The CoQ oxidoreductase FSP1 acts parallel to GPX4 to inhibit ferroptosis
Open accessAbstract
Ferroptosis is a form of regulated cell death that is caused by the iron-dependent peroxidation of lipids 1,2. The glutathione-dependent lipid hydroperoxidase glutathione peroxidase 4 (GPX4) prevents ferroptosis by converting lipid hydroperoxides into non-toxic lipid alcohols 3,4. Ferroptosis has previously been implicated in the cell death that underlies several degenerative conditions 2, and induction of ferroptosis by the inhibition of GPX4 has emerged as a therapeutic strategy to trigger cancer cell death 5. However, sensitivity to GPX4 inhibitors varies greatly across cancer cell lines 6, which suggests that additional factors govern resistance to ferroptosis. Here, using a synthetic lethal CRISPR-Cas9 screen, we identify ferroptosis suppressor protein 1 (FSP1) (previously known as apoptosis-inducing factor mitochondrial 2 (AIFM2)) as a potent ferroptosis-resistance factor. Our data indicate that myristoylation recruits FSP1 to the plasma membrane where it functions as an oxidoreductase that reduces coenzyme Q 10 (CoQ) (also known as ubiquinone-10), which acts as a lipophilic radical-trapping antioxidant that halts the propagation of lipid peroxides. We further find that FSP1 expression positively correlates with ferroptosis resistance across hundreds of cancer cell lines, and that FSP1 mediates resistance to ferroptosis in lung cancer cells in culture and in mouse tumour xenografts. Thus, our data identify FSP1 as a key component of a non-mitochondrial CoQ antioxidant system that acts in parallel to the canonical glutathione-based GPX4 pathway. These findings define a ferroptosis suppression pathway and indicate that pharmacological inhibition of FSP1 may provide an effective strategy to sensitize cancer cells to ferroptosis-inducing chemotherapeutic agents.
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
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?
Lysotracker is a fluorescent acidotropic probe used to detect lysosome localization, quantify lysosome number and size, and monitor autophagy.
“Lysotracker is a fluorescent acidotropic probe for labeling and tracking acidic organelles in live cells, which has been used to detect lysosome localization, quantify the number and sizes of lysosomes48,49 and to monitor autophagy50,51.”
From Genome-wide CRISPRi/a screens in human neurons link lysosomal failure to ferroptosis (2021) · cites this paper as [51]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
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 · see citing works
Self-citationRegulation of Ferroptotic Cancer Cell Death by GPX4
Yang, W. S., SriRamaratnam, R., Welsch, M. E., Shimada, K., Skouta, R., Viswanathan, V. S., Cheah, J. H., Clemons, P. A., Shamji, A. F., Clish, C. B., et al. (2014) · Cell · doi:10.1016/j.cell.2013.12.010 · Cited by 7,713 · see citing works
Ferroptosis: A Regulated Cell Death Nexus Linking Metabolism, Redox Biology, and Disease
Stockwell, B. R., Friedmann Angeli, J. P., Bayir, H., Bush, A. I., Conrad, M., Dixon, S. J., Fulda, S., Gascón, S., Hatzios, S. K., Kagan, V. E., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.021 · Cited by 7,695 · see citing works
Self-citationFSP1 is a glutathione-independent ferroptosis suppressor
Doll, S., Freitas, F. P., Shah, R., Aldrovandi, M., da Silva, M. C., Ingold, I., Goya Grocin, A., Xavier da Silva, T. N., Panzilius, E., Scheel, C. H., et al. (2019) · Nature · doi:10.1038/s41586-019-1707-0 · Cited by 3,341 · see citing works
Peroxidation of polyunsaturated fatty acids by lipoxygenases drives ferroptosis
