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

Role of selenium in male reproduction—A review

Ahsan, U., Kamran, Z., Raza, I., Ahmad, S., Babar, W., Riaz, M. H., & Iqbal, Z. (2014) · Animal Reproduction Science · doi:10.1016/j.anireprosci.2014.01.009 · Cited by 269

Zinc attenuates ferroptosis and promotes functional recovery in contusion spinal cord injury by activating Nrf2/GPX4 defense pathway

Ge, M., Tian, H., Mao, L., Li, D., Lin, J., Hu, H., Huang, S., Zhang, C., & Mei, X. (2021) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13657 · Cited by 273

Composition and Evolution of the Vertebrate and Mammalian Selenoproteomes

Mariotti, M., Ridge, P. G., Zhang, Y., Lobanov, A. V., Pringle, T. H., Guigó, R., Hatfield, D. L., & Gladyshev, V. N. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033066 · Cited by 261

Hierarchical regulation of selenoprotein expression and sex-specific effects of selenium

Schomburg, L., & Schweizer, U. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.03.015 · Cited by 261

Ferroptosis: when metabolism meets cell death

Zheng, J., & Conrad, M. (2024) · Physiological Reviews · doi:10.1152/physrev.00031.2024 · Cited by 286

Transgenic Mice Overexpressing Glutathione Peroxidase 4 Are Protected against Oxidative Stress-induced Apoptosis*

Ran, Q.-T., Liang, H.-Y., Gu, M., Qi, W., Walter, C., Roberts, L., Herman, B., Richardson, A., & Remmen, H. V. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410387200 · Cited by 242

Mitochondria: a hub of redox activities and cellular distress control

Kakkar, P., & Singh, B. K. (2007) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-007-9520-8 · Cited by 255

TrxR1 as a Potent Regulator of the Nrf2-Keap1 Response System

Cebula, M., Schmidt, E. E., & Arnér, E. S. J. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6378 · Cited by 251

Gpx4 ablation in adult mice results in a lethal phenotype accompanied by neuronal loss in brain

Yoo, S.-E., Chen, L., Na, R., Liu, Y., Rios, C. I., Remmen, H. V., Richardson, A. G., & Ran, Q. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.043 · Cited by 256

Epididymis seleno-independent glutathione peroxidase 5 maintains sperm DNA integrity in mice

Chabory, E., Damon‐Soubeyrand, C., Lenoir, A., Kauselmann, G., Kern, H., Zevnik, B., Garrel, C., Saez, F., Cadet, R., Henry-Berger, J., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38940 · Cited by 250

Glutathione peroxidase 4 prevents necroptosis in mouse erythroid precursors

Canli, Ö., Alankuş, Y. B., Grootjans, S., Vegi, N., Hültner, L., Hoppe, P. S., Schroeder, T., Vandenabeele, P., Bornkamm, G. W., & Greten, F. R. (2016) · Blood · doi:10.1182/blood-2015-06-654194 · Cited by 247

Human selenoproteins at a glance

Gromer, S., Eubel, J., Lee, B. L., & Jacob, J. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5143-y · Cited by 250

Role of Selenium on Calcium Signaling and Oxidative Stress-induced Molecular Pathways in Epilepsy

Nazıroğlu, M. (2009) · Neurochemical Research · doi:10.1007/s11064-009-0015-8 · Cited by 241

Is the Mitochondrial Free Radical Theory of Aging Intact?

Sanz, A., Pamplona, R., & Barja, G. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.582 · Cited by 245

Neuronal selenoprotein expression is required for interneuron development and prevents seizures and neurodegeneration

Wirth, E. K., Conrad, M., Winterer, J., Wozny, C., Carlson, B. A., Roth, S., Schmitz, D., Bornkamm, G. W., Coppola, V., Tessarollo, L., et al. (2010) · The FASEB Journal · doi:10.1096/fj.09-143974 · Cited by 237

Depletion of Selenoprotein GPx4 in Spermatocytes Causes Male Infertility in Mice

Imai, H., Hakkaku, N., Iwamoto, R., Suzuki, J., Suzuki, T., Tajima, Y., Konishi, K., Minami, S., Ichinose, S., Ishizaka, K., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.016139 · Cited by 235

The in vivo gene expression signature of oxidative stress

Han, E., Müller, F. L., Pérez, V., Qi, W., Liang, H., Liang, X., Fu, C., Doyle, E., Hickey, M., Cornell, J. E., et al. (2008) · Physiological Genomics · doi:10.1152/physiolgenomics.00239.2007 · Cited by 236

