The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Glutathione Peroxidase-3 Deficiency Promotes Platelet-Dependent Thrombosis In Vivo
Open accessAbstract
Background—: Glutathione peroxidase-3 (GPx-3) is a selenocysteine-containing plasma protein that scavenges reactive oxygen species in the extracellular compartment. A deficiency of this enzyme has been associated with platelet-dependent thrombosis, and a promoter haplotype with reduced function has been associated with stroke risk. Methods and Results—: We recently developed a genetic mouse model to assess platelet function and thrombosis in the setting of GPx-3 deficiency. The GPx-3(−/−)mice showed an attenuated bleeding time and an enhanced aggregation response to the agonist ADP compared with wild-type mice. GPx-3(−/−)mice displayed increased plasma levels of soluble P-selectin and decreased plasma cyclic cGMP compared with wild-type mice. ADP infusion-induced platelet aggregation in the pulmonary vasculature produced a more robust platelet activation response in the GPx-3(−/−)than wild-type mice; histological sections from the pulmonary vasculature of GPx-3(−/−)compared with wild-type mice showed increased platelet-rich thrombi and a higher percentage of occluded vessels. Cremaster muscle preparations revealed endothelial dysfunction in the GPx-3(−/−)compared with wild-type mice. With a no-flow ischemia-reperfusion stroke model, GPx-3(−/−)mice had significantly larger cerebral infarctions compared with wild-type mice and platelet-dependent strokes. To assess the neuroprotective role of antioxidants in this model, we found that manganese(III) meso-tetrakis(4-benzoic acid)porphyrin treatment reduced stroke size in GPx-3(−/−)mice compared with vehicle-treated controls. Conclusions—: These findings demonstrate that GPx-3 deficiency results in a prothrombotic state and vascular dysfunction that promotes platelet-dependent arterial thrombosis. These data illustrate the importance of this plasma antioxidant enzyme in regulating platelet activity, endothelial function, platelet-dependent thrombosis, and vascular thrombotic propensity.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Deficiency of GPx-3 in humans or knockout mice potentiates platelet activation and thrombosis (139, 193, 212).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [193]
In the citing paper
“Furthermore, in GPx-3 knockout mice, deficiency of this extracellular antioxidant causes endothelial dysfunction and increased sensitivity to neuronal injury in a brain model of ischemia reperfusion injury by mechanisms related to its key functions as an antioxidant enzyme and regulator of platelet-dependent thrombosis (193).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [193]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
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
Nitric Oxide Insufficiency, Platelet Activation, and Arterial Thrombosis
Loscalzo, J. (2001) · Circulation Research · doi:10.1161/hh0801.089861 · Cited by 612
Self-citationTakahashi, 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
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 322
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
Day, B. J., Fridovich, I., & Crapo, J. D. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0341 · Cited by 285
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
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
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
Cited by
Sorted by citations
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
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
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 933
Redox regulation of mitochondrial function
Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588
Self-citationInflammaging 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 560
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 455
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 410
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
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
Keshan Disease, Selenium Deficiency, and the Selenoproteome
Loscalzo, J. (2014) · New England Journal of Medicine · doi:10.1056/nejmcibr1402199 · Cited by 245
Self-citationROS 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 244
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 232
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 198
Sakellariou, G. K., Jackson, M. J., & Vasilaki, A. (2014) · Free Radical Research · doi:10.3109/10715762.2013.830718 · Cited by 184
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
Brigelius‐Flohé, R., & Flohé, L. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.08.003 · Cited by 162
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 162
Redox Mechanisms in Neurodegeneration: From Disease Outcomes to Therapeutic Opportunities
Sbodio, J. I., Snyder, S. H., & Paul, B. D. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7321 · Cited by 149
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 125
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 119
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
Platelet Oxidative Stress and Thrombosis
Violi, F., & Pignatelli, P. (2011) · Thrombosis Research · doi:10.1016/j.thromres.2011.12.002 · Cited by 107
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 109
Self-citationYang, 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 93
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 91
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 87
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
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
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
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
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 77
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 71
Zhang, L., Zeng, H., & Cheng, W. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.05.067 · Cited by 67
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 65
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 66
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 64
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
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
