The selenoprotein GPX4 is essential for mouse development and protects from radiation and oxidative damage insults

Free radicals in biology and medicine

Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178

Chelex 100 as a Medium for Simple Extraction of DNA for PCR-Based Typing from Forensic Material

Walsh, P. S., Metzger, D. A., & Higuchi, R. (2013) · BioTechniques · doi:10.2144/000114018 · Cited by 5,850

Free Radicals in Biology and Medicine

Land, E. J. (1990) · International Journal of Radiation Biology · doi:10.1080/09553009014552071 · Cited by 4,871

Toxicity determined in vitro by morphological alterations and neutral red absorption

Borenfreund, E., & Puerner, J. A. (1985) · Toxicology Letters · doi:10.1016/0378-4274(85)90046-3 · Cited by 1,913

Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase

Li, Y., Huang, T.-T., Carlson, E. J., Melov, S., Ursell, P. C., Olson, J. L., Noble, L. J., Yoshimura, M. P., Berger, C., Chan, P. H., et al. (1995) · Nature Genetics · doi:10.1038/ng1295-376 · Cited by 1,789

CLONAL GROWTH OF MAMMALIAN CELLS IN VITRO

Puck, T. T., Marcus, P. I., & Cieciura, S. J. (1956) · The Journal of Experimental Medicine · doi:10.1084/jem.103.2.273 · Cited by 1,143

Tissue-specific functions of individual glutathione peroxidases

Brigelius-Flohé, R. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00173-2 · Cited by 1,114

Dual Function of the Selenoprotein PHGPx During Sperm Maturation

Ursini, F., Heim, S., Kieß, M., Maiorino, M., Roveri, A., Wissing, J. B., & Flohé, L. (1999) · Science · doi:10.1126/science.285.5432.1393 · Cited by 902

Mice Deficient in Cellular Glutathione Peroxidase Develop Normally and Show No Increased Sensitivity to Hyperoxia

Ho, Y., Magnenat, J.-L., Bronson, R. T., Cao, J., Gargano, M. D., Sugawara, M., & Funk, C. D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.26.16644 · Cited by 562

The role of selenium peroxidases in the protection against oxidative damage of membranes

Ursini, F., & Bindoli, A. (1987) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(87)90053-3 · Cited by 391

FSP1 and histone deacetylases suppress cancer persister cell ferroptosis

Higuchi, M., Williams, A. F., Stuhlfire, A. E., Nguyen, A. H., Gervasio, D. A. G., Turkal, C. E., Chon, S., & Hangauer, M. J. (2026) · Science Advances · doi:10.1126/sciadv.aea8771 · Cited by 8

The dual role of ferroptosis in pancreatic cancer: a narrative review

Tang, D., Chen, X., Comish, P. B., & Kang, R. (2021) · Journal of Pancreatology · doi:10.1097/jp9.0000000000000067 · Cited by 8

Cold resistance of mammalian hibernators ∼ a matter of ferroptosis?

Sone, M., & Yamaguchi, Y. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1377986 · Cited by 9

Phospholipid hydroperoxide glutathione peroxidase gene is regulated via an estrogen and estrogen receptor signaling in cultured mouse fetuses

Baek, I., Jung, K. Y., Yon, J., Lee, S.-R., Lee, B. J., Yun, Y. W., & Nam, S.-Y. (2011) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1007/s11626-011-9438-z · Cited by 8

Selenium and Male Reproduction

Turanov, A. A., Malinouski, M., & Gladyshev, V. N. (2011) · Springer eBooks · doi:10.1007/978-1-4614-1025-6_32 · Cited by 8

The Role of Selenoproteins in Resolution of Inflammation

Tukaramrao, D. B., Finch, E. R., Liao, C., Shay, A. E., & Prabhu, K. S. (2016) · Springer eBooks · doi:10.1007/978-3-319-41283-2_42 · Cited by 8

Mouse Models that Target Individual Selenoproteins

Conrad, M., & Schweizer, U. (2016) · Springer eBooks · doi:10.1007/978-3-319-41283-2_47 · Cited by 8

GPX4 overexpression does not alter atherosclerotic plaque development in ApoE knock-out mice

Coornaert, I., Breynaert, A., Hermans, N., Meyer, G. R. Y. D., & Martinet, W. (2024) · Vascular Biology · doi:10.1530/vb-23-0020 · Cited by 7