Crystal Structure and Catalysis of the Selenoprotein Thioredoxin Reductase 1

Cheng, Q., Sandalova, T., Lindqvist, Y., & Arnér, E. S. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807068200 · Cited by 227

An integrated view of lipid metabolism in ferroptosis revisited via lipidomic analysis

Kim, J. W., Lee, J.-Y., Oh, M., & Lee, E. (2023) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-01077-y · Cited by 251

Adaptive homeostasis and the free radical theory of ageing

Pomatto, L. C. D., & Davies, K. J. A. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.06.016 · Cited by 233

Metabolic cell death in cancer: ferroptosis, cuproptosis, disulfidptosis, and beyond

Mao, C., Wang, M., Zhuang, L., & Gan, B. (2024) · Protein & Cell · doi:10.1093/procel/pwae003 · Cited by 237

Rescuing replication and osteogenesis of aged mesenchymal stem cells by exposure to a young extracellular matrix

Sun, Y., Li, W., Lu, Z., Chen, R., Ling, J., Ran, Q., Jilka, R. L., & Chen, X. (2011) · The FASEB Journal · doi:10.1096/fj.10-161497 · Cited by 212

What Is Responsible for the Initiating Chemistry of Iron-Mediated Lipid Peroxidation: An Update

Cheng, Z., & Li, Y. (2007) · Chemical Reviews · doi:10.1021/cr040077w · Cited by 211

GPX4 and vitamin E cooperatively protect hematopoietic stem and progenitor cells from lipid peroxidation and ferroptosis

Hu, Q., Zhang, Y., Lou, H., Ou, Z., Liu, J., Duan, W., Wang, H., Ge, Y., Min, J., Wang, F., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04008-9 · Cited by 219

Ferroptosis: A flexible constellation of related biochemical mechanisms

Dixon, S. J., & Pratt, D. A. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.03.005 · Cited by 219

Role for Selenium in Metabolic Homeostasis and Human Reproduction

Mojadadi, A., Au, A., Salah, W., Witting, P. K., & Ahmad, G. (2021) · Nutrients · doi:10.3390/nu13093256 · Cited by 209

Mice deficient in both Mn superoxide dismutase and glutathione peroxidase-1 have increased oxidative damage and a greater incidence of pathology but no reduction in longevity

Zhang, Y., Ikeno, Y., Qi, W., Chaudhuri, A., Li, Y., Bokov, A., Thorpe, S. R., Baynes, J. W., Epstein, C., Richardson, A., et al. (2009) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/glp132 · Cited by 172

Cooperative function of antioxidant and redox systems against oxidative stress in male reproductive tissues.

Fujii, J., Iuchi, Y., Matsuki, S., & Ishii, T. (2003) · PubMed · Cited by 205

SLC7A11 as a Gateway of Metabolic Perturbation and Ferroptosis Vulnerability in Cancer

Lee, J., & Roh, J. (2022) · Antioxidants · doi:10.3390/antiox11122444 · Cited by 213

Selenium and selenoproteins in mammals: extraordinary, essential, enigmatic

Schomburg, L., Schweizer, U., & Köhrle, J. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4114-z · Cited by 203

B1 and marginal zone B cells but not follicular B2 cells require Gpx4 to prevent lipid peroxidation and ferroptosis

Muri, J., Thut, H., Bornkamm, G. W., & Kopf, M. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.10.070 · Cited by 198

Redox Control Systems in the Nucleus: Mechanisms and Functions

Go, Y., & Jones, D. P. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3021 · Cited by 205

Gene expression changes in mouse brain after exposure to low‐dose ionizing radiation

Yin, E., Nelson, D. O., Coleman, M. A., Peterson, L. E., & Wyrobek, A. J. (2003) · International Journal of Radiation Biology · doi:10.1080/09553000310001610961 · Cited by 206

Reduction in glutathione peroxidase 4 increases life span through increased sensitivity to apoptosis

Ran, Q., Liang, H., Ikeno, Y., Qi, W., Prolla, T. A., Roberts, L. J., Wolf, N., VanRemmen, H., & Richardson, A. (2007) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/62.9.932 · Cited by 195

Selenium and GPX4, a vital symbiosis

Angeli, J. P. F., & Conrad, M. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.03.001 · Cited by 197

Oxidative stress and cell death

Rumora, L., Petrik, J., & Žanić‐Grubišić, T. (2003) · Cited by 192

Glutathione peroxidase 4 overexpression inhibits ROS-induced cell death in diffuse large B-cell lymphoma

