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
Cited by
Sorted by citations
Items 201–300 of 1,002
Mechanisms and Models of Kidney Tubular Necrosis and Nephron Loss
Maremonti, F., Meyer, C., & Linkermann, A. (2022) · Journal of the American Society of Nephrology · doi:10.1681/asn.2021101293 · Cited by 213
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
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
Targeting Cell Death: Pyroptosis, Ferroptosis, Apoptosis and Necroptosis in Osteoarthritis
Yang, J., Hu, S., Bian, Y., Yao, J., Wang, D., Liu, X., Guo, Z., Zhang, S., & Peng, L. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.789948 · Cited by 244
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
Rauf, A., Khalil, A. A., Awadallah, S. M., Khan, S. A., Abu‐Izneid, T., Kamran, M., Hemeg, H. A., Mubarak, M. S., Khalid, A., & Wilairatana, P. (2023) · Food Science & Nutrition · doi:10.1002/fsn3.3784 · Cited by 220
Ferroptosis Mediates Cuprizone-Induced Loss of Oligodendrocytes and Demyelination
Jhelum, P., Santos-Nogueira, E., Teo, W., Haumont, A., Lenoël, I., Stys, P. K., & David, S. (2020) · The Journal of Neuroscience · doi:10.1523/jneurosci.1749-20.2020 · Cited by 214
Du, J., Wang, X., Li, Y., Ren, X., Zhou, Y., Hu, W., Zhou, C., Jing, Q., Yang, C., Wang, L., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03996-y · 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
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
Targeting ferroptosis protects against experimental (multi)organ dysfunction and death
Van Coillie, S., Van San, E., Goetschalckx, I., Wiernicki, B., Mukhopadhyay, B., Tonnus, W., Choi, S. M., Roelandt, R., Dumitrascu, C., Lamberts, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28718-6 · Cited by 186
VDAC1: from structure to cancer therapy
Shoshan‐Barmatz, V., & Mizrachi, D. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00164 · Cited by 200
Miao, R., Fang, X., Zhang, Y., Wei, J., Zhang, Y., & Tian, J. (2023) · Cell Death & Disease · doi:10.1038/s41419-023-05708-0 · Cited by 192
Hinman, A., Holst, C. R., Latham, J. C., Bruegger, J. J., Ulas, G., McCusker, K. P., Amagata, A., Davis, D., Hoff, K. G., Kahn-Kirby, A. H., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0201369 · Cited by 194
Youssef, L. A., Rebbaa, A., Pampou, S., Weisberg, S. P., Stockwell, B. R., Hod, E. A., & Spitalnik, S. L. (2018) · Blood · doi:10.1182/blood-2017-12-822619 · Cited by 186
Self-citationFive-Membered Ring Peroxide Selectively Initiates Ferroptosis in Cancer Cells
Abrams, R. P. M., Carroll, W. L., & Woerpel, K. A. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b00900 · Cited by 193
Takahashi, N., Cho, P., Selfors, L. M., Kuiken, H. J., Kaul, R., Fujiwara, T., Harris, I. S., Zhang, T., Gygi, S. P., & Brugge, J. S. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.10.010 · Cited by 187
Shah, R., Margison, K. D., & Pratt, D. A. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00730 · Cited by 190
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
Autophagy and Ferroptosis—What Is the Connection?
