The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Glutathione Peroxidase 4 Senses and Translates Oxidative Stress into 12/15-Lipoxygenase Dependent- and AIF-Mediated Cell Death
Open accessAbstract
Oxidative stress in conjunction with glutathione depletion has been linked with various acute and chronic degenerative disorders, yet the molecular mechanisms have remained unclear. In contrast to the belief that oxygen radicals are detrimental to cells and tissues by unspecific oxidation of essential biomolecules, we now demonstrate that oxidative stress is sensed and transduced by glutathione peroxidase 4 (GPx4) into a-yet-unrecognized cell-death pathway. Inducible GPx4 inactivation in mice and cells revealed 12/15-lipoxygenase-derived lipid peroxidation as specific downstream event, triggering apoptosis-inducing factor (AIF)-mediated cell death. Cell death could be entirely prevented either by alpha-tocopherol (alpha-Toc), 12/15-lipoxygenase inhibitors, or siRNA-mediated AIF silencing. Accordingly, 12/15-lipoxygenase-deficient cells were highly resistant to glutathione depletion. Neuron-specific GPx4 depletion caused neurodegeneration in vivo and ex vivo, highlighting the importance of this pathway in neuronal cells. Since oxidative stress is common in the etiology of many human disorders, the identified pathway reveals promising targets for future therapies.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“the reduced glutathione (GSH)-dependent enzyme glutathione peroxidase 4 (GPX4)—which is directly targeted by RSL3—has emerged as the main endogenous inhibitor of ferroptosis by virtue of its ability to limit lipid peroxidation by catalyzing the GSH-dependent reduction of lipid hydroperoxides to lipid alcohols [547–550].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [550]
In the citing paper
“Gpx4−/− mice display embryonic lethality with complete penetrance [547, 550, 587, 588].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [550]
In the citing paper
“In the context of ferroptosis, PUFA peroxidation seems to be mainly regulated by the mutually antagonistic activity of LOXs (which directly catalyze lipid peroxidation) and GPX4 (which indirectly inhibits it) [550, 566].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [550]
In the citing paper
“the inducible or tissue-specific ablation of Gpx4 in mice provokes a variety of pathological conditions, including acute renal or hepatic injury [547, 563, 589], neurodegeneration [550, 590, 591], and defective immunity to infection [567], all of which can be prevented or mitigated by ferroptosis-inhibiting strategies.”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [550]
In the citing paper
“An inducible Gpx4 knockout mouse model demonstrated that some cells and tissues, particularly neurons in the brain, accumulate lethal lipid ROS that can be alleviated by vitamin E treatment [44], highlighting the lethal nature of lipid peroxidation in vivo in the absence of Gpx4.”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [44]
In the citing paper
“GPx-4 is expressed as multiple isoforms generated from the same gene: one of these targets the mitochondria where it has a vital role in protecting against membrane lipid peroxidation; in its absence, mitochondria accumulate damaging lipid peroxides, leading to apoptogen release (253, 383).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [383]
In the citing paper
