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 801–900 of 1,000
Liu, T., Luo, H., Zhang, J., Hu, X., & Zhang, J. (2021) · BMC Cancer · doi:10.1186/s12885-021-08541-w · Cited by 26
The key roles of organelles and ferroptosis in Alzheimerʼs disease
Long, H., Cheng, Y., Zhou, Z., Luo, H., Wen, D., & Gao, L. (2022) · Journal of Neuroscience Research · doi:10.1002/jnr.25033 · Cited by 28
Diaw, S. H., Ganos, C., Zittel, S., Plötze‐Martin, K., Kulikovskaja, L., Vos, M. H., Westenberger, A., Raković, A., Lohmann, K., & Dulovic‐Mahlow, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179524 · Cited by 26
Xu, J., Ruan, Z., Guo, Z., Hou, L., Wang, G., Zheng, Z., Zhang, X., Liu, H., Sun, K., & Guo, F. (2024) · Bone and Joint Research · doi:10.1302/2046-3758.133.bjr-2023-0250.r1 · Cited by 26
Role of Glutathione Peroxidase 4 in Glutamate-Induced Oxytosis in the Retina
Sakai, O., Uchida, T., Roggia, M. F., Imai, H., Ueta, T., & Amano, S. (2015) · PLoS ONE · doi:10.1371/journal.pone.0130467 · Cited by 26
Arnér, E. S. J., & Schmidt, E. E. (2024) · Advances in cancer research · doi:10.1016/bs.acr.2024.04.001 · Cited by 25
Iron and ferroptosis in kidney disease: molecular and metabolic mechanisms
Wang, W., Chen, J., Zhan, L., Zou, H., Wang, L., Guo, M., Gao, H., Xu, J., & Wu, W. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1531577 · Cited by 28
Cui, M., Xu, Q., Duan, L., Lu, J., & Hu, J. Y. (2025) · Drug Design Development and Therapy · doi:10.2147/dddt.s509357 · Cited by 25
Cell death and cancer: Metabolic interconnections
Dalseno, D., Gajic, N., Flanagan, L., & Tait, S. W. G. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115804 · Cited by 30
Xu, L., Zhang, W., Sánchez-Tejeda, J. F., Holovan, D., McCain, J., Lovell, T. C., & Cosa, G. (2025) · Nature Chemistry · doi:10.1038/s41557-025-01966-x · Cited by 25
Beyond oxidative stress: Ferroptosis as a novel orchestrator in neurodegenerative disorders
Yi, Y., Jia, P., Xie, P., Peng, X., Zhu, X., Yin, S., Luo, Y., Deng, Y., & Wan, L. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1683876 · Cited by 30
Decoding GPX4 regulation in ferroptosis: mechanisms and therapeutic implications
Chen, X. (2026) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2026.01.008 · Cited by 25
Shi, J., Liu, Y., Wang, Y., Gao, R., Wang, Y., & Liu, J. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1194343 · Cited by 26
Li, Z., Luo, Y., Wang, C., Han, D., & Sun, W. (2023) · Oncology Reports · doi:10.3892/or.2023.8629 · Cited by 25
Bermudez, J. Y., Webber, H. C., Brown, B. J., Braun, T. A., Clark, A. F., & Mao, W. (2017) · PLoS ONE · doi:10.1371/journal.pone.0169671 · Cited by 25
Sex differences in neonatal mouse brain injury after hypoxia‐ischemia and adaptaquin treatment
Li, K., Li, T., Wang, Y., Xu, Y., Zhang, S., Culmsee, C., Wang, X., & Zhu, C. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14790 · Cited by 25
Self-citationChu, J., Jiang, Y., Zhou, W., Zhang, J., Li, H., Yu, Y., & Yu, Y. (2022) · Human & Experimental Toxicology · doi:10.1177/09603271221133547 · Cited by 24
Targeting lipoxygenases to suppress ferroptotic cell death
Pratt, D. A. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2309317120 · Cited by 26
Zhao, J., Wang, Q., Liu, Z., Zhang, M., Li, J., Fu, Z. F., Zhao, L., & Zhou, M. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107168 · Cited by 24
Ferroptosis regulation by Cap’n’collar family transcription factors
Murray, M. B., & Dixon, S. J. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107583 · Cited by 26
From fat to fire: The lipid–inflammasome connection
Anand, P. (2024) · Immunological Reviews · doi:10.1111/imr.13403 · Cited by 27
Taha, S. R., Karimi, M., Mahdavi, B., Tehrani, M. Y., Bemani, A., Kabirian, S., Mohammadi, J., Jabbari, S., Hushmand, M., Mokhtar, A., et al. (2025) · Epigenetics & Chromatin · doi:10.1186/s13072-024-00560-8 · Cited by 24
Zhao, X., Sun, Y., Zou, J., Wu, Y., Huang, M., Kong, H., Liu, G., Gerhardt, H., Gu, W. J., Zhang, Y., et al. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01453-3 · Cited by 25
Bueno, D., Canto, R. F. S., de Souza, V., Andreguetti, R. R., Barbosa, F. A. R., Naime, A. A., Dey, P. N., Wüllner, V., Lopes, M. W., Braga, A. L., et al. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01956-9 · Cited by 24
