Glutaminolysis and transferrin regulate ferroptosis
Open accessAbstract
Ferroptosis has emerged as a new form of regulated necrosis that is implicated in various human diseases. However, the mechanisms of ferroptosis are not well defined. This study reports the discovery of multiple molecular components of ferroptosis and its intimate interplay with cellular metabolism and redox machinery. Nutrient starvation often leads to sporadic apoptosis. Strikingly, we found that upon deprivation of amino acids, a more rapid and potent necrosis process can be induced in a serum-dependent manner, which was subsequently determined to be ferroptosis. Two serum factors, the iron-carrier protein transferrin and amino acid glutamine, were identified as the inducers of ferroptosis. We further found that the cell surface transferrin receptor and the glutamine-fueled intracellular metabolic pathway, glutaminolysis, played crucial roles in the death process. Inhibition of glutaminolysis, the essential component of ferroptosis, can reduce heart injury triggered by ischemia/reperfusion, suggesting a potential therapeutic approach for treating related diseases.
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?
Glutamine and transferrin induce ferroptosis under serum-deprivation conditions through glutaminolysis.
“Glutamine and transferrin were found to induce ferroptosis under serum-deprivation conditions, via the glutaminolysis pathway [38, 39].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [38]
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
Antioxidant Determinations by the Use of a Stable Free Radical
Blois, M. S. (1958) · Nature · doi:10.1038/1811199a0 · Cited by 13,075 · see citing works
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 · see citing works
Apoptosis in the Pathogenesis and Treatment of Disease
Thompson, C. B. (1995) · Science · doi:10.1126/science.7878464 · Cited by 6,524 · see citing works
Cillà, S. D., Farruggio, S., Vujosevic, S., Raina, G., Filippini, D. A., Gatti, V., Clemente, N., Mary, D., Vezzola, D., Casini, G., et al. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479441 · Cited by 5,153 · see citing works
Danial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651 · see citing works
The Biology of Cancer: Metabolic Reprogramming Fuels Cell Growth and Proliferation
DeBerardinis, R. J., Lum, J. J., Hatzivassiliou, G., & Thompson, C. B. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.002 · Cited by 4,088 · see citing works
Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death
Wei, M. C., Zong, W.-X., Cheng, E. H.-Y., Lindsten, T., Panoutsakopoulou, V., Ross, A. J., Roth, K. A., MacGregor, G. R., Thompson, C. B., & Korsmeyer, S. J. (2001) · Science · doi:10.1126/science.1059108 · Cited by 3,988 · see citing works
Inactivation 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 · see citing works
The Pathophysiology of Mitochondrial Cell Death
Green, D. R., & Kroemer, G. (2004) · Science · doi:10.1126/science.1099320 · Cited by 3,416 · see citing works
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 · see citing works
Pyroptosis: host cell death and inflammation
Bergsbaken, T., Fink, S. L., & Cookson, B. T. (2009) · Nature Reviews Microbiology · doi:10.1038/nrmicro2070 · Cited by 3,185 · see citing works
Mixed Lineage Kinase Domain-like Protein Mediates Necrosis Signaling Downstream of RIP3 Kinase
Sun, L., Wang, H., Wang, Z., He, S., Chen, S., Liao, D., Wang, L., Yan, J., Liu, W., Lei, X., et al. (2012) · Cell · doi:10.1016/j.cell.2011.11.031 · Cited by 2,698 · see citing works
Biochemical Pathways of Caspase Activation During Apoptosis
