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Glutathione Peroxidase-1 in Health and Disease: From Molecular Mechanisms to Therapeutic Opportunities
Open accessAbstract
Reactive oxygen species, such as superoxide and hydrogen peroxide, are generated in all cells by mitochondrial and enzymatic sources. Left unchecked, these reactive species can cause oxidative damage to DNA, proteins, and membrane lipids. Glutathione peroxidase-1 (GPx-1) is an intracellular antioxidant enzyme that enzymatically reduces hydrogen peroxide to water to limit its harmful effects. Certain reactive oxygen species, such as hydrogen peroxide, are also essential for growth factor-mediated signal transduction, mitochondrial function, and maintenance of normal thiol redox-balance. Thus, by limiting hydrogen peroxide accumulation, GPx-1 also modulates these processes. This review explores the molecular mechanisms involved in regulating the expression and function of GPx-1, with an emphasis on the role of GPx-1 in modulating cellular oxidant stress and redox-mediated responses. As a selenocysteine-containing enzyme, GPx-1 expression is subject to unique forms of regulation involving the trace mineral selenium and selenocysteine incorporation during translation. In addition, GPx-1 has been implicated in the development and prevention of many common and complex diseases, including cancer and cardiovascular disease. This review discusses the role of GPx-1 in these diseases and speculates on potential future therapies to harness the beneficial effects of this ubiquitous antioxidant enzyme. Antioxid. Redox Signal. 15, 1957–1997.
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“GPx reduces lipid hydroperoxides to alcohols and hydrogen peroxide to water (Lubos et al. 2011).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Lubos et al. 2011
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Cites
Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
Palmer, R. M. J., Ferrige, A. G., & Moncada, S. (1987) · Nature · doi:10.1038/327524a0 · Cited by 10,704 · cited 1×
“Endothelial cells play a crucial role in regulating vascular homeostasis, in part, through their production of NO$ (281).”
Selenium: Biochemical Role as a Component of Glutathione Peroxidase
Rotruck, J. T., Pope, A. L., Ganther, H. E., Swanson, A. B., Hafeman, D. G., & Hoekstra, W. G. (1973) · Science · doi:10.1126/science.179.4073.588 · Cited by 7,815
Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80434-1 · Cited by 7,289
Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programed cell death
Oltval, Z. N., Milliman, C. L., & Korsmeyer, S. J. (1993) · Cell · doi:10.1016/0092-8674(93)90509-o · Cited by 6,003
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827
Wu, Z., Puigserver, P., Andersson, U., Zhang, C., Adelmant, G., Mootha, V., Troy, A., Cinti, S., Lowell, B., Scarpulla, R. C., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80611-x · Cited by 4,139
Endothelial dysfunction in cardiovascular diseases: the role of oxidant stress
Cai, H., & Harrison, D. G. (2000) · Circulation Research · doi:10.1161/01.res.87.10.840 · Cited by 3,839
Du, C., Fang, M., Li, Y., Li, L., & Wang, X. (2000) · Cell · doi:10.1016/s0092-8674(00)00008-8 · Cited by 3,513
Effects of Selenium Supplementation for Cancer Prevention in Patients With Carcinoma of the Skin
Clark, L. (1996) · JAMA · doi:10.1001/jama.276.24.1957 · Cited by 2,988
The Nrf2-antioxidant response element signaling pathway and its activation by oxidative stress
Nguyen, T., Nioi, P., & Pickett, C. B. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.r900010200 · Cited by 2,655
Biochemical Pathways of Caspase Activation During Apoptosis
Budihardjo, I. I., Oliver, H., Lutter, M. L., Luo, X., & Wang, X. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.269 · Cited by 2,577
A model for p53-induced apoptosis
Polyak, K., Xia, Y., Zweier, J. L., Kinzler, K. W., & Vogelstein, B. (1997) · Nature · doi:10.1038/38525 · Cited by 2,500
Characterization of Mammalian Selenoproteomes
Kryukov, G. V., Castellano, S., Novoselov, S. V., Lobanov, A. V., Zehtab, O., Guigó, R., & Gladyshev, V. N. (2003) · Science · doi:10.1126/science.1083516 · Cited by 2,385
Dysfunction of Mitochondria in Human Skeletal Muscle in Type 2 Diabetes
Kelley, D. E., He, J., Menshikova, E. V., & Ritov, V. B. (2002) · Diabetes · doi:10.2337/diabetes.51.10.2944 · Cited by 2,321