Yang, W. S., Kim, K. J., Gaschler, M. M., Patel, M., Shchepinov, M. S., & Stockwell, B. R. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1603244113 · Cited by 2,329 · see citing works
Dixon, S. J., Patel, D. N., Welsch, M., Skouta, R., Lee, E. D., Hayano, M., Thomas, A. G., Gleason, C. E., Tatonetti, N. P., Slusher, B. S., et al. (2014) · eLife · doi:10.7554/elife.02523 · Cited by 2,088 · see citing works
Self-citationSun, X., Ou, Z., Chen, R., Niu, X., Chen, D., Kang, R., & Tang, D. (2016) · Hepatology · doi:10.1002/hep.28251 · Cited by 2,012 · see citing works
Dependency of a therapy-resistant state of cancer cells on a lipid peroxidase pathway
Viswanathan, V. S., Ryan, M. J., Dhruv, H. D., Gill, S., Eichhoff, O. M., Seashore-Ludlow, B., Kaffenberger, S. D., Eaton, J. K., Shimada, K., Aguirre, A. J., et al. (2017) · Nature · doi:10.1038/nature23007 · Cited by 2,011 · see citing works
Drug-tolerant persister cancer cells are vulnerable to GPX4 inhibition
Hangauer, M. J., Viswanathan, V. S., Ryan, M. J., Bole, D., Eaton, J. K., Matov, A., Galeas, J., Dhruv, H. D., Berens, M. E., Schreiber, S. L., et al. (2017) · Nature · doi:10.1038/nature24297 · Cited by 1,799 · see citing works
Selenium Utilization by GPX4 Is Required to Prevent Hydroperoxide-Induced Ferroptosis
Ingold, I., Berndt, C., Schmitt, S., Doll, S. G., Poschmann, G., Buday, K., Roveri, A., Peng, X., Freitas, F. P., Seibt, T., et al. (2017) · Cell · doi:10.1016/j.cell.2017.11.048 · Cited by 1,685 · see citing works
Exogenous Monounsaturated Fatty Acids Promote a Ferroptosis-Resistant Cell State
Magtanong, L., Ko, P., To, M., Cao, J. Y., Forcina, G. C., Tarangelo, A., Ward, C. C., Cho, K., Patti, G. J., Nomura, D. K., et al. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2018.11.016 · Cited by 1,168 · see citing works
Self-citationGlobal survey of cell death mechanisms reveals metabolic regulation of ferroptosis
Shimada, K., Skouta, R., Kaplan, A., Yang, W. S., Hayano, M., Dixon, S. J., Brown, L. M., Valenzuela, C. A., Wolpaw, A. J., & Stockwell, B. R. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2079 · Cited by 1,017 · see citing works
Self-citationZou, Y., Palte, M. J., Deik, A. A., Li, H., Eaton, J. K., Wang, W., Tseng, Y.-Y., Deasy, R., Kost-Alimova, M., Dančík, V., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09277-9 · Cited by 887 · see citing works
Correlating chemical sensitivity and basal gene expression reveals mechanism of action
Rees, M. G., Seashore-Ludlow, B. A., Cheah, J. H., Adams, D., Price, E. V., Gill, S., Javaid, S., Coletti, M. E., Jones, V., Bodycombe, N. E., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1986 · Cited by 874 · see citing works
Stocker, R., Bowry, V. W., & Frei, B. B. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.5.1646 · Cited by 794 · see citing works
Imidazole Ketone Erastin Induces Ferroptosis and Slows Tumor Growth in a Mouse Lymphoma Model
Zhang, Y., Tan, H., Daniels, J. D., Zandkarimi, F., Liu, H., Brown, L. M., Uchida, K., O’Connor, O. A., & Stockwell, B. R. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.01.008 · Cited by 729 · see citing works
Nguyen, T. B., Louie, S. M., Daniele, J. R., Tran, Q., Dillin, A., Zoncu, R., Nomura, D. K., & Olzmann, J. A. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.06.003 · Cited by 610 · see citing works
Self-citationDixon, S. J., & Stockwell, B. R. (2018) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-030518-055844 · Cited by 589 · see citing works
Self-citationHayano, M., Yang, W., Corn, C. K., Pagano, N. C., & Stockwell, B. R. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.93 · Cited by 462 · see citing works
An inducible translocation strategy to rapidly activate and inhibit small GTPase signaling pathways.
