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Measurement of Reactive Oxygen Species in Cardiovascular Studies
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“However, the single-electron transfers are tightly controlled and quickly coupled with the second electron transfer (107, 293, 294).”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [107]
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Wang, H., & Joseph, J. A. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00107-0 · Cited by 2,355
Zelko, I. N., Mariani, T. J., & Folz, R. J. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00905-x · Cited by 2,212
Bass, D., Parce, J. W., DeChatelet, L. R., Szejda, P., Seeds, M. C., & Thomas, M. (1983) · The Journal of Immunology · doi:10.4049/jimmunol.130.4.1910 · Cited by 1,811
Landmesser, U., Dikalov, S., Price, S. R., McCann, L., Fukai, T., Holland, S. M., Mitch, W. E., & Harrison, D. G. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200314172 · Cited by 1,660
Self-citationLandmesser, U., Dikalov, S., Price, S. R., McCann, L. A., Fukai, T., Holland, S. M., Mitch, W. E., & Harrison, D. G. (2003) · Journal of Clinical Investigation · doi:10.1172/jci14172 · Cited by 1,652
Self-citationTopology of superoxide production from different sites in the mitochondrial electron transport chain
St-Pierre, J., Buckingham, J. A., Roebuck, S. J., & Brand, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207217200 · Cited by 1,545
Zhou, M., Diwu, Z. J., Panchuk-Voloshina, N., & Haugland, R. P. (1997) · Analytical Biochemistry · doi:10.1006/abio.1997.2391 · Cited by 1,400
Genetically encoded fluorescent indicator for intracellular hydrogen peroxide
Belousov, V. V., Fradkov, A. F., Lukyanov, K. A., Staroverov, D. B., Shakhbazov, K., Terskikh, A. V., & Lukyanov, S. (2006) · Nature Methods · doi:10.1038/nmeth866 · Cited by 1,286
Electron Paramagnetic Resonance: Elementary Theory and Practical Applications
Weil, J. A., Bolton, J. R., Wertz, J. E., & Buckmaster, H. A. (1995) · Physics Today · doi:10.1063/1.2808029 · Cited by 1,013
Mechanisms of Increased Vascular Superoxide Production in Human Diabetes Mellitus
Guzik, T. J., Mussa, S., Gastaldi, D., Sadowski, J., Ratnatunga, C., Pillai, R. G., & Channon, K. M. (2002) · Circulation · doi:10.1161/01.cir.0000012748.58444.08 · Cited by 979
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Sylvester, J. T., Shimoda, L. A., Aaronson, P. I., & Ward, J. P. T. (2012) · Physiological Reviews · doi:10.1152/physrev.00041.2010 · Cited by 741
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Dikalov, S., & Harrison, D. G. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4886 · Cited by 639
Self-citationMitochondrial Control of Cellular Life, Stress, and Death
Galluzzi, L., Kepp, O., Trojel‐Hansen, C., & Kroemer, G. (2012) · Circulation Research · doi:10.1161/circresaha.112.268946 · Cited by 568
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Stowe, D. F., & Camara, A. K. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2331 · Cited by 471
Griendling, K. K., Touyz, R. M., Zweier, J. L., Dikalov, S., Chilian, W. M., Chen, Y., Harrison, D. G., & Bhatnagar, A. (2016) · Circulation Research · doi:10.1161/res.0000000000000110 · Cited by 470
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Self-citationZielonka, J., Vasquez-Vivar, J. M., & Kalyanaraman, B. (2007) · Nature Protocols · doi:10.1038/nprot.2007.473 · Cited by 421
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Self-citationDikalov, S., Nazarewicz, R. R., Bikineyeva, A. T., Hilenski, L. L., Lassegue, B. P., Griendling, K. K., Harrison, D. G., & Dikalova, A. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4918 · Cited by 312