St-Pierre, J., Drori, S., Uldry, M., Silvaggi, J. M., Rhee, J., Jäger, S., Handschin, C., Zheng, K., Lin, J., Yang, W., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.024 · Cited by 2,233
Effect of Selenium and Vitamin E on Risk of Prostate Cancer and Other Cancers
Lippman, S. M., Klein, E. A., Goodman, P. J., Lucia, M. S., Thompson, I. M., Ford, L. G., Parnes, H. L., Minasian, L. M., Gaziano, J. M., Hartline, J. A., et al. (2008) · JAMA · doi:10.1001/jama.2008.864 · Cited by 2,164
Redox Regulation of Fos and Jun DNA-Binding Activity in Vitro
Abate, C., Patel, L., Rauscher, F. J., & Curran, T. (1990) · Science · doi:10.1126/science.2118682 · Cited by 1,573
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
Rhee, S. G., Chae, H. Z., & Kim, K. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.02.026 · Cited by 1,409
Glutathione peroxidase: A selenoenzyme
Flohé, L., Günzler, W. A., & Schock, H. H. (1973) · FEBS Letters · doi:10.1016/0014-5793(73)80755-0 · Cited by 1,389
A Review of the Antioxidant Mechanisms of Polyphenol Compounds Related to Iron Binding
Perron, N. R., & Brumaghim, J. L. (2009) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-009-9043-x · Cited by 1,370
Specific Aquaporins Facilitate the Diffusion of Hydrogen Peroxide across Membranes
Bienert, G. P., Møller, A. L. B., Kristiansen, K. A., Schulz, A., Møller, I. M., Schjoerring, J. K., & Jahn, T. P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603761200 · Cited by 1,311
Anderson, E. J., Lustig, M. E., Boyle, K. E., Woodlief, T. L., Kane, D. A., Lin, C.-T., Price, J. W., Kang, L., Rabinovitch, P. S., Szeto, H. H., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37048 · Cited by 1,253
Thiol chemistry and specificity in redox signaling
Winterbourn, C. C., & Hampton, M. B. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.05.004 · Cited by 1,226
Radical-free biology of oxidative stress
Jones, D. P. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00283.2008 · Cited by 1,213
Schulz, T. J., Zarse, K., Voigt, A., Urban, N., Birringer, M., & Ristow, M. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.08.011 · Cited by 1,209
(2002) · PubMed · Cited by 1,190
Finkel, T. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80147-6 · Cited by 1,170
The NLRP3 Inflammasome: A Sensor for Metabolic Danger?
Schroder, K., Zhou, R., & Tschopp, J. (2010) · Science · doi:10.1126/science.1184003 · Cited by 1,153
Klivenyi, P., Andreassen, O. A., Ferrante, R. J., Dedeoglu, A., Mueller, G., Lancelot, E., Bogdanov, M., Andersen, J. K., Jiang, D., & Beal, M. F. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-01-00001.2000 · Cited by 1,111
The Central Role of Endothelial Dysfunction in Cardiorenal Syndrome
Zhang, J., Bottiglieri, T., & McCullough, P. A. (2016) · Cardiorenal Medicine · doi:10.1159/000452283 · Cited by 1,084
Cellular and molecular mechanisms of endothelial cell dysfunction.
Harrison, D. G. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119751 · Cited by 1,059
Mancini, G. B. J., Henry, G. C., Macaya, C., O’Neill, B. J., Pucillo, A. L., Carere, R. G., Wargovich, T. J., Mudra, H. G., Lüscher, T. F., Klibaner, M. I., et al. (1996) · Circulation · doi:10.1161/01.cir.94.3.258 · Cited by 1,056
Guanylate cyclase and the ⋅NO/cGMP signaling pathway
Denninger, J. W., & Marletta, M. A. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00024-9 · Cited by 1,040
Impaired vasodilation of forearm resistance vessels in hypercholesterolemic humans.
Creager, M. A., Cooke, J. P., Mendelsohn, M. E., Gallagher, S. J., Coleman, S. M., Loscalzo, J., & Dzau, V. J. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114688 · Cited by 1,017
Self-citationGriendling, 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
Berry, C. E., & Hare, J. M. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.055913 · Cited by 925
[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
Lassègue, B., Sorescu, D., Szöcs, K., Yin, Q., Akers, M., Zhang, Y., Grant, S. L., Lambeth, J. D., & Griendling, K. K. (2001) · Circulation Research · doi:10.1161/hh0901.090299 · Cited by 839
Signaling Functions of Reactive Oxygen Species
Forman, H. J., Maiorino, M., & Ursini, F. (2010) · Biochemistry · doi:10.1021/bi9020378 · Cited by 827
Multiple Bcl-2 family members demonstrate selective dimerizations with Bax.
