Glutathione Peroxidase-3 Deficiency Promotes Platelet-Dependent Thrombosis In Vivo

Nitric oxide regulation of superoxide and peroxynitrite-dependent lipid peroxidation. Formation of novel nitrogen-containing oxidized lipid derivatives

Rubbo, H., Radí, R., Trujillo, M., Telleri, R., Kalyanaraman, B., Barnes, S., KIRK, M. C., & Freeman, B. Α. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47160-8 · Cited by 1,350 · see citing works

Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide

Winterbourn, C. C., & Metodiewa, D. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00051-9 · Cited by 799 · see citing works

Nitric Oxide Insufficiency, Platelet Activation, and Arterial Thrombosis

Loscalzo, J. (2001) · Circulation Research · doi:10.1161/hh0801.089861 · Cited by 612 · see citing works

Purification and characterization of human plasma glutathione peroxidase: A selenoglycoprotein distinct from the known cellular enzyme

Takahashi, K., Avissar, N. E., Whitin, J. C., & Cohen, H. J. (1987) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(87)90624-2 · Cited by 411 · see citing works

Hydrogen Peroxide Is Involved in Collagen-Induced Platelet Activation

Pignatelli, P., Pulcinelli, F. M., Lenti, L., Gazzaniga, P. P., & Violi, F. (1998) · Blood · doi:10.1182/blood.v91.2.484 · Cited by 325 · see citing works

A Comparative Study on the Hydroperoxide and Thiol Specificity of the Glutathione Peroxidase Family and Selenoprotein P

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 · see citing works

Manganic Porphyrins Possess Catalase Activity and Protect Endothelial Cells against Hydrogen Peroxide-Mediated Injury

Day, B. J., Fridovich, I., & Crapo, J. D. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0341 · Cited by 285 · see citing works

The Reaction of Superoxide with Reduced Glutathione

Winterbourn, C. C., & Metodiewa, D. (1994) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1994.1444 · Cited by 269 · see citing works

NAD(P)H oxidase–dependent platelet superoxide anion release increases platelet recruitment

Krötz, F., Sohn, H. Y., GLOE, T. R., Stefan Zahler, A., Riexinger, T., Schiele, T. M., Becker, B. F., Theisen, K., Klauß, V., & Pohl, U. (2002) · Blood · doi:10.1182/blood.v100.3.917 · Cited by 262 · see citing works

A metalloporphyrin superoxide dismutase mimetic protects against paraquat-induced endothelial cell injury, in vitro.

Day, B. J., Shawen, S., Liochev, S. I., & Jd, C. (1995) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)12174-5 · Cited by 196 · see citing works

Involvement of NADH/NADPH Oxidase in Human Platelet ROS Production

Seno, T., Inoue, N., Gao, D., Okuda, M., Sumi, Y., Matsui, K., Yamada, S., Hirata, K., Kawashima, S., Tawa, R., et al. (2001) · Thrombosis Research · doi:10.1016/s0049-3848(01)00341-3 · Cited by 196 · see citing works

Decreased platelet inhibition by nitric oxide in two brothers with a history of arterial thrombosis.

Freedman, J. E., Loscalzo, J., Benoit, S. E., Valeri, C. R., Barnard, M. R., & Michelson, A. D. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118522 · Cited by 171 · see citing works

Superoxide production and reducing activity in human platelets.

Marcus, A. J., Silk, S. T., Safier, L. B., & ULLMAN, H. L. (1977) · Journal of Clinical Investigation · doi:10.1172/jci108613 · Cited by 161 · see citing works

Glutathione peroxidase potentiates the inhibition of platelet function by S-nitrosothiols.

Freedman, J. E., Frei, B. B., Welch, G. N., & Loscalzo, J. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118047 · Cited by 153 · see citing works

Promoter Polymorphisms in the Plasma Glutathione Peroxidase ( GPx-3 ) Gene

Voetsch, B., Jin, R. C., Bierl, C., Benke, K. S., Kenet, G., Simioni, P., Ottaviano, F. G., Damasceno, B. P., Annichino-Bizacchi, J. M., Handy, D. E., et al. (2006) · Stroke · doi:10.1161/01.str.0000252027.53766.2b · Cited by 143 · see citing works

Pure MnTBAP selectively scavenges peroxynitrite over superoxide: Comparison of pure and commercial MnTBAP samples to MnTE-2-PyP in two models of oxidative stress injury, an SOD-specific Escherichia coli model and carrageenan-induced pleurisy

Batinic̈‐Haberle, I., Cuzzocrea, S., Reboucas, J. S., Ferrer‐Sueta, G., Mazzon, E., Paola, R. D., Radí, R., Spasojević, I., Benov, L., & Salvemini, D. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.09.042 · Cited by 140 · see citing works

Superoxide anions enhance platelet adhesion and aggregation

Salvemini, D., Nucci, G. D., Sneddon, J. M., & Vane, J. R. (1989) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.1989.tb12572.x · Cited by 136 · see citing works

Superoxide Anion and Hydroxyl Radical Release by Collagen-induced Platelet Aggregation - Role of Arachidonic Acid Metabolism