“Recent findings, however, suggest that GPx-4 primarily targets oxidized membrane phospholipids (383).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [383]
In the citing paper
“Interestingly, a deficiency of GPx-4 appears to potentiate 12/15-lipoxygenase-mediated lipid peroxidation to increase cell death via the release of AIF, an apoptogen from mitochondria (383).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [383]
In the citing paper
“The role of lipid peroxides in promoting apoptosis was proven by the finding that the lipid-soluble α-tocopherol could prevent apoptosis, whereas N-acetyl Cys or other water-soluble antioxidants could not block cell death in GPx-4-deficient cells (383).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [383]
In the citing paper
“and studies show that deficiency of GPx-4 promotes cellular apoptosis via the accumulation of lipid peroxidation in the absence of exogenous oxidants or stimuli (383).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [383]
Citations
Cites
Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases
Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455
[12] Assays of glutathione peroxidase
Flohé, L., & Günzler, W. A. (1984) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(84)05015-1 · Cited by 4,954
Molecular characterization of mitochondrial apoptosis-inducing factor
Susin, S. A., Lorenzo, H. K., Zamzami, N., Marzo, I., Snow, B. E., Brothers, G. M., Mangion, J., Jacotot, E., Costantini, P., Loeffler, M., et al. (1999) · Nature · doi:10.1038/17135 · Cited by 4,060
Bcl-2 functions in an antioxidant pathway to prevent apoptosis
Hockenbery, D. M., Oltvai, Z. N., Yin, X., Milliman, C. L., & Korsmeyer, S. J. (1993) · Cell · doi:10.1016/0092-8674(93)80066-n · Cited by 3,402
Brewer, G. J., Torricelli, J. R., Evege, E. K., & Price, P. J. (1993) · Journal of Neuroscience Research · doi:10.1002/jnr.490350513 · Cited by 2,325
Schwenk, F., Baron, U., & Rajewsky, K. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.24.5080 · Cited by 1,289
Ursini, F., Maiorino, M., Valente, M., Ferri, L., & Gregolin, C. (1982) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(82)90150-3 · Cited by 884
Mitochondrial Dysfunction in Atherosclerosis
Madamanchi, N. R., & Runge, M. S. (2007) · Circulation Research · doi:10.1161/01.res.0000258450.44413.96 · Cited by 802
Yant, L. J., Ran, Q., Rao, L., Van Remmen, H., Shibatani, T., Belter, J. G., Motta, L., Richardson, A., & Prolla, T. A. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01360-6 · Cited by 797
A role for 12-lipoxygenase in nerve cell death caused by glutathione depletion.
Li, Y., Maher, P., & Schubert, D. (1997) · Neuron · doi:10.1016/s0896-6273(00)80953-8 · Cited by 509
Flagged first, then by citations
Cited by
Sorted by citations
Items 501–600 of 1,000
Dietary selenium and selenoprotein function
Weeks, B. S., Hanna, M. S., & Cooperstein, D. (2012) · Medical Science Monitor · doi:10.12659/msm.883258 · Cited by 66
Yang, M., Luo, H., Yi, X., Wei, X., & Jiang, D. (2023) · MedComm · doi:10.1002/mco2.267 · Cited by 69
Metal Ion Signaling in Biomedicine
Rodriguez, R., Müller, S., Colombeau, L., Solier, S., Sindikubwabo, F., & Cañeque, T. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00577 · Cited by 67
Cardiolipin Signaling Mechanisms: Collapse of Asymmetry and Oxidation
Kagan, V. E., Tyurina, Y. Y., Tyurin, V. A., Mohammadyani, D., Angeli, J. P. F., Баранов, В. С., Klein‐Seetharaman, J., Friedlander, R. M., Mallampalli, R. K., Conrad, M., et al. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6219 · Cited by 65
