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

[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 · see citing works

Protein Oxidation in Aging, Disease, and Oxidative Stress

Berlett, B. S., & Stadtman, E. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.33.20313 · Cited by 3,339 · see citing works

NOX enzymes and the biology of reactive oxygen

Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125 · see citing works

The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen

Boveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626 · see citing works

Glutathione Peroxidase 4 Senses and Translates Oxidative Stress into 12/15-Lipoxygenase Dependent- and AIF-Mediated Cell Death

Seiler, A., Schneider, M., Förster, H., Roth, S., Wirth, E. K., Culmsee, C., Plesnila, N., Kremmer, E., Rådmark, O., Wurst, W., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.07.005 · Cited by 1,470 · see citing works

Mechanisms of Cell Death in Oxidative Stress

Ryter, S. W., Kim, H. P., Hoetzel, A., Park, J. W., Nakahira, K., Wang, X., & Choi, A. M. K. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.9.49 · Cited by 1,262 · see citing works

Hydrogen Peroxide: A Signaling Messenger

Stone, J. R., & Yang, S. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.243 · Cited by 1,175 · see citing works

Oxygen radicals and signaling

Finkel, T. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80147-6 · Cited by 1,170 · see citing works

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 · see citing works

Reversible Inactivation of the Tumor Suppressor PTEN by H2O2

Lee, S.-R., Yang, K., Kwon, J., Lee, C., Jeong, W., & Rhee, S. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111899200 · Cited by 1,061 · see citing works

Modulation of Protein Kinase Activity and Gene Expression by Reactive Oxygen Species and Their Role in Vascular Physiology and Pathophysiology

Griendling, K. K., Sorescu, D., Lassegue, B. P., & Ushio‐Fukai, M. (2000) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.20.10.2175 · Cited by 955 · see citing works

The glutathione peroxidases

Arthur, J. R. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000664 · Cited by 949 · see citing works

Xanthine oxidoreductase and cardiovascular disease: molecular mechanisms and pathophysiological implications

Berry, C. E., & Hare, J. M. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.055913 · Cited by 925 · see citing works

[5] Diversity of glutathione peroxidases

Maiorino, F. M., Brigelius‐Flohé, R., Aumann, K. D., Roveri, A., Schomburg, D., & Flohé, L. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)52007-4 · Cited by 854 · see citing works

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

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 · see citing works

Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins

Rhee, S. G., Kang, S. W., Jeong, W., Chang, T.-S., Yang, K., & Woo, H. A. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.02.004 · Cited by 709 · see citing works

Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors

Kwon, J., Lee, S.-R., Yang, K.-S., Ahn, Y., Kim, Y. J., Stadtman, E. R., & Rhee, S. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407396101 · Cited by 631 · see citing works

Redox regulation of PI 3‐kinase signalling via inactivation of PTEN

Leslie, N. R., Bennett, D., Lindsay, Y. E., Stewart, H., Gray, A., & Downes, C. P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg513 · Cited by 614 · see citing works

Direct evidence for tumor necrosis factor-induced mitochondrial reactive oxygen intermediates and their involvement in cytotoxicity.

Goossens, V., Grooten, J., Vos, K. J. D., & Fiers, W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.18.8115 · Cited by 595 · see citing works

Development of insulin resistance and obesity in mice overexpressing cellular glutathione peroxidase

McClung, J. P., Roneker, C. A., Mu, W., Lisk, D. J., Langlais, P., Liu, F., & Lei, X. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308096101 · Cited by 536 · see citing works

Mice with a Homozygous Null Mutation for the Most Abundant Glutathione Peroxidase, Gpx1, Show Increased Susceptibility to the Oxidative Stress-inducing Agents Paraquat and Hydrogen Peroxide

de Haan, J. B., Bladier, C., Griffiths, P., Kelner, M. J., O’Shea, R. D., Cheung, N. S., Bronson, R. T., Silvestro, M. J., Wild, S., Zheng, S. S., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.35.22528 · Cited by 450 · see citing works

Human αB-Crystallin Mutation Causes Oxido-Reductive Stress and Protein Aggregation Cardiomyopathy in Mice

Rajasekaran, N. S., Connell, P., Christians, E. S., Yan, L.-J., Taylor, R. P., Orosz, A., Zhang, X. Q., Stevenson, T. J., Peshock, R. M., Leopold, J. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.06.044 · Cited by 437 · see citing works

Glutathione peroxidases and redox-regulated transcription factors

Brigelius‐Flohé, R. (2006) · Biological Chemistry · doi:10.1515/bc.2006.166 · Cited by 361 · see citing works

Early embryonic lethality caused by targeted disruption of the mouse PHGPx gene

Imai, H., Hirao, F., Sakamoto, T., Sekine, K., Mizukura, Y., Saito, M., Kitamoto, T., Hayasaka, M., Hanaoka, K., & Nakagawa, Y. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00734-4 · Cited by 357 · see citing works

Overexpression of Glutathione Peroxidase Prevents Left Ventricular Remodeling and Failure After Myocardial Infarction in Mice

Shiomi, T., Tsutsui, H., Matsusaka, H., Murakami, K., Hayashidani, S., Ikeuchi, M., Wen, J., Kubota, T., Utsumi, H., & Takeshita, A. (2004) · Circulation · doi:10.1161/01.cir.0000109701.77059.e9 · Cited by 260 · see citing works

Regulation of enzymatic lipid peroxidation: the interplay of peroxidizing and peroxide reducing enzymes1 1This article is part of a series of reviews on “Regulatory and Cytoprotective Aspects of Lipid Hydroperoxide Metabolism.” The full list of papers may be found on the homepage of the journal.