Budihardjo, I. I., Oliver, H., Lutter, M. L., Luo, X., & Wang, X. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.269 · Cited by 2,562 · see citing works
Cho, Y., Challa, S., Moquin, D., Genga, R., Ray, T. D., Guildford, M., & Chan, F. K.-M. (2009) · Cell · doi:10.1016/j.cell.2009.05.037 · Cited by 2,435 · see citing works
Rahman, I., Kode, A., & Biswas, S. K. (2006) · Nature Protocols · doi:10.1038/nprot.2006.378 · Cited by 2,262 · see citing works
Receptor Interacting Protein Kinase-3 Determines Cellular Necrotic Response to TNF-α
He, S., Wang, L., Miao, L., Wang, T., Du, F., Zhao, L., & Wang, X. (2009) · Cell · doi:10.1016/j.cell.2009.05.021 · Cited by 2,214 · see citing works
Identification of RIP1 kinase as a specific cellular target of necrostatins
Degterev, A., Hitomi, J., Germscheid, M., Ch'en, I. L., Korkina, O., Teng, X., Abbott, D., Cuny, G. D., Yuan, C., Wagner, G., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.83 · Cited by 2,059 · see citing works
Wise, D. R., DeBerardinis, R. J., Mancuso, A., Sayed, N., Zhang, X.-Y., Pfeiffer, H. K., Nissim, I., Daikhin, E., Yudkoff, M., McMahon, S. B., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810199105 · Cited by 2,001 · see citing works
RIP3, an Energy Metabolism Regulator That Switches TNF-Induced Cell Death from Apoptosis to Necrosis
Zhang, D.-W., Shao, J., Lin, J., Zhang, N., Lu, B.-J., Lin, S.-C., Dong, M.-Q., & Han, J. (2009) · Science · doi:10.1126/science.1172308 · Cited by 1,931 · see citing works
Programmed Cell Death in Animal Development and Disease
Fuchs, Y., & Steller, H. (2011) · Cell · doi:10.1016/j.cell.2011.10.033 · Cited by 1,915 · see citing works
Regulated necrosis: the expanding network of non-apoptotic cell death pathways
Berghe, T. V., Linkermann, A., Jouan-Lanhouet, S., Walczak, H., & Vandenabeele, P. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3737 · Cited by 1,735 · see citing works
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 · see citing works
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 · see citing works
Catalytic activity of the caspase-8–FLIPL complex inhibits RIPK3-dependent necrosis
Oberst, A., Dillon, C. P., Weinlich, R., McCormick, L. L., Fitzgerald, P., Pop, C., Hakem, R., Salvesen, G. S., & Green, D. R. (2011) · Nature · doi:10.1038/nature09852 · Cited by 1,278 · cited 19× · see citing works
“However, RIP3 gene deletion did not prevent serum-induced cell death in MEFs, although it completely blocked TNFα-induced necrosis as predicted (Figure 1F, G and Figure S1C).”
BackgroundInfluentialGlutamine and cancer: cell biology, physiology, and clinical opportunities
Hensley, C. T., Wasti, A. T., & DeBerardinis, R. J. (2013) · Journal of Clinical Investigation · doi:10.1172/jci69600 · Cited by 1,262 · see citing works
The Pseudokinase MLKL Mediates Necroptosis via a Molecular Switch Mechanism
Murphy, J. M., Czabotar, P. E., Hildebrand, J. M., Lucet, I. S., Zhang, J.-G., Alvarez-Diaz, S., Lewis, R., Lalaoui, N., Metcalf, D., Webb, A. I., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.06.018 · Cited by 1,220 · see citing works
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 · see citing works
RIP3 mediates the embryonic lethality of caspase-8-deficient mice
Kaiser, W. J., Upton, J. W., Long, A. B., Livingston-Rosanoff, D., Daley-Bauer, L. P., Hakem, R., Caspary, T., & Mocarski, E. S. (2011) · Nature · doi:10.1038/nature09857 · Cited by 1,057 · see citing works
Targeting Mitochondrial Glutaminase Activity Inhibits Oncogenic Transformation
Wang, J.-B., Erickson, J. W., Fuji, R., Ramachandran, S., Gao, P., Dinavahi, R., Wilson, K. F., Ambrosio, A. L. B., Dias, S. M. G., Dang, C. V., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.08.009 · Cited by 821 · see citing works
