The DOI matches its Crossref record; 130 of the 130 references it cites were found in a registry or an index.
Signaling pathways and defense mechanisms of ferroptosis
Open accessAbstract
As a type of lytic cell death driven by unrestricted lipid peroxidation and subsequent plasma membrane damage, ferroptosis occurs and develops because of sophisticated signals and regulatory mechanisms. The reactive oxygen species (ROS) used to initiate ferroptosis come from a variety of sources, including iron‐mediated Fenton reactions, mitochondrial ROS, and membrane‐associated ROS driven by the NOX protein family. Polyunsaturated fatty acid‐containing phospholipids are the main substrates of lipid peroxidation in ferroptosis, which is positively regulated by enzymes, such as ACSL4, LPCAT3, ALOXs, or POR. Selective activation of autophagic degradation pathways promotes ferroptosis by increasing iron accumulation to cause lipid peroxidation. In contrast, system xc–‐glutathione–GPX4 axis plays a central role in limiting lipid peroxidation, although other antioxidants (such as coenzyme Q10 and tetrahydrobiopterin) can also inhibit ferroptosis. A main nuclear mechanism of cell defense against ferroptosis is the activation of the NFE2L2‐dependent antioxidant response by transcriptionally upregulating the expression of antioxidants or cytoprotective genes. Additionally, the membrane damage caused by ferroptotic stimulus can be repaired by ESCRT‐III‐dependent membrane scission machinery. In this review, we summarize recent progress in understanding the signaling pathways and defense mechanisms of ferroptosis.
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.
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
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
Regulation 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
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
Self-citationFerroptosis: mechanisms, biology and role in disease
Jiang, X., Stockwell, B. R., & Conrad, M. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00324-8 · Cited by 7,505
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680
Self-citationACSL4 dictates ferroptosis sensitivity by shaping cellular lipid composition
Doll, S., Proneth, B., Tyurina, Y. Y., Panzilius, E., Kobayashi, S., Ingold, I., Irmler, M., Beckers, J., Aichler, M., Walch, A., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2239 · Cited by 4,293
Ferroptosis: molecular mechanisms and health implications
Tang, D., Chen, X., Kang, R., & Kroemer, G. (2021) · Cell Research · doi:10.1038/s41422-020-00441-1 · Cited by 4,256
Self-citationInactivation of the ferroptosis regulator Gpx4 triggers acute renal failure in mice
Friedmann Angeli, J. P., Schneider, M., Proneth, B., Tyurina, Y. Y., Tyurin, V. A., Hammond, V. J., Herbach, N., Aichler, M., Walch, A., Eggenhofer, E., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3064 · Cited by 3,732
The CoQ oxidoreductase FSP1 acts parallel to GPX4 to inhibit ferroptosis
Bersuker, K., Hendricks, J. M., Li, Z., Magtanong, L., Ford, B., Tang, P. H., Roberts, M. A., Tong, B., Maimone, T. J., Zoncu, R., et al. (2019) · Nature · doi:10.1038/s41586-019-1705-2 · Cited by 3,703
Ferroptosis as a p53-mediated activity during tumour suppression
Jiang, L., Kon, N., Li, T., Wang, S.-J., Su, T., Hibshoosh, H., Baer, R., & Gu, W. (2015) · Nature · doi:10.1038/nature14344 · Cited by 3,398
FSP1 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
Oxidized arachidonic and adrenic PEs navigate cells to ferroptosis
Kagan, V. E., Mao, G., Qu, F., Angeli, J. P. F., Doll, S., Croix, C. S., Dar, H. H., Liu, B., Tyurin, V. A., Ritov, V. B., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2238 · Cited by 3,029
Broadening horizons: the role of ferroptosis in cancer
Chen, X., Kang, R., Kroemer, G., & Tang, D. (2021) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-020-00462-0 · Cited by 2,897
Self-citationThe molecular machinery of regulated cell death