Puxeddu, M., Wu, J., Bai, R., D’Ambrosio, M., Nalli, M., Coluccia, A., Manetto, S., Ciogli, A., Masci, D., Urbani, A., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01457 · Cited by 25
Targeting regulated cell death pathways in acute myeloid leukemia
Garciaz, S., Miller, T. W., Collette, Y., & Vey, N. (2023) · Cancer Drug Resistance · doi:10.20517/cdr.2022.108 · Cited by 25
Shi, W., Wang, J., Li, Z., Xu, S., Wang, J., Zhang, L., & Yang, H. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.01.021 · Cited by 24
Khan, S., Bano, N., Ahamad, S., John, U., Dar, N. J., & Bhat, S. A. (2024) · Aging and Disease · doi:10.14336/ad.2024.0125-1 · Cited by 27
Hosseinkhani, S., Amandadi, M., Ghanavatian, P., Zarein, F., Ataei, F., Nikkhah, M., & Vandenabeele, P. (2024) · Chemical Society Reviews · doi:10.1039/d3cs00743j · Cited by 25
Small molecule probes for cellular death machines
Li, Y., Qian, L., & Yuan, J. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.05.007 · Cited by 23
Targeted fatty acid metabolomics to discover Parkinson's disease associated metabolic alteration
Zhang, J., Liu, L., Zhang, L., Chen, S., Chen, Y., & Cai, C. (2021) · Journal of Mass Spectrometry · doi:10.1002/jms.4781 · Cited by 23
The role of ferroptosis in organ toxicity
Yarmohammadi, F., Hayes, A. W., & Karimi, G. (2021) · Human & Experimental Toxicology · doi:10.1177/09603271211052987 · Cited by 23
The effects of selenium on GPX4‐mediated lipid peroxidation and apoptosis in germ cells
Liu, P., Zhu, J., Yuan, G., Li, D., Wen, Y. R., Huang, S., Lv, Z., Guo, Y., & Cheng, J. (2021) · Journal of Applied Toxicology · doi:10.1002/jat.4273 · Cited by 23
The multifaceted role of ferroptosis in kidney diseases
Lin, Y., Xu, W., Hou, Y., Wang, S., Zhang, H., Ran, M., Huang, Y., Wang, Y., & Yang, G. (2022) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2022.110107 · Cited by 23
Inhibition of autophagy rescues HT22 hippocampal neurons from erastin-induced ferroptosis
Rami, A., & Hanke, N. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.360246 · Cited by 21
Zhu, Y., Gong, P., Wang, J., Cheng, J., Wang, W., Cai, H., Ao, R., Huang, H., Yu, M., Lin, L., et al. (2023) · Angewandte Chemie · doi:10.1002/ange.202218407 · Cited by 23
Remodeling of nuclear architecture by the thiodioxoxpiperazine metabolite chaetocin
Illner, D., Zinner, R., Handtke, V., Rouquette, J., Strickfaden, H., Lanctôt, C., Conrad, M., Seiler, A., Imhof, A., Cremer, T., et al. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.03.008 · Cited by 22
Self-citationThe Role of Glucose and Lipid Metabolism in Growth and Survival of Cancer Cells
Brault, C., & Schulze, A. (2016) · Recent results in cancer research/Recent Results in Cancer Research · doi:10.1007/978-3-319-42118-6_1 · Cited by 22
Panzilius, E., Holstein, F., Dehairs, J., Planque, M., von Toerne, C., Koenig, A.-C., Doll, S. G., Bannier-Hélaouët, M., Ganz, H. M., Hauck, S. M., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/417949 · Cited by 24
Self-citationFerroptosis and bone health: bridging the gap between mechanisms and therapy
Xiao, R., Han, Z., Peng, J., Li, P., Gong, M., Cai, Y., Pang, L., Ye, X., & Jin, S. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1634516 · Cited by 24
Navigating Transition Metal‐Dependent Cell Death: Mechanisms, Crosstalk, and Future Directions
Song, Q., Yang, Y., & Yang, L. (2025) · Advanced Science · doi:10.1002/advs.202501974 · Cited by 24
Targeting ferroptosis in cancer: from mechanistic insights to therapeutic approaches
Wang, J., Guo, D., Jiang, S., Wu, W., & Gao, X. (2026) · Molecular Biomedicine · doi:10.1186/s43556-026-00416-5 · Cited by 27
Defining a pharmacological inhibitor fingerprint for oxytosis/ferroptosis
Soriano‐Castell, D., Currais, A. J. M., & Maher, P. A. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.05.023 · Cited by 22
Ferroptosis Inducers in Thyroid Cancer
Sekhar, K. R., Cyr, S., & Baregamian, N. (2022) · World Journal of Surgery · doi:10.1007/s00268-022-06738-z · Cited by 22
Die hard: cell death mechanisms and their implications in nanotoxicology
Lomphithak, T., & Fadeel, B. (2023) · Toxicological Sciences · doi:10.1093/toxsci/kfad008 · Cited by 24
Nature-Inspired Bioactive Compounds: A Promising Approach for Ferroptosis-Linked Human Diseases?