Lipids grease the chain of cancer progression

Rupert, J. E., Cao, P. H. A., Frigo, D. E., & Kolonin, M. G. (2026) · Trends in cancer · doi:10.1016/j.trecan.2025.11.012 · Cited by 7

Quantitative subcellular proteomics using SILAC reveals enhanced metabolic buffering in the pluripotent ground state

van Mierlo, G., Wester, R. A., & Marks, H. (2018) · Stem Cell Research · doi:10.1016/j.scr.2018.09.017 · Cited by 7

Mapping current research and identifying hotspots of ferroptosis in cardiovascular diseases

Teng, T., Kong, C., Huang, R., Ma, Z., Hu, C., Zhang, X., Hu, M., & Tang, Q. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.1046377 · Cited by 7

Pacidusin B isolated from Phyllanthus acidus triggers ferroptotic cell death in HT1080 cells

Zhu, G., Luo, D., Zhao, Y., Xiang, Z.-R., Chen, C., Li, N., Hao, X., Ding, X., Zhao, Y., & Zhao, Y. (2024) · Natural Products and Bioprospecting · doi:10.1007/s13659-024-00454-y · Cited by 7

The Peroxidase and Cyclooxygenase Activity of Prostaglandin H Synthase

Kudalkar, S. N., Rouzer, C. A., & Marnett, L. J. (2015) · Royal Society of Chemistry eBooks · doi:10.1039/9781782622628-00245 · Cited by 7

Selenium

Cheng, W., & Lei, X. G. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802168-2.00037-3 · Cited by 7

Selenoproteins in Nervous System Development, Function and Degeneration

Schweizer, U. (2016) · Springer eBooks · doi:10.1007/978-3-319-41283-2_36 · Cited by 7

Transporters and Oxidative Stress in AMD

Pow, D., Sullivan, R. K. P., Williams, S., & Woldemussie, E. (2005) · Springer eBooks · doi:10.1007/3-540-26977-0_8 · Cited by 5

Epigenetic regulation of ferroptosis in gastrointestinal cancers (Review)

Gong, L., Wu, L., Zhao, S., Xiao, S., Chu, X., Zhang, Y., Li, F., Li, S., Yang, H., & Jiang, P. (2025) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2025.5534 · Cited by 6

Protection of Epididymal Spermatozoa from Oxidative Stress

Drevet, J. R. (2012) · Humana Press eBooks · doi:10.1007/978-1-61779-776-7_5 · Cited by 6

Absorption and retention characteristics of selenium in dorsal root ganglion neurons

Haratake, M., Koga, K., Inoue, M., Fuchigami, T., & Nakayama, M. (2011) · Metallomics · doi:10.1039/c1mt00111f · Cited by 6

Defining the immunoreactive epitope for the monoclonal anti-human glutathione peroxidase-4 antibody anti-hGPx4 Mab63-1

Borchert, A., Küttner, G., Giessmann, E., Wang, C. C., Wessner, H., Volkmer, R., Höhne, W. E., & Kühn, H. (2010) · Immunology Letters · doi:10.1016/j.imlet.2010.07.006 · Cited by 6

Role of iron overload and ferroptosis in heart disease

Cai, Z., Min, J., Wang, H., Fang, X., & Wang, F. (2019) · Chinese Science Bulletin (Chinese Version) · doi:10.1360/tb-2019-0242 · Cited by 6

Moonlighting in drug metabolism

Philip G. Board, & Anders, M. W. (2020) · Drug Metabolism Reviews · doi:10.1080/03602532.2020.1858857 · Cited by 6

Thiol- and selenol-based peroxidases: Structure and catalytic properties

Trujillo, M., Tairum, C. A., de Oliveira, M. A., & Netto, L. E. S. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90219-9.00008-x · Cited by 6

Synthesis of Nanovesicular Glutathione Peroxidase Mimics with a Selenenylsulfide-Bearing Lipid

Haratake, M., Tachibana, Y., Emaya, Y., Yoshida, S., Fuchigami, T., & Nakayama, M. (2016) · ACS Omega · doi:10.1021/acsomega.6b00046 · Cited by 6

The Molecular Interplay Between p53-Mediated Ferroptosis and Non-Coding RNAs in Cancer

Punziano, C., Trombetti, S., Grosso, M., Tornesello, M. L., & Faraonio, R. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26146588 · Cited by 5

Rottlerin triggers dual degradation of SLC7A11 and GPX4 to drive ferroptosis and chemosensitization in hepatocellular carcinoma