Activity of Protein Kinase RIPK3 Determines Whether Cells Die by Necroptosis or Apoptosis
Newton, K., Dugger, D. L., Wickliffe, K. E., Kapoor, N., de Almagro, M. C., Vucic, D., Komuves, L., Ferrando, R. E., French, D. M., Webster, J., et al. (2014) · Science · doi:10.1126/science.1249361 · Cited by 687 · see citing works
Regulation of Glutaminase Activity and Glutamine Metabolism
Curthoys, N. P., & Watford, M. (1995) · Annual Review of Nutrition · doi:10.1146/annurev.nu.15.070195.001025 · Cited by 643 · see citing works
Andrews, N. C., & Schmidt, P. J. (2006) · Annual Review of Physiology · doi:10.1146/annurev.physiol.69.031905.164337 · Cited by 640 · see citing works
The Role of the Kinases RIP1 and RIP3 in TNF-Induced Necrosis
Vandenabeele, P., Declercq, W., Van Herreweghe, F., & Vanden Berghe, T. (2010) · Science Signaling · doi:10.1126/scisignal.3115re4 · Cited by 482 · see citing works
RIP3: a molecular switch for necrosis and inflammationPreprint
Moriwaki, K., & Chan, F. K.-M. (2013) · Genes & Development · doi:10.1101/gad.223321.113 · Cited by 353 · see citing works
Robinson, M. M., McBryant, S. J., Tsukamoto, T., Rojas, C. J., Ferraris, D. V., Hamilton, S. K., Hansen, J. C., & Curthoys, N. P. (2007) · Biochemical Journal · doi:10.1042/bj20070039 · Cited by 344 · see citing works
Alternative cell death mechanisms in development and beyondPreprint
Yuan, J., & Kroemer, G. (2010) · Genes & Development · doi:10.1101/gad.1984410 · Cited by 290 · see citing works
Nγ-Aryl glutamine analogues as probes of the ASCT2 neutral amino acid transporter binding site
Esslinger, C. S., Cybulski, K. A., & Rhoderick, J. F. (2004) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2004.11.028 · Cited by 151 · see citing works
Central role for aldose reductase pathway in myocardial ischemic injury
Hwang, Y. C., Kaneko, M., Bakr, S. A., Liao, H., Lu, Y., Lewis, E., Yan, S.-D., Ii, S., Itakura, M., Liu, R., et al. (2004) · The FASEB Journal · doi:10.1096/fj.03-1400com · Cited by 129 · see citing works
Self-citationThe transport of glutamine into mammalian cells
John, D. M. (2006) · Frontiers in bioscience · doi:10.2741/2109 · Cited by 128 · see citing works
Glutathione synthetase deficiency
NJÅLSSON, R. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5163-7 · Cited by 92 · see citing works
Blum, E. S., Abraham, M. C., Yoshimura, S., Lu, Y., & Shaham, S. (2012) · Science · doi:10.1126/science.1215156 · Cited by 70 · see citing works
The Molecular Basis of a Case of γ-Glutamylcysteine Synthetase Deficiency
Beutler, E., Gelbart, T., Kondo, T., & Matsunaga, A. T. (1999) · Blood · doi:10.1182/blood.v94.8.2890.420k16_2890_2894 · Cited by 63 · see citing works
Ristoff, E., Augustson, C., Geissler, J., de Rijk, T., Carlsson, K., Luo, J., Andersson, K., Weening, R. S., van Zwieten, R., Larsson, A., et al. (2000) · PubMed · Cited by 49 · see citing works
Ananthakrishnan, R., Kaneko, M., Hwang, Y. C., Quadri, N., Gomez, T., Li, Q., Caspersen, C. S., & Ramasamy, R. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01012.2008 · Cited by 47 · see citing works
Self-citationHirono, A., IYORI, H., Sekine, I., et al. (1996) · Blood · doi:10.1182/blood.v87.5.2071.2071 · Cited by 40 · see citing works
Pereira, M. M., Gelbart, T., Ristoff, E., Crain, K., Bergua, J., Lafuente, A. L., Kalko, S. G., Mateos, E., Beutler, E., & Corrons, J. V. (2007) · Haematologica · doi:10.3324/haematol.11238 · Cited by 19 · see citing works
Developmental changes in plasma transferrin concentrations related to red cell ferritin.