Self-citationTetrahydrobiopterin in Cell Function and Death Mechanisms
Vasquez-Vivar, J. M., Shi, Z., & Tan, S. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0136 · Cited by 66
Yu, S., Li, Z., Zhang, Q., Wang, R., Zhao, Z., Ding, W., Wang, F., Sun, C., Tang, J., Wang, X., et al. (2022) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2022.113413 · Cited by 64
Iron metabolism mediates microglia susceptibility in ferroptosis
Jiao, L., Li, X., Luo, Y., Wei, J., Ding, X., Xiong, H., Liu, X., & Lei, P. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.995084 · Cited by 68
Antioxidant Systems as Modulators of Ferroptosis: Focus on Transcription Factors
Punziano, C., Trombetti, S., Cesaro, E., Grosso, M., & Faraonio, R. (2024) · Antioxidants · doi:10.3390/antiox13030298 · Cited by 75
Bosello-Travain, V., Conrad, M., Cozza, G., Negro, A., Quartesan, S., Rossetto, M., Roveri, A., Toppo, S., Ursini, F., Zaccarin, M., et al. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.02.017 · Cited by 61
Self-citationKoeberle, S. C., Gollowitzer, A., Laoukili, J., Kranenburg, O., Werz, O., Koeberle, A., & Kipp, A. P. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101388 · Cited by 64
Genes Regulating Spermatogenesis and Sperm Function Associated With Rare Disorders
Linn, E., Ghanem, L., Bhakta, H., Greer, C., & Avella, M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.634536 · Cited by 61
Yuk, H., Abdullah, M., Kim, D.-H., Lee, H., & Lee, S. J. (2021) · Antioxidants · doi:10.3390/antiox10091347 · Cited by 65
Molecular Mechanisms of Ferroptosis and Its Roles in Hematologic Malignancies
Zhao, Y., Huang, Z., & Peng, H. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.743006 · Cited by 62
Tanguy, Y., Falluel‐Morel, A., Arthaud, S., Boukhzar, L., Manecka, D.-L., Chagraoui, A., Prévost, G., Élias, S., Dorval, I., Lésage, J., et al. (2011) · Endocrinology · doi:10.1210/en.2011-1246 · Cited by 63
Selenoprotein biosynthesis defect causes progressive encephalopathy with elevated lactate
Anttonen, A.-K., Hilander, T., Linnankivi, T., Isohanni, P., French, R. L., Liu, Y., Simonović, M., Söll, D. G., Somer, M., Muth‐Pawlak, D., et al. (2015) · Neurology · doi:10.1212/wnl.0000000000001787 · Cited by 64
Iron Pathophysiology in Alzheimer’s Diseases
Wang, T., Xu, S.-F., Fan, Y.-G., Li, L.-B., & Guo, C. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-9589-5_5 · Cited by 64
Cell Death and Exosomes Regulation After Myocardial Infarction and Ischemia-Reperfusion
Wu, X., Iroegbu, C. D., Peng, J., Guo, J., Yang, J., & Fan, C. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.673677 · Cited by 64
Piattini, F., Matsushita, M., Muri, J., Bretscher, P., Feng, X., Freigang, S., Dalli, J., Schneider, C., & Köpf, M. (2021) · European Journal of Immunology · doi:10.1002/eji.202049114 · Cited by 64
Wang, M., Tang, G., Zhou, C., Guo, H., Hu, Z., Hu, Q., & Li, G. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110387 · Cited by 62
Li, D., Lu, X., Xu, G., Liu, S., Gong, Z., Lu, F., Xia, X., Jiang, J., Wang, H., Zou, F., et al. (2023) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14150 · Cited by 65
Reactive oxygen species regulation by AIF- and complex I-depleted brain mitochondria
Chinta, S. J., Rane, A., Yadava, N., Andersen, J. K., Nicholls, D. G., & Polster, B. M. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.01.010 · Cited by 64
Ferroptosis in plants: triggers, proposed mechanisms, and the role of iron in modulating cell death