Kühn, H., & Borchert, A. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00855-9 · Cited by 253 · see citing works

Mitochondrial H2O2 Regulates the Angiogenic Phenotype via PTEN Oxidation

Connor, K. M., Subbaram, S., Regan, K. J., Nelson, K. K., Mazurkiewicz, J. E., Bartholomew, P. J., Aplin, A. E., Tai, Y.-T., Aguirre-Ghiso, J., Flores, S. C., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m410690200 · Cited by 251 · see citing works

Role of insulin-induced reactive oxygen species in the insulin signaling pathway

Goldstein, B. J., Mahadev, K., Wu, X., Zhu, L., & Motoshima, H. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.1021 · Cited by 238 · see citing works

Reactive Oxygen Species Regulate Heat-Shock Protein 70 via the JAK/STAT Pathway

Madamanchi, N. R., Li, S., Patterson, C., & Runge, M. S. (2001) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.21.3.321 · Cited by 221 · see citing works

Increased infarct size and exacerbated apoptosis in the glutathione peroxidase‐1 (Gpx‐1) knockout mouse brain in response to ischemia/reperfusion injury

Crack, P. J., Taylor, J. M., Flentjar, N. J., de Haan, J. B., Hertzog, P. J., Iannello, R. C., & Kola, I. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00535.x · Cited by 212 · see citing works

Cellular Glutathione Peroxidase Is the Mediator of Body Selenium To Protect against Paraquat Lethality in Transgenic Mice

Cheng, W., Ho, Y., Valentine, B. A., Ross, D. A., Combs, G. F., & Lei, X. G. (1998) · Journal of Nutrition · doi:10.1093/jn/128.7.1070 · Cited by 212 · see citing works

Mitochondrial Creatine Kinase Activity Prevents Reactive Oxygen Species Generation

Meyer, L. E., Machado, L. B., Santiago, A. P. S. A., da‐Silva, W. S., Felice, F. G. D., Holub, O., de Oliveira, M. F., & Galina, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604123200 · Cited by 210 · see citing works

Overexpression of cellular glutathione peroxidase rescues homocyst(e)ine-induced endothelial dysfunction

Weiss, N., Zhang, Y., Heydrick, S. J., Bierl, C., & Loscalzo, J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.231428998 · Cited by 205 · see citing works

The effects of superoxide dismutase on H2O2 formation

Liochev, S. I., & Fridovich, I. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.02.015 · Cited by 202 · see citing works

Heterozygous Cellular Glutathione Peroxidase Deficiency in the Mouse: Abnormalities in Vascular and Cardiac Function and Structure

Forgione, M. A., Cap, A., Liao, R., Moldovan, N. I., Eberhardt, R. T., Lim, C. C., Jones, J., Goldschmidt-Clermont, P. J., & Loscalzo, J. (2002) · Circulation · doi:10.1161/01.cir.0000026820.87824.6a · Cited by 200 · see citing works

Cellular glutathione peroxidase deficiency and endothelial dysfunction

Forgione, M. A., Weiss, N., Heydrick, S., Cap, A., Klings, E. S., Bierl, C., Eberhardt, R. T., Farber, H. W., & Loscalzo, J. (2002) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00598.2001 · Cited by 199 · see citing works

TheGpx1Gene Encodes Mitochondrial Glutathione Peroxidase in the Mouse Liver

Esworthy, R. S., Ho, Y., & Chu, F. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.9901 · Cited by 165 · see citing works

Glucose-6-phosphate Dehydrogenase Modulates Vascular Endothelial Growth Factor-mediated Angiogenesis

Leopold, J. A., Walker, J. L., Scribner, A. W., Voetsch, B., Zhang, Y., Loscalzo, A. J., Stanton, R. C., & Loscalzo, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301293200 · Cited by 163 · see citing works

Comparative study of the enzymatic defense systems against oxygen-derived free radicals: The key role of glutathione peroxidase

Raes, M., Michiels, C., & Remacle, J. (1987) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(87)90032-3 · Cited by 160 · see citing works

Impaired Angiogenesis in Glutathione Peroxidase-1–Deficient Mice Is Associated With Endothelial Progenitor Cell Dysfunction

Galasso, G., Schiekofer, S., Sato, K., Shibata, R., Handy, D. E., Ouchi, N., Leopold, J. A., Loscalzo, J., & Walsh, K. (2005) · Circulation Research · doi:10.1161/01.res.0000200740.57764.52 · Cited by 159 · see citing works

Hydrogen peroxide generated extracellularly by receptor–ligand interaction facilitates cell signaling

DeYulia, G. J., Cárcamo, J. M., Bórquez-Ojeda, O., Shelton, C. C., & Golde, D. W. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501154102 · Cited by 159 · see citing works

Scavenging of Extracellular H2O2 by Catalase Inhibits the Proliferation of HER-2/Neu-transformed Rat-1 Fibroblasts through the Induction of a Stress Response

Preston, T. J., Muller, W. J., & Singh, G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m004617200 · Cited by 152 · see citing works

Mitochondrial Catalase Overexpression Protects Insulin-Producing Cells Against Toxicity of Reactive Oxygen Species and Proinflammatory Cytokines

Gurgul-Convey, E., Lortz, S., Tiedge, M., Jörns, A., & Lenzen, S. (2004) · Diabetes · doi:10.2337/diabetes.53.9.2271 · Cited by 150 · see citing works

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 · see citing works

Regulation of the protein disulfide proteome by mitochondria in mammalian cells

Yang, Y., Song, Y., & Loscalzo, J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702027104 · Cited by 129 · see citing works

An imbalance in antioxidant defense affects cellular function: the pathophysiological consequences of a reduction in antioxidant defense in the glutathione peroxidase-1 (Gpx1) knockout mouse

de Haan, J. B., Crack, P. J., Flentjar, N. J., Iannello, R. C., Hertzog, P. J., & Kola, I. (2003) · Redox Report · doi:10.1179/135100003125001378 · Cited by 102 · see citing works

The Role of Phospholipid Hydroperoxide Glutathione Peroxidase Isoforms in Murine Embryogenesis

Borchert, A., Wang, C. C., Ufer, C., Schiebel, H., Savaskan, N. E., & Kühn, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601195200 · Cited by 97 · see citing works

PTEN, but not SHIP and SHIP2, suppresses the PI3K/Akt pathway and induces growth inhibition and apoptosis of myeloma cells