Luo, H., Jin, X., Gao, C., Deng, Q., Han, L., Hu, F., Tong, R., Li, D. G., Yang, H., & Bian, X. (2026) · Cell Death Discovery · doi:10.1038/s41420-026-02942-1 · Cited by 5

The Role of Ferroptosis in Diabetes Pathogenesis: Therapeutic Implications of Hydrogen Sulfide and Its Reactive Metabolites

Otašević, V., Markelic, M. B., Miler, M., Savić, N., Veličković, K., Gudelj, A., Grigorov, I., & Stancic, A. (2026) · Antioxidants · doi:10.3390/antiox15030369 · Cited by 5

Study of age-related changes in plasma metabolites and enzyme activity of healthy small dogs that underwent medical checkups

Kusaba, A., Tago, E., KUSABA, H., & Kawasumi, K. (2024) · Frontiers in Veterinary Science · doi:10.3389/fvets.2024.1437805 · Cited by 5

Food-derived compounds targeting ferroptosis for cancer therapy: from effects to mechanisms

Zhao, J.-W., Zhao, W., & Yu, Z. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1568391 · Cited by 5

Selenocysteine biosynthesis and mechanism of incorporation into growing proteins

Varlamova, E. G., Goltyaev, M. V., Novoselov, S. V., Novoselov, V. I., & Fesenko, E. E. (2013) · Molecular Biology · doi:10.1134/s0026893313040134 · Cited by 5

A Mouse Model of Sporadic Alzheimer’s Disease with Elements of Major Depression

Бобкова, Н. В., Chuvakova, L. N., Kovalev, V. I., Zhdanova, D. Y., Chaplygina, A. V., Rezvykh, A. P., & Evgen’ev, M. B. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04346-7 · Cited by 5

Ultrasound combined with FeSO4 facilitated the occurrence of ferroptosis in Vibrio parahaemolyticus

Peng, S., Yao, L., Zhu, X., Ge, W., Deng, J., Li, H., Xu, D., Hu, L., & Mo, H. (2024) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2024.107080 · Cited by 5

Manipulating Redox Signaling to Block Tumor Angiogenesis

Mugoni, V., & Mattia, M. (2013) · InTech eBooks · doi:10.5772/54593 · Cited by 7

Window of Opportunity for Neuroprotection with an Antioxidant, A llene O xide S ynthase, after Hypoxia–Ischemia in Adult Male Rats

Mathai, S., Gunn, A. J., Backhaus, R. A., & Guan, J. (2012) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12004 · Cited by 5

Expression Silencing of Glutathione Peroxidase 4 in Mouse Erythroleukemia Cells Delays In Vitro Erythropoiesis

Rademacher, M., Kühn, H., & Borchert, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22157795 · Cited by 5

Glutathione Peroxidases

Mishima, E., & Conrad, M. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-95488-4.00009-7 · Cited by 5

When Pathways Converge: Iron, Lipid Peroxidation, and α‐Synuclein in Ferroptosis‐Driven Dopaminergic Neurodegeneration

Sperlich, C. L., Stockwell, B. R., & Farina, M. (2026) · Journal of Neurochemistry · doi:10.1111/jnc.70438 · Cited by 5

Therapeutic exploitation of ferroptosis

Walravens, M., Koeken, I., & Berghe, T. V. (2024) · Biochemical Society Transactions · doi:10.1042/bst20230550 · Cited by 5

Iron and Selenium: At the Crossroads of Development and Death in Oligodendrocytes

Ma, C., Wurlitzer, K., Nunes, L. G. A., Hoffmann, P. R., & Pitts, M. W. (2025) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2025.110509 · Cited by 5

Ferroptosis: Physiological and pathophysiological aspects

Conrad, M., & da Silva, M. C. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-818606-0.00010-9 · Cited by 4

Hydroxycitric acid inhibits ferroptosis and ameliorates benign prostatic hyperplasia by upregulating the Nrf2/GPX4 pathway

Yang, D., Zhai, C., Ren, J., Bai, J., Li, T., Lu, M. L., Tang, Y., Wei, L., Luo, R., & Tong, F. (2025) · World Journal of Urology · doi:10.1007/s00345-025-05637-x · Cited by 4

Glutathione Peroxidase 4 and Ferroptosis

Angeli, J. P. F., Proneth, B., & Conrad, M. (2016) · Springer eBooks · doi:10.1007/978-3-319-41283-2_43 · Cited by 4

Embryonic cell migratory capacity is impaired upon exposure to glucose in vivo and in vitro