Inoue, T., Heo, W. D., Grimley, J. S., Wandless, T. J., & Meyer, T. (2005) · Nature Methods · doi:10.1038/nmeth763 · Cited by 424 · see citing works
Bersuker, K., Peterson, C. W. H., To, M., Sahl, S. J., Savikhin, V., Grossman, E. A., Nomura, D. K., & Olzmann, J. A. (2018) · Developmental Cell · doi:10.1016/j.devcel.2017.11.020 · Cited by 346 · see citing works
Self-citationGenome-scale measurement of off-target activity using Cas9 toxicity in high-throughput screens
Morgens, D. W., Wainberg, M., Boyle, E. A., Ursu, O., Araya, C. L., Tsui, C. K., Haney, M. S., Hess, G. T., Han, K., Jeng, E. E., et al. (2017) · Nature Communications · doi:10.1038/ncomms15178 · Cited by 345 · see citing works
Self-citationA simplified method for the preparation of detergent-free lipid rafts
MacDonald, J. L., & PIKE, L. J. (2005) · Journal of Lipid Research · doi:10.1194/jlr.d400041-jlr200 · Cited by 339 · see citing works
Wu, M., Xu, L., Li, X., Zhai, Z., & Shu, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202285200 · Cited by 241 · see citing works
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 204 · see citing works
HPLC Analysis of Reduced and Oxidized Coenzyme Q10 in Human Plasma
Tang, P., Miles, M. V., DeGrauw, A. J., Hershey, A. D., & Pesce, A. J. (2001) · Clinical Chemistry · doi:10.1093/clinchem/47.2.256 · Cited by 164 · see citing works
Self-citationTribble, D. L., van den Berg, J. J. M., Motchnik, P. A., Ames, B. N., Lewis, D. M., Chait, A., & Krauss, R. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.3.1183 · Cited by 163 · see citing works
N-Myristoyl transferase-mediated protein labelling in vivo
Heal, W. P., Wickramasinghe, S. R., Leatherbarrow, R. J., et al. (2008) · Organic & Biomolecular Chemistry · doi:10.1039/b803258k · Cited by 135 · see citing works
Zhao, J., Dar, H. H., Deng, Y., Croix, C. M. S., Li, Z., Minami, Y., Shrivastava, I. H., Tyurina, Y. Y., Etling, E. B., Rosenbaum, J. C., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1921618117 · Cited by 120 · see citing works
Self-citationOhiro, Y., Garkavtsev, I., Kobayashi, S., Sreekumar, K. R., Nantz, R., Higashikubo, B. T., Duffy, S., Higashikubo, R., Usheva, A., Gius, D. R., et al. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03049-1 · Cited by 117 · see citing works
Cysteine Depletion, a Key Action to Challenge Cancer Cells to Ferroptotic Cell Death
Daher, B., Vučetić, M., & Pouysségur, J. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00723 · Cited by 117 · see citing works
Marshall, K. R., Gong, M., Wodke, L., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414018200 · Cited by 112 · see citing works
Therapy-induced lipid uptake and remodeling underpin ferroptosis hypersensitivity in prostate cancer
Tousignant, K. D., Rockstroh, A., Poad, B. L. J., Talebi, A., Young, R. S. E., Fard, A. T., Gupta, R., Zang, T., Wang, C., Lehman, M., et al. (2020) · Cancer & Metabolism · doi:10.1186/s40170-020-00217-6 · Cited by 111 · see citing works
Distribution of ubiquinone and ubiquinol homologues in rat tissues and subcellular fractions
Takahashi, T., Okamoto, T., Mori, K., Sayo, H., & Kishi, T. (1993) · Lipids · doi:10.1007/bf02536234 · Cited by 66 · see citing works
Ubiquinol regeneration by plasma membrane ubiquinone reductase
Arroyo, A., Navarro, F., Navas, P., et al. (1998) · PROTOPLASMA · doi:10.1007/bf01279300 · Cited by 31 · see citing works
Meza-Torres, C., Hernández‐Camacho, J. D., Cortés-Rodríguez, A. B., Fang, L., Thanh, T. B., Rodríguez-Bies, E., Navas, P., & López‐Lluch, G. (2020) · Antioxidants · doi:10.3390/antiox9050431 · Cited by 18 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Ferroptosis: past, present and future
Li, J., Cao, F., Yin, H.-L., Huang, Z.-J., Lin, Z.-T., Mao, N., Sun, B., & Wang, G. (2020) · Cell Death & Disease · doi:10.1038/s41419-020-2298-2 · Cited by 4,171 · see citing works
Targeting Ferroptosis as a Vulnerability in Cancer
Lei, G., Zhuang, L., & Gan, B. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-022-00459-0 · Cited by 2,252 · see citing works
Lipid peroxidation and ferroptosis: The role of GSH and GPx4
Ursini, F., & Maiorino, M. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.02.027 · Cited by 1,954 · see citing works
NLRP3 inflammasome activation and cell death