Tang, D., Kang, R., Berghe, T. V., Vandenabeele, P., & Kroemer, G. (2019) · Cell Research · doi:10.1038/s41422-019-0164-5 · Cited by 2,549
Self-citationMitochondria as multifaceted regulators of cell death
Bock, F. J., & Tait, S. W. G. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0173-8 · Cited by 2,450
Autophagy promotes ferroptosis by degradation of ferritin
Hou, W., Xie, Y., Song, X., Sun, X., Lotze, M. T., Zeh, H. J., Kang, R., & Tang, D. (2016) · Autophagy · doi:10.1080/15548627.2016.1187366 · Cited by 2,332
Self-citationPeroxidation 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
Role of Mitochondria in Ferroptosis
Gao, M., Yi, J., Zhu, J., Minikes, A. M., Monian, P., Thompson, C. B., & Jiang, X. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.10.042 · Cited by 2,120
Ferroptosis: machinery and regulation
Chen, X., Li, J., Kang, R., Klionsky, D. J., & Tang, D. (2021) · Autophagy · doi:10.1080/15548627.2020.1810918 · Cited by 2,099
Self-citationGlutaminolysis and transferrin regulate ferroptosis
Gao, M., Monian, P., Quadri, N., Ramasamy, R., & Jiang, X. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.06.011 · Cited by 2,069
Sun, X., Ou, Z., Chen, R., Niu, X., Chen, D., Kang, R., & Tang, D. (2016) · Hepatology · doi:10.1002/hep.28251 · Cited by 2,012
Self-citationThe Role of Mitochondria in Apoptosis
Wang, C., & Youle, R. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134850 · Cited by 1,987
RAS Proteins and Their Regulators in Human Disease
Simanshu, D. K., Nissley, D. V., & McCormick, F. (2017) · Cell · doi:10.1016/j.cell.2017.06.009 · Cited by 1,943
Ferroptosis is an autophagic cell death process
Gao, M., Monian, P., Pan, Q., Zhang, W., Xiang, J., & Jiang, X. (2016) · Cell Research · doi:10.1038/cr.2016.95 · Cited by 1,899
Yang, W. S., & Stockwell, B. R. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.02.010 · Cited by 1,876
NRF2 and the Hallmarks of Cancer
Rojo de la Vega, M., Chapman, E., & Zhang, D. D. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.03.022 · Cited by 1,672
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
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
Dolma, 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
The Metabolic Underpinnings of Ferroptosis
Zheng, J., & Conrad, M. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.10.011 · Cited by 1,329
GTP Cyclohydrolase 1/Tetrahydrobiopterin Counteract Ferroptosis through Lipid Remodeling
Kraft, V. A. N., Bezjian, C. T., Pfeiffer, S., Ringelstetter, L., Müller, C., Zandkarimi, F., Merl-Pham, J., Bao, X., Anastasov, N., Kössl, J., et al. (2020) · ACS Central Science · doi:10.1021/acscentsci.9b01063 · Cited by 1,298
Exogenous Monounsaturated Fatty Acids Promote a Ferroptosis-Resistant Cell State
Magtanong, L., Ko, P.-J., 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 1,147
Ferrostatins Inhibit Oxidative Lipid Damage and Cell Death in Diverse Disease Models
Skouta, R., Dixon, S. J., Wang, J., Dunn, D. E., Orman, M., Shimada, K., Rosenberg, P. A., Lo, D. C., Weinberg, J. M., Linkermann, A., et al. (2014) · Journal of the American Chemical Society · doi:10.1021/ja411006a · Cited by 1,146
Energy-stress-mediated AMPK activation inhibits ferroptosis
Lee, H., Zandkarimi, F., Zhang, Y., Meena, J. K., Kim, J., Zhuang, L., Tyagi, S., Ma, L., Westbrook, T. F., Steinberg, G. R., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0461-8 · Cited by 1,128
Synchronized renal tubular cell death involves ferroptosis
Linkermann, A., Skouta, R., Himmerkus, N., Mulay, S. R., Dewitz, C., De Zen, F., Prokai, A., Zuchtriegel, G., Krombach, F., Welz, P.-S., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1415518111 · Cited by 1,126
Intercellular interaction dictates cancer cell ferroptosis via NF2–YAP signalling
Wu, J., Minikes, A. M., Gao, M., Bian, H., Li, Y., Stockwell, B. R., Chen, Z.-N., & Jiang, X. (2019) · Nature · doi:10.1038/s41586-019-1426-6 · Cited by 1,110
RAS-targeted therapies: is the undruggable drugged?