Hajj, S. E., Canabady‐Rochelle, L., & Gaucher, C. (2023) · Molecules · doi:10.3390/molecules28062636 · Cited by 24
Mitophagy contributes to zinc-induced ferroptosis in porcine testis cells
Li, Q., Yang, Q., Guo, P., Feng, Y., Wang, S., Guo, J., Tang, Z., Yu, W., & Liao, J. (2023) · Food and Chemical Toxicology · doi:10.1016/j.fct.2023.113950 · Cited by 22
Insight into the Role of Ferroptosis in Epilepsy
Huang, L., Liu, H., & Liu, S. (2024) · Journal of Integrative Neuroscience · doi:10.31083/j.jin2306113 · Cited by 22
Selenoproteins of the Glutathione Peroxidase Family
Flohé, L., & Brigelius‐Flohé, R. (2011) · Springer eBooks · doi:10.1007/978-1-4614-1025-6_13 · Cited by 22
Ferroptosis: a new target for hepatic ischemia-reperfusion injury?
Guo, S., Li, Z., Liu, Y., Cheng, Y., & Jia, D. (2024) · Free Radical Research · doi:10.1080/10715762.2024.2386075 · Cited by 23
Ajmone‐Cat, M. A., Simone, R. D., Tartaglione, A. M., Biase, A. D., Benedetto, R. D., D’Archivio, M., Varı́, R., Ricceri, L., Aureli, F., Iacoponi, F., et al. (2022) · Nutrients · doi:10.3390/nu14091850 · Cited by 22
Zhang, W., Li, X., Xu, J., Wang, Y., Xing, Z., Hu, S., Fan, Q., Lu, S., Cheng, J., Gu, J., et al. (2022) · Cancers · doi:10.3390/cancers14215233 · Cited by 21
Miyauchi, W., Shishido, Y., Matsumi, Y., Matsunaga, T., Makinoya, M., Shimizu, S., Miyatani, K., Sakamoto, T., Umekita, Y., Hasegawa, T., et al. (2022) · Esophagus · doi:10.1007/s10388-022-00982-x · Cited by 26
Gleitze, S., Ramírez, O. A., Vega-Vásquez, I., Yan, J., Lobos, P., Bading, H., Núñez, M. T., Paula-Lima, A. C., & Hidalgo, C. (2023) · Antioxidants · doi:10.3390/antiox12030705 · Cited by 21
Tak, J., Joo, M. S., Kim, Y. S., Park, H. W., Lee, C. H., Park, G., Hwang, S., & Kim, S. G. (2024) · Theranostics · doi:10.7150/thno.89703 · Cited by 22
SECIS-Binding Protein 2 Promotes Cell Survival by Protecting Against Oxidative Stress
Papp, L. V., Lu, J., Bolderson, E., Boucher, D., Singh, R. N., Holmgren, A., & Khanna, K. K. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2913 · Cited by 21
Role of Glutathione Peroxidase 4 in Conjunctival Epithelial Cells
Sakai, O., Uchida, T., Imai, H., Ueta, T., & Amano, S. (2015) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.14-15463 · Cited by 21
Bertelsmann, H., Keppler, S. L., Höltershinken, M., Bollwein, H., BEHNE, D., Alber, D., Bukalis, G., Kyriakopoulos, A. M., & Sieme, H. (2010) · Reproduction Fertility and Development · doi:10.1071/rd10032 · Cited by 21
NSC ‐34 motor neuron‐like cells are sensitized to ferroptosis upon differentiation
Martinez, A. M., Mirkovic, J., Stanisz, Z., Patwari, F. S., & Yang, W. S. (2018) · FEBS Open Bio · doi:10.1002/2211-5463.12577 · Cited by 22
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
Copper and iron orchestrate cell-state transitions in cancer and immunity
Müller, S., Cañeque, T., Solier, S., & Rodriguez, R. (2024) · Trends in Cell Biology · doi:10.1016/j.tcb.2024.07.005 · Cited by 20