Choi, Y., Zhang, J., Murga, C., Yu, H., Koller, E., Monia, B. P., Gutkind, J. S., & Li, W. (2002) · Oncogene · doi:10.1038/sj.onc.1205650 · Cited by 93 · see citing works

Reactive Oxygen Species–Mediated Signal Transduction in the Endothelium

Chen, K., & Keaney, J. F. (2004) · Endothelium · doi:10.1080/10623320490482655 · Cited by 91 · see citing works

Potential Contribution of NF-κB in Neuronal Cell Death in the Glutathione Peroxidase-1 Knockout Mouse in Response to Ischemia-Reperfusion Injury

Crack, P. J., Taylor, J. M., Ali, U., Mansell, A. S., & Hertzog, P. J. (2006) · Stroke · doi:10.1161/01.str.0000221708.17159.64 · Cited by 88 · see citing works

Blocking tumor cell eicosanoid synthesis by GPx4 impedes tumor growth and malignancy

Heirman, I., Ginneberge, D., Brigelius‐Flohé, R., Hendrickx, N., Agostinis, P., Brouckaert, P., Rottiers, P., & Grooten, J. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.08.033 · Cited by 87 · see citing works

Glutathione Peroxidase Overexpression Inhibits Cytochrome c Release and Proapoptotic Mediators to Protect Neurons From Experimental Stroke

Hoehn, B. D., Yenari, M. A., Sapolsky, R., & Steinberg, G. K. (2003) · Stroke · doi:10.1161/01.str.0000091268.25816.19 · Cited by 81 · see citing works

GPx2 Counteracts PGE 2 Production by Dampening COX-2 and mPGES-1 Expression in Human Colon Cancer Cells

Banning, A., Florian, S., Deubel, S., Thalmann, S., Schmehl, K., Jacobasch, G., & Brigelius‐Flohé, R. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2047 · Cited by 80 · see citing works

Adenosine-Dependent Induction of Glutathione Peroxidase 1 in Human Primary Endothelial Cells and Protection Against Oxidative Stress

Zhang, Y., Handy, D. E., & Loscalzo, J. (2005) · Circulation Research · doi:10.1161/01.res.0000164401.21929.cf · Cited by 77 · see citing works

Overexpression of Phospholipid-hydroperoxide Glutathione Peroxidase in Human Dermal Fibroblasts Abrogates UVA Irradiation-induced Expression of Interstitial Collagenase/Matrix Metalloproteinase-1 by Suppression of Phosphatidylcholine Hydroperoxide-mediated NFκB Activation and Interleukin-6 Release

Wenk, J., Schüller, J., Hinrichs, C., Syrovets, T., Azoitei, N., Podda, M., Wlaschek, M., Brenneisen, P., Schneider, L.-A., Sabiwalsky, A., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408893200 · Cited by 76 · see citing works

Fibroblasts derived from Gpx1 knockout mice display senescent-like features and are susceptible to H2O2-mediated cell death

de Haan, J. B., Bladier, C., Lotfi-Miri, M., Taylor, J. M., Hutchinson, P. E., Crack, P. J., Hertzog, P. J., & Kola, I. (2003) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2003.10.020 · Cited by 73 · see citing works

Membrane Redox State and Apoptosis: Death by Peroxide

Loscalzo, J. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.08.004 · Cited by 68 · see citing works

Suppression of the Malignant Phenotype in Pancreatic Cancer by Overexpression of Phospholipid Hydroperoxide Glutathione Peroxidase

Liu, J., Du, J., Zhang, Y., Sun, W., Smith, B. J., Oberley, L. W., & Cullen, J. J. (2006) · Human Gene Therapy · doi:10.1089/hum.2006.17.105 · Cited by 67 · see citing works

Overexpression of Cu/Zn-superoxide dismutase and/or catalase in mice inhibits aorta smooth muscle cell proliferation

Shi, M. (2004) · American Journal of Hypertension · doi:10.1016/j.amjhyper.2003.12.019 · Cited by 52 · see citing works

Expression of 5-lipoxygenase in pulmonary artery endothelial cells

Zhang, Y., Walker, J. L., Huang, A., Keaney, J. F., Clish, C. B., Serhan, C. N., & Loscalzo, J. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3610267 · Cited by 51 · see citing works

Role of Mitochondrial Phospholipid Hydroperoxide Glutathione Peroxidase (PHGPx) as a Antiapoptotic Factor

Nakagawa, Y. (2004) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.27.956 · Cited by 49 · see citing works

Mitochondrial localization of catalase provides optimal protection from H2O2-induced cell death in lung epithelial cells

Arita, Y., Harkness, S. H., Kazzaz, J. A., Koo, H.-C., Joseph, A., Melendez, J. A., Davis, J. M., Chander, A., & Li, Y. (2005) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00296.2005 · Cited by 45 · see citing works

Expression of 5-lipoxygenase in pulmonary artery endothelial cells

ZHANG, Y.-Y., Walker, J. L., Huang, A., et al. (2002) · Biochemical Journal · doi:10.1042/bj3610267 · Cited by 31 · see citing works

Catalase reverses tumorigenicity in a malignant cell line by an epidermal growth factor receptor pathway

Finch, J. S., Tome, M. E., Kwei, K. A., & Bowden, G. T. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.10.036 · Cited by 30 · see citing works

Overexpression of Phospholipid Hydroperoxide Glutathione Peroxidase Modulates Acetyl-CoA, 1-O-Alkyl-2-lyso-sn-glycero-3-phosphocholine Acetyltransferase Activity

Sakamoto, H., Tosaki, T., & Nakagawa, Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204190200 · Cited by 27 · see citing works

Nrf2-Keap1 signaling in oxidative and reductive stress

Bellezza, I., Giambanco, I., Minelli, A., & Donato, R. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.02.010 · Cited by 2,096 · see citing works

Glutathione peroxidases

Brigelius-Flohé, R., & Maiorino, M. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.11.020 · Cited by 1,904 · see citing works