Distéfano, A. M., López, G. A., Setzes, N., Marchetti, F., Cainzos, M., Cascallares, M. M., Zabaleta, E. J., & Pagnussat, G. C. (2020) · Journal of Experimental Botany · doi:10.1093/jxb/eraa425 · Cited by 63
Recent progress on nanomedicine-induced ferroptosis for cancer therapy
Zafar, H., Raza, F., Ma, S., Wei, Y., Zhang, J., & Shen, Q. (2021) · Biomaterials Science · doi:10.1039/d1bm00721a · Cited by 63
Molecular characterization of AIFM2/FSP1 inhibition by iFSP1-like molecules
da Silva, T. N. X., Schulte, C., Nunes‐Alves, A., Maric, H. M., & Angeli, J. P. F. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05787-z · Cited by 61
Protein modification and degradation in ferroptosis
Wang, Y., Ding, Y., Liu, J., Tang, D., & Chen, X. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103259 · Cited by 64
Reactive oxygen species in the pathogenesis of sarcopenia
Xu, H., Brown, J. L., Bhaskaran, S., & Van Remmen, H. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.11.046 · Cited by 61
Mechanisms of ferroptosis sensitization and resistance
Lee, W. C., & Dixon, S. J. (2025) · Developmental Cell · doi:10.1016/j.devcel.2025.02.004 · Cited by 61
Karlupia, N., Manley, N. C., Prasad, K., Schäfer, R., & Steinberg, G. K. (2014) · Stem Cell Research & Therapy · doi:10.1186/scrt434 · Cited by 61
Zhao, J., Wu, Y., Liang, S., & Piao, H. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.01.017 · Cited by 59
Schwarz, M., Löser, A., Cheng, Q., Wichmann-Costaganna, M., Schädel, P., Werz, O., Arnér, E. S. J., & Kipp, A. P. (2023) · Redox Biology · doi:10.1016/j.redox.2022.102593 · Cited by 60
Wang, Y.-H., Chang, D., Zhao, M., & Chen, M. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0169 · Cited by 64
Effects of DNA, RNA, and Protein Methylation on the Regulation of Ferroptosis
Wang, X., Kong, X., Feng, X., & Jiang, D. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.85454 · Cited by 62
Negative modulation of mitochondrial calcium uniporter complex protects neurons against ferroptosis
Marmolejo-Garza, A., Krabbendam, I. E., Luu, M. D. A., Brouwer, F., Trombetta-Lima, M., Unal, O., O’Connor, S. J., Majerníková, N., Elzinga, C. R. S., Mammucari, C., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06290-1 · Cited by 61
Volpe, J. J., Kinney, H. C., Jensen, F. E., & Rosenberg, P. A. (2011) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2011.07.008 · Cited by 59
Thiol switches in mitochondria: operation and physiological relevance
Riemer, J., Schwarzländer, M., Conrad, M., & Herrmann, J. M. (2015) · Biological Chemistry · doi:10.1515/hsz-2014-0293 · Cited by 58
Self-citationZhao, X., Gao, M., Liang, J., Chen, Y., Wang, Y., Wang, Y., Xiao, Y., Zhao, Z., Wan, X., Jiang, M., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.639851 · Cited by 60
Peng, C., Fu, X., Wang, K., Chen, L., Luo, B., Huang, N., Luo, Y., & Chen, W. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174461 · Cited by 59
Wu, X., Jin, S., Yang, Y., Lu, X., Dai, X., Xu, Z., Zhang, C., & Xiang, L. F. (2022) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.13032 · Cited by 59
Molybdenum Cofactor Deficiency in Humans
Johannes, L., Fu, C.-Y., & Schwarz, G. (2022) · Molecules · doi:10.3390/molecules27206896 · Cited by 59
Ren, X., Santhosh, S. M., Coppo, L., Ogata, F. T., Lu, J., & Holmgren, A. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.01.037 · Cited by 59
Nitric oxide protects against ferroptosis by aborting the lipid peroxidation chain reaction