Moore, A. R., Rosenberg, S. C., McCormick, F., & Malek, S. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0068-6 · Cited by 1,103
Emerging Mechanisms and Disease Relevance of Ferroptosis
Stockwell, B. R., Jiang, X., & Gu, W. (2020) · Trends in Cell Biology · doi:10.1016/j.tcb.2020.02.009 · Cited by 1,099
Identification of ACSL4 as a biomarker and contributor of ferroptosis
Yuan, H., Li, X., Zhang, X., Kang, R., & Tang, D. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.08.124 · Cited by 1,071
Self-citationHuman Haploid Cell Genetics Reveals Roles for Lipid Metabolism Genes in Nonapoptotic Cell Death
Dixon, S. J., Winter, G. E., Musavi, L. S., Lee, E. D., Snijder, B., Rebsamen, M., Superti-Furga, G., & Stockwell, B. R. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00245 · Cited by 1,043
Global 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
The chemical basis of ferroptosis
Conrad, M., & Pratt, D. A. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0408-1 · Cited by 1,002
Iron Metabolism in Ferroptosis
Chen, X., Yu, C., Kang, R., & Tang, D. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.590226 · Cited by 959
Self-citationThe Tumor Suppressor p53 Limits Ferroptosis by Blocking DPP4 Activity
Xie, Y., Zhu, S., Song, X., Sun, X., Fan, Y., Liu, J., Zhong, M., Yuan, H., Zhang, L., Billiar, T. R., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.07.055 · Cited by 952
Self-citationPEBP1 Wardens Ferroptosis by Enabling Lipoxygenase Generation of Lipid Death Signals
Wenzel, S. E., Tyurina, Y. Y., Zhao, J., St. Croix, C. M., Dar, H. H., Mao, G., Tyurin, V. A., Anthonymuthu, T. S., Kapralov, A. A., Amoscato, A. A., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.044 · Cited by 950
ALOX12 is required for p53-mediated tumour suppression through a distinct ferroptosis pathway
Chu, B., Kon, N., Chen, D., Li, T., Liu, T., Jiang, L., Song, S., Tavana, O., & Gu, W. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0305-6 · Cited by 882
Plasticity of ether lipids promotes ferroptosis susceptibility and evasion
Zou, Y., Henry, W. S., Ricq, E. L., Graham, E. T., Phadnis, V. V., Maretich, P., Paradkar, S., Boehnke, N., Deik, A. A., Reinhardt, F., et al. (2020) · Nature · doi:10.1038/s41586-020-2732-8 · Cited by 834
Ferroptosis in infection, inflammation, and immunity
Chen, X., Kang, R., Kroemer, G., & Tang, D. (2021) · Journal of Experimental Medicine · doi:10.1084/jem.20210518 · Cited by 824
Self-citationAutophagy-Dependent Ferroptosis: Machinery and Regulation
Liu, J., Kuang, F., Kroemer, G., Klionsky, D. J., Kang, R., & Tang, D. (2020) · Cell Chemical Biology · doi:10.1016/j.chembiol.2020.02.005 · Cited by 812
Self-citationNFS1 undergoes positive selection in lung tumours and protects cells from ferroptosis
Alvarez, S. W., Sviderskiy, V. O., Terzi, E. M., Papagiannakopoulos, T., Moreira, A. L., Adams, S., Sabatini, D. M., Birsoy, K., & Possemato, R. (2017) · Nature · doi:10.1038/nature24637 · Cited by 787
Unsolved mysteries: How does lipid peroxidation cause ferroptosis?