Selenoproteins: Molecular Pathways and Physiological Roles

Labunskyy, V. M., Hatfield, D. L., & Gladyshev, V. N. (2014) · Physiological Reviews · doi:10.1152/physrev.00039.2013 · Cited by 1,412 · see citing works

Mitochondrial energetics in the kidney

Bhargava, P., & Schnellmann, R. G. (2017) · Nature Reviews Nephrology · doi:10.1038/nrneph.2017.107 · Cited by 1,363 · see citing works

Glutathione Peroxidase-1 in Health and Disease: From Molecular Mechanisms to Therapeutic Opportunities

Lubos, E., Loscalzo, J., & Handy, D. E. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3586 · Cited by 1,280 · see citing works

Redox regulation of mitochondrial function

Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works

Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling

Cox, A. G., Winterbourn, C. C., & Hampton, M. B. (2009) · Biochemical Journal · doi:10.1042/bj20091541 · Cited by 530 · see citing works

Orchestrating Redox Signaling Networks through Regulatory Cysteine Switches

Paulsen, C. E., & Carroll, K. S. (2009) · ACS Chemical Biology · doi:10.1021/cb900258z · Cited by 478 · see citing works

Metabolic Responses to Reductive Stress

Xiao, W., & Loscalzo, J. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7803 · Cited by 467 · see citing works

Regulatory Phenomena in the Glutathione Peroxidase Superfamily

Brigelius‐Flohé, R., & Flohé, L. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7905 · Cited by 400 · see citing works

Mitochondrial Function Controls Proliferation and Early Differentiation Potential of Embryonic Stem Cells

Mandal, S., Lindgren, A., Srivastava, A., Clark, A. T., & Banerjee, U. K. (2010) · Stem Cells · doi:10.1002/stem.590 · Cited by 326 · see citing works

Interplay between oxidant species and energy metabolism

Quijano, C., Trujillo, M., Castro, L., & Trostchansky, A. (2015) · Redox Biology · doi:10.1016/j.redox.2015.11.010 · Cited by 303 · see citing works

Mitochondrial ROS control of cancer

Idelchik, M. D. P. S., Begley, U., Begley, T. J., & Melendez, J. A. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.04.005 · Cited by 306 · see citing works

The role of glutathione peroxidase-1 in health and disease

Handy, D. E., & Loscalzo, J. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.06.004 · Cited by 288 · see citing works

Reductive Stress in Inflammation-Associated Diseases and the Pro-Oxidant Effect of Antioxidant Agents

Pérez-Torres, I., Guarner‐Lans, V., & Rubio-Ruiz, M. E. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18102098 · Cited by 252 · see citing works

Basic Biology of Oxidative Stress and the Cardiovascular System

Sack, M. N., Fyhrquist, F., Saijonmaa, O. J., Fuster, V., & Kovacic, J. C. (2017) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2017.05.034 · Cited by 243 · see citing works

Redox crosstalk at endoplasmic reticulum (ER) membrane contact sites (MCS) uses toxic waste to deliver messages

Yoboue, E. D., Sitia, R., & Simmen, T. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0033-4 · Cited by 238 · see citing works

A systems biology perspective on Nrf2-mediated antioxidant response

Zhang, Q., Pi, J., Woods, C. G., & Andersen, M. E. (2009) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.08.018 · Cited by 217 · see citing works

Redox Control of Liver Function in Health and Disease

Marı́, M., Colell, A., Morales, A., von Montfort, C., García‐Ruiz, C., & Fernández-Checa, J. C. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2634 · Cited by 201 · see citing works

Redox Regulation of Epidermal Growth Factor Receptor Signaling through Cysteine Oxidation

Truong, T. H., & Carroll, K. S. (2012) · Biochemistry · doi:10.1021/bi301441e · Cited by 198 · see citing works

Both Maximal Expression of Selenoproteins and Selenoprotein Deficiency Can Promote Development of Type 2 Diabetes-Like Phenotype in Mice

Labunskyy, V. M., Lee, B. C., Handy, D. E., Loscalzo, J., Hatfield, D. L., & Gladyshev, V. N. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3526 · Cited by 189 · see citing works

Redox regulation of protein kinases

Truong, T. H., & Carroll, K. S. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.790873 · Cited by 172 · see citing works

DJ-1 protects the nigrostriatal axis from the neurotoxin MPTP by modulation of the AKT pathway

Aleyasin, H., Rousseaux, M. W. C., Marcogliese, P. C., Hewitt, S. J., Irrcher, I., Joselin, A. P., Parsanejad, M., Kim, R. H., Rizzu, P., Callaghan, S. M., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914876107 · Cited by 168 · see citing works

The protective effects of selenium on cadmium-induced oxidative stress and apoptosis via mitochondria pathway in mice kidney

Wang, Y., Wu, Y., Luo, K., Liu, Y., Zhou, M., Yan, S., Shi, H., & Cai, Y. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.04.013 · Cited by 160 · see citing works

Regulation of Redox Signaling by Selenoproteins

Hawkes, W. C., & Alkan, Z. (2010) · Biological Trace Element Research · doi:10.1007/s12011-010-8656-7 · Cited by 151 · see citing works

Responses to reductive stress in the cardiovascular system

Handy, D. E., & Loscalzo, J. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.12.006 · Cited by 147 · see citing works

Probucol Increases Glutathione Peroxidase-1 Activity and Displays Long-Lasting Protection against Methylmercury Toxicity in Cerebellar Granule Cells

Farina, M., Campos, F., Vendrell, I., Berenguer, J., Barzi, M., Pons, S., & Sunol, C. E. (2009) · Toxicological Sciences · doi:10.1093/toxsci/kfp219 · Cited by 144 · see citing works

ROS transfer at peroxisome-mitochondria contact regulates mitochondrial redox

DiGiovanni, L. F., Khroud, P. K., Carmichael, R. E., Schrader, T. A., Gill, S. K., Germain, K., Jomphe, R. Y., Wiesinger, C., Boutry, M., Kamoshita, M., et al. (2025) · Science · doi:10.1126/science.adn2804 · Cited by 139 · see citing works

Selenium and viral infection: are there lessons for COVID-19?

