z., Ju, Y., Ali, Z., Yin, H. Y., Sheng, F., Lin, J., Wang, B., & Hou, Y. (2019) · Nature Communications · doi:10.1038/s41467-019-12142-4 · Cited by 233
Selective killing of K-ras mutant cancer cells by small molecule inducers of oxidative stress
Shaw, A. T., Winslow, M. M., Magendantz, M., Ouyang, C., Dowdle, J. A., Subramanian, A., Lewis, T. A., Maglathin, R. L., Tolliday, N. J., & Jacks, T. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105941108 · Cited by 232
Yamaguchi, Y., Kasukabe, T., & Kumakura, S. (2018) · International Journal of Oncology · doi:10.3892/ijo.2018.4259 · Cited by 232
Chemistry and biology of ferritin
Plays, M., Müller, S., & Rodriguez, R. (2021) · Metallomics · doi:10.1093/mtomcs/mfab021 · Cited by 232
Dietary Lipids Induce Ferroptosis in Caenorhabditiselegans and Human Cancer Cells
Perez, M. A., Magtanong, L., Dixon, S. J., & Watts, J. L. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.06.019 · Cited by 226
Ironing out the role of ferroptosis in immunity
Bell, H. N., Stockwell, B. R., & Zou, W. (2024) · Immunity · doi:10.1016/j.immuni.2024.03.019 · Cited by 238
Self-citationYu, H., Yang, C., Lei, J., Guo, S., Chen, R., Li, K., Qu, F., Tao, K. X., Fu, Y., Luo, F., et al. (2019) · Oncology Reports · doi:10.3892/or.2019.7189 · Cited by 225
New Insights into the Role of Ferritin in Iron Homeostasis and Neurodegenerative Diseases
Zhang, N., Yu, X., Xie, J., & Xu, H. (2021) · Molecular Neurobiology · doi:10.1007/s12035-020-02277-7 · Cited by 223
Targeting ferroptosis in acute kidney injury
Ni, L., Cheng, Y., & Wu, X. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04628-9 · Cited by 228
The mechanism of ferroptosis and its related diseases
Feng, S., Tang, D., Wang, Y., Li, X., Bao, H., Tang, C., Dong, X., Li, X., Yang, Q., Yan, Y., et al. (2023) · Molecular Biomedicine · doi:10.1186/s43556-023-00142-2 · Cited by 241
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
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
Dangol, S., Chen, Y., Hwang, B. K., & Jwa, N. (2018) · The Plant Cell · doi:10.1105/tpc.18.00535 · Cited by 212
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-citationIron and copper: critical executioners of ferroptosis, cuproptosis and other forms of cell death
Li, Y., Du, Y., Zhou, Y., Chen, Q., Luo, Z., Ren, Y., Chen, X., & Chen, G. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01267-1 · Cited by 225
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
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
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
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
Metadata
- Authors
- Yang, W. S., & Stockwell, B. R.
- Affiliations
- Columbia University (US)
- Corresponding author
- Stockwell, Brent R.
- Venue
- Chemistry & Biology
- Publisher
- Elsevier BV
- Published
- 2008-03
- Volume
- 15
- Issue
- 3
- Pages
- 234-245
- ISSN
- 1074-5521 (ISSN-L)
- PMC
- PMC2683762
- OpenAlex
- W2114138419
- Cited by
- 1,876
- References
- 35
- Citations by year
- 2026: 138 · 2025: 231 · 2024: 319 · 2023: 312 · 2022: 271 · 2021: 202 · 2020: 135 · 2019: 66 · 2018: 58 · 2017: 38 · 2016: 35 · 2015: 19 · 2014: 11 · 2013: 7 · 2012: 10
- FWCI
- 3.16
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Chemistry & Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (R01CA097061)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Ferroptosis and cancer prognosis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- synthetic lethality, oncogenic Ras, RSL3, erastin, non-apoptotic cell death, iron-dependent cell death, oxidative cell death, VDAC3, voltage-dependent anion channel, transferrin receptor 1, ferritin, iron metabolism, small molecule screening, cancer cell death
- MeSH terms
- Drug Evaluation, Preclinical, Humans, Iron, Mutation, Neoplasms, Piperazines, Substrate Specificity, Gene Expression Regulation, Neoplastic, Proto-Oncogene Proteins p21(ras), Cell Death, Apoptosis, Cell Line, Tumor, Voltage-Dependent Anion Channels, Small Molecule Libraries
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review