Fundamentals on the biochemistry of peroxynitrite and protein tyrosine nitration
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In this review we provide an analysis of the biochemistry of peroxynitrite and tyrosine nitration. Peroxynitrite is the product of the diffusion-controlled reaction between superoxide (O 2 • - ) and nitric oxide ( • NO). This process is in competition with the enzymatic dismutation of O 2 •- and the diffusion of • NO across cells and tissues and its reaction with molecular targets ( e.g. guanylate cyclase). Understanding the kinetics and compartmentalization of the O 2 •- / • NO interplay is critical to rationalize the shift of • NO from a physiological mediator to a cytotoxic intermediate. Once formed, peroxynitrite (ONOO - and ONOOH; pKa = 6,8) behaves as a strong one and two-electron oxidant towards a series of biomolecules including transition metal centers and thiols. In addition, peroxynitrite anion can secondarily evolve to secondary radicals either via its fast reaction with CO 2 or through proton-catalyzed homolysis. Thus, peroxynitrite can participate in direct (bimolecular) and indirect (through secondary radical intermediates) oxidation reactions; through these processes peroxynitrite can participate as cytotoxic effector molecule against invading pathogens and/or as an endogenous pathogenic mediator. Peroxynitrite can cause protein tyrosine nitration in vitro and in vivo . Indeed, tyrosine nitration is a hallmark of the reactions of • NO-derived oxidants in cells and tissues and serves as a biomarker of oxidative damage. Protein tyrosine nitration can mediate changes in protein structure and function that affect cell homeostasis. Tyrosine nitration in biological systems is a free radical process that can be promoted either by peroxynitrite-derived radicals or by other related • NO-dependent oxidative processes. Recently, mechanisms responsible of tyrosine nitration in hydrophobic biostructures such as membranes and lipoproteins have been assessed and involve the parallel occurrence and connection with lipid peroxidation. Experimental strategies to reveal the proximal oxidizing mechanism during tyrosine nitration in given pathophysiologically-relevant conditions include mapping and identification of the tyrosine nitration sites in specific proteins.
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The irreversible modification 3-nitrotyrosine is formed by nitration of tyrosine via attack of the nitrogen dioxide radical at the ortho-position of the aromatic ring.
“The irreversible modification 3-nitrotyrosine (3-NT) is formed by nitration of tyrosine via attack of the nitrogen dioxide radical at the ortho-position of the aromatic ring [74].”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [74]
The “Nitration as a free radical process” section (page unavailable) states that nitration places a nitro group at position 3 of tyrosine’s phenolic ring and that the tyrosine radical reacts with •NO2 to yield 3-nitrotyrosine. It does not establish that the resulting 3-nitrotyrosine modification is irreversible; its discussion of reversal concerns the tyrosine-radical intermediate, not the nitrated product. (LLM, conf=0.85)
Experimental — accuracy not yet measuredPeroxynitrite can modify proteins by nitration or oxidation of amino acids, involving cysteine, tyrosine, and methionine.
“In addition, peroxynitrite can modify proteins by nitration or oxidation of amino acids, involving cysteine, tyrosine, and methionine (Bartesaghi and Radi 2018).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Bartesaghi and Radi 2018
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Cites
Nitric oxide: physiology, pathophysiology, and pharmacology.
Moncada, S., Palmer, R. M., & Higgs, E. A. (1991) · Pharmacological Reviews · doi:10.1016/s0031-6997(25)06663-3 · Cited by 15,525 · see citing works
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 · see citing works
Nitric Oxide and Peroxynitrite in Health and Disease
Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390 · see citing works
Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide.
Ignarro, L. J., Buga, G. M., Wood, K. S., Byrns, R. E., & Chaudhuri, G. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.24.9265 · Cited by 5,074 · see citing works
Sies, H., Berndt, C., & Jones, D. P. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045037 · Cited by 3,520 · see citing works
Fridovich (1978) · doi:10.1126/science.210504 · Cited by 3,329 · see citing works
Peroxynitrite oxidation of sulfhydryls.
Radí, R., Beckman, J. S., Bush, K., & Freeman, B. Α. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64313-7 · Cited by 2,499 · see citing works
Sies, H. (2017) · Redox Biology · doi:10.1016/j.redox.2016.12.035 · Cited by 2,148 · see citing works
Peroxynitrite: biochemistry, pathophysiology and development of therapeutics
Szabó, C., Ischiropoulos, H., & Radi, R. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2222 · Cited by 2,134 · see citing works
Self-citationFridovich, I. (1975) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.44.070175.001051 · Cited by 1,735 · see citing works
Giasson, B. I., Duda, J. E., Murray, I. V. J., Chen, Q., Souza, J. M., Hurtig, H. I., Ischiropoulos, H., Trojanowski, J. Q., & Lee, V. M. ‐. (2000) · Science · doi:10.1126/science.290.5493.985 · Cited by 1,551 · see citing works
Nitric oxide, oxidants, and protein tyrosine nitration
Radí, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307446101 · Cited by 1,456 · see citing works
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
Peroxynitrite, a cloaked oxidant formed by nitric oxide and superoxide
Koppenol, W. H., Moreno, J. J., Pryor, W. A., Ischiropoulos, H., & Beckman, J. S. (1992) · Chemical Research in Toxicology · doi:10.1021/tx00030a017 · Cited by 1,338 · see citing works
Nitric oxide : biology and pathobiology
Ignarro, L. J. (2000) · Cited by 1,300 · see citing works
Biosynthesis And Metabolism Of Endothelium-Derived Nitric Oxide
Ignarro, L. J. (1990) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.30.040190.002535 · Cited by 1,300 · see citing works
Cleeter, M. W. J., Cooper, J. M., Darley-Usmar, V. M., Moncada, S., & Schapira, A. H. V. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00424-2 · Cited by 1,241 · see citing works
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 · see citing works
Fridovich, I. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83102-7 · Cited by 964 · see citing works
BABIOR, B. M., Lambeth, J. D., & Nauseef, W. M. (2002) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2642 · Cited by 911 · see citing works
Peroxynitrite, a Stealthy Biological Oxidant
Radí, R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.472936 · Cited by 891 · see citing works
Endothelial dysfunction: a multifaceted disorder (The Wiggers Award Lecture)
Félétou, M., & Vanhoutte, P. M. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00292.2006 · Cited by 818 · cited 1× · see citing works
“Protein tyrosine nitration is consistently observed in several pathologies such as cardiovascular disease [76], neurodegeneration [77–79], inflammation and cancer [80].”