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Vinh, A., Chen, W., Blinder, Y., Weiss, D., Taylor, W. R., Goronzy, J. J., Weyand, C. M., Harrison, D. G., & Guzik, T. J. (2010) · Circulation · doi:10.1161/circulationaha.109.930446 · Cited by 305
Self-citationMethods to Monitor ROS Production by Fluorescence Microscopy and Fluorometry
Wojtala, A., Bonora, M., Malińska, D., Pinton, P., Duszyński, J., & Wieckowski, M. R. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-416618-9.00013-3 · Cited by 298
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Karlsson, M., Kurz, T., Brunk, U. T., NILSSON, S. E. G., & Frennesson, C. I. (2010) · Biochemical Journal · doi:10.1042/bj20100208 · Cited by 278
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Girouard, H., Wang, G., Gallo, E. F., Anrather, J., Zhou, P., Pickel, V. M., & Iadecola, C. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.0133-09.2009 · Cited by 254
Kröller‐Schön, S., Steven, S., Kossmann, S., Scholz, A., Daub, S., Oelze, M. W., Xia, N., Hausding, M., Mikhed, Y., Zinßius, E., et al. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4953 · Cited by 249
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Ayer, A., Zarjou, A., Agarwal, A., & Stocker, R. (2016) · Physiological Reviews · doi:10.1152/physrev.00003.2016 · Cited by 248
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Jaquet, V., Scapozza, L., Clark, R. A., Krause, K. H., & Lambeth, J. D. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2585 · Cited by 245
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Wind, S., Beuerlein, K., Eucker, T., Müller, H., Scheurer, P., Armitage, M., Ho, H., Schmidt, H., & Wingler, K. (2010) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2010.00920.x · Cited by 241
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Hall, J. E., Granger, J. P., do Carmo, J. M., da Silva, A. A., Dubinion, J., George, E., Hamza, S., Speed, J., & Hall, M. E. (2012) · Comprehensive Physiology · doi:10.1002/cphy.c110058 · Cited by 232
Lee, R., Margaritis, M., Channon, K. M., & Antoniades, C. A. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712800493057 · Cited by 231
Mukhopadhyay, A., Joshi, N., Chattopadhyay, K., & De, G. (2011) · ACS Applied Materials & Interfaces · doi:10.1021/am201166m · Cited by 225
Selemidis, S., Dusting, G. J., Peshavariya, H., Kemp‐Harper, B. K., & Drummond, G. R. (2007) · Cardiovascular Research · doi:10.1016/j.cardiores.2007.03.030 · Cited by 226
Dikalov, S., Itani, H. A., Richmond, B. W., Arslanbaeva, L., Vergeade, A., Rahman, S. M. J., Boutaud, O. G., Blackwell, T. S., Massion, P. P., Harrison, D. G., et al. (2019) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00595.2018 · Cited by 221
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Mellor, K. M., Bell, J. R., Young, M. J., Ritchie, R. H., & Delbridge, L. M. D. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.03.002 · Cited by 200
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Zhang, H., Limphong, P., Pieper, J., Liu, Q., Rodesch, C. K., Christians, E., & Benjamin, I. J. (2011) · The FASEB Journal · doi:10.1096/fj.11-199869 · Cited by 200
Herbert, K. E., Mistry, Y., Hastings, R., Poolman, T. M., Niklason, L. E., & Williams, B. (2007) · Circulation Research · doi:10.1161/circresaha.107.158626 · Cited by 192
Mitochondrial ROS production under cellular stress: comparison of different detection methods
Kuznetsov, A. V., Kehrer, I., Kozlov, A. V., Haller, M., Redl, H. R., Hermann, M., Grimm, M. F., & Troppmair, J. (2011) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-011-4764-2 · Cited by 187
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Nisbet, R. E., Bland, J. M., Kleinhenz, D. J., Mitchell, P. O., Walp, E. R., Sutliff, R. L., & Hart, C. M. (2009) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2008-0132oc · Cited by 188