Kinowaki, Y., Kurata, M., Ishibashi, S., Ikeda, M., Tatsuzawa, A., Yamamoto, M., Miura, O., Kitagawa, M., & Yamamoto, K. (2018) · Laboratory Investigation · doi:10.1038/s41374-017-0008-1 · Cited by 194

Short Form Glutathione Peroxidase 4 Is the Essential Isoform Required for Survival and Somatic Mitochondrial Functions

Liang, H., Yoo, S.-E., Na, R., Walter, C. A., Richardson, A., & Ran, Q. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.032839 · Cited by 191

Vitamin E hydroquinone is an endogenous regulator of ferroptosis via redox control of 15-lipoxygenase

Hinman, A., Holst, C. R., Latham, J. C., Bruegger, J. J., Ulas, G., McCusker, K. P., Amagata, A., Davis, D., Hoff, K. G., Kahn-Kirby, A. H., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0201369 · Cited by 194

Glutathione Peroxidase-1 Regulates Mitochondrial Function to Modulate Redox-dependent Cellular Responses

Handy, D. E., Lubos, E., Yang, Y., Galbraith, J. D., Kelly, N., Zhang, Y.-Y., Leopold, J. A., & Loscalzo, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900392200 · Cited by 187

Reactive oxygen species: A radical role in development?

Hernández-García, D., Wood, C. D., Castro‐Obregón, S., & Covarrubias, L. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.03.020 · Cited by 199

Selenium and Alzheimer's Disease: A Systematic Review

Loef, M., Schrauzer, G. N., & Walach, H. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110414 · Cited by 182

The selenoproteome exhibits widely varying, tissue-specific dependence on selenoprotein P for selenium supply

Hoffmann, P. R., Hoge, S., Li, P.-A., Hoffmann, F. W., Hashimoto, A. C., & Berry, M. J. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm355 · Cited by 181

The Role of Antioxidant Enzymes in the Ovaries

Wang, S., He, G., Chen, M., Zuo, T., Xu, W., & Liu, X. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/4371714 · Cited by 180

Creatine kinase B suppresses ferroptosis by phosphorylating GPX4 through a moonlighting function

Wu, K., Yan, M., Liu, T., Wang, Z., Duan, Y., Xia, Y., Ji, G., Shen, Y., Wang, L., Li, L., et al. (2023) · Nature Cell Biology · doi:10.1038/s41556-023-01133-9 · Cited by 189

Glutathione peroxidase 4 (Gpx4) and ferroptosis: what's so special about it?

Conrad, M., & Angeli, J. P. F. (2015) · Molecular & Cellular Oncology · doi:10.4161/23723556.2014.995047 · Cited by 187

Recommendations for robust and reproducible research on ferroptosis

Mishima, E., Nakamura, T., Doll, S. G., Proneth, B., Fedorova, M., Pratt, D. A., Angeli, J. P. F., Dixon, S. J., Wahida, A., & Conrad, M. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-025-00843-2 · Cited by 211

Implications of Oxidative Stress and Cell Membrane Lipid Peroxidation in Human Cancer (Spain)

Cejas, P., Casado, E., Belda-Iniesta, C., de Castro, J., Espinosa, E., Redondo, A., Sereno, M., García‐Cabezas, M. Á., Vara, J. Á. F., Domínguez-Cáceres, A., et al. (2004) · Cancer Causes & Control · doi:10.1023/b:caco.0000036189.61607.52 · Cited by 179

Selenoproteins and Their Impact on Human Health Through Diverse Physiological Pathways

Moghadaszadeh, B., & Beggs, A. H. (2006) · Physiology · doi:10.1152/physiol.00021.2006 · Cited by 176

Programmed Necrosis and Disease:We interrupt your regular programming to bring you necroinflammation

Kim, E. H., Wong, S., & Martinez, J. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0179-3 · Cited by 181

Specific Excision of the Selenocysteine tRNA[Ser]Sec (Trsp) Gene in Mouse Liver Demonstrates an Essential Role of Selenoproteins in Liver Function

Carlson, B. A., Novoselov, S. V., Kumaraswamy, E., Lee, B. J., Anver, M. R., Gladyshev, V. N., & Hatfield, D. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310470200 · Cited by 177

Selenocysteine Incorporation Machinery and the Role of Selenoproteins in Development and Health

Hatfield, D. L., Carlson, B. A., Xu, X., Mix, H., & Gladyshev, V. N. (2006) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(06)81003-2 · Cited by 175

Gene expression profiling of aging reveals activation of a p53-mediated transcriptional program