Homma, T., Kobayashi, S., Conrad, M., Konno, H., Yokoyama, C., & Fujii, J. (2021) · Nitric Oxide · doi:10.1016/j.niox.2021.07.003 · Cited by 59
Self-citationGSK-3β manipulates ferroptosis sensitivity by dominating iron homeostasis
Wang, L., Ouyang, S., Li, B., Wu, H., & Wang, F. (2021) · Cell Death Discovery · doi:10.1038/s41420-021-00726-3 · Cited by 60
Ferroptosis: The Entanglement between Traditional Drugs and Nanodrugs in Tumor Therapy
Liu, K., Huang, L., Qi, S., Liu, S., Xie, W., Du, L., Jing, C., Zhang, X., Zhang, B., Liu, L., et al. (2023) · Advanced Healthcare Materials · doi:10.1002/adhm.202203085 · Cited by 59
Ichihara, G., Katsumata, Y., Sugiura, Y., Matsuoka, Y., Maeda, R., Endo, J., Anzai, A., Shirakawa, K., Moriyama, H., Kitakata, H., et al. (2023) · Circulation Research · doi:10.1161/circresaha.123.323517 · Cited by 63
Cytosolic cytochrome c represses ferroptosis
Song, X., Zhou, Z., Liu, J., Li, J., Yu, C., Zeh, H. J., Klionsky, D. J., Stockwell, B. R., Wang, J., Kang, R., et al. (2025) · Cell Metabolism · doi:10.1016/j.cmet.2025.03.014 · Cited by 61
Lippmann, J., Petri, K., Fulda, S., & Liese, J. (2020) · Translational Oncology · doi:10.1016/j.tranon.2020.100785 · Cited by 58
Schriever, S. C., Zimprich, A., Pfuhlmann, K., Baumann, P., Giesert, F., Klaus, V., Kabra, D. G., Hafen, U., Romanov, A., Tschöp, M. H., et al. (2017) · Neuroscience · doi:10.1016/j.neuroscience.2017.05.050 · Cited by 58
Self-citationC-ferroptosis is an iron-dependent form of regulated cell death in cyanobacteria
Aguilera, A., Berdun, F., Bartoli, C. G., Steelheart, C., Alegre, M. L., Bayır, H., Tyurina, Y. Y., Kagan, V. E., Salerno, G. L., Pagnussat, G. C., et al. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.201911005 · Cited by 58
Ferroptosis in tumor immunity and therapy
Gong, C., Ji, Q., Wu, M., Tu, Z., Lei, K., Luo, M., Liu, J., Lin, L., Li, K., Li, J., et al. (2022) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17529 · Cited by 56
Biological and Catalytic Properties of Selenoproteins
Chaudière, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241210109 · Cited by 64
Selenium in the Redox Regulation of the Nrf2 and the Wnt Pathway
Brigelius‐Flohé, R., & Kipp, A. P. (2013) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-405882-8.00004-0 · Cited by 58
Control of Redox State and Redox Signaling by Neural Antioxidant Systems
Lewerenz, J., & Maher, P. A. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3600 · Cited by 57
Disorders of selenium metabolism and selenoprotein function
Schweizer, U., Dehina, N., & Schomburg, L. (2011) · Current Opinion in Pediatrics · doi:10.1097/mop.0b013e32834877da · Cited by 56
Self-citationFerroptosis Is Regulated by Mitochondria in Neurodegenerative Diseases
Zhou, J.-P., Jin, Y., Lei, Y.-H., Liu, T., Wan, Z., Meng, H., & Wang, H. (2020) · Neurodegenerative Diseases · doi:10.1159/000510083 · Cited by 57
Neuroprotective Effects of Quercetin on Ischemic Stroke: A Literature Review
Zhang, L., Ma, J., Yang, F., Li, S., Ma, W., Chang, X., & Yang, L. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.854249 · Cited by 57
Selenoproteins in brain development and function
Schweizer, U., & Fabiano, M. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.07.022 · Cited by 58
Self-citationTyurina, Y. Y., Kapralov, A. A., Tyurin, V. A., Shurin, G. V., Amoscato, A. A., Rajasundaram, D., Tian, H., Bunimovich, Y. L., Nefedova, Y., Herrick, W. G., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102650 · Cited by 60