Global Profiling of Reactive Oxygen and Nitrogen Species in Biological Systems
Zielonka, J., Zielonka, M., Sikora, A., Adamus, J., Joseph, J., Hardy, M., Ouari, O., Dranka, B. P., & Kalyanaraman, B. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.309062 · Cited by 186
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Kanti Das, T., Wati, M. R., & Fatima-Shad, K. (2014) · Archives of Neuroscience · doi:10.5812/archneurosci.20078 · Cited by 177
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Self-citationThe Role of NADPH Oxidase in Chronic Intermittent Hypoxia-Induced Pulmonary Hypertension in Mice
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Self-citationBernatchez, P. N., Sharma, A., Bauer, P. M., Marin, E. P., & Sessa, W. C. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44778 · Cited by 126
Wang, Q., & Zou, M.-H. (2018) · Methods in Molecular Biology · doi:10.1007/978-1-4939-7598-3_32 · Cited by 125
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Dikalov, S., Losik, T., & Arbiser, J. L. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.06.012 · Cited by 125
Self-citationUsselman, R. J., Hill, I., Singel, D. J., & Martino, C. F. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093065 · Cited by 126
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Dikalov, S., Polienko, Y. F., & Kirilyuk, I. A. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7396 · Cited by 122
Self-citationKopf, P. G., Huwe, J. K., & Walker, M. K. (2008) · Cardiovascular Toxicology · doi:10.1007/s12012-008-9027-x · Cited by 119
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Sorce, S., Stocker, R., Seredenina, T. S., Holmdahl, R., Aguzzi, A., Chiò, A., Depaulis, A., Heitz, F., Olofsson, P., Olsson, T. P., et al. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.08.006 · Cited by 113
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Wingler, K., Hermans, J., Schiffers, P., Moens, A., Paul, M., & Schmidt, H. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01249.x · Cited by 113
Zhang, C., Liu, L., Pan, Y., Qin, R., Wang, W., Zhou, M., & Zhang, Y. (2024) · Separation and Purification Technology · doi:10.1016/j.seppur.2024.129578 · Cited by 113
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Greenberg, H. Z. E., Zhao, G., Shah, A. M., & Zhang, M. (2021) · Cardiovascular Research · doi:10.1093/cvr/cvab142 · Cited by 115
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Burger, D. E., Turner, M., Xiao, F., Munkonda, M. N., Akbari, S., & Burns, K. D. (2017) · Diabetologia · doi:10.1007/s00125-017-4331-2 · Cited by 110
Laurindo, F. R. M., Fernandes, D. C., & Santos, C. X. C. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)01213-5 · Cited by 108
Mesquita, F. S., Dyer, S. N., Heinrich, D. A., Bulun, S. E., Marsh, E. E., & Nowak, R. A. (2009) · Biology of Reproduction · doi:10.1095/biolreprod.108.075887 · Cited by 101
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Self-citationDennis, K. E., Aschner, J. L., Milatović, D., Schmidt, J. W., Aschner, M., Kaplowitz, M. R., Zhang, Y., & Fike, C. D. (2009) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.90568.2008 · Cited by 94
Nitric oxide reduces NADPH oxidase 5 (Nox5) activity by reversible S-nitrosylation
Qian, J., Chen, F., Kovalenkov, Y. O., Pandey, D., Moseley, M. A., Foster, M. W., Black, S. M., Venema, R. C., Stepp, D. W., & Fulton, D. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.029 · Cited by 100
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Wang, J., Zhang, Y., Ogunnaike, E. A., Ligler, F. S., & Gu, Z. (2017) · Advanced Biosystems · doi:10.1002/adbi.201700084 · Cited by 96
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Razali, N. N. M., Ng, C. T., & Fong, L. Y. (2019) · Planta Medica · doi:10.1055/a-1008-6138 · Cited by 95