Sedlak, T. W., Oltvai, Z. N., Yang, E., Wang, K., Boise, L., Thompson, C. B., & Korsmeyer, S. J. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.17.7834 · Cited by 816
Mills, G. C. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70608-x · Cited by 799
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
Imai, H., & Nakagawa, Y. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01197-8 · Cited by 776
Endothelial cell superoxide generation: regulation and relevance for cardiovascular pathophysiology
Li, J.-M., & Shah, A. M. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00124.2004 · Cited by 773
Pigeolet, E., Corbisier, P., Houbion, A., Lambert, D., Michiels, C., Raes, M. J., Zachary, M.-D., & Remacle, J. (1990) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(90)90078-t · Cited by 747
The Refined Structure of the Selenoenzyme Glutathione Peroxidase at 0.2‐nm Resolution
Epp, O., Ladenstein, R., & Wendel, A. (1983) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1983.tb07429.x · Cited by 689
Chambers, I., Frampton, J., Goldfarb, P. S., Affara, N. A., McBain, W., & Harrison, P. R. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04350.x · Cited by 667
Glutathione Peroxidase: The Primary Agent for the Elimination of Hydrogen Peroxide in Erythrocytes*
Cohen, G., & Hochstein, P. (1963) · Biochemistry · doi:10.1021/bi00906a038 · Cited by 666
Borrás, C., Sastre, J., García-Sala, D., Lloret, A., Pallardó, F. V., & Viña, J. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01356-4 · Cited by 654
Berry, M. J., Banu, L., Chen, Y., Mandel, S. J., Kieffer, J. D., Harney, J. W., & Larsen, P. R. (1991) · Nature · doi:10.1038/353273a0 · Cited by 652
Targeting an antioxidant to mitochondria decreases cardiac ischemia-reperfusion injury
Adlam, V. J., Harrison, J. C., Porteous, C. M., James, A. M., Smith, R. A. J., Murphy, M. P., & Sammut, I. A. (2005) · The FASEB Journal · doi:10.1096/fj.05-3718com · Cited by 618
Doxorubicin Induces Apoptosis in Normal and Tumor Cells via Distinctly Different Mechanisms
Wang, S., Konorev, E. A., Kotamraju, S., Joseph, J., Kalivendi, S. V., & Kalyanaraman, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400944200 · Cited by 610
Glutathione Peroxidase 1 Activity and Cardiovascular Events in Patients with Coronary Artery Disease
Blankenberg, S., Rupprecht, H. J., Bickel, C., Torzewski, M., Hafner, G., Tiret, L., Smieja, M., Cambien, F., Meyer, J., & Lackner, K. J. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa030535 · Cited by 602
Mitochondrial Energetics in the Heart in Obesity-Related Diabetes
Boudina, S., Sena, S., Theobald, H., Sheng, X., Wright, J. J., Hu, X. X., Aziz, S., Johnson, J. I., Bugger, H., Zaha, V. G., et al. (2007) · Diabetes · doi:10.2337/db07-0481 · Cited by 586
Reactive oxygen species enhance insulin sensitivity
Loh, K., Deng, H., Fukushima, A., Cai, X., Boivin, B., Galic, S., Bruce, C., Shields, B. J., Skiba, B., Ooms, L. M., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.08.009 · Cited by 581
Impaired progenitor cell activity in age-related endothelial dysfunction
Heiss, C., Keymel, S., Niesler, U., Ziemann, J., Kelm, M., & Kalka, C. (2005) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2004.12.074 · Cited by 573
Kemp, M. L., Go, Y., & Jones, D. P. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.11.008 · Cited by 573
Hydrogen peroxide regulation of endothelial function: Origins, mechanisms, and consequences
Cai, H. “. (2005) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.06.021 · Cited by 571
Yamaguchi, T., Sano, K., Takakura, K., Saito, I., Shinohara, Y., Asano, T., & Yasuhara, H. (1998) · Stroke · doi:10.1161/01.str.29.1.12 · Cited by 558
The human selenoproteome: recent insights into functions and regulation
Reeves, M. A., & Hoffmann, P. R. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0032-4 · Cited by 540
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
Inactivation of glutathione peroxidase by superoxide radical
Blum, J., & Fridovich, I. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90056-6 · Cited by 534
Duffield‐Lillico, A. J., Dalkin, B. L., Reid, M. E., Turnbull, B. W., Slate, E. H., Jacobs, E. T., Marshall, J. R., Clark, L. C., & for the Nutritional Prevention of Cancer Study Group (2003) · British Journal of Urology · doi:10.1046/j.1464-410x.2003.04167.x · Cited by 514
Wilschanski, M. A., Yahav, Y., Yaacov, Y., Blau, H., Bentur, L., Rivlin, J., Aviram, M., Bdolah‐Abram, T., Bebők, Z., Shushi, L., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa022170 · Cited by 511
Selenocompounds in Plants and Animals and their Biological Significance
Whanger, P. D. (2002) · Journal of the American College of Nutrition · doi:10.1080/07315724.2002.10719214 · Cited by 502
Glutathione Peroxidase Protects against Peroxynitrite-mediated Oxidations
Sies, H., Sharov, V. S., Klotz, L., & Briviba, K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.44.27812 · Cited by 488
Orchestrating Redox Signaling Networks through Regulatory Cysteine Switches
Paulsen, C. E., & Carroll, K. S. (2009) · ACS Chemical Biology · doi:10.1021/cb900258z · Cited by 487
Endothelial Dysfunction The First Step Toward Coronary Arteriosclerosis
Vanhoutte, P. M. (2009) · Circulation Journal · doi:10.1253/circj.cj-08-1169 · Cited by 470
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 456
Knowing when not to stop: selenocysteine incorporation in eukaryotes
Low, S. C., & Berry, M. J. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)80016-8 · Cited by 449
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
Self-citationMolecular mechanisms underlying the activation of eNOS
Fleming, I. (2010) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-009-0767-7 · Cited by 437
Zhong, L., & Holmgren, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000690200 · Cited by 430
Peroxiredoxin 6: A Bifunctional Enzyme with Glutathione Peroxidase and Phospholipase A 2 Activities
Fisher, A. B. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3412 · Cited by 410 · cited 1×
“Recent findings suggest that peroxiredoxin 6 may also reduce phospholipid targets in cells (123).”