Bermano, G., Méplan, C., Mercer, D. K., & Hesketh, J. E. (2020) · British Journal Of Nutrition · doi:10.1017/s0007114520003128 · Cited by 114 · see citing works

Selenium, a Micronutrient That Modulates Cardiovascular Health via Redox Enzymology

Handy, D. E., Joseph, J., & Loscalzo, J. (2021) · Nutrients · doi:10.3390/nu13093238 · Cited by 106 · see citing works

Redox Signaling in Neurotransmission and Cognition During Aging

Kumar, A., Yegla, B., & Foster, T. C. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7111 · Cited by 104 · see citing works

Selenoproteins in Tumorigenesis and Cancer Progression

Short, S. P., & Williams, C. S. (2017) · Advances in cancer research · doi:10.1016/bs.acr.2017.08.002 · Cited by 104 · see citing works

Mitochondrial catalase overexpressed transgenic mice are protected against lung fibrosis in part via preventing alveolar epithelial cell mitochondrial DNA damage

Kim, S.-J., Cheresh, P., Jablonski, R. P., Morales‐Nebreda, L., Cheng, Y., Hogan, E., Yeldandi, A. V., Chi, M., Aillon, R. P., Ridge, K. M., et al. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.11.007 · Cited by 92 · see citing works

Mitochondrial Reactive Oxygen Species in Infection and Immunity

Mukherjee, A., Ghosh, K. K., Chakrabortty, S., Gulyás, B. Z., Padmanabhan, P., & Ball, W. B. (2024) · Biomolecules · doi:10.3390/biom14060670 · Cited by 92 · see citing works

S-adenosylhomocysteine induces inflammation through NFkB: A possible role for EZH2 in endothelial cell activation

Barroso, M., Kao, D. D., Blom, H. J., de Almeida, I. T., Castro, R., Loscalzo, J., & Handy, D. E. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.10.019 · Cited by 82 · see citing works

Mitochondrial Redox Signaling and Tumor Progression

Chen, Y., Zhang, H., Zhou, H. J., Ji, W., & Wang, M. (2016) · Cancers · doi:10.3390/cancers8040040 · Cited by 80 · see citing works

Selenium—More than Just a Fortuitous Sulfur Substitute in Redox Biology

Maia, L. B., Maiti, B. K., Moura, I., & Moura, J. J. G. (2023) · Molecules · doi:10.3390/molecules29010120 · Cited by 81 · see citing works

Selenium and Cancer: A Story that Should not be Forgotten-Insights from Genomics

Méplan, C., & Hesketh, J. E. (2013) · Cancer treatment and research · doi:10.1007/978-3-642-38007-5_9 · Cited by 76 · see citing works

Subcellular Localization of Oxidants and Redox Modulation of Endothelial Nitric Oxide Synthase

Maron, B. A., & Michel, T. M. (2012) · Circulation Journal · doi:10.1253/circj.cj-12-1207 · Cited by 75 · see citing works

Closure of VDAC causes oxidative stress and accelerates the Ca2+-induced mitochondrial permeability transition in rat liver mitochondria

Tikunov, A. P., Johnson, C. B., Pediaditakis, P., Markevich, N. I., Macdonald, J. M., Lemasters, J. J., & Holmuhamedov, E. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.01.008 · Cited by 74 · see citing works

The protection of selenium on cadmium-induced inhibition of spermatogenesis via activating testosterone synthesis in mice

Ren, X., Wang, G., Xu, D., Luo, K., Liu, Y., Zhong, Y., & Cai, Y. (2012) · Food and Chemical Toxicology · doi:10.1016/j.fct.2012.07.021 · Cited by 73 · see citing works

A Synthetic Superoxide Dismutase/Catalase Mimetic EUK-207 Mitigates Radiation Dermatitis and Promotes Wound Healing in Irradiated Rat Skin

Doctrow, S. R., Luna, M. A. L., Schock, A. M., Duncan, N. E., Jourdan, M. M., Olasz, E. B., Moulder, J. E., Fish, B. L., Mäder, M., Lazar, J., et al. (2012) · Journal of Investigative Dermatology · doi:10.1038/jid.2012.410 · Cited by 68 · see citing works

Glutathione peroxidase‐1 overexpression reduces oxidative stress, and improves pathology and proteome remodeling in the kidneys of old mice

Chu, Y., Lan, R. S.-L., Huang, R., Feng, H., Kumar, R., Dayal, S., Chan, K., & Dai, D. (2020) · Aging Cell · doi:10.1111/acel.13154 · Cited by 66 · see citing works

Selenoproteins in colon cancer

Peters, K. M., Carlson, B. A., Gladyshev, V. N., & Tsuji, P. A. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.05.075 · Cited by 63 · see citing works

Age-Related Changes in Hepatic Activity and Expression of Detoxification Enzymes in Male Rats

Vyskočilová, E., Szotáková, B., Skálová, L., Bártíková, H., Hlaváčová, J., & Boušová, I. (2013) · BioMed Research International · doi:10.1155/2013/408573 · Cited by 62 · see citing works

Catalase, a target of glycation damage in rat liver mitochondria with aging

Bakala, H., Hamelin, M., Mary, J., Borot, C., & Friguet, B. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.05.016 · Cited by 61 · see citing works

Iron and Cadmium Entry Into Renal Mitochondria: Physiological and Toxicological Implications

Thévenod, F., Lee, W., & Garrick, M. D. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00848 · Cited by 59 · see citing works

Glutathione peroxidase-1 and neuromodulation: Novel potentials of an old enzyme

Sharma, G., Shin, E., Sharma, N., Nah, S.-Y., Nhu, H., Nguyen, B. T., Jeong, J. H., Lei, X. G., & Kim, H. (2020) · Food and Chemical Toxicology · doi:10.1016/j.fct.2020.111945 · Cited by 53 · see citing works