Liu, L., Zhang, Y., Wang, L., Liu, Y., Chen, H., Hu, Q., Xie, C., Meng, X., & Shen, X. (2023) · Phytotherapy Research · doi:10.1002/ptr.7928 · Cited by 56
Singlet Oxygen Plays an Essential Role in the Root’s Response to Osmotic Stress
Chen, T., & Fluhr, R. (2018) · PLANT PHYSIOLOGY · doi:10.1104/pp.18.00634 · Cited by 56
Carresi, C., Mollace, R., Macrì, R., Scicchitano, M., Bosco, F., Scarano, F., Coppoletta, A. R., Guarnieri, L., Ruga, S., Zito, M. C., et al. (2021) · Antioxidants · doi:10.3390/antiox10030387 · Cited by 58
Mechanisms and pharmacological applications of ferroptosis: a narrative review
Zhang, J., Du, J., Kong, N., Zhang, G., Liu, M., & Liu, C. (2021) · Annals of Translational Medicine · doi:10.21037/atm-21-1595 · Cited by 58
Ferroptosis: A Critical Moderator in the Life Cycle of Immune Cells
Wang, P., & Lu, Y. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.877634 · Cited by 57
Cahuzac, K. M., Lubin, A., Bosch, K. N., Stokes, N., Schoenfeld, S., Zhou, R. W., Lemon, H., Asara, J. M., & Parsons, R. E. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112536 · Cited by 57
Xu, Z., Zhang, M., Wang, W., Zhou, S., Yu, M., Qiu, X., Jiang, S., Wang, X., Tang, C., Li, S., et al. (2023) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2023.116595 · Cited by 59
Inflammation-induced epigenetic imprinting regulates intestinal stem cells
Zhao, D., Ravikumar, V., Leach, T. J., Kraushaar, D. C., Lauder, E., Li, L., Sun, Y., Oravecz-Wilson, K. I., Keller, E. T., Chen, F., et al. (2024) · Cell stem cell · doi:10.1016/j.stem.2024.08.006 · Cited by 58
Lymph node environment drives FSP1 targetability in metastasizing melanoma
Palma, M., Chaufan, M., Breuer, C. B., Müller, S., Sabatier, M., Fraser, C. S., Szylo, K. J., Yavari, M., Carmona, A., Kaur, M., et al. (2025) · Nature · doi:10.1038/s41586-025-09709-1 · Cited by 55
Self-citationCardoso, B. R., Hare, D. J., Lind, M., McLean, C., Volitakis, I., Laws, S. M., Masters, C. L., Bush, A. I., & Roberts, B. R. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00014 · Cited by 55
12/15 lipoxygenase: A crucial enzyme in diverse types of cell death
Li, Q.-Q., Li, Q., Jia, J.-N., Liu, Z., Zhou, H., & Mao, X. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2018.04.002 · Cited by 56
Antitumor Effect of 5-Aminolevulinic Acid Through Ferroptosis in Esophageal Squamous Cell Carcinoma
Shishido, Y., Amisaki, M., Matsumi, Y., Yakura, H., Nakayama, Y., Miyauchi, W., Miyatani, K., Matsunaga, T., Hanaki, T., Kihara, K., et al. (2020) · Annals of Surgical Oncology · doi:10.1245/s10434-020-09334-4 · Cited by 59
The role of ferroptosis in melanoma
Talty, R., & Bosenberg, M. (2021) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.13009 · Cited by 58
The fate of melanocyte: Mechanisms of cell death in vitiligo
Wu, X., Yang, Y., Xiang, L. F., & Zhang, C. (2020) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.12955 · Cited by 54
Cell Death via Lipid Peroxidation and Protein Aggregation Diseases
Iuchi, K., Takai, T., & Hisatomi, H. (2021) · Biology · doi:10.3390/biology10050399 · Cited by 56
Cui, Z., Wang, H., Li, S., Qin, T., Shi, H., Ma, J., Li, L., Yu, G., Jiang, T., & Li, C. (2021) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2021.09.008 · Cited by 57
Majerníková, N., den Dunnen, W. F. A., & Dolga, A. M. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.745046 · Cited by 56
Ferroptosis spreads to neighboring cells via plasma membrane contacts