Caccese, D., Praticò, D., Ghiselli, A., Natoli, S., Pignatelli, P., Sanguigni, V., Iuliano, L., & Violi, F. (2000) · Thrombosis and Haemostasis · doi:10.1055/s-0037-1613841 · Cited by 100 · see citing works

Three Novel Sarco/endoplasmic Reticulum Ca2+-ATPase (SERCA) 3 Isoforms

Martin, V., Bredoux, R., Corvazier, E., van Gorp, R. M. A., Kovàcs, T., Gélébart, P., & Enouf, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202011200 · Cited by 100 · see citing works

Effect of hydrogen peroxide on Ca2+ mobilisation in human platelets through sulphydryl oxidation dependent and independent mechanisms

Redondo, P. C., Salido, G. M., Rosado, J. A., & Pariente, J. A. (2003) · Biochemical Pharmacology · doi:10.1016/j.bcp.2003.09.031 · Cited by 99 · see citing works

Role of hydroxyl radicals in the activation of human platelets

Iuliano, L., Pedersen, J. Z., Praticò, D., Rotilio, G., & Violi, F. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb18782.x · Cited by 95 · see citing works

Kinetic Analysis of Intracellular Concentrations of Reactive Nitrogen Species

Lim, C. H., Dedon, P. C., & Deen, W. M. (2008) · Chemical Research in Toxicology · doi:10.1021/tx800213b · Cited by 93 · see citing works

Release of Calcium from Mitochondrial and Nonmitochondrial Intracellular Stores in Mouse Pancreatic Acinar Cells by Hydrogen Peroxide

Pariente, J. A., Camello, C., Camello, P. J., & Salido, G. M. (2001) · The Journal of Membrane Biology · doi:10.1007/s002320010034 · Cited by 91 · see citing works

Oxidative damage to sarcoplasmic reticulum Ca2+-ATPase at submicromolar iron concentrations: evidence for metal-catalyzed oxidation

Moreau, V. H., Castilho, R. F., Ferreira, S. T., & Carvalho-Alves, P. C. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00084-7 · Cited by 71 · see citing works

Role of Promoter Polymorphisms in the Plasma Glutathione Peroxidase ( GPx-3 ) Gene as a Risk Factor for Cerebral Venous Thrombosis

Voetsch, B., Jin, R. C., Bierl, C., Deus-Silva, L., Camargo, E. C., Annichino-Bizacchi, J. M., Handy, D. E., & Loscalzo, J. (2007) · Stroke · doi:10.1161/strokeaha.107.490094 · Cited by 67 · see citing works

Dual effect of hydrogen peroxide on store-mediated calcium entry in human platelets

Redondo, P. C., Salido, G. M., Pariente, J. A., & Rosado, J. A. (2003) · Biochemical Pharmacology · doi:10.1016/j.bcp.2003.10.028 · Cited by 65 · see citing works

Oxidation of tetrahydrobiopterin by peroxynitrite or oxoferryl species occurs by a radical pathway

Kohnen, S. L., Mouithys-Mickalad, A. A., Deby-Dupont, G. P., Deby, C. M. T., Lamy, M., & Noels, A. F. (2001) · Free Radical Research · doi:10.1080/10715760100301221 · Cited by 43 · see citing works

Plasma, platelet and erythrocyte glutathione peroxidases as risk factors in ischaemic heart disease in man

Porter, M., Pearson, D. J., SUAREZ‐MENDEZ, V. J., & Blann, A. D. (1992) · Clinical Science · doi:10.1042/cs0830343 · Cited by 37 · see citing works

Lipid peroxides and antioxidant status in serum of patients with angiographically defined coronary atherosclerosis

Doğru‐Abbasoğlu, S., Kanbağlı, Ö., Bulur, H., Babalık, E., Öztürk, S., Aykaç‐Toker, G., & Uysal, M. (1999) · Clinical Biochemistry · doi:10.1016/s0009-9120(99)00076-4 · Cited by 31 · see citing works

Reactive oxygen species and human platelet GP IIb/IIIa receptor activation

Sill, J. C., Proper, J. A., Johnson, M. E., Uhl, C. B., & Katušić, Z. S. (2007) · Platelets · doi:10.1080/09537100701481385 · Cited by 27 · see citing works

Glutathione regulates integrin αIIbβ3-mediated cell adhesion under flow conditions

Ball, C., Vijayan, K. V., Nguyen, T. C., Anthony, K., Bray, P. F., Essex, D. W., & Dong, J.-F. (2008) · Thrombosis and Haemostasis · doi:10.1160/th08-02-0095 · Cited by 17 · see citing works

The influence of organic peroxides on platelet aggregation and sensitivity to nitric oxide

Naseem, K. M., & Bruckdorfer, K. R. (1999) · Platelets · doi:10.1080/09537109976220 · Cited by 7 · see citing works

The influence of organic peroxides on platelet aggregation and sensitivity to nitric oxide

Naseem, K. M., & Bruckdorfer, K. R. (1999) · Platelets · doi:10.1080/09537109909169178 · Cited by 4 · see citing works