Kang, R., & Tang, D. (2017) · Current Pathobiology Reports · doi:10.1007/s40139-017-0139-5 · Cited by 186
Chaudhary, N., Choudhary, B. S., Shah, S. G., Khapare, N., Dwivedi, N., Gaikwad, A., Joshi, N., Raichanna, J., Basu, S., Gurjar, M., et al. (2021) · International Journal of Cancer · doi:10.1002/ijc.33711 · Cited by 185
Ferroptosis, a Recent Defined Form of Critical Cell Death in Neurological Disorders
Wu, J., Tuo, Q., & Lei, P. (2018) · Journal of Molecular Neuroscience · doi:10.1007/s12031-018-1155-6 · Cited by 184
Qiongyue, Z., Xin, Y., Meng, P., Mi, S., Yanlin, W., Li, X., & Xuemin, S. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.857067 · Cited by 188
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
Cozza, G., Rossetto, M., Bosello-Travain, V., Maiorino, M., Roveri, A., Toppo, S., Zaccarin, M., Zennaro, L., & Ursini, F. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.07.010 · Cited by 188
Quantitative Profiling of Protein Carbonylations in Ferroptosis by an Aniline-Derived Probe
Chen, Y., Liu, Y., Lan, T., Qin, W., Zhu, Y., Qin, K., Gao, J., Wang, H., Hou, X., Chen, N., et al. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b01462 · Cited by 186
Dai, J., Dan, W., Schneider, U., & Wang, J. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.08.027 · Cited by 181
Fan, B., Pang, Y., Li, W., Zhao, C.-X., Zhang, Y., Wang, X., Ning, G., Kong, X., Liu, C., Yao, X. X., et al. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.293157 · Cited by 186
Ding, H., Chen, S., Pan, X., Dai, X., Pan, G., Li, Z., Mai, X., Tian, Y., Zhang, S., Liu, B., et al. (2021) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12700 · Cited by 187
Nanomaterial-induced ferroptosis for cancer specific therapy
Liu, M., Liu, B., Liu, Q., Du, K., Wang, Z., & He, N. (2019) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2018.12.015 · Cited by 180
Ferroptosis and ferritinophagy in diabetes complications
He, J., Li, Z., Xia, P., Shi, A., FuChen, X., Zhang, J., & Yu, P. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101470 · Cited by 187
MYCN mediates TFRC-dependent ferroptosis and reveals vulnerabilities in neuroblastoma
Lu, Y., Yang, Q., Su, Y., Ji, Y., Li, G., Yang, X., Xu, L., Lu, Z., Dong, J., Wu, Y., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03790-w · Cited by 187
HMGB1 regulates erastin-induced ferroptosis via RAS-JNK/p38 signaling in HL-60/NRASQ61L cells.
Ye, F., Chai, W., Xie, M., Yang, M., Yan, Y., Cao, L., & Yang, L. (2019) · PubMed Central · Cited by 174
Zhao, T., Guo, X., & Sun, Y. (2021) · Aging and Disease · doi:10.14336/ad.2020.0912 · Cited by 180
PPARα alleviates iron overload‐induced ferroptosis in mouse liver
Xing, G., Meng, L., Cao, S., Liu, S., Wu, J., Li, Q., Huang, W., & Zhang, L. (2022) · EMBO Reports · doi:10.15252/embr.202052280 · Cited by 179
The neglected significance of “antioxidative stress”
Poljsak, B., & Milisav, I. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/480895 · Cited by 177
Ou, W., Mulik, R. S., Anwar, A., McDonald, J. G., He, X., & Corbin, I. R. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.09.002 · Cited by 179
Targeting de novo lipogenesis and the Lands cycle induces ferroptosis in KRAS-mutant lung cancer
Bartolacci, C., Andreani, C., do Vale, G. D., Berto, S., Melegari, M., Crouch, A. C., Baluya, D. L., Kemble, G. W., Hodges, K. B., Starrett, J. H., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31963-4 · Cited by 183
Emerging Role of Ferroptosis in Acute Kidney Injury
Hu, Z., Zhang, H., Yang, S., Wu, X., He, D., Cao, K., & Zhang, W. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8010614 · Cited by 180
Lehár, J., Stockwell, B. R., Giaever, G., & Nislow, C. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.120 · Cited by 172
Self-citationTorti, S. V., & Torti, F. M. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-2017 · Cited by 183