Manuvakhova, M., Keeling, K. M., & Bedwell, D. M. (2000) · RNA · doi:10.1017/s1355838200000716 · Cited by 410
M ECHANISM AND R EGULATION OF S ELENOPROTEIN S YNTHESIS
Driscoll, D. M., & Copeland, P. R. (2003) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.23.011702.073318 · Cited by 409
Myhrstad, M. C. W., Carlsen, H., Nordström, O., Blomhoff, R., & Moskaug, J. Ø. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00812-7 · Cited by 408
Beer, S. M., Taylor, E. R., Brown, S. E., Dahm, C. C., Costa, N. J., Runswick, M. J., & Murphy, M. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408011200 · Cited by 404
Hydrogen peroxide is the major oxidant product of xanthine oxidase
Kelley, E. E., Khoo, N. K. H., Hundley, N. J., Malik, U. Z., Freeman, B. Α., & Tarpey, M. M. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.11.012 · Cited by 399
A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs
Copeland, P. R., Fletcher, J. E., Carlson, B. A., Hatfield, D. L., & Driscoll, D. M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.2.306 · Cited by 398
p53-Induced Up-Regulation of MnSOD and GPx but not Catalase Increases Oxidative Stress and Apoptosis
Hussain, S. P., Amstad, P., He, P., Robles, A. I., Lupold, S. E., Kaneko, I., Ichimiya, M., Sengupta, S., Mechanic, L. E., Okamura, S., et al. (2004) · Cancer Research · doi:10.1158/0008-5472.can-2287-2 · Cited by 394
Regulation and function of selenoproteins in human disease
Bellinger, F. P., Raman, A. V., Reeves, M. A., & Berry, M. J. (2009) · Biochemical Journal · doi:10.1042/bj20090219 · Cited by 393
Dikalov, S., Dikalova, A., Bikineyeva, A. T., Schmidt, H. H. H. W., Harrison, D. G., & Griendling, K. K. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.08.013 · Cited by 391
Endothelial dysfunction in a murine model of mild hyperhomocyst(e)inemia
Eberhardt, R. T., Forgione, M. A., Cap, A., Leopold, J. A., Rudd, M. A., Trolliet, M. R., Heydrick, S. J., Stark, R., Klings, E. S., Moldovan, N. I., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci8342 · Cited by 391
Self-citationChang, T.-S., Cho, C.-S., Park, S., Yu, S., Kang, S. W., & Rhee, S. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407707200 · Cited by 388
Pinto, R., & Bartley, W. (1969) · Biochemical Journal · doi:10.1042/bj1120109 · Cited by 378
Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme
Toppo, S., Flohé, L., Ursini, F., Vanin, S., & Maiorino, M. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.04.007 · Cited by 368
Anderson, T. J., Elstein, E., Haber, H. E., & Charbonneau, F. (2000) · Journal of the American College of Cardiology · doi:10.1016/s0735-1097(99)00537-9 · Cited by 362
Purification and properties of human erythrocyte glutathione peroxidase.
Awasthi, Y. C., Beutler, E., & Srivastava, S. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41289-1 · Cited by 361
Prdx1 inhibits tumorigenesis via regulating PTEN/AKT activity
Cao, J., Schulte, J., Knight, A., Leslie, N. R., Zagożdżon, A., Bronson, R. T., Manevich, Y., Beeson, C., & Neumann, C. A. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.101 · Cited by 351
Outinen, P. A., Sood, S. K., Pfeifer, S. I., Pamidi, S., Podor, T. J., Li, J., Weitz, J. I., & Austin, R. C. (1999) · Blood · doi:10.1182/blood.v94.3.959.415k20_959_967 · Cited by 349
Scheubel, R. J., Zorn, H., Silber, R., Kuß, O., Morawietz, H., Holtz, J., & Simm, A. (2003) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2003.07.025 · Cited by 345
The GI-GPx Gene Is a Target for Nrf2
Banning, A., Deubel, S., Kluth�, D., Zhou, Z., & Brigelius‐Flohé, R. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.12.4914-4923.2005 · Cited by 344
Wang, H. D., Xu, S., Johns, D. G., Du, Y., Quinn, M. T., Cayatte, A. J., & Cohen, R. A. (2001) · Circulation Research · doi:10.1161/hh0901.089987 · Cited by 342
Glutathione Peroxidase, V. The kinetic mechanism
Flohé, L., Loschen, G., Günzler, W. A., & Eichele, E. (1972) · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · doi:10.1515/bchm2.1972.353.1.987 · Cited by 340 · cited 1×
“Enzymatic reduction of peroxides involves the formation of intermediate stable modifications to the Sec active site (127, 128, 204, 348, 369).”