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Meng, D., Zhang, P., Zhang, L., Wang, H., Ho, C., Li, S., Shahidi, F., & Zhao, H. (2017) · Journal of Functional Foods · doi:10.1016/j.jff.2017.08.008 · Cited by 95
Owens, A. P., Subramanian, V., Moorleghen, J. J., Guo, Z., McNamara, C. A., Cassis, L. A., & Daugherty, A. (2009) · Circulation Research · doi:10.1161/circresaha.109.212837 · Cited by 97
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Taiwo, R. O., Sandouka, S., Saadi, A., & Shekh‐Ahmad, T. (2020) · Antioxidants · doi:10.3390/antiox9100990 · Cited by 91
Heiß, E. H., Schachner, D., Werner, E. R., & Dirsch, V. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.009175 · Cited by 89
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Jaffer, O. A., Carter, A. B., Sanders, P. N., Dibbern, M. E., Winters, C. J., Murthy, S., Ryan, A. J., Rokita, A. G., Prasad, A. M., Zabner, J., et al. (2014) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2013-0519oc · Cited by 86
Osgood, M. J., Hocking, K. M., Voskresensky, I. V., Li, F. D., Komalavilas, P., Cheung‐Flynn, J., & Brophy, C. M. (2013) · Journal of Vascular Surgery · doi:10.1016/j.jvs.2013.06.004 · Cited by 87
Caldiz, C. I., Garciarena, C. D., Dulce, R. A., Novaretto, L. P., Yeves, A. M., Ennis, I. L., Cingolani, H. E., de Cingolani, G. C., & Pérez, N. G. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.141689 · Cited by 86
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Itani, H. A., Dikalova, A., McMaster, W. G., Nazarewicz, R. R., Bikineyeva, A. T., Harrison, D. G., & Dikalov, S. (2016) · Hypertension · doi:10.1161/hypertensionaha.115.07085 · Cited by 86
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Hellack, B., Nickel, C., Albrecht, C., Kuhlbusch, T. A. J., Boland, S., Baeza‐Squiban, A., Wohlleben, W., & Schins, R. P. F. (2017) · Environmental Science Nano · doi:10.1039/c7en00346c · Cited by 85
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Yu, Q., Lee, C. F., Wang, W., Karamanlidis, G., Kuroda, J., Matsushima, S., Sadoshima, J., & Tian, R. (2014) · Journal of the American Heart Association · doi:10.1161/jaha.113.000555 · Cited by 85
Lubos, E., Kelly, N. J., Oldebeken, S. R., Leopold, J. A., Zhang, Y., Loscalzo, J., & Handy, D. E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.205708 · Cited by 84
Tomczyk, M. M., Cheung, K. G., Xiang, B., Tamanna, N., Teixeira, A. L. F., Agarwal, P., Kereliuk, S. M., Spicer, V., Lin, L., Treberg, J., et al. (2022) · Circulation Heart Failure · doi:10.1161/circheartfailure.121.008547 · Cited by 81
Metadata
- Authors
- Dikalov, S., Griendling, K. K., & Harrison, D. G.
- Affiliations
- United States Department of Veterans Affairs (US)
- Venue
- Hypertension
- Published
- 2007-04
- Volume
- 49
- Issue
- 4
- Pages
- 717-727
- ISSN
- 0194-911X (ISSN-L)
- 1524-4563
- PMC
- PMC1993891
- OpenAlex
- W2168961368
- Cited by
- 532
- References
- 88
- Citations by year
- 2026: 7 · 2025: 15 · 2024: 20 · 2023: 19 · 2022: 18 · 2021: 27 · 2020: 33 · 2019: 23 · 2018: 24 · 2017: 49 · 2016: 41 · 2015: 25 · 2014: 41 · 2013: 32 · 2012: 36
- FWCI
- 3.10
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Hypertension (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (5p01hl075209-05, 5r01hl059248-04)
- National Heart, Lung, and Blood Institute (HL 58000, HL 59248, HL38206, R01HL039006, HL-075209, R01HL038206, HL58863, R37HL038206, P0-1 HL-075209, P01HL058000, HL-39006, R01HL073101, R01HL058863)
- Topics
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- reactive oxygen species, oxidative stress, cardiovascular disease
- MeSH terms
- Animals, Cardiovascular System, Cardiovascular Physiological Phenomena, Humans, Reactive Oxygen Species, Biomedical Research
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