Reactive Oxygen Species in Metabolic and Inflammatory Signaling

Forrester, S. J., Kikuchi, D. S., Hernandes, M. S., Xu, Q., & Griendling, K. K. (2018) · Circulation Research · doi:10.1161/circresaha.117.311401 · Cited by 2,081 · 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

Neutrophil extracellular traps promote deep vein thrombosis in mice

Brill, A. G., Fuchs, T. A., Savchenko, A. S., Thomas, G. M., Martinod, K., Meyer, S. F. D., Bhandari, A. A., & Wagner, D. D. (2011) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2011.04544.x · Cited by 900 · 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

Inflammaging and Oxidative Stress in Human Diseases: From Molecular Mechanisms to Novel Treatments

Zuo, L., Prather, E. R., Stetskiv, M., Garrison, D. E., Meade, J. R., Peace, T. I., & Zhou, T. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20184472 · Cited by 545 · see citing works

Paradoxical Roles of Antioxidant Enzymes: Basic Mechanisms and Health Implications

Lei, X. G., Zhu, J., Cheng, W.-H., Bao, Y., Ho, Y.-S., Reddi, A. R., Holmgren, A., & Arnér, E. S. J. (2015) · Physiological Reviews · doi:10.1152/physrev.00010.2014 · Cited by 437 · 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

Selenium and Its Supplementation in Cardiovascular Disease—What do We Know?

Benstoem, C., Goetzenich, A., Kraemer, S., Borosch, S., Manzanares, W., Hardy, G., & Stoppe, C. (2015) · Nutrients · doi:10.3390/nu7053094 · Cited by 326 · see citing works

The glutathione peroxidase family: Discoveries and mechanism

Flohé, L., Toppo, S., & Orian, L. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.05.003 · Cited by 259 · see citing works

Keshan Disease, Selenium Deficiency, and the Selenoproteome

Loscalzo, J. (2014) · New England Journal of Medicine · doi:10.1056/nejmcibr1402199 · Cited by 245 · see citing works

ROS in Platelet Biology: Functional Aspects and Methodological Insights

Masselli, E., Pozzi, G., Vaccarezza, M., Mirandola, P., Galli, D., Vitale, M., Carubbi, C., & Gobbi, G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21144866 · Cited by 232 · see citing works

Extracellular Glutathione Peroxidase GPx3 and Its Role in Cancer

Chang, C. A., Worley, B. L., Phaëton, R., & Hempel, N. (2020) · Cancers · doi:10.3390/cancers12082197 · Cited by 226 · see citing works

Hydrogen Peroxide Promotes Aging-Related Platelet Hyperactivation and Thrombosis

Dayal, S., Wilson, K. M., Motto, D. G., Miller, F. J., Chauhan, A. K., & Lentz, S. R. (2013) · Circulation · doi:10.1161/circulationaha.112.000966 · Cited by 192 · see citing works

Redefining the major contributors to superoxide production in contracting skeletal muscle. The role of NAD(P)H oxidases

Sakellariou, G. K., Jackson, M. J., & Vasilaki, A. (2014) · Free Radical Research · doi:10.3109/10715762.2013.830718 · Cited by 184 · see citing works

Immediate Antioxidant and Antiplatelet Effect of Atorvastatin via Inhibition of Nox2

Pignatelli, P., Carnevale, R., Pastori, D., Cangemi, R., Napoleone, L., Bartimoccia, S., Nocella, C., Basili, S., & Violi, F. (2012) · Circulation · doi:10.1161/circulationaha.112.095554 · Cited by 182 · see citing works

Selenium and redox signaling

Brigelius‐Flohé, R., & Flohé, L. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.08.003 · Cited by 162 · see citing works

A tough nitric oxide-eluting hydrogel coating suppresses neointimal hyperplasia on vascular stent

Chen, Y., Gao, P., Huang, L., Tan, X., Zhou, N., Yang, T., Qiu, H., Dai, X., Michael, S. A., Tu, Q., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27368-4 · Cited by 158 · see citing works

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 143 · see citing works

Atherothrombosis and Oxidative Stress: Mechanisms and Management in Elderly

Violi, F., Loffredo, L., Carnevale, R., Pignatelli, P., & Pastori, D. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6963 · Cited by 121 · see citing works

Reactive Oxygen Species in Venous Thrombosis

Gutmann, C., Siow, R. C. M., Gwozdz, A. M., Saha, P., & Smith, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21061918 · Cited by 118 · see citing works

Selenoprotein P – Selenium transport protein, enzyme and biomarker of selenium status

Schomburg, L. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.08.022 · Cited by 110 · see citing works

Platelet Oxidative Stress and Thrombosis

Violi, F., & Pignatelli, P. (2011) · Thrombosis Research · doi:10.1016/j.thromres.2011.12.002 · Cited by 107 · 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

mTORC1 promotes aging-related venous thrombosis in mice via elevation of platelet volume and activation

Yang, J., Zhou, X., Fan, X., Xiao, M., Yang, D., Liang, B., Dai, M., Shan, L., Lu, J., Lin, Z., et al. (2016) · Blood · doi:10.1182/blood-2015-10-672964 · Cited by 91 · see citing works