Feng, H., & Stockwell, B. R. (2018) · PLOS Biology · doi:10.1371/journal.pbio.2006203 · Cited by 759
AMPK-Mediated BECN1 Phosphorylation Promotes Ferroptosis by Directly Blocking System Xc– Activity
Song, X., Zhu, S., Chen, P., Hou, W., Wen, Q., Liu, J., Xie, Y., Liu, J., Klionsky, D. J., Kroemer, G., et al. (2018) · Current Biology · doi:10.1016/j.cub.2018.05.094 · Cited by 746
Self-citationESCRT-dependent membrane repair negatively regulates pyroptosis downstream of GSDMD activation
Rühl, S., Shkarina, K., Demarco, B., Heilig, R., Santos, J. C., & Broz, P. (2018) · Science · doi:10.1126/science.aar7607 · Cited by 742
Cytochrome P450 oxidoreductase contributes to phospholipid peroxidation in ferroptosis
Zou, Y., Li, H., Graham, E. T., Deik, A. A., Eaton, J. K., Wang, W., Sandoval-Gomez, G., Clish, C. B., Doench, J. G., & Schreiber, S. L. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0472-6 · Cited by 734
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 721
Lipidomics for studying metabolism
Han, X. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.98 · Cited by 718
Metallothionein‐1G facilitates sorafenib resistance through inhibition of ferroptosis
Sun, X., Niu, X., Chen, R., He, W., Chen, D., Kang, R., & Tang, D. (2016) · Hepatology · doi:10.1002/hep.28574 · Cited by 703
Self-citationThe tumor suppressor protein p53 and the ferroptosis network
Kang, R., Kroemer, G., & Tang, D. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.05.074 · Cited by 698
Self-citationESCRT-III Acts Downstream of MLKL to Regulate Necroptotic Cell Death and Its Consequences
Gong, Y.-N., Guy, C., Olauson, H., Becker, J. U., Yang, M., Fitzgerald, P., Linkermann, A., & Green, D. R. (2017) · Cell · doi:10.1016/j.cell.2017.03.020 · Cited by 689
T cell lipid peroxidation induces ferroptosis and prevents immunity to infection
Matsushita, M., Freigang, S., Schneider, C., Conrad, M., Bornkamm, G. W., & Kopf, M. (2015) · Journal of Experimental Medicine · doi:10.1084/jem.20140857 · Cited by 672
The release and activity of HMGB1 in ferroptosis
Wen, Q., Liu, J., Kang, R., Zhou, B., & Tang, D. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.01.090 · Cited by 672
Self-citationHSPB1 as a novel regulator of ferroptotic cancer cell death
Sun, X., Ou, Z., Xie, M., Kang, R., Fan, Y., Niu, X., Wang, H., Cao, L., & Tang, D. (2015) · Oncogene · doi:10.1038/onc.2015.32 · Cited by 666
Self-citationCellular degradation systems in ferroptosis
Chen, X., Yu, C., Kang, R., Kroemer, G., & Tang, D. (2021) · Cell Death & Differentiation · doi:10.1038/s41418-020-00728-1 · Cited by 628
Self-citationFerroptosis is induced following siramesine and lapatinib treatment of breast cancer cells
Ma, S., Henson, E. S., Chen, Y., & Gibson, S. B. (2016) · Cell Death & Disease · doi:10.1038/cddis.2016.208 · Cited by 622
Yan, B., Ai, Y., Sun, Q., Ma, Y., Cao, Y., Wang, J., Zhang, Z., & Wang, X. (2021) · Molecular Cell · doi:10.1016/j.molcel.2020.11.024 · Cited by 617
Heme oxygenase-1 accelerates erastin-induced ferroptotic cell death
Kwon, M.-Y., Park, E., Lee, S.-J., & Chung, S. W. (2015) · Oncotarget · doi:10.18632/oncotarget.5162 · Cited by 612
Tang, D., & Kroemer, G. (2020) · Current Biology · doi:10.1016/j.cub.2020.09.068 · Cited by 605