Huang, Y., Xu, W., & Zhou, R. (2021) · Cellular & Molecular Immunology · doi:10.1038/s41423-021-00740-6 · Cited by 1,527 · see citing works
The hallmarks of cancer metabolism: still emerging
Pavlova, N. N., Zhu, J., & Thompson, C. B. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.01.007 · Cited by 1,418 · see citing works
Ferroptosis: Mechanisms and links with diseases
Yan, H.-F., Zou, T., Tuo, Q.-Z., Xu, S., Li, H., Belaidi, A. A., & Lei, P. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00428-9 · Cited by 1,471 · see citing works
Jomova, K., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2024) · Archives of Toxicology · doi:10.1007/s00204-024-03696-4 · Cited by 1,445 · see citing works
The emerging role of ferroptosis in inflammation
Sun, Y., Chen, P., Zhai, B., Zhang, M., Xiang, Y., Fang, J., Xu, S., Gao, Y., Chen, X., Sui, X., et al. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110108 · Cited by 739 · see citing works
Iron Homeostasis and Ferroptosis in Human Diseases: Mechanisms and Therapeutic Prospects
Ru, Q., Li, Y., Chen, L., Wu, Y., Min, J., & Wang, F. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01969-z · Cited by 724 · see citing works
p53 in ferroptosis regulation: The new weapon for the old guardian
Liu, Y., & Gu, W. (2022) · Cell Death & Differentiation · doi:10.1038/s41418-022-00943-y · Cited by 540 · see citing works
Genome-wide CRISPRi/a screens in human neurons link lysosomal failure to ferroptosis
Tian, R., Abarientos, A., Hong, J., Hashemi, S. H., Yan, R., Dräger, N., Leng, K., Nalls, M. A., Singleton, A. B., Xu, K., et al. (2021) · Nature Neuroscience · doi:10.1038/s41593-021-00862-0 · Cited by 414 · see citing works
The chemistry and biology of ferroptosis
Stockwell, B. R., & Jiang, X. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.03.013 · Cited by 429 · see citing works
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 · see citing works
Lipid Metabolism and Ferroptosis
Lee, J.-Y., Kim, W. K., Bae, K.-H., Lee, S. C., & Lee, E.-W. (2021) · Biology · doi:10.3390/biology10030184 · Cited by 374 · see citing works
iPLA2β-mediated lipid detoxification controls p53-driven ferroptosis independent of GPX4
Chen, D., Chu, B., Yang, X., Liu, Z., Jin, Y., Kon, N., Rabadan, R., Jiang, X., Stockwell, B. R., & Gu, W. (2021) · Nature Communications · doi:10.1038/s41467-021-23902-6 · Cited by 348 · see citing works
Acetyl-CoA metabolism in cancer
Guertin, D. A., & Wellen, K. E. (2023) · Nature Reviews Cancer · doi:10.1038/s41568-022-00543-5 · Cited by 303 · see citing works
Thirty years of NRF2: advances and therapeutic challenges.
Zhang, D. D. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-025-01145-0 · Cited by 282 · see citing works
Lytic cell death in metabolic liver disease
Gautheron, J., Gores, G. J., & Rodrigues, C. M. P. (2020) · Journal of Hepatology · doi:10.1016/j.jhep.2020.04.001 · Cited by 225 · see citing works
“Recently, the ferroptosis suppressor protein 1 (FSP1), previously known as apoptosis-inducing factor mitochondrial 2 (AIFM2), was identified as a key component of a non-mitochondrial CoQ10 (ubiquinone) antioxidant system that acts in parallel to the GPX4 canonical pathway to halt the progression of lipid peroxides [58…”
BackgroundSmall molecules regulating reactive oxygen species homeostasis for cancer therapy
Zhang, J., Duan, D., Song, Z., Liu, T., Hou, Y., & Fang, J. (2021) · Medicinal Research Reviews · doi:10.1002/med.21734 · Cited by 184 · see citing works
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 · see citing works
Self-citationCREB stimulates GPX4 transcription to inhibit ferroptosis in lung adenocarcinoma
Wang, Z., Zhang, X., Tian, X., Yang, Y., Ma, L., Wang, J., & Yu, Y. (2021) · Oncology Reports · doi:10.3892/or.2021.8039 · Cited by 122 · see citing works
Van San, E., Debruyne, A. C., Veeckmans, G., Tyurina, Y. Y., Tyurin, V. A., Zheng, H., Choi, S. M., Augustyns, K., van Loo, G., Michalke, B., et al. (2023) · Cell Death & Differentiation · doi:10.1038/s41418-023-01195-0 · Cited by 103 · see citing works
“Recently, several key genetic factors have been identified to be crucial in controlling ferroptosis such as GTP cyclohydrolase 1 (GCH1) [19], ferroptosis suppressor protein (FSP1) [20], and dihydroorotate dehydrogenase (DHODH) [21].”