Fradejas‐Villar, N., Zhao, W., Reuter, U., Doengi, M., Ingold, I., Bohleber, S., Conrad, M., & Schweizer, U. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102188 · Cited by 21
Self-citationSkv, M., Maity, S., Poornima, R., Yau, S., Vaishali, K., Stellwagen, D., & Komal, P. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.03.039 · Cited by 20
Hao, Y., Ou, Y., Zhang, C., Chen, H., Hu, Y., Yang, Z., Zhong, X., Hu, W., & Sun, P. (2022) · Brain Research · doi:10.1016/j.brainres.2022.148073 · Cited by 20
Caveolae and the oxidative stress response
Wu, Y., Lim, Y., & Parton, R. G. (2023) · Biochemical Society Transactions · doi:10.1042/bst20230121 · Cited by 20
Lu, L., Jifu, C., Xia, J., & Wang, J. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116753 · Cited by 26
CRISPR activation screens identify the SWI/SNF ATPases as suppressors of ferroptosis
Bhat, K. P., Vijay, J., Vilas, C. K., Asundi, J., Zou, J., Lau, T., Cai, X. T., Ahmed, M., Kabza, M., Weng, J., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114345 · Cited by 23
Role of hypoxia-inducible-factor-1α (HIF-1α) in ferroptosis of adipose tissue during ketosis
Fan, Y., Ma, L., Fang, X., Du, S., Mauck, J., Loor, J. J., Sun, X., Jia, H., Xu, C., & Xu, Q. (2024) · Journal of Dairy Science · doi:10.3168/jds.2024-24822 · Cited by 20
Grisard, E., Névo, N., Lescure, A., Doll, S. G., Corbé, M., Jouve, M. J., Lavieu, G., Joliot, A., Nery, E. D., Jaular, L. M., et al. (2022) · Journal of Extracellular Vesicles · doi:10.1002/jev2.12242 · Cited by 18
A network approach to micronutrient genetics: interactions with lipid metabolism
Lietz, G., & Hesketh, J. E. (2009) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e3283295ecf · Cited by 20
Liu, C., Tian, Q., Li, Z., Wang, G., Han, W., Jiang, S., Sun, Z., Xu, Q., Wang, L., Liao, J., et al. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103550 · Cited by 19
RetractedROS scavengers decrease γH2ax spots in motor neuronal nuclei of ALS model mice in vitro
Junghans, M., John, F., Cihankaya, H., Schliebs, D., Winklhofer, K. F., Bader, V., Matschke, J., Theiß, C., & Matschke, V. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.963169 · Cited by 20
Schweizer, U., Wirth, E. K., Klopstock, T., Hölter, S. M., Becker, L., Moskovitz, J., Grune, T., Fuchs, H., Gailus‐Durner, V., de Angelis, M. H., et al. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102490 · Cited by 19
Self-citationOutlook of Ferroptosis-Targeted Lipid Peroxidation in Cardiovascular Disease
Wu, Z.-F., Liu, X.-Y., Deng, N.-H., Ren, Z., & Jiang, Z. (2022) · Current Medicinal Chemistry · doi:10.2174/0929867330666221111162905 · Cited by 21
Fan, X., Zhong, Y., Yuan, F., Zhang, L., Cai, Y., & Liao, L. (2023) · Scientific Reports · doi:10.1038/s41598-023-27676-3 · Cited by 19
Wild-type and mutant p53 in cancer-related ferroptosis. A matter of stress management?