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
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
Biological and Catalytic Properties of Selenoproteins
Chaudière, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241210109 · Cited by 64
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 60
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
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 57
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 63
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
Self-citationPang, 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 50
Self-citationUnderstanding thrombosis: the critical role of oxidative stress
Li, P., Ma, X., & Huang, G. (2024) · Hematology · doi:10.1080/16078454.2023.2301633 · Cited by 49
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
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
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
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
Self-citationMeshkini, A., & Tahmasbi, M. (2017) · Journal of Acupuncture and Meridian Studies · doi:10.1016/j.jams.2017.02.007 · Cited by 41
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 42
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 40
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 39
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
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 40
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 40
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
Modulators of platelet function in aging
Iyer, K. S., & Dayal, S. (2019) · Platelets · doi:10.1080/09537104.2019.1665641 · Cited by 35
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
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
Potaczek, D. P., Jankowska, E. A., Wypasek, E., & Undas, A. (2016) · Polskie Archiwum Medycyny Wewnętrznej · doi:10.20452/pamw.3311 · Cited by 32
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
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
Self-citationDecharatchakul, 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 30
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
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
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
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 29
Vyletelová, V., Nováková, M., & Pašková, Ľ. (2022) · Pharmaceuticals · doi:10.3390/ph15101278 · Cited by 30
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
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
Method parameters’ impact on mortality and variability in mouse stroke experiments: a meta-analysis
Ingberg, E., Dock, H., Theodorsson, E., Theodorsson, A., & Ström, J. (2016) · Scientific Reports · doi:10.1038/srep21086 · Cited by 20
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 26
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 25
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 25
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 23
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
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
Redox Mechanisms of Platelet Activation in Aging
Gu, S. X., & Dayal, S. (2022) · Antioxidants · doi:10.3390/antiox11050995 · Cited by 23
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
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
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
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 21
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
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
Nitric oxide in vascular biology: elegance in complexity
Loscalzo, J. (2024) · Journal of Clinical Investigation · doi:10.1172/jci176747 · Cited by 20
Self-citationOxidative 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
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
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
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
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
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
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
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
Wolin, M. S. (2011) · Circulation · doi:10.1161/circulationaha.111.028688 · Cited by 17
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 18
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
Metadata
- Authors
- Jin, R. C., Mahoney, C. E., (Coleman) Anderson, L., Ottaviano, F., Croce, K., Leopold, J. A., Zhang, Y.-Y., Tang, S.-S., Handy, D. E., & Loscalzo, J.
- Affiliations
- Brigham and Women's Hospital (US)
- From the Cardiovascular Division, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA.
- ORCID
- Venue
- Circulation
- Published
- 2011-05-10
- Volume
- 123
- Issue
- 18
- Pages
- 1963-1973
- ISSN
- 0009-7322 (ISSN-L)
- 1524-4539
- PMC
- PMC3107543
- OpenAlex
- W2058584041
- Cited by
- 186
- References
- 33
- Citations by year
- 2026: 5 · 2025: 13 · 2024: 16 · 2023: 13 · 2022: 22 · 2021: 11 · 2020: 7 · 2019: 11 · 2018: 9 · 2017: 8 · 2016: 19 · 2015: 13 · 2014: 11 · 2013: 14 · 2012: 5
- FWCI
- 8.10
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Circulation (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (n01hv28178-12-0-0)
- National Heart, Lung, and Blood Institute (HL 089734, HL081587, HL 070819, K08HL086672, U54HL070819, HL086672, P01HL081587, N01-HV-028178, R21HL089734, R01HL105301, P01HL048743, HL-061795, R37HL061795)
- Topics
- Health Sciences › Medicine › Hematology › Platelet Disorders and Treatments
- Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
- Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
- Keywords
- glutathione peroxidase 3, platelet aggregation, ADP-induced aggregation, soluble P-selectin, pulmonary vasculature, endothelial dysfunction, cerebral infarction, manganese porphyrin, antioxidants, reactive oxygen species, selenocysteine, genetic mouse models
- MeSH terms
- Adenosine Diphosphate, Animals, Antioxidants, Bleeding Time, Blood Platelets, Disease Models, Animal, Endothelium, Vascular, Genotype, Glutathione, Glutathione Peroxidase, Cyclic GMP, Platelet Aggregation, Risk Factors, Thrombosis, Reactive Oxygen Species, Mice, Knockout, P-Selectin, Infarction, Middle Cerebral Artery, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review