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
Cited by
Sorted by citations
Items 701–800 of 1,000
Ashoub, M. H., Razavi, R., Heydaryan, K., Salavati‐Niasari, M., & Amiri, M. (2024) · European journal of medical research · doi:10.1186/s40001-024-01822-7 · Cited by 37
Chen, Y.-L., Lee, D., Kwan, K., Wu, M., Wang, G., Zhang, M. S., Deng, H., Cheu, J. W., Lau, M. M. Y., Chan, C., et al. (2025) · Journal of Hepatology · doi:10.1016/j.jhep.2025.06.034 · Cited by 42
NATURAL ANTIOXIDANTS AS DEFENSE SYSTEM AGAINST CANCER
Chahal, A., Saini, A. K., Chhillar, A. K., & Saini, R. V. (2018) · Asian Journal of Pharmaceutical and Clinical Research · doi:10.22159/ajpcr.2018.v11i5.24119 · Cited by 36
APD-Containing Cyclolipodepsipeptides Target Mitochondrial Function in Hypoxic Cancer Cells
Jacobsen, K. M., Villadsen, N. L., Tørring, T., Nielsen, C. B., Salomón, T., Nielsen, M. M., Tsakos, M., Sibbersen, C., Scavenius, C., Nielsen, R., et al. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.07.010 · Cited by 36
HILAQ: A Novel Strategy for Newly Synthesized Protein Quantification
Ma, Y., McClatchy, D. B., Barkallah, S., Wood, W. W., & Yates, J. R. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00005 · Cited by 36
Rroji, O., Kumar, A., Karuppagounder, S. S., & Ratan, R. R. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105145 · Cited by 36
Ferroptosis Is a Potential Novel Diagnostic and Therapeutic Target for Patients With Cardiomyopathy
Zhai, Z., Zou, P., Liu, F., Xia, Z., & Li, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.649045 · Cited by 38
Emerging roles of ferroptosis in infectious diseases
Bagayoko, S., & Meunier, É. (2021) · FEBS Journal · doi:10.1111/febs.16244 · Cited by 36
Ferroptosis Involvement in Glioblastoma Treatment
Mitre, A. O., Florian, I. A., Buruiană, A., Boer, A., Moldovan, I. M., Şoriţău, O., Florian, I. Ş., & Șușman, S. (2022) · Medicina · doi:10.3390/medicina58020319 · Cited by 39
Role of Ferroptosis in Fibrotic Diseases
Zhou, J., Tan, Y., Wang, R., & Li, X. (2022) · Journal of Inflammation Research · doi:10.2147/jir.s358470 · Cited by 36
Selenoprotein P protects cells from lipid hydroperoxides generated by 15-LOX-1
Rock, C., & Moos, P. J. (2010) · Prostaglandins Leukotrienes and Essential Fatty Acids · doi:10.1016/j.plefa.2010.08.006 · Cited by 36
Grim, J. M., Hyndman, K. A., Kriska, T., Girotti, A. W., & Crockett, E. L. (2011) · Journal of Experimental Biology · doi:10.1242/jeb.058214 · Cited by 36
Epigenetic Regulation of Ferroptosis-Associated Genes and Its Implication in Cancer Therapy
Pei, Y.-Z., Qian, Y., Wang, H., & Tan, L. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.771870 · Cited by 35
Mitochondria-related signaling pathways involved in breast cancer regulate ferroptosis
Dong, X., Ye, L., Sheng, X., Zhou, W., Sun, A., & Dai, H. (2023) · Genes & Diseases · doi:10.1016/j.gendis.2023.03.019 · Cited by 38
Fefelova, N., Wongjaikam, S., Pamarthi, S. H., Siri‐Angkul, N., Comollo, T. W., Kumari, A., Garg, V., Ivessa, A., Chattipakorn, S. C., Chattipakorn, N., et al. (2023) · Basic Research in Cardiology · doi:10.1007/s00395-023-00990-7 · Cited by 35
A review on the relationship between Arachidonic acid 15-Lipoxygenase (ALOX15) and diabetes mellitus
He, K., Zhou, X., Du, H., Zhao, J., Deng, R., & Wang, J. (2023) · PeerJ · doi:10.7717/peerj.16239 · Cited by 39
Ferroptosis-like cell death promotes and prolongs inflammation in Drosophila
Davidson, A. J., Heron, R., Das, J., Overholtzer, M., & Wood, W. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01450-7 · Cited by 41
Conrad, M., Schick, J., & Angeli, J. P. F. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.01.010 · Cited by 35
Self-citationSakai, O., Yasuzawa, T., Yoshie, S., Ueta, T., Imai, H., Sawabe, A., & Ueshima, S. (2016) · Pathophysiology · doi:10.1016/j.pathophys.2016.11.002 · Cited by 35
Bromfield, E. G., Mihalas, B. P., Dun, M. D., Aitken, R. J., McLaughlin, E. A., Walters, J. L. H., & Nixon, B. (2017) · Biology of Reproduction · doi:10.1093/biolre/iox005 · Cited by 35
Bioactive metal-containing nanomaterials for ferroptotic cancer therapy