A promising new approach to cancer therapy: Targeting iron metabolism in cancer stem cells
El-Hout, M., Santos, L. D., Hamaï, A., & Mehrpour, M. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.07.009 · Cited by 173
Non-coding RNAs and ferroptosis: potential implications for cancer therapy
Balihodzic, A., Prinz, F., Dengler, M. A., Călin, G. A., Jost, P. J., & Pichler, M. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-00998-x · Cited by 175
The emerging roles of MAPK-AMPK in ferroptosis regulatory network
Wang, X., Tan, X., Zhang, J., Wu, J., & Shi, H. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01170-9 · Cited by 178
Posttranslational Modifications in Ferroptosis
Wei, X., Yi, X., Zhu, X., & Jiang, D. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/8832043 · Cited by 165
Exploiting ferroptosis vulnerabilities in cancer
Nakamura, T., & Conrad, M. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01425-8 · Cited by 172
Lee, E., Song, C.-H., Bae, S.-J., Ha, K.-T., & Karki, R. (2023) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-01069-y · Cited by 164
Autophagy, Pyroptosis, and Ferroptosis: New Regulatory Mechanisms for Atherosclerosis
Lin, L., Zhang, M.-X., Zhang, L., Zhang, D., Li, C., & Li, Y. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.809955 · Cited by 166
Lin, Z., Liu, Y., Xue, N., Zheng, R., Yan, Y., Wang, Z., Li, Y., Ying, C.-Z., Song, Z., Tian, J., et al. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/7769355 · Cited by 173
Ferroptosis in Cancer Progression: Role of Noncoding RNAs
Zuo, Y.-B., Zhang, Y., Zhang, R., Tian, J., Lv, X., Li, R., Li, S., Cheng, M.-D., Shan, J., Zhao, Z., et al. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.66917 · Cited by 171
Regulation and function of autophagy in pancreatic cancer
Li, J., Chen, X., Kang, R., Zeh, H. J., Klionsky, D. J., & Tang, D. (2020) · Autophagy · doi:10.1080/15548627.2020.1847462 · Cited by 167
Kong, R., Wang, N., Han, W., Bao, W., & Lu, J. (2021) · Journal of Leukocyte Biology · doi:10.1002/jlb.3ma1220-815rrr · Cited by 164
Mitochondrial event as an ultimate step in ferroptosis
Oh, S. J., Ikeda, M., Ide, T., Hur, K. Y., & Lee, M. (2022) · Cell Death Discovery · doi:10.1038/s41420-022-01199-8 · Cited by 167
The Relationship between Ferroptosis and Tumors: A Novel Landscape for Therapeutic Approach
Xia, X., Fan, X., Zhao, M., & Zhu, P. (2019) · Current Gene Therapy · doi:10.2174/1566523219666190628152137 · Cited by 161
Adjemian, S., Oltean, T., Martens, S., Wiernicki, B., Goossens, V., Berghe, T. V., Cappe, B., Ladik, M., Riquet, F. B., Heyndrickx, L., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03209-y · Cited by 173
She, R., Liu, D., Liao, J., Wang, G., Ge, J., & Mei, Z. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1191629 · Cited by 163
Drug Resistance in Colorectal Cancer: From Mechanism to Clinic
Wang, Q., Shen, X., Chen, G., & Du, J. (2022) · Cancers · doi:10.3390/cancers14122928 · Cited by 160
Wang, Y., Wu, S., Li, Q., Sun, H., & Wang, H. (2023) · Advanced Science · doi:10.1002/advs.202300325 · Cited by 171
Ferroptosis and NRF2: an emerging battlefield in the neurodegeneration of Alzheimer's disease
Lane, D. J. R., Metselaar, B., Greenough, M., Bush, A. I., & Ayton, S. (2021) · Essays in Biochemistry · doi:10.1042/ebc20210017 · Cited by 160
Identification of PRDX6 as a regulator of ferroptosis
Lu, B., Chen, X., Hong, Y., Zhu, H., He, Q., Yang, B., Ying, M., & Cao, J. (2019) · Acta Pharmacologica Sinica · doi:10.1038/s41401-019-0233-9 · Cited by 160
Jiang, M., Qiao, M., Zhao, C., Deng, J., Li, X., & Zhou, C. (2020) · Translational Lung Cancer Research · doi:10.21037/tlcr-20-341 · Cited by 158
Magtanong, L., & Dixon, S. J. (2018) · Developmental Neuroscience · doi:10.1159/000496922 · Cited by 156
Li, R., Zhang, J., Zhou, Y., Gao, Q., Wang, R., Fu, Y., Zheng, L., & Yu, H. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/3469840 · Cited by 159