Chalupský, K., & Cai, H. “. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409594102 · Cited by 338
Genetic analysis of NF‐κB/Rel transcription factors defines functional specificities
Hoffmann, A., Leung, T., & Baltimore, D. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg534 · Cited by 337
Early anthracycline cardiotoxicity
Bristow, M. R., Thompson, P. D., Martin, R. P., Mason, J. W., Billingham, M. E., & Harrison, D. C. (1978) · The American Journal of Medicine · doi:10.1016/0002-9343(78)90802-1 · Cited by 334
Li, S., Yan, T., Yang, J., Oberley, T. D., & Oberley, L. W. (2000) · PubMed · Cited by 332
Dernbach, E., Urbich, C., Brandes, R. P., Hofmann, W. K., Zeiher, A. M., & Dimmeler, S. (2004) · Blood · doi:10.1182/blood-2003-12-4103 · Cited by 331
NFκB and AP-1 mediate transcriptional responses to oxidative stress in skeletal muscle cells
Zhou, L. Z.-H., Johnson, A. P., & Rando, T. A. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00719-5 · Cited by 323
Gadd45β mediates the NF-κB suppression of JNK signalling by targeting MKK7/JNKK2
Papa, S., Zazzeroni, F., Bubici, C., Jayawardena, S., Alvarez, K., Matsuda, S., Nguyen, D. U., Pham, C. G., Nelsbach, A. H., Melis, T., et al. (2004) · Nature Cell Biology · doi:10.1038/ncb1093 · Cited by 321
Johansson, C., Lillig, C. H., & Holmgren, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312719200 · Cited by 320 · cited 1×
“Glutaredoxin-2 may play a significant role in preserving thiol function by modulating reversible protein thiol-glutathionylation in the mitochondria and nucleus (27, 188), and its actions may serve to limit oxidative damage and decrease apoptosis (230).”
Takebe, G., Yarimizu, J., Saito, Y., Hayashi, T., Nakamura, H., Yodoi, J., Nagasawa, S., & Takahashi, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202773200 · Cited by 318
Hu, Y. J., & Diamond, A. M. (2003) · PubMed · Cited by 314
Glutathione peroxidases in different stages of carcinogenesis
Brigelius‐Flohé, R., & Kipp, A. P. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.03.006 · Cited by 311
Bacteria-Induced Intestinal Cancer in Mice with DisruptedGpx1andGpx2Genes
Chu, F., Esworthy, R. S., Chu, P. G., Longmate, J., Huycke, M. M., Wilczynski, S. P., & Doroshow, J. H. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-2272 · Cited by 310
Inactivation of Glutathione Peroxidase by Nitric Oxide
Asahi, M., Fujii, J., Suzuki, K., Seo, H. G., Kuzuya, T., Hori, M., Tada, M., Fujii, S., & Taniguchi, N. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.36.21035 · Cited by 309
Role of Hydrogen Peroxide in NF-κB Activation: From Inducer to Modulator
Oliveira-Marques, V., Marinho, H. S., Cyrne, L., & Antunes, F. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2601 · Cited by 308
Decoding apparatus for eukaryotic selenocysteine insertion
Tujebajeva, R. M., Copeland, P. R., Xu, X., Carlson, B. A., Harney, J. W., Driscoll, D. M., Hatfield, D. L., & Berry, M. J. (2000) · EMBO Reports · doi:10.1093/embo-reports/kvd033 · Cited by 307
Mice with combined disruption of Gpx1 and Gpx2 genes have colitis
Esworthy, R. S., Aranda, R., Martı́n, M. G., Doroshow, J. H., Binder, S. W., & Chu, F. (2001) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.2001.281.3.g848 · Cited by 299
Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation
Fagegaltier, D., Hubert, N., Yamada, K., Mizutani, T., Carbon, P., & Krol, A. (2000) · The EMBO Journal · doi:10.1093/emboj/19.17.4796 · Cited by 294
Identification of a selenocysteyl-tRNASer in mammalian cells that recognizes the nonsense codon, UGA
Lee, B. J., Worland, P. J., Davis, J. N., Stadtman, T. C., & Hatfield, D. L. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81714-8 · Cited by 289
Tissue-specific regulation of selenoenzyme gene expression during selenium deficiency in rats
Bermano, G., Nicol, F., Dyer, J. A., Sunde, R. A., Beckett, G. J., Arthur, J. R., & Hesketh, J. E. (1995) · Biochemical Journal · doi:10.1042/bj3110425 · Cited by 287
Environmental lead toxicity and nutritional factors
Ahamed, M., & Siddiqui, M. K. J. (2007) · Clinical Nutrition · doi:10.1016/j.clnu.2007.03.010 · Cited by 287
Wang, S., Kotamraju, S., Konorev, E. A., Kalivendi, S. V., Joseph, J., & Kalyanaraman, B. (2002) · Biochemical Journal · doi:10.1042/bj20020752 · Cited by 286
Kretz‐Remy, C., Mehlen, P., Mirault, M.-É., & Arrigo, A. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.133.5.1083 · Cited by 283
Skurk, C., Maatz, H., Kim, H.-S., Jiang, Y., Abid, M. R., Aird, W. C., & Walsh, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m304736200 · Cited by 271
Lee, S.-R., Barnoy, S., Kwon, J., Levine, R. L., Stadtman, T. C., & Rhee, S. G. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.050579797 · Cited by 269
Catalase and glutathione peroxidase mimics
Day, B. J. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.09.029 · Cited by 269
H2O2-induced O⨪2Production by a Non-phagocytic NAD(P)H Oxidase Causes Oxidant Injury
Li, W. G., Miller, F. J., Zhang, H. J., Spitz, D. R., Oberley, L. W., & Weintraub, N. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102124200 · Cited by 260