Fei, W., Zhang, Y., Ye, Y., Li, C., Yao, Y., Zhang, M., Li, F., & Zheng, C. (2020) · Journal of Materials Chemistry B · doi:10.1039/d0tb02138e · Cited by 35
Selenoproteins and Selenoproteomes
Gladyshev, V. N. (2011) · Springer eBooks · doi:10.1007/978-1-4614-1025-6_9 · Cited by 35
Iron nitroprusside as a chemodynamic agent and inducer of ferroptosis for ovarian cancer therapy
Asif, K., Adeel, M., Rahman, M. M., Caligiuri, I., Perin, T., Čemažar, M., Canzonieri, V., & Rizzolio, F. (2023) · Journal of Materials Chemistry B · doi:10.1039/d2tb02691k · Cited by 34
Ramakrishna, K., Karuturi, P., Siakabinga, Q., Viswanadh, M. K., Dumala, N., Guntupalli, C., Nalluri, B. N., Venkateswarlu, K., Prasanna, V. S., Gutti, G., et al. (2024) · Phytotherapy Research · doi:10.1002/ptr.8122 · Cited by 34
Analysis and identification of oxidative stress-ferroptosis related biomarkers in ischemic stroke
Zhang, L.-M., Liang, X.-L., Xiong, G.-F., Xing, X.-L., Zhang, Q., Zhang, B.-R., & Liu, M. (2024) · Scientific Reports · doi:10.1038/s41598-024-54555-2 · Cited by 35
Kuri, S., Billah, M. M., Rana, S. M. M., Naim, Z., Islam, M. M., Hasanuzzaman, M., Ali, M. R., & Banik, R. (2014) · Asian Pacific Journal of Tropical Biomedicine · doi:10.12980/apjtb.4.2014c677 · Cited by 34
Rabenau, M., Unger, M., Drewe, J., & Culmsee, C. (2018) · Phytomedicine · doi:10.1016/j.phymed.2018.09.177 · Cited by 34
Self-citationDefense systems to avoid ferroptosis caused by lipid peroxidation-mediated membrane damage
Fujii, J., & Yamada, K. (2023) · Free Radical Research · doi:10.1080/10715762.2023.2244155 · Cited by 38
A guide to ferroptosis, the biological rust of cellular membranes
Veeckmans, G., San, E. V., & Berghe, T. V. (2023) · FEBS Journal · doi:10.1111/febs.16993 · Cited by 35
Zolkipli‐Cunningham, Z., Pedersen, C. B., Lamhonwah, A., Gregersen, N., & Tein, I. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017534 · Cited by 35
Contrasting roles of dietary selenium and selenoproteins in chemically induced hepatocarcinogenesis
Kasaikina, M. V., Turanov, A. A., Avanesov, A. S., Schweizer, U., Seeher, S., Bronson, R. T., Novoselov, S. N., Carlson, B. A., Hatfield, D. L., & Gladyshev, V. N. (2013) · Carcinogenesis · doi:10.1093/carcin/bgt011 · Cited by 33
Self-citationIdentification of prenylated phenolics in mulberry leaf and their neuroprotective activity
Wen, L., Zhou, T., Jiang, Y., Gong, L., & Yang, B. J. (2021) · Phytomedicine · doi:10.1016/j.phymed.2021.153641 · Cited by 33
Thallium(I and III) exposure leads to liver damage and disorders of fatty acid metabolism in mice
Li, D., Yao, H., Du, L., Zeng, X., & Xiao, Q. (2022) · Chemosphere · doi:10.1016/j.chemosphere.2022.135618 · Cited by 33
Molecular Mechanisms of Epigenetic Regulation, Inflammation, and Cell Death in ADPKD
Agborbesong, E., Li, L. X., Li, L., & Li, X. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.922428 · Cited by 33
A tryparedoxin-dependent peroxidase protects African trypanosomes from membrane damage
Diechtierow, M., & Krauth‐Siegel, R. L. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.05.014 · Cited by 33
Caro, A. A., Thompson, S., & Tackett, J. (2011) · Cell Biology and Toxicology · doi:10.1007/s10565-011-9198-2 · Cited by 33
Elevated oxidative membrane damage associated with genetic modifiers of Lyst-mutant phenotypes
Trantow, C. M., Hedberg-Buenz, A., Iwashita, S., Moore, S. A., & Anderson, M. G. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001008 · Cited by 32
An, F., Zhang, J., Gao, P., Xiao, Z., Chang, W., Song, J., Wang, Y., Ma, H., Zhang, R., Chen, Z., et al. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1297024 · Cited by 34
Rai, A., Patwardhan, R. S., Jayakumar, S., Pachpatil, P. K., Das, D., Panigrahi, G. C., Gota, V., Patwardhan, S., & Sandur, S. K. (2024) · Acta Pharmacologica Sinica · doi:10.1038/s41401-024-01233-8 · Cited by 32
A guide to ferroptosis in cancer
Yapici, F. I., Bebber, C. M., & von Karstedt, S. (2024) · Molecular Oncology · doi:10.1002/1878-0261.13649 · Cited by 35
Is Ferroptosis a Future Direction in Exploring Cryptococcal Meningitis?