Zhou, Y., Shen, Y., Chen, C., Sui, X., Yang, J., Wang, L., & Zhou, J. (2019) · Cancer Biology and Medicine · doi:10.20892/j.issn.2095-3941.2019.0158 · Cited by 157
Synergistic effect of fasting-mimicking diet and vitamin C against KRAS mutated cancers
Tano, M. D., Raucci, F., Vernieri, C., Caffa, I., Buono, R., Fanti, M., Brandhorst, S., Curigliano, G., Nencioni, A., de Braud, F., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16243-3 · Cited by 155
Wu, Y., Jiao, H., Yue, Y., He, K., Jin, Y., Zhang, J., Zhang, J., Wei, Y., Luo, H.-Y., Hao, Z., et al. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-00957-6 · Cited by 153
Nagpal, A., Redvers, R. P., Ling, X., Ayton, S., Fuentes, M., Tavancheh, E., Diala, I., Lalani, A. S., Loi, S., David, S., et al. (2019) · Breast Cancer Research · doi:10.1186/s13058-019-1177-1 · Cited by 155
Sigma‐1 receptor protects against ferroptosis in hepatocellular carcinoma cells
Bai, T., Lei, P., Zhou, H., Liang, R., Zhu, R., Wang, W., Zhou, L., & Sun, Y. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14594 · Cited by 152
Targeting Ferroptosis: New Hope for As-Yet-Incurable Diseases
Conrad, M., Lorenz, S., & Proneth, B. (2020) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2020.08.010 · Cited by 155
Current Use of Fenton Reaction in Drugs and Food
Abe, C., Miyazawa, T., & Miyazawa, T. (2022) · Molecules · doi:10.3390/molecules27175451 · Cited by 156
Ferroptosis: mechanisms and implications for cancer development and therapy response
dos Santos, A. F., Fazeli, G., da Silva, T. N. X., & Angeli, J. P. F. (2023) · Trends in Cell Biology · doi:10.1016/j.tcb.2023.04.005 · Cited by 154
Ferroptosis contributes to developmental cell death in rice blast
Shen, Q., Liang, M., Yang, F., Deng, Y., & Naqvi, N. I. (2020) · New Phytologist · doi:10.1111/nph.16636 · Cited by 147
The Nrf2 induction prevents ferroptosis in Friedreich's Ataxia
Rosa, P. L., Petrillo, S., Turchi, R., Berardinelli, F., Schirinzi, T., Vasco, G., Lettieri‐Barbato, D., Fiorenza, M. T., Bertini, E., Aquilano, K., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101791 · Cited by 150
Weïwer, M., Spoonamore, J. E., Wei, J., Guichard, B., Ross, N. T., Masson, K., Silkworth, W., Dandapani, S., Palmer, M. A. J., Scherer, C., et al. (2012) · ACS Medicinal Chemistry Letters · doi:10.1021/ml300246r · Cited by 147
A compendium of kinetic modulatory profiles identifies ferroptosis regulators
Conlon, M., Poltorack, C. D., Forcina, G. C., Armenta, D. A., Mallais, M., Perez, M. A., Wells, A. C., Kahanu, A., Magtanong, L., Watts, J. L., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00751-4 · Cited by 152
Ferritinophagy and ferroptosis in cardiovascular disease: Mechanisms and potential applications
Qin, Y., Qiao, Y., Wang, D., Tang, C., & Yan, G. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111872 · Cited by 150
Li, W., Li, W., Wang, Y., Leng, Y., & Xia, Z. (2021) · Cell Death Discovery · doi:10.1038/s41420-021-00656-0 · Cited by 145
Wang, J., Wang, Y., Liu, Y., Cai, X., Huang, X., Fu, W., Wang, L., Qiu, L., Li, J., & Sun, L. (2022) · Cell Death Discovery · doi:10.1038/s41420-022-00931-8 · Cited by 146
Shibata, Y., Yasui, H., Higashikawa, K., Miyamoto, N., & Kuge, Y. (2019) · PLoS ONE · doi:10.1371/journal.pone.0225931 · Cited by 150
Ferroptosis response segregates small cell lung cancer (SCLC) neuroendocrine subtypes
Bebber, C. M., Thomas, E. S., Stroh, J., Chen, Z., Androulidaki, A., Schmitt, A., Höhne, M. N., Stüker, L., Alves, C. D. P., Khonsari, A., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22336-4 · Cited by 144
Zhou, L., Guan, Q., Li, W., Zhang, Z., Li, Y., & Dong, Y. (2021) · Small · doi:10.1002/smll.202101368 · Cited by 144
Apatinib induced ferroptosis by lipid peroxidation in gastric cancer