Self-citationChaperone-mediated autophagy is involved in the execution of ferroptosis
Wu, Z., Geng, Y., Lu, X., Shi, Y., Wu, G., Zhang, M., Shan, B., Pan, H., & Yuan, J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1819728116 · Cited by 577
Prominin2 Drives Ferroptosis Resistance by Stimulating Iron Export
Brown, C. W., Amante, J. J., Chhoy, P., Elaimy, A. L., Liu, H., Zhu, L. J., Baer, C. E., Dixon, S. J., & Mercurio, A. M. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.10.007 · Cited by 575
Basit, F., van Oppen, L. M., Schöckel, L., Bossenbroek, H. M., van Emst-de Vries, S. E., Hermeling, J. C., Grefte, S., Kopitz, C., Heroult, M., HGM Willems, P., et al. (2017) · Cell Death & Disease · doi:10.1038/cddis.2017.133 · Cited by 565
Stearoyl-CoA Desaturase 1 Protects Ovarian Cancer Cells from Ferroptotic Cell Death
Tesfay, L., Paul, B. T., Konstorum, A., Deng, Z., Cox, A. O., Lee, J., Furdui, C. M., Hegde, P., Torti, F. M., & Torti, S. V. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-0369 · Cited by 551
Oxidative Damage and Antioxidant Defense in Ferroptosis
Kuang, F., Liu, J., Tang, D., & Kang, R. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.586578 · Cited by 531
Self-citationIron homeostasis and iron-regulated ROS in cell death, senescence and human diseases
Nakamura, T., Naguro, I., & Ichijo, H. (2019) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2019.06.010 · Cited by 523
Heme oxygenase-1 mediates BAY 11-7085 induced ferroptosis
Chang, L.-C., Chiang, S.-K., Chen, S.-E., Yu, Y.-L., Chou, R.-H., & Chang, W.-C. (2018) · Cancer Letters · doi:10.1016/j.canlet.2017.12.025 · Cited by 521
Lipid storage and lipophagy regulates ferroptosis
Bai, Y., Meng, L., Han, L., Jia, Y., Zhao, Y., Gao, H., Kang, R., Wang, X., Tang, D., & Dai, E. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.12.039 · Cited by 507
Self-citationCISD1 inhibits ferroptosis by protection against mitochondrial lipid peroxidation
Yuan, H., Li, X., Zhang, X., Kang, R., & Tang, D. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.08.034 · Cited by 504
Self-citationCharacteristics and Biomarkers of Ferroptosis
Chen, X., Comish, P. B., Tang, D., & Kang, R. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.637162 · Cited by 504
Self-citationThe Deubiquitylase OTUB1 Mediates Ferroptosis via Stabilization of SLC7A11
Liu, T., Jiang, L., Tavana, O., & Gu, W. (2019) · Cancer Research · doi:10.1158/0008-5472.can-18-3037 · Cited by 490
Quality control of the mitochondrial proteome
Song, J., Herrmann, J. M., & Becker, T. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00300-2 · Cited by 483
Yu, Y., Xie, Y., Cao, L., Yang, L., Yang, M., Lotze, M. T., Zeh, H. J., Kang, R., & Tang, D. (2015) · Molecular & Cellular Oncology · doi:10.1080/23723556.2015.1054549 · Cited by 468
Self-citationHayano, M., Yang, W. S., Corn, C. K., Pagano, N. C., & Stockwell, B. R. (2016) · Cell Death & Differentiation · doi:10.1038/cdd.2015.93 · Cited by 457
The Hippo Pathway Effector TAZ Regulates Ferroptosis in Renal Cell Carcinoma
Yang, W.-H., Ding, C.-K. C., Sun, T., Rupprecht, G., Lin, C.-C., Hsu, D., & Chi, J.-T. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.07.107 · Cited by 455
Schmidt, O., & Teis, D. (2012) · Current Biology · doi:10.1016/j.cub.2012.01.028 · Cited by 454