Mitochondrial Transcription Factor A Induction by Redox Activation of Nuclear Respiratory Factor 1
Piantadosi, C. A., & Suliman, H. B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508805200 · Cited by 259
Homocysteine and coronary atherosclerosis: from folate fortification to the recent clinical trials
Antoniades, C. A., Antonopoulos, A. S., Tousoulis, D., Marinou, K., & Stefanadis, C. (2008) · European Heart Journal · doi:10.1093/eurheartj/ehn515 · Cited by 258
Borrás, C., Gambini, J., Gómez-Cabrera, M. C., Sastre, J., Pallardó, F., Mann, G., & Viña, J. (2005) · Aging Cell · doi:10.1111/j.1474-9726.2005.00151.x · Cited by 257
Transcriptional Activation of the Human Glutathione Peroxidase Promoter by p53
Tan, M., Li, S., Swaroop, M., Guan, K., Oberley, L. W., & Sun, Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.17.12061 · Cited by 255
Brennan, J. P., Bardswell, S. C., Burgoyne, J. R., Fuller, W., Schröder, E., Wait, R., Begum, S., Kentish, J. C., & Eaton, P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603952200 · Cited by 252
Singh, A., Rangasamy, T., Thimmulappa, R. K., Lee, H., Osburn, W. O., Brigelius‐Flohé, R., Kensler, T. W., Yamamoto, M. P., & Biswal, S. S. (2006) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2005-0325oc · Cited by 248
Ravn‐Haren, G., Olsen, A., Tjønneland, A. M., Dragsted, L. O., Nexø, B. A., Wallin, H., Overvad, K., Raaschou‐Nielsen, O., & Vogel, U. B. (2005) · Carcinogenesis · doi:10.1093/carcin/bgi267 · Cited by 248
Mitochondrial dysfunction in neurodegenerative diseases and cancer
de Moura, M. B., Santana‐Santos, L., & Houten, B. V. (2010) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20575 · Cited by 247
Lewis, P., Stefanovic, N., Pete, J., Calkin, A. C., Giunti, S., Thallas‐Bonke, V., Jandeleit-Dahm, K. A. M., Allen, T. J., Kola, I., Cooper, M. E., et al. (2007) · Circulation · doi:10.1161/circulationaha.106.664250 · Cited by 247
Glutathione peroxidase codon 198 polymorphism variant increases lung cancer risk.
Ratnasinghe, D., Tangrea, J. A., Andersen, M. R., Barrett, M. J., Virtamo, J. R. K., Taylor, P. R., & Albanes, D. (2000) · PubMed · Cited by 243
He, T., Peterson, T. E., Holmuhamedov, E., Terzic, A., Caplice, N. M., Oberley, L. W., & Katušić, Z. S. (2004) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000142810.27849.8f · Cited by 240
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
Garlic ameliorates gentamicin nephrotoxicity: relation to antioxidant enzymes
Pedraza‐Chaverrí, J., Maldonado, P. D., Medina‐Campos, O. N., et al. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00354-3 · Cited by 232
Guimarães, M. J., Peterson, D., Vicari, A. P., Cocks, B. G., Copeland, N. G., Gilbert, D. J., Jenkins, N. A., Ferrick, D. A., Kastelein, R. A., Bazán, J. F., et al. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.26.15086 · Cited by 231
Hydrogen Peroxide as a Paracrine Vascular Mediator: Regulation and Signaling Leading to Dysfunction
Ardanaz, N., & Pagano, P. J. (2006) · Experimental Biology and Medicine · doi:10.1177/153537020623100302 · Cited by 230
The protective effect of taurine against gentamicin‐induced acute tubular necrosis in rats
Erdem, A., Gündoğan, N. Ü., Usubutün, A., et al. (2000) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/15.8.1175 · Cited by 229
Mitochondrial oxidative stress in mice lacking the glutathione peroxidase-1 gene
Esposito, L. A., Kokoszka, J. E., Waymire, K. G., Cottrell, B., MacGregor, G. R., & Wallace, D. C. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00161-1 · Cited by 228
Ohlemiller, K. K., McFadden, S. L., Ding, D., Lear, P. M., & Ho, Y. (2000) · Journal of the Association for Research in Otolaryngology · doi:10.1007/s101620010043 · Cited by 227
Hamanishi, T., Furuta, H., Kato, H., Doi, A., Tamai, M., Shimomura, H., Sakagashira, S., Nishi, M., Sasaki, H., Sanke, T., et al. (2004) · Diabetes · doi:10.2337/diabetes.53.9.2455 · Cited by 224
Angiotensin-Converting Enzyme and Vascular Remodeling
Heeneman, S., Sluimer, J. C., & Daemen, M. J. A. P. (2007) · Circulation Research · doi:10.1161/circresaha.107.148338 · Cited by 224
Selenium as a component of glutathione peroxidase isolated from ovine erythrocytes
Oh, S.-H., Ganther, H. E., & Hoekstra, W. G. (1974) · Biochemistry · doi:10.1021/bi00706a008 · Cited by 221
Højlund, K., Wrzesinski, K., Larsen, P. M., Fey, S. J., Roepstorff, P., Handberg, A., Dela, F., Vinten, J., McCormack, J. G., Reynet, C., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212881200 · Cited by 221
Chaudière, J., Wilhelmsen, E. C., & Tappel, A. L. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43563-0 · Cited by 220
Leopold, J. A., Zhang, Y., Scribner, A. W., Stanton, R. C., & Loscalzo, J. (2003) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000056744.26901.ba · Cited by 219
Self-citationNonn, L., Berggren, M. M., & Powis, G. (2003) · PubMed · Cited by 215
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
Glutathione peroxidase protects mice from viral‐induced myocarditis