Roeck, B. F., Nasudivar, S. L., Vorndran, M. R. H., Schueller, L., Yapici, F. I., Rübsam, M., von Karstedt, S., Niessen, C. M., & García‐Sáez, A. J. (2025) · Nature Communications · doi:10.1038/s41467-025-58175-w · Cited by 57
SK2 channels regulate mitochondrial respiration and mitochondrial Ca2+ uptake
Honrath, B., Matschke, L. A., Meyer, T., Magerhans, L., Perocchi, F., Ganjam, G. K., Zischka, H., Krasel, C., Gerding, A., Bakker, B. M., et al. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.2 · Cited by 54
Self-citationYagami, T., Yamamoto, Y., & Koma, H. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1277-4 · Cited by 56
Ferroptosis Contributes to Isoflurane Neurotoxicity
Xia, Y., Sun, X., Luo, Y., & Stary, C. M. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00486 · Cited by 54
Doxorubicin loaded ferritin nanoparticles for ferroptosis enhanced targeted killing of cancer cells
Yang, R., Li, Y., Wang, X., Yan, J., Pan, D., Xu, Y., Wang, L., & Yang, M. (2019) · RSC Advances · doi:10.1039/c9ra04478g · Cited by 57
Juggling with lipids, a game of Russian roulette
Aldrovandi, M., Fedorova, M., & Conrad, M. (2021) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2021.04.012 · Cited by 52
Self-citationTang, L., Liu, S., Li, S., Chen, Y., Xie, B., & Zhou, J. F. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241210127 · Cited by 57
Ferroptosis mechanism and Alzheimer's disease
Feng, L., Sun, J. J., Xia, L., Shi, Q., Hou, Y., Zhang, L., Li, M., Fan, C., & Sun, B. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.389362 · Cited by 56
Progress of Ferroptosis in Ischemic Stroke and Therapeutic Targets
Tian, X., Li, X., Pan, M., Yang, L. Z., Li, Y., & Fang, W. (2024) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-024-01457-6 · Cited by 59
Peleman, C., Hellemans, S., Veeckmans, G., Arras, W., Zheng, H., Koeken, I., San, E. V., Hassannia, B., Walravens, M., Kayirangwa, E., et al. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01348-9 · Cited by 60
Latchoumycandane, C., Marathe, G. K., Zhang, R., & McIntyre, T. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.300012 · Cited by 53
Ferroptosis increases obesity: Crosstalk between adipocytes and the neuroimmune system
Zhang, S., Sun, Z., Jiang, X. Y., Lu, Z., Ding, L., Li, C., Tian, X., & Wang, Q. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1049936 · Cited by 56
Ferroptosis-mediated immune responses in cancer
Qi, D., & Peng, M. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1188365 · Cited by 53
Bortoli, M., Wolters, L. P., Orian, L., & Bickelhaupt, F. M. (2016) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.6b00253 · Cited by 52
Yan, J., Zeng, Y., Guan, Z., Li, Z., Luo, S., Niu, J., Zhao, J., Gong, H., Huang, T., Li, Z., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114636 · Cited by 54
N-acetyl-l-cysteine averts ferroptosis by fostering glutathione peroxidase 4
Zheng, J., Zhang, W., Ito, J., Henkelmann, B., Xu, C., Mishima, E., & Conrad, M. (2025) · Cell chemical biology · doi:10.1016/j.chembiol.2025.04.002 · Cited by 58
Self-citationA fin-loop-like structure in GPX4 underlies neuroprotection from ferroptosis
Lorenz, S., Wahida, A., Bostock, M. J., Seibt, T., Mourão, A., Levkina, A., Trümbach, D., Soudy, M., Emler, D., Rothammer, N., et al. (2025) · Cell · doi:10.1016/j.cell.2025.11.014 · Cited by 61