Selenoproteins in Nervous System Development and Function

Pitts, M. W., Byrns, C. N., Ogawa-Wong, A. N., Kremer, P. M., & Berry, M. J. (2014) · Biological Trace Element Research · doi:10.1007/s12011-014-0060-2 · Cited by 88 · see citing works

Progress in the emerging role of selenoproteins in cardiovascular disease: focus on endoplasmic reticulum-resident selenoproteins

Rocca, C., Pasqua, T., Boukhzar, L., Anouar, Y., & Angelone, T. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03195-1 · Cited by 85 · see citing works

Aging‐Related Decline of Glutathione Peroxidase 3 and Risk of Cardiovascular Events in Patients With Atrial Fibrillation

Pastori, D., Pignatelli, P., Farcomeni, A., Menichelli, D., Nocella, C., Carnevale, R., & Violi, F. (2016) · Journal of the American Heart Association · doi:10.1161/jaha.116.003682 · Cited by 83 · see citing works

Extracellular Thiol Isomerases and Their Role in Thrombus Formation

Schulman, S., Bendapudi, P. K., Sharda, A. V., Chen, V. M. Y., Bellido‐Martín, L., Jasuja, R., Furie, B. C., Flaumenhaft, R. C., & Furie, B. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6530 · Cited by 79 · see citing works

The Role of Oxidative Stress in Acute Ischemic Stroke‐Related Thrombosis

Li, Z., Bi, R., Sun, S., Chen, S., Chen, J., Hu, B., & Jin, H. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/8418820 · Cited by 76 · see citing works

Selenium and selenoproteins in prostanoid metabolism and immunity

Qian, F., Misra, S., & Prabhu, K. S. (2019) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2020.1717430 · Cited by 74 · see citing works

Age-associated changes in gene expression in human brain and isolated neurons

Kumar, A., Gibbs, J. R., Beilina, A. G., Dillman, A., Kumaran, R., Trabzuni, D., Ryten, M., WALKER, R. E., Smith, C., Traynor, B. J., et al. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.10.021 · Cited by 73 · see citing works

Platelet NOX, a novel target for anti-thrombotic treatment

Pignatelli, P., & Violi, F. (2014) · Thrombosis and Haemostasis · doi:10.1160/th13-10-0818 · Cited by 68 · see citing works

Beneficial and paradoxical roles of selenium at nutritional levels of intake in healthspan and longevity

Zhang, L., Zeng, H., & Cheng, W. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.05.067 · Cited by 66 · see citing works

Targetting ferroptosis for blood cell-related diseases

Chen, Z., Jiang, J., Fu, N., & Chen, L. (2021) · Journal of drug targeting · doi:10.1080/1061186x.2021.1971237 · Cited by 63 · see citing works

Retinal Vascular Caliber Is Associated with Cardiovascular Biomarkers of Oxidative Stress and Inflammation: The POLA Study

Daïen, V., Carrière, I., Kawasaki, R., Cristol, J., Villain, M., Fesler, P., Ritchie, K. A., & Delcourt, C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0071089 · Cited by 62 · see citing works

Glutathionyl systems and metabolic dysfunction in obesity

Picklo, M. J., Long, E. K., & Vomhof‐DeKrey, E. E. (2015) · Nutrition Reviews · doi:10.1093/nutrit/nuv042 · Cited by 62 · see citing works

Selenoprotein H is an essential regulator of redox homeostasis that cooperates with p53 in development and tumorigenesis

Cox, A. G., Tsomides, A., Kim, A. J., Saunders, D. C., Hwang, K. L., Evason, K. J., Heidel, J. R., Brown, K., Yuan, M., Lien, E. C., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1600204113 · Cited by 63 · see citing works

Berberine mitigates high glucose-potentiated platelet aggregation and apoptosis by modulating aldose reductase and NADPH oxidase activity

Paul, M., Hemshekhar, M., Kemparaju, K., & Girish, K. S. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.453 · Cited by 61 · see citing works

Platelet Signaling Pathways and New Inhibitors

Grover, S. P., Bergmeier, W., & Mackman, N. (2018) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.118.310224 · Cited by 61 · see citing works

Dietary selenium deficiency or selenomethionine excess drastically alters organ selenium contents without altering the expression of most selenoproteins in mice

Akahoshi, N., Anan, Y., Hashimoto, Y., Tokoro, N., Mizuno, R., Hayashi, S., Yamamoto, S., Shimada, K., Kamata, S., & Ishii, I. (2019) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2019.03.020 · Cited by 58 · see citing works

Biological and Catalytic Properties of Selenoproteins

Chaudière, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241210109 · Cited by 64 · see citing works

Tolerance to Selenoprotein Loss Differs between Human and Mouse

Santesmasses, D., Mariotti, M., & Gladyshev, V. N. (2019) · Molecular Biology and Evolution · doi:10.1093/molbev/msz218 · Cited by 56 · see citing works

The C718T polymorphism in the 3′-untranslated region of glutathione peroxidase-4 gene is a predictor of cerebral stroke in patients with essential hypertension