Valaitis, A. P., & Theil, E. C. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43525-3 · Cited by 7 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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-citationGalluzzi, 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 · see citing works
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
Ferroptosis: process and function
Xie, Y., Hou, W., Song, X., Yu, Y., Huang, J., Sun, X., Kang, R., & Tang, D. (2016) · Cell Death & Differentiation · doi:10.1038/cdd.2015.158 · Cited by 3,727 · see citing works
Ferroptosis: Death by Lipid Peroxidation
Yang, W. S., & Stockwell, B. R. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.10.014 · Cited by 3,088 · 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
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 · see citing works
Self-citationRole of GPX4 in ferroptosis and its pharmacological implication
Seibt, T. M., Proneth, B., & Conrad, M. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.014 · Cited by 1,520 · see citing works
Cao, J. Y., & Dixon, S. J. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2194-1 · Cited by 1,515 · 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
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 · see citing works
Self-citationTargeting mutant p53 for efficient cancer therapy
Bykov, V. J. N., Eriksson, S. E., Bianchi, J., & Wiman, K. G. (2018) · Nature Reviews Cancer · doi:10.1038/nrc.2017.109 · Cited by 889 · see citing works
Ferroptosis: Role of lipid peroxidation, iron and ferritinophagy
Latunde-Dada, G. O. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.05.019 · Cited by 892 · 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
RSL3 Drives Ferroptosis Through GPX4 Inactivation and ROS Production in Colorectal Cancer
Sui, X., Zhang, R., Liu, S., Duan, T., Zhai, L., Zhang, M., Han, X., Xiang, Y., Huang, X., Lin, H., et al. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01371 · Cited by 703 · see citing works
Kim, S. E., Zhang, L., Ma, K., Riegman, M., Chen, F., Ingold, I., Conrad, M., Turker, M. Z., Gao, M., Jiang, X., et al. (2016) · Nature Nanotechnology · doi:10.1038/nnano.2016.164 · Cited by 622 · see citing works
Self-citationRegulated necrosis: disease relevance and therapeutic opportunities
Conrad, M., Angeli, J. P. F., Vandenabeele, P., & Stockwell, B. R. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2015.6 · Cited by 630 · see citing works
HSPA5 Regulates Ferroptotic Cell Death in Cancer Cells
Zhu, S., Zhang, Q., Sun, X., Zeh, H. J., Lotze, M. T., Kang, R., & Tang, D. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-1979 · Cited by 576 · see citing works
Ferroptosis Inhibition: Mechanisms and Opportunities
Angeli, J. P. F., Shah, R., Pratt, D. A., & Conrad, M. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.02.005 · Cited by 563 · 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
Iron and cancer: recent insights
Manz, D. H., Blanchette, N. L., Paul, B. T., Torti, F. M., & Torti, S. V. (2016) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.13008 · Cited by 507 · see citing works
Regulation of lipid peroxidation and ferroptosis in diverse species
Conrad, M., Kagan, V. E., Bayir, H., Pagnussat, G. C., Head, B., Traber, M. G., & Stockwell, B. R. (2018) · Genes & Development · doi:10.1101/gad.314674.118 · Cited by 544 · see citing works
Glutaminolysis as a target for cancer therapy
Jin, L., Alesi, G. N., & Kang, S. (2016) · Oncogene · doi:10.1038/onc.2015.447 · Cited by 459 · see citing works
Masaldan, S., Clatworthy, S. A. S., Gamell, C., Meggyesy, P. M., Rigopoulos, A.-T., Haupt, S., Haupt, Y., Denoyer, D., Adlard, P. A., Bush, A. I., et al. (2018) · Redox Biology · doi:10.1016/j.redox.2017.08.015 · Cited by 452 · see citing works
The Role of Ferroptosis in Cancer Development and Treatment Response
Lu, B., Chen, X. B., Ying, M. D., He, Q. J., Cao, J., & Yang, B. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00992 · Cited by 444 · see citing works
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 · 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
Self-citationLipid 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
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 · see citing works
Dixon, S. J. (2017) · Immunological Reviews · doi:10.1111/imr.12533 · Cited by 314 · 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
“In the non-canonical pathway, increased iron uptake by transferrin receptor (TFRC) and reduced iron export by ferroportin promote oxidative damage and ferroptosis [60, 61].”