Breakdown of an Ironclad Defense System: The Critical Role of NRF2 in Mediating Ferroptosis
Anandhan, A., Dodson, M., Schmidlin, C. J., Liu, P., & Zhang, D. D. (2020) · Cell Chemical Biology · doi:10.1016/j.chembiol.2020.03.011 · Cited by 442
Dai, E., Han, L., Liu, J., Xie, Y., Zeh, H. J., Kang, R., Bai, L., & Tang, D. (2020) · Nature Communications · doi:10.1038/s41467-020-20154-8 · Cited by 420
Self-citationHeme oxygenase-1 mitigates ferroptosis in renal proximal tubule cells
Adedoyin, O., Boddu, R., Traylor, A., Lever, J. M., Bolisetty, S., George, J. F., & Agarwal, A. (2018) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00044.2017 · Cited by 368
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
NRF2 Is a Major Target of ARF in p53-Independent Tumor Suppression
Chen, D., Tavana, O., Chu, B., Erber, L., Chen, Y., Baer, R., & Gu, W. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.09.009 · Cited by 317
Achieving Life through Death: Redox Biology of Lipid Peroxidation in Ferroptosis
Bayır, H., Anthonymuthu, T. S., Tyurina, Y. Y., Patel, S. J., Amoscato, A. A., Lamade, A. M., Yang, Q., Vladimirov, G. K., Philpott, C. C., & Kagan, V. E. (2020) · Cell Chemical Biology · doi:10.1016/j.chembiol.2020.03.014 · Cited by 317
Ferroptotic pores induce Ca2+ fluxes and ESCRT-III activation to modulate cell death kinetics
Pedrera, L., Espiritu, R. A., Ros, U., Weber, J., Schmitt, A., Stroh, J., Hailfinger, S., von Karstedt, S., & García-Sáez, A. J. (2021) · Cell Death & Differentiation · doi:10.1038/s41418-020-00691-x · Cited by 314
Yang, W.-H., Huang, Z., Wu, J., Ding, C.-K. C., Murphy, S. K., & Chi, J.-T. (2020) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-19-0691 · Cited by 301
NUPR1 is a critical repressor of ferroptosis
Liu, J., Song, X., Kuang, F., Zhang, Q., Xie, Y., Kang, R., Kroemer, G., & Tang, D. (2021) · Nature Communications · doi:10.1038/s41467-021-20904-2 · Cited by 290
Self-citationKinome screen of ferroptosis reveals a novel role of ATM in regulating iron metabolism
Chen, P.-H., Wu, J., Ding, C.-K. C., Lin, C.-C., Pan, S., Bossa, N., Xu, Y., Yang, W.-H., Mathey-Prevot, B., & Chi, J.-T. (2020) · Cell Death & Differentiation · doi:10.1038/s41418-019-0393-7 · Cited by 287
Structures, Functions, and Dynamics of ESCRT-III/Vps4 Membrane Remodeling and Fission Complexes
McCullough, J., Frost, A., & Sundquist, W. I. (2018) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100616-060600 · Cited by 276
ESCRT-III–dependent membrane repair blocks ferroptosis
Dai, E., Meng, L., Kang, R., Wang, X., & Tang, D. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.11.110 · Cited by 273
Self-citationFerroptosis 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 273
Poursaitidis, I., Wang, X., Crighton, T., Labuschagne, C., Mason, D., 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 272
Kim, E. H., Shin, D., Lee, J., Jung, A. R., & Roh, J.-L. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.06.018 · Cited by 261
Song, X., Liu, J., Kuang, F., Chen, X., Zeh, H. J., Kang, R., Kroemer, G., Xie, Y., & Tang, D. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108767 · Cited by 260
Self-citationChen, X., Xu, S., Zhao, C., & Liu, B. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.06.015 · Cited by 258