Inhibition of Cellular Methyltransferases Promotes Endothelial Cell Activation by Suppressing Glutathione Peroxidase 1 Protein Expression

Barroso, M., Florindo, C., Kalwa, H., Silva, Z., Turanov, A. A., Carlson, B. A., de Almeida, I. T., Blom, H. J., Gladyshev, V. N., Hatfield, D. L., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.549782 · Cited by 52 · see citing works

The protective effect of selenium from heat stress-induced porcine small intestinal epithelial cell line (IPEC-J2) injury is associated with regulation expression of selenoproteins

Tang, J., Cao, L., Jia, G., Liu, G., Chen, X., Tian, G., Cai, J., Shang, H., & Zhao, H. Y. (2019) · British Journal Of Nutrition · doi:10.1017/s0007114519001910 · Cited by 52 · see citing works

Molecular Consequences of Genetic Variations in the Glutathione Peroxidase 1 Selenoenzyme

Zhuo, P., Goldberg, M. L., Herman, L. C., Lee, B., Wang, H., Brown, R. L., Foster, C. B., Peters, U., & Diamond, A. M. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-1791 · Cited by 51 · see citing works

Cysteine mutant of mammalian GPx4 rescues cell death induced by disruption of the wild‐type selenoenzyme

Mannes, A. M., Seiler, A., Bosello-Travain, V., Maiorino, M., & Conrad, M. (2011) · The FASEB Journal · doi:10.1096/fj.10-177147 · Cited by 51 · see citing works

Role of GSH and Iron-Sulfur Glutaredoxins in Iron Metabolism—Review

Trnka, D., Hossain, M. F., Jordt, L. M., Gellert, M., & Lillig, C. H. (2020) · Molecules · doi:10.3390/molecules25173860 · Cited by 50 · see citing works

Nucleotide biosynthesis links glutathione metabolism to ferroptosis sensitivity

Tarangelo, A., Rodencal, J., Kim, J. T., Magtanong, L., Long, J. Z., & Dixon, S. J. (2022) · Life Science Alliance · doi:10.26508/lsa.202101157 · Cited by 49 · see citing works

Understanding Metal Dynamics Between Cancer Cells and Macrophages: Competition or Synergism?

Serra, M., Columbano, A., Ammarah, U., Mazzone, M., & Menga, A. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00646 · Cited by 49 · see citing works

PER1 interaction with GPX1 regulates metabolic homeostasis under oxidative stress

Sun, Q., Yang, Y., Wang, Z., Yang, X., Gao, Y., Zhao, Y., Ge, W., Liu, J.-H., Xu, X., Guan, W., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101694 · Cited by 48 · see citing works

Simulated microgravity‐induced mitochondrial dysfunction in rat cerebral arteries

Zhang, R., Ran, H., Cai, L., Zhu, L., Sun, J., Peng, L., Liu, X., Zhang, L. Y., Fang, Z., Fan, Y., et al. (2014) · The FASEB Journal · doi:10.1096/fj.13-245654 · Cited by 48 · see citing works

Role of selenoprotein S (SEPS1) -105G>A polymorphisms and PI3K/Akt signaling pathway in Kashin-Beck disease

Du, X., Wang, H. M., Dai, X., Kou, Y., Wu, R. P., Chen, Q., Cao, J., Mo, X., & Xiong, Y.-W. (2014) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2014.11.017 · Cited by 46 · see citing works

Selenium-Dependent Glutathione Peroxidases During Tumor Development

Kipp, A. P. (2017) · Advances in cancer research · doi:10.1016/bs.acr.2017.07.004 · Cited by 45 · see citing works

The interplay between oxidative stress and bioenergetic failure in neuropsychiatric illnesses: can we explain it and can we treat it?

Morris, G., Walder, K. R., Berk, M., Marx, W., Walker, A. J., Maes, M. H. J., & Puri, B. K. (2020) · Molecular Biology Reports · doi:10.1007/s11033-020-05590-5 · Cited by 46 · see citing works

Selenium effect on selenoprotein transcriptome in chondrocytes

Yan, J., Zheng, Y., Min, Z., Ning, Q., & Lu, S. (2013) · BioMetals · doi:10.1007/s10534-013-9610-x · Cited by 44 · see citing works

Single in vitro bovine embryo production: Coculture with autologous cumulus cells, developmental competence, embryo quality and gene expression profiles

Goovaerts, I., Leroy, J., Rizos, D. V., Bermejo‐Álvarez, P., Gutiérrez‐Adán, A., Jorssen, E. P. A., & Bols, P. E. J. (2011) · Theriogenology · doi:10.1016/j.theriogenology.2011.05.036 · Cited by 43 · see citing works

Investigation of the mechanism of triclosan induced mouse liver tumors

Wang, Z., Li, X., & Klaunig, J. E. (2017) · Regulatory Toxicology and Pharmacology · doi:10.1016/j.yrtph.2017.03.001 · Cited by 43 · see citing works

Dynamic comparisons of high-resolution expression profiles highlighting mitochondria-related genes between in vivo and in vitro fertilized early mouse embryos

Ren, L., Wang, Z., An, L., Zhang, Z., Tan, K., Miao, K., Tao, L., Cheng, L., Zhang, Z., Yang, M., et al. (2015) · Human Reproduction · doi:10.1093/humrep/dev228 · Cited by 42 · see citing works

Fumonisin B1 induces oxidative stress in oesophageal (SNO) cancer cells

Khan, R. B., Phulukdaree, A., & Chuturgoon, A. A. (2017) · Toxicon · doi:10.1016/j.toxicon.2017.12.041 · Cited by 42 · see citing works

Protective roles of estradiol against vascular oxidative stress in ovariectomized female rats exposed to normoxia or intermittent hypoxia

Ribon‐Demars, A., Pialoux, V., Boreau, A., Marcouiller, F., Larivière, R., Bairam, A., & Joseph, V. (2018) · Acta Physiologica · doi:10.1111/apha.13159 · Cited by 42 · see citing works

Molecular characterization of novel mitochondrial peroxiredoxins from the Antarctic emerald rockcod and their gene expression in response to environmental warming