Herion, N. J., Krüger, C., Staszkiewicz, J., Kappen, C., & Salbaum, J. M. (2018) · Birth Defects Research · doi:10.1002/bdr2.1398 · Cited by 4

Gpx4 and Ferroptosis

Ran, Q., & Mozolewska, P. (2019) · Springer eBooks · doi:10.1007/978-3-030-26780-3_6 · Cited by 4

Maternal cholecalciferol supplementation during gestation improves antioxidant capacities in gilts and piglets

Zhao, L., Mao, Z., Mou, D., Huang, L. S., Yang, M., Ding, D., Yan, H., Fang, Z., Che, L., Zhuo, Y., et al. (2021) · Italian Journal of Animal Science · doi:10.1080/1828051x.2021.1961616 · Cited by 4

Compartmentation of Redox Signaling and Control: Discrimination of Oxidative Stress in Mitochondria, Cytoplasm, Nuclei, and Endoplasmic Reticulum

Halvey, P. J., Hansen, J. M., Lash, L. H., & Jones, D. P. (2008) · Wiley eBooks · doi:10.1002/9780470372531.ch18 · Cited by 4

Thioredoxin and glutaredoxin systems under oxidative and nitrosative stress

Ren, X. (2017) · Figshare · Cited by 4

Teneligliptin, a DPP4 inhibitor protects dopaminergic neurons in PD models via inhibiting of oxidative stress and ferroptosis

Huang, L., Pi, J., Gu, L., Liao, Z., & Wang, W. (2025) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2025.177782 · Cited by 5

MNQ derivative D19 alleviates LPS-induced inflammation and oxidative stress in sheep follicular granulosa cells through the GPX4-mediated ferroptosis

Chen, C., Lu, J., Qu, Y., Dong, J., Hong, Y., Ren, Y., Jiang, S., Baptista, R., Wang, D., Mur, L. A. J., et al. (2025) · Frontiers in Veterinary Science · doi:10.3389/fvets.2025.1621738 · Cited by 3

Ferroptosis-related stress during aging and its relevance to disease

Maher, P. A., Soriano‐Castell, D., Dar, N. J., Soriano, S., & Currais, A. J. M. (2025) · GeroScience · doi:10.1007/s11357-025-01929-7 · Cited by 6

Mitochondrial non-energetic function and embryonic cardiac development

Shi, J., Jin, Y., Lin, S., Li, X., Zhang, D., Wu, J., Qi, Y., & Li, Y. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1475603 · Cited by 4

Mechanistic Insights Into the Role of Selenoprotein M in Nickel-Induced Lung Fibrosis

Guan, H., Sun, Y., Qiao, S., Li, D., Cai, J., & Zhang, Z. (2025) · Biological Trace Element Research · doi:10.1007/s12011-025-04636-8 · Cited by 3

Selenium

Alexander, J. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-822946-0.00035-0 · Cited by 3

Insulin-like growth factor-1 (IGF-1) selectively modulates the metabolic and lipid profile of bovine embryos according to their kinetics of development

Annes, K., de Lima, C. B., Ispada, J., dos Santos, É. C., Fontes, P. K., Nichi, M., Nogueira, M. F. G., Sudano, M. J., & Milazzotto, M. P. (2023) · Theriogenology · doi:10.1016/j.theriogenology.2023.03.020 · Cited by 3

Role of Oxidative Stress in Aging

Knoefler, D., Tienson, H. L., & Jakob, U. (2013) · Springer eBooks · doi:10.1007/978-94-007-5787-5_14 · Cited by 3

Medium-chain triglycerides reduce glomerulosclerosis and induce expression of redox genes in NSY mice with diabetic nephropathy

Hagiwara, M., Ishiyama, S., & Mochizuki, K. (2022) · PharmaNutrition · doi:10.1016/j.phanu.2022.100325 · Cited by 3

Selenium: Roles in Cancer Prevention and Therapies

Geng, X., Liu, L., Tsai, K.-J., & Liu, Z. (2017) · Molecular and integrative toxicology · doi:10.1007/978-3-319-55448-8_3 · Cited by 3

Mouse Models for Glutathione Peroxidase 4 (GPx4)

Conrad, M. (2011) · Springer eBooks · doi:10.1007/978-1-4614-1025-6_43 · Cited by 3

Schizophrenia, Oxidative Stress and Selenium

Pitts, M. W., Raman, A. V., & Berry, M. J. (2011) · Springer eBooks · doi:10.1007/978-1-4614-1025-6_28 · Cited by 3