Tumor heterogeneity in autophagy-dependent ferroptosis
Li, J., Liu, J., Xu, Y., Wu, R., Chen, X., Song, X., Zeh, H., Kang, R., Klionsky, D. J., Wang, X., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.1872241 · Cited by 245
Self-citationFerroptosis is a lysosomal cell death process
Gao, H., Bai, Y., Jia, Y., Zhao, Y., Kang, R., Tang, D., & Dai, E. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.07.078 · Cited by 244
Self-citationIdentification of baicalein as a ferroptosis inhibitor by natural product library screening
Xie, Y., Song, X., Sun, X., Huang, J., Zhong, M., Lotze, M. T., Zeh, H. J., Kang, R., & Tang, D. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.03.052 · Cited by 243
Self-citationWu, M., Xu, L.-G., Li, X., Zhai, Z., & Shu, H.-B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202285200 · Cited by 241
AIFM2 blocks ferroptosis independent of ubiquinol metabolism
Dai, E., Zhang, W., Cong, D., Kang, R., Wang, J., & Tang, D. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.01.066 · Cited by 232
Self-citationBröker, L. E., Huisman, C., Span, S. W., Rodriguez, J. A., Kruyt, F. A. E., & Giaccone, G. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-3060 · Cited by 206
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 201
Self-citationMGST1 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
Self-citationSTING1 Promotes Ferroptosis Through MFN1/2-Dependent Mitochondrial Fusion
Li, C., Liu, J., Hou, W., Kang, R., & Tang, D. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.698679 · Cited by 180
Self-citationIron and carcinogenesis: from Fenton reaction to target genes
Toyokuni, S. (2002) · Redox Report · doi:10.1179/135100002125000596 · Cited by 166
Aldo-keto reductases protect metastatic melanoma from ER stress-independent ferroptosis
Gagliardi, M., Cotella, D., Santoro, C., Corà, D., Barlev, N. A., Piacentini, M., & Corazzari, M. (2019) · Cell Death & Disease · doi:10.1038/s41419-019-2143-7 · Cited by 165
Regulation and function of autophagy in pancreatic cancer
Li, J., Chen, X., Kang, R., Zeh, H., Klionsky, D. J., & Tang, D. (2021) · Autophagy · doi:10.1080/15548627.2020.1847462 · Cited by 162
Self-citationLipid Metabolism in Ferroptosis
Lin, Z., Liu, J., Kang, R., Yang, M., & Tang, D. (2021) · Advanced Biology · doi:10.1002/adbi.202100396 · Cited by 158
Self-citationNEDD4L-mediated LTF protein degradation limits ferroptosis
Wang, Y., Liu, Y., Liu, J., Kang, R., & Tang, D. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.07.032 · Cited by 155
Self-citationA Glutathione-Nrf2-Thioredoxin Cross-Talk Ensures Keratinocyte Survival and Efficient Wound Repair
Telorack, M., Meyer, M., Ingold, I., Conrad, M., Bloch, W., & Werner, S. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1005800 · Cited by 117
Cathepsin B is a mediator of organelle-specific initiation of ferroptosis
Kuang, F., Liu, J., Li, C., Kang, R., & Tang, D. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.10.035 · Cited by 116
Self-citationRoles of specific lipid species in the cell and their molecular mechanism
Kimura, T., Jennings, W., & Epand, R. M. (2016) · Progress in Lipid Research · doi:10.1016/j.plipres.2016.02.001 · Cited by 113
ESCRT-III-mediated membrane repair in cell death and tumor resistance