Self-citationMohammedi, K., Patente, T. A., Bellili-Muñoz, N., Driss, F., Nagard, H. L., Fumeron, F., Roussel, R., Hadjadj, S., Corrêa‐Giannella, M. L., Marre, M., et al. (2015) · Metabolism · doi:10.1016/j.metabol.2015.10.004 · Cited by 51
Barayuga, S. M., Pang, X., Andres, M. A., Panee, J., & Bellinger, F. P. (2013) · NeuroToxicology · doi:10.1016/j.neuro.2013.05.009 · Cited by 51
Seeher, S., Carlson, B. A., Miniard, A. C., Wirth, E. K., Mahdi, Y., Hatfield, D. L., Driscoll, D. M., & Schweizer, U. (2014) · Biochemical Journal · doi:10.1042/bj20140423 · Cited by 53
Self-citationHe, W. D., Elkhooly, T. A., Liu, X., Cavallaro, A., Taheri, S., Vasilev, K. A., & Feng, Q. (2016) · Journal of Materials Chemistry B · doi:10.1039/c5tb02482j · Cited by 51
Unveiling the Molecular Mechanisms Behind Selenium-Related Diseases Through Knockout Mouse Studies
Conrad, M., & Schweizer, U. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2912 · Cited by 51
Self-citationChiang, S., Kalinowski, D. S., Jansson, P. J., Richardson, D. R., & Huang, M. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.08.002 · Cited by 48
Ferroptosis: A Promising Therapeutic Target for Neonatal Hypoxic-Ischemic Brain Injury
Peeples, E. S., & Genaro‐Mattos, T. C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137420 · Cited by 51
HOIP modulates the stability of GPx4 by linear ubiquitination
Dong, K., Wei, R., Jin, T., Zhang, M., Shen, J., Xiang, H., Shan, B., Yuan, J., & Li, Y. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2214227119 · Cited by 52
Lv, Y., Chen, D., Tian, X., Xiao, J., Xu, C., Du, L., Li, J., Zhou, S., Chen, Y., Zhuang, R., et al. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04111-9 · Cited by 52
Metadata
- Authors
- Seiler, A., Schneider, M., Förster, H., Roth, S., Wirth, E. K., Culmsee, C., Plesnila, N., Kremmer, E., Rådmark, O., Wurst, W., Bornkamm, G. W., Schweizer, U., & Conrad, M.
- Affiliations
- Helmholtz Munich (DE)
- Charité – Universitätsmedizin Berlin (DE)
- Philipps University of Marburg (DE)
- Ludwig-Maximilians-Universität München (DE)
- Karolinska Institutet (SE)
- Corresponding author
- Conrad, Marcus
- ORCID
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2008-09
- Volume
- 8
- Issue
- 3
- Pages
- 237-248
- ISSN
- 1550-4131 (ISSN-L)
- OpenAlex
- W2007794772
- Cited by
- 1,470
- References
- 33
- Citations by year
- 2026: 121 · 2025: 157 · 2024: 175 · 2023: 169 · 2022: 140 · 2021: 131 · 2020: 103 · 2019: 70 · 2018: 65 · 2017: 48 · 2016: 40 · 2015: 32 · 2014: 37 · 2013: 27 · 2012: 31
- FWCI
- 16.89
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Site cant be reached (submittedVersion)
- Funders
- Bundesministerium für Bildung und Forschung (01GN0512, 01GR0430, 01GS0476)
- Verband der Chemischen Industrie
- Boehringer Ingelheim (DFG SFB596, DFG SFB665, Ko922/11-1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Keywords
- GPX4, oxidative stress sensing, 12/15-lipoxygenase, apoptosis-inducing factor, lipid peroxidation, glutathione depletion, alpha-tocopherol, neurodegeneration, neuronal cell death, cell death signaling
- MeSH terms
- Phospholipid Hydroperoxide Glutathione Peroxidase, Alleles, Animals, Arachidonate 12-Lipoxygenase, Arachidonate 15-Lipoxygenase, Cells, Cultured, Fluorenes, Genotype, Glutathione Peroxidase, Hippocampus, Humans, Mice, Inbred C57BL, Neurons, Lipid Peroxidation, Cell Death, Mice, Knockout, Oxidative Stress, Reverse Transcriptase Polymerase Chain Reaction, Mice, Congenic, alpha-Tocopherol, RNA, Small Interfering, Apoptosis Inducing Factor, Mice
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