Edwards, M. G., Anderson, R. M., Yuan, M., Kendziorski, C. M., Weindruch, R., & Prolla, T. A. (2007) · BMC Genomics · doi:10.1186/1471-2164-8-80 · Cited by 174

Interference of selenium and selenoproteins with the insulin-regulated carbohydrate and lipid metabolism

Steinbrenner, H. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.016 · Cited by 177

Glutathione Peroxidase 4 is associated with Neuromelanin in Substantia Nigra and Dystrophic Axons in Putamen of Parkinson's brain

Bellinger, F. P., Bellinger, M. T., Seale, L. A., Takemoto, A. S., Raman, A. V., Miki, T., Manning-Bog, A., Berry, M. J., White, L. R., & Ross, G. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-8 · Cited by 173

Oxr1 Is Essential for Protection against Oxidative Stress-Induced Neurodegeneration

Oliver, P. L., Finelli, M. J., Edwards, B., Bitoun, E., Butts, D. L., Becker, E. B. E., Cheeseman, M. T., Davies, B., & Davies, K. E. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002338 · Cited by 172

Mitochondria-specific transgenic overexpression of phospholipid hydroperoxide glutathione peroxidase (GPx4) attenuates ischemia/reperfusion-associated cardiac dysfunction

Dabkowski, E. R., Williamson, C. L., & Hollander, J. M. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.06.021 · Cited by 171

Selenium in mammalian spermiogenesis

Flohé, L. (2007) · Biological Chemistry · doi:10.1515/bc.2007.112 · Cited by 170

A promising new approach to cancer therapy: Targeting iron metabolism in cancer stem cells

El-Hout, M., Santos, L. D., Hamaï, A., & Mehrpour, M. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.07.009 · Cited by 173

Regulation of the selenoprotein SelS by glucose deprivation and endoplasmic reticulum stress – SelS is a novel glucose‐regulated protein

Gao, Y., Feng, H. C., Walder, K. R., Bolton, K. A., Sunderland, T., Bishara, N., Quick, M., Kantham, L., & Collier, G. R. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00296-0 · Cited by 165

IFNγ-mediated repression of system xc− drives vulnerability to induced ferroptosis in hepatocellular carcinoma cells

Kong, R., Wang, N., Han, W., Bao, W., & Lu, J. (2021) · Journal of Leukocyte Biology · doi:10.1002/jlb.3ma1220-815rrr · Cited by 164

Loss of the Oxidative Stress Sensor NPGPx Compromises GRP78 Chaperone Activity and Induces Systemic Disease

Wei, P., Hsieh, Y., Su, M.-I., Jiang, X., Hsu, P., Lo, W., Weng, J.-Y., Jeng, Y., Wang, J., Chen, P., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.10.007 · Cited by 159

Combined Deficiency in Glutathione Peroxidase 4 and Vitamin E Causes Multiorgan Thrombus Formation and Early Death in Mice

Wortmann, M., Schneider, M., Pircher, J., Hellfritsch, J., Aichler, M., Naidu, V. M., Kölle, P., Kuhlencordt, P., Walch, A. K., Pohl, U., et al. (2013) · Circulation Research · doi:10.1161/circresaha.113.279984 · Cited by 163

To eat or not to eat — the metabolic flavor of ferroptosis

Gao, M., & Jiang, X. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.11.001 · Cited by 160

The roles of glutathione peroxidases during embryo development

Ufer, C. (2011) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2011.00012 · Cited by 168

Role of Se-dependent glutathione peroxidases in gastrointestinal inflammation and cancer

Chu, F., Esworthy, R. S., & Doroshow, J. H. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.04.010 · Cited by 160

Ferroptosis and Brain Injury

Magtanong, L., & Dixon, S. J. (2018) · Developmental Neuroscience · doi:10.1159/000496922 · Cited by 156

Knowledge Domain and Emerging Trends in Ferroptosis Research: A Bibliometric and Knowledge-Map Analysis

Zhang, J., Song, L., Xu, L., Fan, Y., Wang, T., Tian, W., Ju, J., & Xu, H. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.686726 · Cited by 153

Targeting Ferroptosis: New Hope for As-Yet-Incurable Diseases

Conrad, M., Lorenz, S., & Proneth, B. (2020) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2020.08.010 · Cited by 155

Mitochondrial outer membrane protein FUNDC2 promotes ferroptosis and contributes to doxorubicin-induced cardiomyopathy

Ta, N., Qu, C., Wu, H., Zhang, D., Sun, T., Li, Y., Wang, J., Wang, X., Tang, T.-S., Chen, Q., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2117396119 · Cited by 151