Probing the in Vivo Relevance of Oxidative Stress in Aging Using Knockout and Transgenic Mice

Müller, F. L., Mele, J., Remmen, H. V., & Richardson, A. G. (2003) · Springer eBooks · doi:10.1007/978-94-017-0667-4_10 · Cited by 3

Baseline Selenium and Prostate Cancer Risk: Comments and Open Questions

Frankel, P. H., Parker, R. S., Madsen, F. C., & Whanger, P. D. (2014) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/dju005 · Cited by 3

Dissertation zur Erlangung des Doktorgrades der Fakultät für Biologie

München, L.-M.-U. (2013) · Cited by 3

Repression of ferroptotic cell death by mitochondrial calcium signalingPreprint

Wen, H., Chen, J., Zhao, B. L., Wang, S., Ma, A., Dong, H., Cheng, X., Lin, S., Li, X., Herring, L. E., et al. (2023) · Research Square · doi:10.21203/rs.3.rs-3029860/v1 · Cited by 3

Renal Epithelial Mitochondria: Implications for Hypertensive Kidney Disease

Stadler, K., & Ilatovskaya, D. V. (2023) · Comprehensive physiology · doi:10.1002/cphy.c220033 · Cited by 12

Enhancing Challenging Target Screening via Multimodal Protein-Ligand Contrastive LearningPreprint

Wang, Z., Wang, Z., Yang, M., Pang, L., Nie, F., Liu, S., Gao, Z., Zhao, G., Ji, X., Huang, D., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.22.609123 · Cited by 6

Lipid peroxidation intrinsically induces mitochondrial iron overload via Bach1-HO-1 signaling to promote cardiac ferroptosisPreprint

Guo, X., Chen, Y., Zeng, Y., Mo, X., Hong, S., He, H., Li, J., Zhang, K. S., & Liu, Q. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.15.682717 · Cited by 4

Overburdened ferroptotic stress impairs tooth morphogenesis

Wang, H., Wang, X., Huang, L., Wang, C., Yu, F., & Ye, L. (2023) · eLife · doi:10.7554/elife.88745 · Cited by 2

In Vitro Maturation of Bovine Oocytes in the Presence of Resveratrol and Ellagic Acid but Not Chlorogenic Acid Modulates Blastocyst Antioxidant Gene Expression Without Impacting Embryo Development and Oxygen Consumption

Giller, K., Schmid, D., Şerbetçi, İ., Meleán, M., Greve, S., von Meyenn, F., Bollwein, H., & Herrera, C. (2025) · Antioxidants · doi:10.3390/antiox14060621 · Cited by 2

Emerging paradigms in redox regulation: the role of selenoproteins in normal and malignant hematopoiesis

Aoyama, Y., Yamazaki, H., & Inoue, D. (2025) · Experimental Hematology · doi:10.1016/j.exphem.2025.105346 · Cited by 3

Caspase-3/7 deficiency results in enhanced intestinal inflammation and reduced tumorigenesis

Xie, W., Wyckaert, L., Vadi, M., Verstraeten, B., Divert, T., Haerinck, J., Rycke, R. M. D., Baeke, F., Lamkanfi, M., Berx, G., et al. (2026) · Science Advances · doi:10.1126/sciadv.adz5906 · Cited by 2

HCN2, NRTN, CAPS and GPX4 genes are not associated with simple febrile seizures in Chinese Han population

Yinan, M., Zhiyue, C., Liping, Z., Fang, F., Liwen, W., Song, F., Zhang, J., Dingfang, B., Tianjun, W., Qing, L., et al. (2015) · Journal of Pediatric Neurology · doi:10.1055/s-0035-1557316 · Cited by 2

Transcriptome Profiling Reveals the Response of Seed Germination of Peganum harmala to Drought Stress

Zhang, Z., Su, H., Li, Q., & Li, M. (2024) · Plants · doi:10.3390/plants13121649 · Cited by 2

Cellular Signaling by Reactive Oxygen Species: Biochemical Basis and Physiological Scope

Tolédano, M. B., Fourquet, S., & D’Autréaux, B. (2009) · Springer eBooks · doi:10.1007/978-3-642-02112-1_17 · Cited by 2

The regulation of LIV‐1 mRNA in MDA‐MB‐231 human breast cancer cells and its association with E‐cadherin

Chong, L., Sankavaram, K., & Freake, H. C. (2010) · The FASEB Journal · doi:10.1096/fasebj.24.1_supplement.928.5 · Cited by 2