Beck, M. A., Esworthy, R. S., Ho, Y., & Chu, F. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.12.1143 · Cited by 212
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
Kalivendi, S. V., Konorev, E. A., Cunningham, S., Vanamala, S. K., Kaji, E. H., Joseph, J., & Kalyanaraman, B. (2005) · Biochemical Journal · doi:10.1042/bj20050285 · Cited by 209
Sung, B., Pandey, M., & Aggarwal, B. (2007) · Molecular Pharmacology · doi:10.1124/mol.107.034512 · Cited by 207
Méplan, C., Crosley, L. K., Nicol, F., Beckett, G. J., Howie, A. F., Hill, K. E., Horgan, G. W., Mathers, J. C., Arthur, J. R., & Hesketh, J. E. (2007) · The FASEB Journal · doi:10.1096/fj.07-8166com · Cited by 206
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
Self-citationSunde, R. A., Raines, A. M., Barnes, K. M., & Evenson, J. K. (2008) · Bioscience Reports · doi:10.1042/bsr20080146 · Cited by 204
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 204
Inhibitory effect of selenomethionine on the growth of three selected human tumor cell lines
Redman, C., Scott, J. A., Baines, A. T., et al. (1998) · Cancer Letters · doi:10.1016/s0304-3835(97)00497-7 · Cited by 203
Jaeschke, H., Ho, Y.-S., Fisher, M. A., Lawson, J. A., & Farhood, A. I. (1999) · Hepatology · doi:10.1002/hep.510290222 · Cited by 202
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
Self-citationBiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast.
Simons, J. F., Ferro‐Novick, S., Rose, M. D., & Helenius, A. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.130.1.41 · Cited by 199
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
Self-citationWingler, K., Böcher, M., Flohé, L., Kollmus, H., & Brigelius‐Flohé, R. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00012.x · Cited by 196
Anilkumar, N. P., Weber, R., Zhang, M., Brewer, A. C., & Shah, A. M. (2008) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.108.164277 · Cited by 195
Nève, J. (1995) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/s0946-672x(11)80013-1 · Cited by 193
Servais, H., Ortíz, A., Devuyst, O., Denamur, S., Tulkens, P. M., & Mingeot‐Leclercq, M. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0151-z · Cited by 193
Ribosomal protein L30 is a component of the UGA-selenocysteine recoding machinery in eukaryotes
Chavatte, L., Brown, B. A., & Driscoll, D. M. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb922 · Cited by 189
Nakajima, H., Amano, W., Fujita, A., Fukuhara, A., Azuma, Y., Hata, F., Inui, T., & Takeuchi, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704199200 · Cited by 189
Guo, Z., Ran, Q., Roberts, L. J., Zhou, L., Richardson, A., Sharan, C., Wu, D., & Yang, H. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.09.009 · Cited by 188
Prevention of Oxidative Damage to Rat Erythrocytes by Dietary Selenium
Rotruck, J. T., Pope, A. L., Ganther, H. E., et al. (1972) · Journal of Nutrition · doi:10.1093/jn/102.5.689 · Cited by 188
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
Self-citationTorzewski, M., Ochsenhirt, V., Kleschyov, A. L., Oelze, M. W., Daiber, A., Li, H., Rossmann, H., Tsimikas, S., Reifenberg, K., Cheng, F., et al. (2007) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000258809.47285.07 · Cited by 186
Low, S. C., Harney, J. W., & Berry, M. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.37.21659 · Cited by 186
Suzuki, K., Koike, H., Matsui, H., Ono, Y., Hasumi, M., Nakazato, H., Okugi, H., Sekine, Y., Oki, K., Ito, K., et al. (2002) · International Journal of Cancer · doi:10.1002/ijc.10428 · Cited by 184
Harmon, J. S., Bogdani, M., Parazzoli, S. D., Mak, S. S. M., Oseid, E. A., Berghmans, M., LeBoeuf, R. C., & Robertson, R. P. (2009) · Endocrinology · doi:10.1210/en.2009-0708 · Cited by 183
Weisbrot-Lefkowitz, M., Reuhl, K. R., Perry, B., et al. (1998) · Molecular Brain Research · doi:10.1016/s0169-328x(97)00313-6 · Cited by 182
The Catalytic Site of Glutathione Peroxidases
Tosatto, S. C. E., Bosello-Travain, V., Fogolari, F., Mauri, P., Roveri, A., Toppo, S., Flohé, L., Ursini, F., & Maiorino, M. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2055 · Cited by 181
Bastaki, M., Huen, K., Manzanillo, P. S., et al. (2006) · Pharmacogenetics and Genomics · doi:10.1097/01.fpc.0000199498.08725.9c · Cited by 175
Zhuo, H., Smith, A. H., & Steinmaus, C. (2004) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.771.13.5 · Cited by 175
Purification and properties of a recombinant sulfur analog of murine selenium‐glutathione peroxidase
Rocher, C., Lalanne, J., & Chaudière, J. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb16862.x · Cited by 173
The Reaction of Ebselen with Peroxynitrite
Masumoto, H., & Sies, H. (1996) · Chemical Research in Toxicology · doi:10.1021/tx950115u · Cited by 171
Kinetic mechanism and substrate specificity of glutathione peroxidase activity of ebselen (PZ51)
Maiorino, M., Roveri, A., Coassin, M., & Ursini, F. (1988) · Biochemical Pharmacology · doi:10.1016/0006-2952(88)90591-6 · Cited by 168
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 166
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
Is mitochondrial dysfunction a cause of insulin resistance?