Xu, X., Lin, D., Tu, S., Gao, S., Shao, A., & Sheng, J. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.598601 · Cited by 33
Physiological Effects of Ferroptosis on Organ Fibrosis
Du, X., Dong, R., Wu, Y., & Ni, B. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/5295434 · Cited by 33
Aspirin mediates protection from diabetic kidney disease by inducing ferroptosis inhibition
Wu, Z., Li, D., Tian, D., Liu, X., & Wu, Z. (2022) · PLoS ONE · doi:10.1371/journal.pone.0279010 · Cited by 33
Yi, Z., Li, S., Ke, J., Wang, Y., Zhao, M., Li, J., Li, M., & Zhu, Z. (2022) · Current Issues in Molecular Biology · doi:10.3390/cimb44120422 · Cited by 32
Mallick, R., Bhowmik, P., & Duttaroy, A. K. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115591 · Cited by 35
Deng, L., Di, Y., Chen, C., Xia, J., Lei, B., Li, N., & Zhang, Q. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06486-z · Cited by 32
Shen, J., Xie, P., Wang, J., Yang, F., Li, S., Jiang, H., Wu, X., Zhou, F., & Li, J. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103196 · Cited by 31
Emerging Therapeutic Strategies Targeting GPX4-Mediated Ferroptosis in Head and Neck Cancer
Lee, J., Seo, Y. J., & Roh, J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26136452 · Cited by 36
Pace, M., Giorgi, C., Lombardozzi, G., Cimini, A., Castelli, V., & d’Angelo, M. (2025) · Biomolecules · doi:10.3390/biom15081115 · Cited by 37
Partners in Crime: The Interplay of Proteins and Membranes in Regulated Necrosis
Ros, U., Pedrera, L., & García‐Sáez, A. J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072412 · Cited by 33
Ferroptosis: Mechanism and potential applications in cervical cancer
Chang, X., & Miao, J. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1164398 · Cited by 30
Yang, J., Shi, X., Wang, Y., Ma, M., Liu, H., Wang, J., & Xu, Z. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230593 · Cited by 33
Chai, Z., Zheng, J.-S., & Shen, J. F. (2024) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14865 · Cited by 31
Leonardi, A., Evke, S., Lee, M., Melendez, J. A., & Begley, T. J. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.08.030 · Cited by 29
A lipid perspective on regulated cell death
Flores‐Romero, H., Ros, U., & García‐Sáez, A. J. (2019) · International review of cytology · doi:10.1016/bs.ircmb.2019.11.004 · Cited by 32
Jovanović, M., Dragoj, M., Zhukovsky, D., Dar’in, D. V., Krasavin, M., Pešić, M., & Podolski-Renić, A. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.586146 · Cited by 30
Ferroptosis Meets Cell–Cell Contacts
Dietrich, C., & Hofmann, T. G. (2021) · Cells · doi:10.3390/cells10092462 · Cited by 30
Mechanisms of ferroptosis in chronic kidney disease
Zhuo, W.-Q., Wen, Y., Luo, H., Luo, Z., & Wang, L. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.975582 · Cited by 29
Male infertility and somatic health — insights into lipid damage as a mechanistic link
Burke, N. D., Nixon, B., Roman, S. D., Schjenken, J. E., Walters, J. L. H., Aitken, R. J., & Bromfield, E. G. (2022) · Nature Reviews Urology · doi:10.1038/s41585-022-00640-y · Cited by 31
Dar, H. H., Mikulska‐Ruminska, K., Tyurina, Y. Y., Luci, D. K., Yasgar, A., Самович, С. Н., Kapralov, A. A., Souryavong, A. B., Tyurin, V. A., Amoscato, A. A., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2218896120 · Cited by 34
lnc-MRGPRF-6:1 Promotes ox-LDL-Induced Macrophage Ferroptosis via Suppressing GPX4
You, Z., Ye, X., Jiang, M., Gu, N., & Liang, C. (2023) · Mediators of Inflammation · doi:10.1155/2023/5513245 · Cited by 30