Polonikov, A., Вялых, Е. К., Churnosov, M. I., Illig, T., Freidin, M. B., Васильева, О. В., Bushueva, O. Y., Николаевна, Р. В., Булгакова, И. В., & Solodilova, M. A. (2011) · Hypertension Research · doi:10.1038/hr.2011.213 · Cited by 55 · see citing works

Role of oxidative stress on platelet hyperreactivity during aging

Eduardo Fuentes, Q., & Palomo, I. F. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.02.026 · Cited by 55 · see citing works

Endothelial Cell Regulation of Pulmonary Vascular Tone, Inflammation, and Coagulation

Goldenberg, N. M., & Kuebler, W. M. (2015) · Comprehensive physiology · doi:10.1002/cphy.c140024 · Cited by 62 · see citing works

High-Resolution Imaging of Selenium in Kidneys: A Localized Selenium Pool Associated with Glutathione Peroxidase 3

Malinouski, M., Kehr, S., Finney, L. A., Vogt, S., Carlson, B. A., Seravalli, J., Jin, R. C., Handy, D. E., Park, T. J., Loscalzo, J., et al. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3997 · Cited by 47 · see citing works

Pre-clinical model of severe glutathione peroxidase-3 deficiency and chronic kidney disease results in coronary artery thrombosis and depressed left ventricular function

Pang, P. D., Abbott, M., Abdi, M., Fucci, Q., Chauhan, N., Mistri, M., Proctor, B. M., Chin, M. C., Wang, B., Yin, W., et al. (2017) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfx304 · Cited by 47 · see citing works

Understanding thrombosis: the critical role of oxidative stress

Li, P., Ma, X., & Huang, G. (2024) · Hematology · doi:10.1080/16078454.2023.2301633 · Cited by 49 · see citing works

Abundance of Plasma Antioxidant Proteins Confers Tolerance to Acute Hypobaric Hypoxia Exposure

Padhy, G., Sethy, N. K., Ganju, L., & Bhargava, K. (2013) · High Altitude Medicine & Biology · doi:10.1089/ham.2012.1095 · Cited by 44 · see citing works

Glutathione (GSH) and the GSH synthesis gene Gclm modulate vascular reactivity in mice

Weldy, C. S., Luttrell, I. P., White, C. C., Morgan‐Stevenson, V., Bammler, T. K., Beyer, R. P., Afsharinejad, Z., Kim, F., Chitaley, K., & Kavanagh, T. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.07.006 · Cited by 42 · see citing works

Strong associations of serum selenoprotein P with all-cause mortality and mortality due to cancer, cardiovascular, respiratory and gastrointestinal diseases in older German adults

Schöttker, B., Holleczek, B., Hybsier, S., Köhrle, J., Schomburg, L., & Brenner, H. (2024) · European Journal of Epidemiology · doi:10.1007/s10654-023-01091-4 · Cited by 41 · see citing works

Differential expression and anti‐oxidant function of glutathione peroxidase 3 in mouse uterus during decidualization

Xu, X. P., Leng, J.-Y., Gao, F., Zhao, Z., Deng, W., Liang, X., Zhang, Y.-J., Zhang, Z., Li, M., Sha, A., et al. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.02.043 · Cited by 40 · see citing works

Antiplatelet Aggregation Activity of Walnut Hull Extract via Suppression of Reactive Oxygen Species Generation and Caspase Activation

Meshkini, A., & Tahmasbi, M. (2017) · Journal of Acupuncture and Meridian Studies · doi:10.1016/j.jams.2017.02.007 · Cited by 41 · see citing works

Nox-2 up-regulation and platelet activation: Novel insights

Pastori, D., Pignatelli, P., Carnevale, R., & Violi, F. (2015) · Prostaglandins & Other Lipid Mediators · doi:10.1016/j.prostaglandins.2015.03.010 · Cited by 41 · see citing works

Expanding the Frontiers of Guardian Antioxidant Selenoproteins in Cardiovascular Pathophysiology

Angelone, T., Rocca, C., Lionetti, V., Penna, C. R. R., & Pagliaro, P. (2024) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0285 · Cited by 39 · see citing works

Functional Characterisation of a GWAS Risk Locus Identifies GPX3 as a Lead Candidate Gene in ALS

Restuadi, R., Steyn, F. J., Kabashi, E., Ngo, S. T., Cheng, F., Nabais, M. F., Thompson, M. J., Qi, T., Wu, Y., Henders, A. K., et al. (2020) · Genome Medicine · doi:10.1186/s13073-021-01006-6 · Cited by 38 · see citing works

A Self‐Adaptive Biomimetic Periosteum Employing Nitric Oxide Release for Augmenting Angiogenesis in Bone Defect Regeneration

Zhou, Z., Liu, Y., Li, W., Zhao, Z., Xia, X., Liu, J., Deng, Y., Wu, Y., Pan, X., He, F., et al. (2023) · Advanced Healthcare Materials · doi:10.1002/adhm.202302153 · Cited by 38 · see citing works

Insights into the Role of Glutathione Peroxidase 3 in Non-Neoplastic Diseases

Zhang, N., Liao, H., Lin, Z., & Tang, Q. (2024) · Biomolecules · doi:10.3390/biom14060689 · Cited by 39 · see citing works