BackgroundInfluentialRelB-activated GPX4 inhibits ferroptosis and confers tamoxifen resistance in breast cancer
Xu, Z., Wang, X., Sun, W., Xu, F., Kou, H., Hu, W., Zhang, Y., Jiang, Q., Tang, J., & Xu, Y. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102952 · Cited by 76 · see citing works
Yue, M., Wei, J., Chen, W., Hong, D., Chen, T., & Fang, X. (2022) · Nutrients · doi:10.3390/nu14224886 · Cited by 62 · see citing works
Liu, B., & Wang, H. (2022) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2022.11321 · Cited by 56 · see citing works
Cheng, X., Zhao, F., Ke, B., Chen, D., & Liu, F. (2023) · Cancers · doi:10.3390/cancers15215209 · Cited by 44 · see citing works
Genome-wide CRISPRi/a screens in human neurons link lysosomal failure to ferroptosis
Tian, R., Abarientos, A., Hong, J., Hashemi, S. H., Yan, R., Dräger, N., Leng, K., Nalls, M. A., Singleton, A. B., Xu, K., et al. (2020) · doi:10.1101/2020.06.27.175679 · Cited by 414 · see citing works
Ferrous iron–activatable drug conjugate achieves potent MAPK blockade in <i>KRAS</i> -driven tumors
Jiang, H., Muir, R. K., Gonciarz, R. L., Olshen, A. B., Yeh, I., Hann, B. C., Zhao, N., Wang, Y.-H., Behr, S. C., Korkola, J. E., et al. (2022) · Journal of Experimental Medicine · doi:10.1084/jem.20210739 · Cited by 33 · see citing works
Unveiling ferroptosis as a promising therapeutic avenue for colorectal cancer and colitis treatment
Kao, A. T., Cabanlong, C. V., Padilla, K., & Xue, X. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.05.025 · Cited by 30 · see citing works
AP-1 inhibitor induces ferroptosis via the PI3K/AKT pathway in multiple myeloma cells
Tang, S., Liu, J., Li, F., Yan, Y., Long, X., & Fu, Y. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e34397 · Cited by 13 · see citing works
- Authors
- Bersuker, K., Hendricks, J. M., Li, Z., Magtanong, L., Ford, B., Tang, P. H., Roberts, M. A., Tong, B., Maimone, T. J., Zoncu, R., Bassik, M. C., Nomura, D. K., Dixon, S. J., & Olzmann, J. A.
- Affiliations
- University of California, Berkeley (US)
- Stanford University (US)
- Cincinnati Children's Hospital Medical Center (US)
- Stanford Medicine (US)
- Chan Zuckerberg Biohub San Francisco (US)
- Corresponding author
- Olzmann, James A.
- ORCID
- Venue
- Nature
- Published
- 2019-10-21
- Volume
- 575
- Issue
- 7784
- Pages
- 688-692
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC6883167
- OpenAlex
- W2980472864
- Cited by
- 3,703
- References
- 36
- Citations by year
- 2026: 578 · 2025: 675 · 2024: 754 · 2023: 592 · 2022: 507 · 2021: 389 · 2020: 186 · 2019: 8 · 2017: 1 · 2016: 3 · 2015: 1 · 2014: 1
- FWCI
- 206.82
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Cancer Institute (DP2CA195761)
- National Institute of General Medical Sciences (R01GM127763, R01GM112948, R01GM122923)
- National Institute of Environmental Health Sciences (P42ES004705)
- Topics
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Ferroptosis and cancer prognosis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- ferroptosis, S100A4, AIFM2, GPX4, coenzyme Q10, oxidative enzymes, lipid peroxidation, ferroptosis resistance, myristoylation, plasma membrane, synthetic lethality, lung cancer, cancer cell death
- MeSH terms
- Ferroptosis, Phospholipid Hydroperoxide Glutathione Peroxidase, Animals, Cell Membrane, Humans, Lipid Peroxides, Male, Ubiquinone, Gene Expression Regulation, Enzymologic, Mice, SCID, Mitochondrial Proteins, Cell Line, Tumor, Apoptosis Regulatory Proteins, Mice, Heterografts
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