Zhao, L., Peng, Y., He, S., Li, R., Wang, Z., Huang, J., Lei, X., Li, G., & Ma, Q. (2021) · Gastric Cancer · doi:10.1007/s10120-021-01159-8 · Cited by 141
Cui, C., Yang, F., & Li, Q. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.901565 · Cited by 145
Mitochondrial VDAC1: Function in Cell Life and Death and a Target for Cancer Therapy
Shoshan‐Barmatz, V., & Golan, M. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712798992110 · Cited by 142
Iron overload: Effects on cellular biochemistry
Nogueira, L. S., Oliveira, M. M., Pessoa, M. T., & Barbosa, L. A. (2019) · Clinica Chimica Acta · doi:10.1016/j.cca.2019.11.029 · Cited by 149
Ferroptosis in colorectal cancer: Potential mechanisms and effective therapeutic targets
Wang, Y., Zhang, Z., Sun, W., Zhang, J., Xu, Q., Zhou, X., & Mao, L. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113524 · Cited by 143
Hydropersulfides Inhibit Lipid Peroxidation and Protect Cells from Ferroptosis
Wu, Z., Khodade, V. S., Chauvin, J. R., Rodriguez, D., Toscano, J. P., & Pratt, D. A. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c06804 · Cited by 142
Dong, B., Song, W., Lu, Y., Sun, Y., & Lin, W. (2020) · ACS Sensors · doi:10.1021/acssensors.0c02015 · Cited by 137
Ferroptosis: A New Regulatory Mechanism in Osteoporosis
Liu, P., Wang, W., Li, Z., Li, Y., Yu, X., Tu, J., & Zhang, Z. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/2634431 · Cited by 146
Elevated FSP1 protects KRAS-mutated cells from ferroptosis during tumor initiation
Müller, F., Lim, J. K. M., Bebber, C. M., Seidel, E., Tishina, S., Dahlhaus, A., Stroh, J., Beck, J., Yapici, F. I., Nakayama, K., et al. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01096-8 · Cited by 140
Modulatory profiling identifies mechanisms of small molecule-induced cell death
Wolpaw, A. J., Shimada, K., Skouta, R., Welsch, M. E., Akavia, U. D., Pe'er, D., Shaik, F., Bulinski, J. C., & Stockwell, B. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106149108 · Cited by 133
Self-citationZhang, C., Liu, Z., Zhang, Y., Ma, L., Song, E., & Song, Y. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2384-5 · Cited by 140
IMCA Induces Ferroptosis Mediated by SLC7A11 through the AMPK/mTOR Pathway in Colorectal Cancer
Zhang, L., Liu, W., Liu, F., Wang, Q., Song, M., Yu, Q., Tang, K., Teng, T., Wu, D., Wang, X.-J., et al. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/1675613 · Cited by 139
Induction and application of ferroptosis in cancer therapy
Nie, Q. H., Hu, Y., Yu, X. H., Li, X., & Fang, X. (2022) · Cancer Cell International · doi:10.1186/s12935-021-02366-0 · Cited by 146
Rai, P., Young, J. J., Burton, D. G. A., Giribaldi, M. G., Önder, T. T., & Weinberg, R. A. (2010) · Oncogene · doi:10.1038/onc.2010.520 · Cited by 138
Recent advances in small-molecule fluorescent probes for studying ferroptosis
Qi, Y., Wang, H., Chen, L., Duan, Y., Yang, S., & Zhu, H. (2022) · Chemical Society Reviews · doi:10.1039/d1cs01167g · Cited by 138
Non-Canonical Cell Death Induced by p53
Ranjan, A., & Iwakuma, T. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17122068 · Cited by 140
Ferroptosis: A Novel Therapeutic Target for Ischemia-Reperfusion Injury
Chen, Y., Fan, H., Wang, S., Tang, G., Zhai, C., & Shen, L. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.688605 · Cited by 139
Ribosome stalling during selenoprotein translation exposes a ferroptosis vulnerability
Li, Z., Ferguson, L., Deol, K. K., Roberts, M. A., Magtanong, L., Hendricks, J. M., Mousa, G. A., Kilinc, S., Schaefer, K., Wells, J. A., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01033-3 · Cited by 134
Ferroptosis: An emerging approach for targeting cancer stem cells and drug resistance
Elgendy, S. M., Alyammahi, S. K., Alhamad, D. W., Abdin, S. M., & Omar, H. A. (2020) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2020.103095 · Cited by 134
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