Antioxidant and antiplatelet effects of atorvastatin by Nox2 inhibition

Violi, F., Carnevale, R., Pastori, D., & Pignatelli, P. (2013) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2013.09.006 · Cited by 39 · see citing works

Glutathione Peroxidase 3 Serum Levels and GPX3 Gene Polymorphisms in Subjects with Metabolic Syndrome

Báez-Duarte, B. G., Mendoza‐Carrera, F., Garcı́a-Zapién, A. G., Flores-Martí­nez, S. E., Sánchez‐Corona, J., Zamora‐Ginez, I., Torres‐Rasgado, E., León‐Chávez, B. A., & Pérez-Fuentes, R. (2014) · Archives of Medical Research · doi:10.1016/j.arcmed.2014.05.001 · Cited by 35 · see citing works

Modulators of platelet function in aging

Iyer, K. S., & Dayal, S. (2019) · Platelets · doi:10.1080/09537104.2019.1665641 · Cited by 34 · see citing works

Regulation and function of avian selenogenome

Li, S., Gao, F., Huang, J., Wu, Y., Wu, S., & Lei, X. G. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.03.029 · Cited by 34 · see citing works

Comparative transcriptome analysis of SARS-CoV, MERS-CoV, and SARS-CoV-2 to identify potential pathways for drug repurposing

Krishnamoorthy, P., Raj, A. S., Roy, S., Kumar, N. S., & Kumar, H. (2020) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2020.104123 · Cited by 33 · see citing works

Iron deficiency: a novel risk factor of recurrence in patients after unprovoked venous thromboembolism

Potaczek, D. P., Jankowska, E. A., Wypasek, E., & Undas, A. (2016) · Polskie Archiwum Medycyny Wewnętrznej · doi:10.20452/pamw.3311 · Cited by 32 · see citing works

Determination of Essential and Toxic Elements in Cattle Blood: Serum vs Plasma

Luna, D., López‐Alonso, M., Cedeño, Y., Rigueira, L., Pereira, V., & Miranda, M. (2019) · Animals · doi:10.3390/ani9070465 · Cited by 32 · see citing works

NEDD9 Is a Novel and Modifiable Mediator of Platelet–Endothelial Adhesion in the Pulmonary Circulation

Alba, G. A., Samokhin, A. O., Wang, R., Zhang, Y., Wertheim, B. M., Arons, E., Greenfield, E. A., Slingsby, M. H. L., Ceglowski, J. R., Haley, K. J., et al. (2021) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.202003-0719oc · Cited by 32 · see citing works

Association of combined genetic variations in SOD3, GPX3, PON1, and GSTT1 with hypertension and severity of coronary artery disease

Decharatchakul, N., Settasatian, C., Settasatian, N., Komanasin, N., Kukongviriyapan, U., Intharapetch, P., Senthong, V., & Sawanyawisuth, K. (2020) · Heart and Vessels · doi:10.1007/s00380-020-01564-6 · Cited by 32 · see citing works

Constructing sodium alginate/carboxymethyl chitosan coating capable of catalytically releasing NO or CO for improving the hemocompatibility and endothelialization of magnesium alloys

Pan, C., Zuo, C., Chen, J., Zhang, Q., Deng, L., Liu, Y., & Ding, P. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.135166 · Cited by 31 · see citing works

Expression and function of IL-1R8 (TIR8/SIGIRR), a regulatory member of the IL-1 receptor family in platelets

Anselmo, A., Riva, F., Gentile, S., Soldani, C., Barbagallo, M., Mazzon, C., Feruglio, F., Polentarutti, N., Somma, P., Carullo, P., et al. (2016) · Cardiovascular Research · doi:10.1093/cvr/cvw162 · Cited by 31 · see citing works

Associations between urinary heavy metal concentrations and blood pressure in residents of Asian countries

Mizuno, Y., Shimizu-Furusawa, H., Konishi, S., Inaoka, T., Ahmad, S. A., Sekiyama, M., Abdoellah, O. S., Gunawan, B., Parajuli, R. P., Ikemoto, Y., et al. (2021) · Environmental Health and Preventive Medicine · doi:10.1186/s12199-021-01027-y · Cited by 31 · see citing works

Selenium metabolism and selenoproteins function in brain and encephalopathy

Li, N., Zhang, Z.-H., Shen, L., Song, G.-L., Tian, J., Liu, Q., & Ni, J. (2024) · Science China Life Sciences · doi:10.1007/s11427-023-2621-7 · Cited by 28 · see citing works

Alterations of HDL’s to piHDL’s Proteome in Patients with Chronic Inflammatory Diseases, and HDL-Targeted Therapies

Vyletelová, V., Nováková, M., & Pašková, Ľ. (2022) · Pharmaceuticals · doi:10.3390/ph15101278 · Cited by 28 · see citing works

Platelets redox balance assessment: Current evidence and methodological considerations

Komosa, A., Rzymski, P., Perek, B., Ropacka‐Lesiak, M., Lesiak, M., Siller-Matula, J. M., & Poniedziałek, B. (2017) · Vascular Pharmacology · doi:10.1016/j.vph.2017.06.002 · Cited by 28 · see citing works