Gong, G., Méplan, C., Gautrey, H., Hall, J., & Hesketh, J. E. (2011) · Genes & Nutrition · doi:10.1007/s12263-011-0256-4 · Cited by 30
Brütsch, S. H., Rademacher, M., Roth, S. R., Müller, K., Eder, S., Viertel, D., Franz, C., Kühn, H., & Borchert, A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.738930 · Cited by 30
Self-citationMolecular mechanisms of ferroptosis and its antitumor applications in natural products
Yu, D., Wang, Q., Zhang, Q., Cai, M., Liu, S., & Zhang, W. (2023) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2023120 · Cited by 30
Particulate Matter Induces Oxidative Stress and Ferroptosis in Human Lung Epithelial Cells
Ahn, Y., Yim, Y., & Yoo, H. M. (2024) · Toxics · doi:10.3390/toxics12020161 · Cited by 30
Metalloptosis: metal ions-induced programmed cell death based on nanomaterials for cancer therapy
Wang, S., Ma, R., Mei, Z., & Hou, Y. (2024) · MedMat. · doi:10.1097/mm9.0000000000000004 · Cited by 30
Nanobiotechnology boosts ferroptosis: opportunities and challenges
Han, S., Zou, J., Xiao, F., Xian, J., Liu, Z., Li, M., Luo, W., Feng, C., & Kong, N. (2024) · Journal of Nanobiotechnology · doi:10.1186/s12951-024-02842-5 · Cited by 34
Interplay of ferroptotic and apoptotic cell death and its modulation by BH3-mimetics
Qiu, Y., Hüther, J. A., Wank, B., Rath, A., Tykwe, R., Aldrovandi, M., Henkelmann, B., Mergner, J., Nakamura, T., Laschat, S., et al. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01514-7 · Cited by 33
Self-citationInvestigating Nonapoptotic Cell Death Using Chemical Biology Approaches
Armenta, D. A., & Dixon, S. J. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.03.005 · Cited by 29
The molecular mosaic of regulated cell death in the cardiovascular system
Martens, M. D., Karch, J. M., & Gordon, J. W. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2021.166297 · Cited by 31
Insights Into Ferroptosis, a Novel Target for the Therapy of Cancer
Wang, H., Ju, J., Wang, S., Zhang, Y., Liu, C.-Y., Wang, T., Yu, X. M., Wang, F., Cheng, X.-R., Wang, K., et al. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.812534 · Cited by 30
Current progress of ferroptosis study in ovarian cancer
Tan, Z., Huang, H., Sun, W., Li, Y., & Jia, Y. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.966007 · Cited by 29
Ying, T.-H., Chen, C.-W., Hsiao, Y., Hung, S., Chung, J., & Yang, J. (2013) · PubMed · Cited by 29
Wang, L., Harris, S. M., Espinoza, H. M., McClain, V., & Gallagher, E. P. (2012) · Aquatic Toxicology · doi:10.1016/j.aquatox.2012.02.025 · Cited by 29
Membrane Dynamics and Cation Handling in Ferroptosis
Hirata, Y., & Mishima, E. (2024) · Physiology · doi:10.1152/physiol.00029.2023 · Cited by 33
Luteolin attenuates CCl4-induced hepatic injury by inhibiting ferroptosis via SLC7A11
Han, Z., Batudeligen, Chen, H., Narisu, Anda, Xu, Y., & Xue, L. (2024) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-024-04486-2 · Cited by 30
Mechanisms of Vitamins Inhibiting Ferroptosis
Zhang, M., Chen, X., & Zhang, Y. (2024) · Antioxidants · doi:10.3390/antiox13121571 · Cited by 32
Epithelial-mesenchymal transition promotes metabolic reprogramming to suppress ferroptosis
Guo, W., Duan, Z., Wu, J., & Zhou, B. P. (2025) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2025.02.013 · Cited by 33
An atlas of ferroptosis-induced secretomes
Yapici, F. I., Seidel, E., Dahlhaus, A., Weber, J., Schmidt, C., Filho, A. D. B. C., Yang, M., Nenchova, M., Güngör, E., Stroh, J., et al. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01517-4 · Cited by 29
Interaction between iron and omega-3 fatty acids metabolisms: where is the cross-link?