Corazzari, M., & Collavin, L. (2023) · Frontiers in Genetics · doi:10.3389/fgene.2023.1148192 · Cited by 21
Consoli, V., Fallica, A. N., Sorrenti, V., Pittalà, V., & Vanella, L. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0179 · Cited by 21
Wu, F., Chen, H., Li, Q., Liu, R., Suo, Y., Li, B., Kong, X., Cheng, Z., Liu, H., & Chang, Y. (2023) · Chemical Engineering Journal · doi:10.1016/j.cej.2023.143827 · Cited by 19
Ferroptosis: a dual-edged sword in tumour growth
Zhao, X., Li, X., & Xu, Y. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1330910 · Cited by 21
Dhas, N. L., Kudarha, R. R., Tıwarı, R., Tiwari, G., Garg, N., Kumar, P., Kulkarni, S., Kulkarni, J., Soman, S., Hegde, A. R., et al. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.122629 · Cited by 20
Oxidative Stress, Selenium Redox Systems Including GPX/TXNRD Families
Ingold, I., & Conrad, M. (2018) · Molecular and integrative toxicology · doi:10.1007/978-3-319-95390-8_6 · Cited by 19
Self-citationChoudhary, R., Malairaman, U., & Katyal, A. (2017) · Neuroscience · doi:10.1016/j.neuroscience.2017.07.015 · Cited by 19
Selenium and Alzheimer's disease
Gu, J., Gu, J., & Yu, L. (2024) · Chinese Chemical Letters · doi:10.1016/j.cclet.2024.110727 · Cited by 18
Ferroptosis: potential targets and emerging roles in pancreatic diseases
Huang, Z., Ma, Y., Sun, Z., Cheng, L., & Wang, G. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03625-x · Cited by 19
A tangible method to assess native ferroptosis suppressor activity
Nakamura, T., Ito, J., Mourão, A., Wahida, A., Nakagawa, K., Mishima, E., & Conrad, M. (2024) · Cell Reports Methods · doi:10.1016/j.crmeth.2024.100710 · Cited by 19
Self-citationThe Role of Vitamin K in the Development of Neurodegenerative Diseases
Diachenko, A. I., Родин, И. А., Krasnova, T. N., Klychnikov, O. I., & Нефедова, Л. Н. (2024) · Biochemistry (Moscow) · doi:10.1134/s0006297924140049 · Cited by 18
Viktorínová, A. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.07.022 · Cited by 18
Zhao, W., Bohleber, S., Schmidt, H., Seeher, S., Howard, M. T., Braun, D., Arndt, S., Reuter, U., Wende, H., Birchmeier, C., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009369 · Cited by 18
Self-citationRegulated lytic cell death in breast cancer
Liu, M., Wang, L., Xia, X., Wu, Y., Zhu, C., Duan, M., Wei, X., Hu, J., & Lei, L. (2021) · Cell Biology International · doi:10.1002/cbin.11705 · Cited by 19
Liu, J., Wang, Y., Meng, H., Yin, Y., Zhu, H., & Ni, T. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.735013 · Cited by 18
Wu, M., Huang, Z., Zeng, L., Wang, C., & Wang, D. (2022) · Cardiology Research and Practice · doi:10.1155/2022/6558060 · Cited by 19
Synthesis of 1,3‐Selenazol‐2(3H)‐imines
Atanassov, P. K., Linden, A., & Heimgartner, H. (2010) · Helvetica Chimica Acta · doi:10.1002/hlca.200900452 · Cited by 18
Rong, X., Zhou, Y., Liu, Y., Zhao, B., Wang, B., Wang, C., Gong, X., Tang, P., Lu, L., Li, Y., et al. (2017) · Development · doi:10.1242/dev.144261 · Cited by 18
Lin, Y., Huang, A., Kuo, C., Yang, J., Lan, Y., Yu, C.-C., Huang, W.-W., & Chung, J. (2013) · Nutrition and Cancer · doi:10.1080/01635581.2013.757627 · Cited by 18
Glucose starvation causes ferroptosis-mediated lysosomal dysfunction
Miki, K., Yagi, M., Kang, D., Kunisaki, Y., Yoshimoto, K., & Uchiumi, T. (2024) · iScience · doi:10.1016/j.isci.2024.109735 · Cited by 17
Mechanisms and Therapeutic Potential of GPX4 in Pain Modulation
Fan, S., Wang, K., Zhang, T., Deng, D., Shen, J., Zhao, B., Fu, D., & Chen, X. (2024) · Pain and Therapy · doi:10.1007/s40122-024-00673-8 · Cited by 19
Copper-based nanoplatforms and their role in cancer therapy
García-Peiro, J. I., Bonet‐Aleta, J., & Hueso, J. L. (2025) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2025.216542 · Cited by 17
Zhang, Z., Yang, Z., Wang, S., Wang, X., & Mao, J. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102770 · Cited by 18
Selenium and selenoproteins: key regulators of ferroptosis and therapeutic targets in cancer
Lee, J., & Roh, J. (2025) · Journal of Molecular Medicine · doi:10.1007/s00109-025-02563-8 · Cited by 17
SharathBabu, B. N., Shivangi, S., Valiyaveettil, A., Annaraj, B., & Mugesh, G. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.06.047 · Cited by 20
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