Novel anti-thrombotic agent for modulation of protein disulfide isomerase family member ERp57 for prophylactic therapy

Cui, G., Shan, L., Guo, L., Chu, I. K., Li, G., Quan, Q., Zhao, Y., Chong, C. M., Zhang, Z., Yu, P., et al. (2015) · Scientific Reports · doi:10.1038/srep10353 · Cited by 27 · see citing works

Method parameters’ impact on mortality and variability in mouse stroke experiments: a meta-analysis

Ingberg, E., Dock, H., Theodorsson, E., Theodorsson, A., & Ström, J. O. (2016) · Scientific Reports · doi:10.1038/srep21086 · Cited by 25 · see citing works

Serum Levels of Glutathione Peroxidase 3 in Overweight and Obese Subjects from Central Mexico

Báez-Duarte, B. G., Zamora‐Ginez, I., Mendoza‐Carrera, F., Ruiz‐Vivanco, G., Torres‐Rasgado, E., González-Mejía, M. E., Garcı́a-Zapién, A. G., Flores-Martí­nez, S. E., & Pérez-Fuentes, R. (2012) · Archives of Medical Research · doi:10.1016/j.arcmed.2012.09.001 · Cited by 25 · see citing works

Platelet Redox Imbalance in Hypercholesterolemia: A Big Problem for a Small Cell

Morotti, A., Barale, C., Melchionda, E., & Russo, I. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911446 · Cited by 24 · see citing works

Peroxiredoxin II Is an Antioxidant Enzyme That Negatively Regulates Collagen-stimulated Platelet Function

Jang, J. Y., Wang, S. B., Min, J. H., Chae, Y. H., Baek, J. Y., Yu, D., & Chang, T. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.644260 · Cited by 24 · see citing works

Glutathione Peroxidase Activity and Expression Levels are Significantly Increased in Acute Coronary Syndromes

Holley, A., Pitman, J. L., Miller, J. H., Harding, S. A., & Larsen, P. (2017) · Journal of Investigative Medicine · doi:10.1136/jim-2016-000361 · Cited by 24 · see citing works

Microcystin-LR promotes necroptosis in primary mouse hepatocytes by overproducing reactive oxygen species

Wu, Y., He, Y., Shi, J., Zheng, T.-X., Lin, X., & Lin, X. (2019) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2019.114626 · Cited by 23 · see citing works

Glutathione infusion before primary percutaneous coronary intervention: a randomised controlled pilot study

Tanzilli, G., Truscelli, G., Arrivi, A., Carnevale, R., Placanica, A., Viceconte, N., Raparelli, V., Mele, R., Cammisotto, V., Nocella, C., et al. (2019) · BMJ Open · doi:10.1136/bmjopen-2018-025884 · Cited by 22 · see citing works

Redox Mechanisms of Platelet Activation in Aging

Gu, S. X., & Dayal, S. (2022) · Antioxidants · doi:10.3390/antiox11050995 · Cited by 21 · see citing works

Relationship between Proinflammatory and Antioxidant Proteins with the Severity of Cardiovascular Disease in Type 2 Diabetes Mellitus

García-Fontana, B., Morales, S., Longobardo, V., Reyes‐García, R., Rozas-Moreno, P., Garcia-Salcedo, J. A., & Muñoz‐Torres, M. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16059469 · Cited by 21 · see citing works

Is There an Interplay Between Adherence to Mediterranean Diet, Antioxidant Status, and Vascular Disease in Atrial Fibrillation Patients?

Pastori, D., Carnevale, R., Menichelli, D., Nocella, C., Bartimoccia, S., Novo, M., Leo, I., Violi, F., & Pignatelli, P. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6839 · Cited by 21 · see citing works

High-fat diet–induced plasma protein and liver changes in obese rats can be attenuated by melatonin supplementation

Wongchitrat, P., Klosen, P., Pannengpetch, S., Kitidee, K., Govitrapong, P., & Isarankura‐Na‐Ayudhya, C. (2017) · Nutrition Research · doi:10.1016/j.nutres.2017.04.011 · Cited by 21 · see citing works

Sprayable Reactive Oxygen Species-Responsive Hydrogel Coatings Restore Endothelial Barrier Integrity for Functional Vascular Healing

Zhao, J., Jia, F., Li, J., Tao, Y.-C., Hu, J.-Y., Ren, K., Ji, J., Fu, J., Fu, G., & Huang, H. (2025) · ACS Nano · doi:10.1021/acsnano.5c05477 · Cited by 20 · see citing works

Retinal Vascular Caliber in Coronary Heart Disease and Its Risk Factors

Liang, C., Gu, C., & Wang, N. (2022) · Ophthalmic Research · doi:10.1159/000526753 · Cited by 20 · see citing works

Glutathione (GSH) and the GSH synthesis geneGclmmodulate plasma redox and vascular responses to acute diesel exhaust inhalation in mice