Liu, J., Kang, R., & Tang, D. (2020) · Cancer Gene Therapy · doi:10.1038/s41417-020-0200-0 · Cited by 109
Self-citationCathepsin B is an executioner of ferroptosis
Nagakannan, P., Islam, M. R., Conrad, M., & Eftekharpour, E. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118928 · Cited by 100
Ferroptosis is associated with oxygen-glucose deprivation/reoxygenation-induced Sertoli cell death
Li, L., Yu, H., Zhao, Y., Wang, H., Zhao, X., Jiang, Y., & Gao, F. (2018) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2018.3469 · Cited by 94
Acid sphingomyelinase promotes mitochondrial dysfunction due to glutamate-induced regulated necrosis
Novgorodov, S. A., Voltin, J. R., Gooz, M. A., Li, L., Lemasters, J. J., & Gudz, T. I. (2017) · Journal of Lipid Research · doi:10.1194/jlr.m080374 · Cited by 79
Loperamide, pimozide, and STF-62247 trigger autophagy-dependent cell death in glioblastoma cells
Zielke, S., Meyer, N. E., Mari, M. C., Abou‐El‐Ardat, K., Reggiori, F., van Wijk, S. J. L., Kögel, D., & Fulda, S. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1003-1 · Cited by 74
The Intersection of DNA Damage Response and Ferroptosis—A Rationale for Combination Therapeutics
Chen, P., Tseng, W. H.-S., & Chi, J. (2020) · Biology · doi:10.3390/biology9080187 · Cited by 53
Delorme-Axford, E., & Klionsky, D. (2018) · Autophagy · doi:10.1080/15548627.2018.1539585 · Cited by 51
NOX, NOX Who is There? The Contribution of NADPH Oxidase One to Beta Cell Dysfunction
Taylor, D. (2013) · Frontiers in Endocrinology · doi:10.3389/fendo.2013.00040 · Cited by 46
NOX-Dependent Signaling Dysregulation in Severe COVID-19: Clues to Effective Treatments
Damiano, S., Sozio, C., Rosa, G. L., & Santillo, M. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.608435 · Cited by 35
Divergent mechanisms of iron-containing enzymes for hydrocarbon biosynthesis
Wise, C. E., Grant, J. L., Amaya, J. A., Ratigan, S. C., Hsieh, C. H., Manley, O. M., & Makris, T. M. (2016) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-016-1425-0 · Cited by 25
Emerging aspects in the regulation of ferroptosis
Nehring, H., Meierjohann, S., & Angeli, J. P. F. (2020) · Biochemical Society Transactions · doi:10.1042/bst20200523 · Cited by 22
Overcoming Challenges in Expressing Iron–Sulfur Enzymes in Yeast
Biz, A., & Mahadevan, R. (2020) · Trends in biotechnology · doi:10.1016/j.tibtech.2020.11.005 · Cited by 20
Cited by
GPX4 in cell death, autophagy, and disease
Xie, Y., Kang, R., Klionsky, D. J., & Tang, D. (2023) · Autophagy · doi:10.1080/15548627.2023.2218764 · Cited by 623
Self-citationPhotodynamic therapy: Innovative approaches for antibacterial and anticancer treatments
Kolarikova, M., Hosikova, B., Dilenko, H., Barton‐Tomankova, K., Valkova, L., Bajgar, R., Malina, L., & Kolarova, H. (2023) · Medicinal Research Reviews · doi:10.1002/med.21935 · Cited by 282
Metadata
- Authors
- Liu, J., Kang, R., & Tang, D.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2021-06-17
- Volume
- 289
- Issue
- 22
- Pages
- 7038-7050
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W3169941200
- Cited by
- 787
- References
- 130
- FWCI
- 51.77
- Type
- journal article
- Language
- en
- Open access
- bronze
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.