Turner, N. A., & Heilbronn, L. K. (2008) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2008.08.001 · Cited by 165
Keeling, K. M. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.3.291 · Cited by 165
The Amino-Acid Sequence of Bovine Glutathione Peroxidase
Günzler, W. A., STEFFENS, G. J., Grossmann, A., Kim, S.-M. A., Ötting, F., Wendel, A., & Flohé, L. (1984) · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · doi:10.1515/bchm2.1984.365.1.195 · Cited by 164
Compounds for the prevention and treatment of noise-induced hearing loss
Lynch, E. D., & Kil, J. (2005) · Drug Discovery Today · doi:10.1016/s1359-6446(05)03561-0 · Cited by 164
Silva, A. L., & Romão, L. (2009) · FEBS Letters · doi:10.1016/j.febslet.2008.12.058 · Cited by 162
Determinants of Human Plasma Glutathione Peroxidase (GPx-3) Expression
Bierl, C., Voetsch, B., Jin, R. C., Handy, D. E., & Loscalzo, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401907200 · Cited by 161
Self-citationAntunes, F., Han, D., & Cadenas, E. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01016-x · Cited by 161
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
Self-citationWang, X. D., Vatamaniuk, M. Z., Wang, S. K., Roneker, C. A., Simmons, R. A., & Lei, X. G. (2008) · Diabetologia · doi:10.1007/s00125-008-1055-3 · Cited by 159
Irons, R., Carlson, B. A., Hatfield, D. L., & Davis, C. D. (2006) · Journal of Nutrition · doi:10.1093/jn/136.5.1311 · Cited by 158
Selenium and Colorectal Adenoma: Results of a Pooled Analysis
Jacobs, E. T., Jiang, R., Alberts, D. S., Greenberg, E. R., Gunter, E. W., Karagas, M. R., Lanza, E., Ratnasinghe, L. D., Reid, M. E., Schatzkin, A. G., et al. (2004) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djh310 · Cited by 156
Weitzel, F., Ursini, F., & Wendel, A. (1990) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(90)90018-r · Cited by 155
Ülker, S., McMaster, D., McKeown, P., & Bayraktutan, U. (2003) · Cardiovascular Research · doi:10.1016/s0008-6363(03)00424-3 · Cited by 154
Primary Structure of Human Plasma Glutathione Peroxidase Deduced from eDNA Sequences1
Takahashi, K., Akasaka, M., Yamamoto, Y., Kobayashi, C., Mizoguchi, J., & Koyaxna, J. (1990) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a123172 · Cited by 153
Gouazé‐Andersson, V., Mirault, M.-É., Carpentier, S., Salvayre, R., Levade, T., & Andrieu‐Abadie, N. (2001) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)12610-7 · Cited by 153
Copeland, P. R., & Driscoll, D. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25447 · Cited by 152
Interaction of peroxynitrite with selenoproteins and glutathione peroxidase mimics
Sies, H., & Arteel, G. E. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00253-7 · Cited by 149
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Redox regulation of mitochondrial function
Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588
Self-citation
Metadata
- Authors
- Lubos, E., Loscalzo, J., & Handy, D. E.
- Affiliations
- Johannes Gutenberg University Mainz (DE)
- Brigham and Women's Hospital (US)
- Corresponding author
- Handy, Diane E.
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2011-10
- Volume
- 15
- Issue
- 7
- Pages
- 1957-1997
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- PMC
- PMC3159114
- OpenAlex
- W1963668163
- Cited by
- 1,280
- References
- 420
- Citations by year
- 2026: 85 · 2025: 126 · 2024: 146 · 2023: 136 · 2022: 138 · 2021: 131 · 2020: 107 · 2019: 94 · 2018: 61 · 2017: 56 · 2016: 55 · 2015: 40 · 2014: 45 · 2013: 24 · 2012: 27
- FWCI
- 2.15
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Antioxidants and Redox Signaling (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- National Institutes of Health (HL 61795, HL081587)
- National Heart, Lung, and Blood Institute (HL61795, HL 089734, HL081587, P01HL081587, R21HL089734, R01HL061795)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Physical Sciences › Chemistry › Organic Chemistry › Organoselenium and organotellurium chemistry
- Keywords
- glutathione peroxidase 1, reactive oxygen species, hydrogen peroxide, oxidative stress, antioxidant enzymes, selenocysteine incorporation, selenium, mitochondrial function, cancer, cardiovascular disease
- MeSH terms
- Glutathione Peroxidase GPX1, Amino Acid Sequence, Animals, Cardiovascular Diseases, Diabetes Mellitus, Enzyme Inhibitors, Gene Expression Regulation, Glutathione Peroxidase, Humans, Molecular Sequence Data, Neoplasms, Oxidation-Reduction, Polymorphism, Genetic, Protein Conformation, Risk Factors, Gene Expression, Cell Death, Selenocysteine, Reactive Oxygen Species, Oxidative Stress, Genetic Predisposition to Disease
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