Weldy, C. S., Luttrell, I. P., White, C. C., Morgan‐Stevenson, V., Cox, D. P., Carosino, C. M., Larson, T. V., Stewart, J. A., Kaufman, J. D., Kim, F., et al. (2013) · Inhalation Toxicology · doi:10.3109/08958378.2013.801004 · Cited by 19 · see citing works

Nitric oxide in vascular biology: elegance in complexity

Loscalzo, J. (2024) · Journal of Clinical Investigation · doi:10.1172/jci176747 · Cited by 19 · see citing works

Oxidative Stress, Selenium Redox Systems Including GPX/TXNRD Families

Ingold, I., & Conrad, M. (2018) · Molecular and integrative toxicology · doi:10.1007/978-3-319-95390-8_6 · Cited by 19 · see citing works

Association between High On-Aspirin Platelet Reactivity and Reduced Superoxide Dismutase Activity in Patients Affected by Type 2 Diabetes Mellitus or Primary Hypercholesterolemia

Barale, C., Cavalot, F. L., Frascaroli, C., Bonomo, K., Morotti, A., Guerrasio, A., & Russo, I. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21144983 · Cited by 19 · see citing works

Blood hydrogen peroxide break-down activity in healthy subjects and in patients at risk of cardiovascular events

Carnevale, R., Nocella, C., Pignatelli, P., Bartimoccia, S., Stefanini, L., Basili, S., Novo, M., D’Amico, A., Cammisotto, V., Pastori, D., et al. (2018) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2018.04.025 · Cited by 19 · see citing works

Selenium, Stroke, and Infection: A Threefold Relationship; Where Do We Stand and Where Do We Go?

Liampas, A., Zis, P., Hadjigeorgiou, G. M., & Vavougios, G. D. (2023) · Nutrients · doi:10.3390/nu15061405 · Cited by 18 · see citing works

The Role of Glutathione in Prevention of COVID-19 Immunothrombosis: A Review

Glassman, I., Le, N., Mirhosseini, M., Alcantara, C. A., Asif, A., Goulding, A., Muneer, S., Singh, M., Robison, J., Guilford, F., et al. (2023) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2803059 · Cited by 18 · see citing works

Post-ischemic protein restriction induces sustained neuroprotection, neurological recovery, brain remodeling, and gut microbiota rebalancing

de Carvalho, T. S., Singh, V., Yusuf, A. M., Wang, J., Moreira, A. R. S., Sánchez-Mendoza, E. H., Sardari, M., Melo, L. M. N., Doeppner, T. R., Kehrmann, J., et al. (2021) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2021.11.016 · Cited by 17 · see citing works

Statins as Regulators of Redox Signaling in Platelets

Violi, F., & Pignatelli, P. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5527 · Cited by 18 · see citing works

Plasma antioxidant enzymes and lipoperoxidation status in children with Down syndrome

He, J., Li, T., Chen, J., Liu, Y., Xiong, F., Yang, J., & Song, C. (2015) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2015.08.026 · Cited by 17 · see citing works

Plasma Glutathione Peroxidase Activity is Potentially a Key Regulator of Vascular Disease-Associated Thrombosis

Wolin, M. S. (2011) · Circulation · doi:10.1161/circulationaha.111.028688 · Cited by 17 · see citing works

Platelet Reactive Oxygen Species, Oxidised Lipid Stress, Current Perspectives, and an Update on Future Directions

Cheah, L. T., Hindle, M. S., Khalil, J. S., Duval, C., Unsworth, A. J., & Naseem, K. M. (2025) · Cells · doi:10.3390/cells14070500 · Cited by 16 · see citing works

Dualistic role of platelets in living donor liver transplantation: Are they harmful?

Chen, L., Takahashi, K., Furuya, K., Ohkohchi, N., & Oda, T. (2022) · World Journal of Gastroenterology · doi:10.3748/wjg.v28.i9.897 · Cited by 16 · see citing works

Abstract 5302: Glutathione Peroxidase-3 Deficiency Promotes Platelet-dependent Thrombosis and Thrombotic Stroke in vivo

Jin, R. C., Mahoney, C. E., Zhang, Y., Handy, D. E., & Loscalzo, J. (2009) · Circulation · doi:10.1161/circ.120.suppl_18.s1080-d

Abstract 5451: Deficiency of Glutathione Peroxidase-3 Promotes Platelet Activation in vivo

Jin, R. C., Mahoney, C. E., Coleman, L., Ottaviano, F. G., Zhang, Y., Handy, D. E., & Loscalzo, J. (2008) · Circulation · doi:10.1161/circ.118.suppl_18.s_552

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

Selenium Dependent Glutathione Peroxidase: A Physiological Regulatory System for Platelet Function

Perona, G., Schiavon, R., Guidi, G. C., Veneri, D., & Minuz, P. (1990) · Thrombosis and Haemostasis · doi:10.1055/s-0038-1647308 · Cited by 53 · see citing works

Vascular pentraxin 3 controls arterial thrombosis by targeting collagen and fibrinogen induced platelets aggregation

Bonacina, F., Barbieri, S. S., Cutuli, L., Amadio, P., Doni, A., Sironi, M., Tartari, S., Mantovani, A., Bottazzi, B., Garlanda, C., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.03.007 · Cited by 42 · see citing works