Ogłuszka, M., Lipiński, P., & Starzyński, R. R. (2020) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2020.1862047 · Cited by 28
Ferroptosis in plants: regulation of lipid peroxidation and redox status
Distéfano, A. M., López, G. A., Bauer, V., Zabaleta, E. J., & Pagnussat, G. C. (2022) · Biochemical Journal · doi:10.1042/bcj20210682 · Cited by 29
Ferroptosis regulation by methylation in cancer
Hao, M., Jiang, Y., Zhang, Y., Yang, X., & Han, J. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.188972 · Cited by 28
Chen, B., & Jin, W. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1200061 · Cited by 29
Ferroptosis and renal fibrosis: mechanistic insights and emerging therapeutic targets
Lyu, G., Liao, H., & Li, R. (2025) · Renal Failure · doi:10.1080/0886022x.2025.2498629 · Cited by 28
Liu, Z., Xia, X., Lv, X., Song, E., & Song, Y. (2021) · Environmental Pollution · doi:10.1016/j.envpol.2021.117345 · Cited by 27
Research progress on the mechanism of ferroptosis and its clinical application
Xia, J., Si, H., Yao, W., Li, C., Guo, Y., Tian, Y., & Hao, C. (2021) · Experimental Cell Research · doi:10.1016/j.yexcr.2021.112932 · Cited by 27
Lyu, T., Li, X., & Song, Y. (2023) · Chinese Medical Journal · doi:10.1097/cm9.0000000000002642 · Cited by 31
Agbor, T. A., Demma, Z., Mrsny, R. J., Castillo, A., Boll, E. J., & McCormick, B. A. (2014) · Cellular Microbiology · doi:10.1111/cmi.12290 · Cited by 27
Hiller, C., Nißen, A., Benítez, D., Comini, M. A., & Krauth‐Siegel, R. L. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004075 · Cited by 27
Todorčević, M., Škugor, S., & Ruyter, B. (2010) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2010.04.010 · Cited by 27
Musee, J., & Marnett, L. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.381202 · Cited by 27
Maneb causes pro-oxidant effects in the hippocampus of Nrf2 knockout mice
Kurzatkowski, D. M., & Trombetta, L. D. (2013) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2013.04.016 · Cited by 27
Chronic iron limitation confers transient resistance to oxidative stress in marine diatoms
van Creveld, S. G., Rosenwasser, S., Levin, Y., & Vardi, A. (2016) · PLANT PHYSIOLOGY · doi:10.1104/pp.16.00840 · Cited by 27
Tomás-Sanchez, C., Blanco-Álvarez, V. M., Martínez‐Fong, D., González-Barrios, J. A., Gonzalez-Vazquez, A., Aguilar-Peralta, A. K., Torres-Soto, M., Soto-Rodríguez, G., Limón, I. D., Brambila, E., et al. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/9416432 · Cited by 27
Ferroptosis, Metabolic Rewiring, and Endometrial Cancer
Žalytė, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010075 · Cited by 29
Auberger, P., Favreau, C., Savy, C., Jacquel, A., & Robert, G. (2024) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-024-00613-6 · Cited by 28
Activating the NFE2L1-ubiquitin-proteasome system by DDI2 protects from ferroptosis
Ofoghi, A., Kotschi, S., Lemmer, I. L., Haas, D. T., Willemsen, N., Bayer, B., Jung, A., Möller, S., Haberecht-Müller, S., Krüger, E., et al. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01398-z · Cited by 26
The role of ferroptosis in colorectal cancer and its potential synergy with immunotherapy
Xia, W., Lv, Y., Zou, Y., Kang, Z., Li, Z., Tian, J., Zhou, H., Su, W., & Zhong, J. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1526749 · Cited by 27
Tobe, R., Naranjo‐Suarez, S., Everley, R. A., Carlson, B. A., Turanov, A. A., Tsuji, P. A., Yoo, M., Gygi, S. P., Gladyshev, V. N., & Hatfield, D. L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.446666 · Cited by 26
Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4
Janowski, R., Scanu, S., Niessing, D., & Madl, T. (2016) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x16013686 · Cited by 26
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