Selenoproteins and Protection against Oxidative Stress: Selenoprotein N as a Novel Player at the Crossroads of Redox Signaling and Calcium Homeostasis

Arbogast, S., & Ferreiro, A. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2890 · Cited by 167

Epigenetic effects of selenium and their implications for health

Speckmann, B., & Grune, T. (2015) · Epigenetics · doi:10.1080/15592294.2015.1013792 · Cited by 146

Delineating the Role of Glutathione Peroxidase 4 in Protecting Cells Against Lipid Hydroperoxide Damage and in Alzheimer's Disease

Yoo, M., Gu, X., Xu, X.-M., Kim, J. Y., Carlson, B. A., Patterson, A. D., Cai, H., Gladyshev, V. N., & Hatfield, D. L. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2891 · Cited by 148

Targeting GPX4 in human cancer: Implications of ferroptosis induction for tackling cancer resilience

Lee, J., & Roh, J. (2023) · Cancer Letters · doi:10.1016/j.canlet.2023.216119 · Cited by 152

Hepatic selenoprotein P (SePP) expression restores selenium transport and prevents infertility and motor-incoordination in Sepp -knockout mice

Renko, K., Werner, M., Renner‐Müller, I., Cooper, T. G., Yeung, C. H., Hollenbach, B., Scharpf, M. O., Köhrle, J., Schomburg, L., & Schweizer, U. (2008) · Biochemical Journal · doi:10.1042/bj20071172 · Cited by 146

Mitochondria as a source and target of lipid peroxidation products in healthy and diseased heart

Anderson, E. J., Katunga, L. A., & Willis, M. S. (2011) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2011.05641.x · Cited by 146

Mammalian glutathione peroxidases control acquisition and maintenance of spermatozoa integrity 1

Chabory, E., Damon‐Soubeyrand, C., Lenoir, A., Henry-Berger, J., Vernet, P., Cadet, R., Saez, F., & Drevet, J. R. (2009) · Journal of Animal Science · doi:10.2527/jas.2009-2583 · Cited by 145

Reduced reliance on the trace element selenium during evolution of mammals

Lobanov, A. V., Hatfield, D. L., & Gladyshev, V. N. (2008) · Genome biology · doi:10.1186/gb-2008-9-3-r62 · Cited by 148

Role of Ferroptosis in Stroke

Xu, Y., Li, K., Zhao, Y., Zhou, L., Liu, Y., & Zhao, J. (2022) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-022-01196-6 · Cited by 151

Mycobacterium tuberculosis-macrophage interaction: Molecular updates

Bo, H., Moure, U. A. E., Yang, Y., Pan, J., Li, L., Wang, M., Ke, X., & Cui, H. (2023) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2023.1062963 · Cited by 157

Erastin, a ferroptosis-inducing agent, sensitized cancer cells to X-ray irradiation via glutathione starvation in vitro and in vivo

Shibata, Y., Yasui, H., Higashikawa, K., Miyamoto, N., & Kuge, Y. (2019) · PLoS ONE · doi:10.1371/journal.pone.0225931 · Cited by 150

Selective Rescue of Selenoprotein Expression in Mice Lacking a Highly Specialized Methyl Group in Selenocysteine tRNA

Carlson, B. A., Xu, X., Gladyshev, V. N., & Hatfield, D. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411725200 · Cited by 142

Redox Mechanisms in Neurodegeneration: From Disease Outcomes to Therapeutic Opportunities

Sbodio, J. I., Snyder, S. H., & Paul, B. D. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7321 · Cited by 149

Selenium: Tracing Another Essential Element of Ferroptotic Cell Death

Conrad, M., & Proneth, B. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.03.012 · Cited by 147

Nanozymes for regulation of reactive oxygen species and disease therapy

Dai, Y., Ding, Y., & Li, L. (2021) · Chinese Chemical Letters · doi:10.1016/j.cclet.2021.03.036 · Cited by 142

Physiological role of phospholipid hydroperoxide glutathione peroxidase in mammals

Conrad, M., Schneider, M., Seiler, A., & Bornkamm, G. W. (2007) · Biological Chemistry · doi:10.1515/bc.2007.130 · Cited by 136

Therapies targeting lipid peroxidation in traumatic brain injury

Anthonymuthu, T. S., Kenny, E., & Bayır, H. (2016) · Brain Research · doi:10.1016/j.brainres.2016.02.006 · Cited by 141

Ovarian Toxicity from Reactive Oxygen Species

Luderer, U. (2014) · Vitamins and hormones · doi:10.1016/b978-0-12-800095-3.00004-3 · Cited by 136

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