Tolomeo, A. M., Carraro, A., Bakiu, R., Toppo, S., Garofalo, F., Pellegrino, D., Gerdol, M., Ferro, D., Place, S. P., & Santovito, G. (2019) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2019.108580 · Cited by 39 · see citing works

Oxidative Stress, Proton Fluxes, and Chloroquine/Hydroxychloroquine Treatment for COVID-19

Klouda, C. B., & Stone, W. L. (2020) · Antioxidants · doi:10.3390/antiox9090894 · Cited by 42 · see citing works

Homocysteine-mediated thrombosis and angiostasis in vascular pathobiology

Loscalzo, J. (2009) · Journal of Clinical Investigation · doi:10.1172/jci40924 · Cited by 41 · see citing works

Targeted Antioxidants in Exercise-Induced Mitochondrial Oxidative Stress: Emphasis on DNA Damage

Williamson, J., & Davison, G. W. (2020) · Antioxidants · doi:10.3390/antiox9111142 · Cited by 41 · see citing works

Oxidative stress rather than triglyceride accumulation is a determinant of mitochondrial dysfunction in in vitro models of hepatic cellular steatosis

Lockman, K. A., Baren, J. P., Pemberton, C. J., Baghdadi, H., Burgess, K. E., Plevris‐Papaioannou, N., Lee, P. J., Howie, F. A., Beckett, G. J., Pryde, A., et al. (2012) · Liver International · doi:10.1111/j.1478-3231.2012.02775.x · Cited by 40 · see citing works

Glutathione peroxidases in poultry biology: Part 1. Classification and mechanisms of action

Surai, P. F., Kochish, I. I., & Fisinin, V. I. (2018) · World s Poultry Science Journal · doi:10.1017/s0043933918000284 · Cited by 38 · see citing works

The Plasticizer Bisphenol A Perturbs the Hepatic Epigenome: A Systems Level Analysis of the miRNome

Renaud, L., da Silveira, W. A., Hazard, E. S., Simpson, J., Falcinelli, S., Chung, D., Carnevali, O., & Hardiman, G. (2017) · Genes · doi:10.3390/genes8100269 · Cited by 36 · see citing works

Do glutathione and copper interact to modify Alzheimer's disease pathogenesis?

Ho, T., Ahmadi, S., & Kerman, K. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.01.025 · Cited by 37 · see citing works

More than Just Antioxidants: Redox-Active Components and Mechanisms Shaping Redox Signalling Network

Kuczyńska, M., Jakubek, P., & Bartoszek, A. (2022) · Antioxidants · doi:10.3390/antiox11122403 · Cited by 36 · see citing works

Vasoconstrictor Mechanisms in Chronic Hypoxia-Induced Pulmonary Hypertension: Role of Oxidant Signaling

Yan, S., Resta, T. C., & Jernigan, N. L. (2020) · Antioxidants · doi:10.3390/antiox9100999 · Cited by 36 · see citing works

Damage to the myogenic differentiation of C2C12 cells by heat stress is associated with up-regulation of several selenoproteins

Tang, J., He, A., Yan, H., Jia, G., Liu, G., Chen, X., Cai, J., Tian, G., Shang, H., & Zhao, H. Y. (2018) · Scientific Reports · doi:10.1038/s41598-018-29012-6 · Cited by 36 · see citing works

Relationship between selenium status, selenoproteins and COVID-19 and other inflammatory diseases: A critical review

Golin, A., Tinkov, A. A., Aschner, M., Farina, M., & da Rocha, J. B. T. (2022) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2022.127099 · Cited by 35 · see citing works

Selenium-modified bone cement promotes osteoporotic bone defect repair in ovariectomized rats by restoring GPx1-mediated mitochondrial antioxidant functions

Zhou, Q., Chen, W., Gu, C., Liu, H., Hu, X., Deng, L., He, W., Xu, Y. X., Zhu, X., Yang, H., et al. (2023) · Regenerative Biomaterials · doi:10.1093/rb/rbad011 · Cited by 35 · see citing works

The Role of Glutathione and Its Precursors in Type 2 Diabetes

Tuell, D. S., Ford, G., LOS, E. A., & Stone, W. L. (2024) · Antioxidants · doi:10.3390/antiox13020184 · Cited by 35 · see citing works

MitoQ modulates oxidative stress and decreases inflammation following hemorrhage

Powell, R. D., Swet, J. H., Kennedy, K. L., Huynh, T. T., Murphy, M. P., McKillop, I. H., & Evans, S. L. (2015) · The Journal of Trauma: Injury, Infection, and Critical Care · doi:10.1097/ta.0000000000000533 · Cited by 31 · see citing works

Mitochondrial dependent oxidative stress in cell culture induced by laser radiation at 1265 nm

Saenko, Y., Глущенко, Е. С., Золотовский, И. О., Шолохов, Е. М., & Курков, А. С. (2016) · Lasers in Medical Science · doi:10.1007/s10103-015-1861-z · Cited by 32 · see citing works

Epitranscriptomic systems regulate the translation of reactive oxygen species detoxifying and disease linked selenoproteins

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 · see citing works

The Protective Effect of Selenium on T-2-Induced Nephrotoxicity Is Related to the Inhibition of ROS-Mediated Apoptosis in Mice Kidney

Zhang, X., Wang, Q., Zhang, J., Song, M., Shao, B., Han, Y., Yang, X., & Li, Y. (2021) · Biological Trace Element Research · doi:10.1007/s12011-021-02614-4 · Cited by 30 · see citing works

Behavioural impairment and oxidative stress by acute exposure of zebrafish to a commercial formulation of tebuconazole

Vieira, R. S. F., Venâncio, C. A. S., & Félix, L. M. (2022) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2022.103823 · Cited by 27 · see citing works

Hypoxia followed by re-oxygenation induces oxidation of tyrosine phosphatases

Sandin, Å., Dagnell, M., Gonon, A. T., Pernow, J., Stangl, V., Aspenström, P., Kappert, K., & Östman, A. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.01.004 · Cited by 26 · see citing works