The Use of Gpx4 Knockout Mice and Transgenic Mice to Study the Roles of Lipid Peroxidation in Diseases and Aging

Ran, Q., & Liang, H. (2011) · Humana Press eBooks · doi:10.1007/978-1-60761-956-7_12 · Cited by 2

Selenoproteins in Nervous System Development, Function, and Degeneration

Schweizer, U. (2011) · Springer eBooks · doi:10.1007/978-1-4614-1025-6_18 · Cited by 2

Antithetical Roles of Reactive Oxygen Species in Mammalian Reproduction

Fujii, J., Tsunoda, S., & Kimura, N. (2014) · Springer eBooks · doi:10.1007/978-3-642-30018-9_108 · Cited by 2

Selenium and Neurodevelopment

Fradejas‐Villar, N., & Schweizer, U. (2018) · Molecular and integrative toxicology · doi:10.1007/978-3-319-95390-8_9 · Cited by 3

Prolonged maternal exposure to glucocorticoids alters selenoprotein expression in the developing brain

Toh, P., Seale, L. A., Berry, M. J., & Torres, D. J. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1115993 · Cited by 2

The Association of Measures of the Micro- and Macro-Vasculature with Selenium and GPx Activity in a Young Bi-Ethnic Population: The African-PREDICT Study

Swart, R., Schutte, A. E., van Rooyen, J. M., Smith, W. T., & Mels, C. M. C. (2019) · Journal of the American College of Nutrition · doi:10.1080/07315724.2019.1570479 · Cited by 2

Selenoproteins in Cellular Redox Regulation and Signaling

Raman, A. V., & Berry, M. J. (2011) · Wiley eBooks · doi:10.1002/9781118148143.ch14 · Cited by 2

Untersuchungen zur Diagnostik der Selenversorgung von Milchkühen

Raven, J. (2014) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-11580 · Cited by 2

Oxidative stress sensing by the translation elongation machinery promotes production of detoxifying selenoproteinsPreprint

Rehfeld, F., Lundstrom, C., Zhang, H., & Mendell, J. T. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.13.682107 · Cited by 3

The Ongoing Search for a Biomarker of Ferroptosis

Kolbrink, B., von Samson‐Himmelstjerna, F. A., Riebeling, T., Schulte, K., & Krautwald, S. (2023) · Springer eBooks · doi:10.1007/978-3-031-39171-2_6 · Cited by 1

l-cysteine rescues radiation induced ferroptosis and boosts wound healing through fibroblasts proliferation and migration.

Yang, M., Huang, C.-L., Luo, W., Gong, P., Huang, B., & Yao, Y. (2025) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2025.152599 · Cited by 1

Analysis of the Correlation Between Depression-like Behaviors and Lipid Peroxidation in the Prefrontal Cortex of Mice: The Impact of Early Life Stress

Mi, X., Ye, Z.-L., Zhang, X., Dai, X., & Luo, Z. (2025) · Brain Sciences · doi:10.3390/brainsci15101112 · Cited by 1

Ferroptosis in biliary tract cancer: Molecular mechanisms and therapeutic applications (Review)

Zou, R.-Q., Dai, Y.-S., Yang, S., Hu, H., Li, F., & Liu, F. (2025) · International Journal of Oncology · doi:10.3892/ijo.2025.5819 · Cited by 2

EEFSEC deficiency underlies a human selenopathy with primary neurodevelopmental origins via midbrain-hindbrain hypoplasia

Xia, Z., Hui, L. I. U., Guo, P., Chen, C., Ge, L., Tang, L., Zhang, Y., & Ma, Y. (2026) · Human Genetics and Genomics Advances · doi:10.1016/j.xhgg.2026.100563 · Cited by 2

Evaluation of urine glutathione peroxidase 4 in cats with chronic kidney disease

Hsu, W.-L., Huang, S.-H., Hseu, Z.-Y., Wu, V., Chen, Y., & Lee, Y.-J. (2026) · Frontiers in Veterinary Science · doi:10.3389/fvets.2025.1756038 · Cited by 1

Sodium propionate alleviates bronchopulmonary dysplasia by inhibiting ferroptosis through the SLC7A11/GPX4 pathway in pulmonary endothelial cells

Xie, A., Chen, X., Bao, Z., Yu, P., & Yu, R. (2026) · Respiratory Research · doi:10.1186/s12931-026-03535-3 · Cited by 1

Ten controversies defining the boundaries of ferroptosis

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