BackgroundEntosis Is Induced by Glucose Starvation
Hamann, J. C., Surcel, A., Chen, R., Teragawa, C., Albeck, J. G., Robinson, D. N., & Overholtzer, M. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.06.037 · Cited by 203 · see citing works
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 · see citing works
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 · see citing works
p53 as a hub in cellular redox regulation and therapeutic target in cancer
Eriksson, S. E., Ceder, S., Bykov, V. J. N., & Wiman, K. G. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz005 · Cited by 123 · see citing works
CREB 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
Wei, X.-B., Jiang, W.-Q., Zeng, J.-H., Huang, L.-Q., Ding, H.-G., Jing, Y.-W., Han, Y.-L., Li, Y.-C., & Chen, S.-L. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02738-1 · Cited by 123 · see citing works
Toyokuni, S. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.401 · Cited by 102 · see citing works
Signalome-wide RNAi screen identifies GBA1 as a positive mediator of autophagic cell death
Dasari, S. K., Bialik, S., Levin-Zaidman, S., Levin-Salomon, V., Merrill, A. H., Futerman, A. H., & Kimchi, A. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.80 · Cited by 95 · see citing works
Liver stage malaria infection is controlled by host regulators of lipid peroxidation
Kain, H. S., Glennon, E. K. K., Vijayan, K., Arang, N., Douglass, A. N., Fortin, C. L., Zuck, M., Lewis, A. J., Whiteside, S. L., Dudgeon, D. R., et al. (2020) · Cell Death & Differentiation · doi:10.1038/s41418-019-0338-1 · Cited by 91 · see citing works
An Overview of Pathways of Regulated Necrosis in Acute Kidney Injury
Kers, J., Leemans, J. C., & Linkermann, A. (2016) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2016.03.002 · Cited by 80 · see citing works
Metabolism and iron signaling in ferroptotic cell death
Gao, M., Monian, P., & Jiang, X. (2015) · Oncotarget · doi:10.18632/oncotarget.5671 · Cited by 71 · see citing works
Self-citationDeciphering the acetylation code of p53 in transcription regulation and tumor suppression
Xia, Z., Kon, N., Gu, A. P., Tavana, O., & Gu, W. (2022) · Oncogene · doi:10.1038/s41388-022-02331-9 · Cited by 60 · see citing works
Leu, J. I.-J., Murphy, M. E., & George, D. L. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2009943117 · Cited by 47 · see citing works
Sun, G. G., Wang, C., Mazzarino, R. C., Perez-Corredor, P. A., Davtyan, H., Blurton-Jones, M., Lopera, F., Arboleda-Velasquez, J. F., & Shi, Y. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114982 · Cited by 36 · see citing works
Shining a light on metabolic vulnerabilities in non-small cell lung cancer
Dowling, C. M., Zhang, H., Chonghaile, T. N., & Wong, K.-K. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2020.188462 · Cited by 26 · see citing works
- Authors
- Gao, M., Monian, P., Quadri, N., Ramasamy, R., & Jiang, X.
- Affiliations
- Memorial Sloan Kettering Cancer Center (US)
- NYU Langone Health (US)
- Corresponding author
- Jiang, Xuejun
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2015-07
- Volume
- 59
- Issue
- 2
- Pages
- 298-308
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC4506736
- OpenAlex
- W1589007430
- Cited by
- 2,069
- References
- 48
- Citations by year
- 2026: 199 · 2025: 297 · 2024: 317 · 2023: 311 · 2022: 314 · 2021: 237 · 2020: 151 · 2019: 103 · 2018: 63 · 2017: 43 · 2016: 24 · 2015: 6 · 2014: 1
- FWCI
- 35.91
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (P01AG026467)
- National Heart, Lung, and Blood Institute (R01HL102022, P01HL060901, P01-HL60901)
- National Cancer Institute (R01CA166413, P30CA008748)
- National Institute of General Medical Sciences (R01GM113013)
- Topics
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Ferroptosis and cancer prognosis
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- ferroptosis, glutaminolysis, transferrin, transferrin receptor, glutamine, amino acid starvation, nutrient deprivation, iron metabolism, redox regulation, cellular metabolism, regulated necrosis
- MeSH terms
- Animals, Cells, Cultured, Culture Media, Cystine, Glutamine, Glutathione, Humans, Iron, Male, Mice, Inbred C57BL, Necrosis, Oxidation-Reduction, Receptors, Transferrin, Transferrin, Myocardial Reperfusion Injury, Cell Death, Apoptosis, Mice, Receptor-Interacting Protein Serine-Threonine Kinases, Metabolic Networks and Pathways
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