Tualang Honey Protects the Rat Midbrain and Lung against Repeated Paraquat Exposure

Tang, S. P., Salam, S. K. N. M., Jaafar, H., Gan, S. H., Mustapha, M., & Sulaiman, S. A. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/4605782 · Cited by 26 · see citing works

Gemcitabine Resistance in Pancreatic Ductal Carcinoma Cell Lines Stems from Reprogramming of Energy Metabolism

Fujiwara‐Tani, R., Sasaki, T., Takagi, T., Mori, S., Kishi, S., Nishiguchi, Y., Ohmori, H., Fujii, K., & Kuniyasu, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147824 · Cited by 26 · see citing works

Phyllanthus urinaria induces mitochondrial dysfunction in human osteosarcoma 143B cells associated with modulation of mitochondrial fission/fusion proteins

Huang, S., Bi, K.-W., Kuo, H., Lin, T., Liao, P.-L., Wang, P., Chuang, J., & Liou, C. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.05.002 · Cited by 26 · see citing works

Ginsenoside Re protects against phencyclidine-induced behavioral changes and mitochondrial dysfunction via interactive modulation of glutathione peroxidase-1 and NADPH oxidase in the dorsolateral cortex of mice

Tran, T.-V., Shin, E., Dang, D., Ko, S. K., Jeong, J. H., Nah, S.-Y., Jang, C., Lee, Y. J., Toriumi, K., Nabeshima, T., et al. (2017) · Food and Chemical Toxicology · doi:10.1016/j.fct.2017.10.019 · Cited by 26 · see citing works

Glutathione and γ-Glutamylcysteine in Hydrogen Peroxide Detoxification

Quintana–Cabrera, R., & Bolaños, J. P. (2013) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-405882-8.00007-6 · Cited by 26 · see citing works

Low oxygen concentrations improve yak oocyte maturation and enhance the developmental competence of preimplantation embryos

He, H., Zhang, H., Li, Q., Fan, J., Pan, Y., Zhang, T., Niayale, R., Zhao, L., Hu, X., Han, X., et al. (2020) · Theriogenology · doi:10.1016/j.theriogenology.2020.06.022 · Cited by 26 · see citing works

Oxidative Stress in Type 2 Diabetes: The Case for Future Pediatric Redoxomics Studies

Alu, S. N., LOS, E. A., Ford, G. A., & Stone, W. L. (2022) · Antioxidants · doi:10.3390/antiox11071336 · Cited by 25 · see citing works

Understanding the Metabolic Profile of Macrophages During the Regenerative Process in Zebrafish

Paredes, L. C., Câmara, N. O. S., & Braga, T. T. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00617 · Cited by 23 · see citing works

The Role of Reductive Stress in the Pathogenesis of Endocrine-Related Metabolic Diseases and Cancer

Mladenov, M. I., Sazdova, I., Hadzi‐Petrushev, N., Konakchieva, R., & Gagov, H. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26051910 · Cited by 23 · see citing works

The effects of selenium and the GPx-1 selenoprotein on the phosphorylation of H2AX

Jerome‐Morais, A., Bera, S., Rachidi, W., Gann, P. H., & Diamond, A. M. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.03.010 · Cited by 23 · see citing works

IFNγ regulates NAD+ metabolism to promote the respiratory burst in human monocytes

McCann, K. J., Christensen, S. M., Colby, D. H., McGuire, P. J., Myles, I. A., Zerbe, C. S., Dalgard, C. L., Sukumar, G., Leonard, W. J., McCormick, B. A., et al. (2022) · Blood Advances · doi:10.1182/bloodadvances.2021005776 · Cited by 22 · see citing works

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 · see citing works

Antioxidant and physiological effects of Si-Wu-Tang on skin and liver: a randomized, double-blind, placebo-controlled clinical trial

Chiu, H., Wu, Y., Shen, Y., Wang, S.-J., Venkatakrishnan, K., & Wang, C. (2016) · Chinese Medicine · doi:10.1186/s13020-016-0102-0 · Cited by 21 · see citing works

Effects of Dextran-Coated Superparamagnetic Iron Oxide Nanoparticles on Mouse Embryo Development, Antioxidant Enzymes and Apoptosis Genes Expression, and Ultrastructure of Sperm, Oocytes and Granulosa Cells.

Bakhtari, A., Nazari, S., Alaee, S., Kargar-Abarghouei, E., Mesbah, F., Mirzaei, E., & Molaei, M. J. (2020) · PubMed Central · doi:10.22074/ijfs.2020.6167 · Cited by 21 · see citing works

Glutathione Peroxidase-1 in Health and Disease: From Molecular Mechanisms to Therapeutic Opportunities

Lubos, E., Loscalzo, J., & Handy, D. E. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3586 · Cited by 1,280 · see citing works

GPx1-Dependent Regulatory Processes in Health and Disease

Handy, D. E., & Loscalzo, J. (2018) · CRC Press eBooks · doi:10.1201/9781351261760-4

Abstract 1538: Role of mitochondrial dysfunction in GPX regulation and glutathione metabolism

Lu, W., Li, F., Zhang, H., & Huang, P. (2010) · Cancer Research · doi:10.1158/1538-7445.am10-1538

Glutathione peroxidase 1 (GPX1) genetic polymorphism, erythrocyte GPX activity, and prostate cancer risk

Aydın, A., Eken, A., Erdem, O., Arsova‐Sarafinovska, Z., Sayal, A., Dimovski, A. J., Savaşer, A., Özgök, Y., & Erten, K. (2009) · Toxicology Letters · doi:10.1016/j.toxlet.2009.06.711 · Cited by 14 · see citing works

Glutathione peroxidase-1 regulates ASK1-dependent apoptosis via interaction with TRAF2 in RIPK3-negative cancer cells

Lee, S., Lee, E., Kang, D. H., Lee, J., Hong, S. H., Jeong, W., & Kang, S. W. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00642-7 · Cited by 34 · see citing works