BackgroundChemical biology of peroxynitrite: Kinetics, diffusion, and radicals
Ferrer-Sueta, G., & Radi, R. (2009) · ACS Chemical Biology · doi:10.1021/cb800279q · Cited by 776 · see citing works
MacMillan-Crow, L.-A., Crow, J. P., Kerby, J. D., Beckman, J. S., & Thompson, J. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11853 · Cited by 768 · see citing works
Unraveling peroxynitrite formation in biological systems
Radi, R., Peluffo, G., Alvarez, M. N., Naviliat, M., & Cayota, A. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00373-7 · Cited by 735 · see citing works
Self-citationEndothelium‐derived nitric oxide: actions and properties
Ignarro, L. J. (1989) · The FASEB Journal · doi:10.1096/fasebj.3.1.2642868 · Cited by 679 · see citing works
Kissner, R., Nauser, T., Bugnon, P., Lye, P. G., & Koppenol, W. H. (1997) · Chemical Research in Toxicology · doi:10.1021/tx970160x · Cited by 629 · see citing works
Denicola, A., Freeman, B. A., Trujillo, M., & Radi, R. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0363 · Cited by 593 · see citing works
Self-citationProduction of Nitric Oxide by Mitochondria
Giulivi, C., Poderoso, J. J., & Boveris, A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.18.11038 · Cited by 572 · see citing works
Peroxynitrite reactivity with amino acids and proteins
Alvarez, B., & Radi, R. (2003) · Amino Acids · doi:10.1007/s00726-003-0018-8 · Cited by 560 · see citing works
Protein Nitration in Parkinsonʼs Disease
Good, P. F., Hsu, A., Werner, P., Perl, D. P., & Olanow, C. W. (1998) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199804000-00006 · Cited by 540 · see citing works
Protein Tyrosine Nitration: Biochemical Mechanisms and Structural Basis of Functional Effects
Radi, R. (2013) · Accounts of Chemical Research · doi:10.1021/ar300234c · Cited by 525 · see citing works
Self-citationSuperoxide sensitivity of the Escherichia coli aconitase.
Gardner, P. R., & Fridovich, I. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55001-8 · Cited by 514 · see citing works
Klug-Roth, D., Rabani, J., & Fridovich, I. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44987-9 · Cited by 495 · see citing works
Yamakura, F., Taka, H., Fujimura, T., & Murayama, K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.23.14085 · Cited by 442 · see citing works
Protein tyrosine nitration—Functional alteration or just a biomarker?
Souza, J. M., Peluffo, G., & Radí, R. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.04.010 · Cited by 394 · see citing works
Vasoprotection by nitric oxide: mechanisms and therapeutic potential
Gewaltig, M. T. (2002) · Cardiovascular Research · doi:10.1016/s0008-6363(02)00327-9 · Cited by 369 · see citing works
One- and two-electron oxidations of methionine by peroxynitrite.
PRYOR, W. A., Jin, X., & Squadrito, G. L. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.23.11173 · Cited by 324 · see citing works
The Reaction of Nitric Oxide with Organic Peroxyl Radicals
Padmaja, S., & Huie, R. E. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.2079 · Cited by 323 · see citing works
Factors Determining the Selectivity of Protein Tyrosine Nitration
Souza, J. M., Daikhin, E., Yudkoff, M., Raman, C. S., & Ischiropoulos, H. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1480 · Cited by 315 · see citing works
Sulfenic Acid Formation in Human Serum Albumin by Hydrogen Peroxide and Peroxynitrite
Carballal, S., Radí, R., KIRK, M. C., Barnes, S., Freeman, B. Α., & Álvarez, B. (2003) · Biochemistry · doi:10.1021/bi027434m · Cited by 313 · see citing works
Direct EPR Detection of the Carbonate Radical Anion Produced from Peroxynitrite and Carbon Dioxide
Bonini, M. G., Radi, R., Ferrer-Sueta, G., Ferreira, A. M. D. C., & Augusto, O. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.16.10802 · Cited by 293 · see citing works
Antioxidation mechanisms of uric acid
Simic, M. G., & Jovanović, S. V. (1989) · Journal of the American Chemical Society · doi:10.1021/ja00197a042 · Cited by 290 · see citing works
Peroxynitrite-Dependent Tryptophan Nitration
Álvarez, B., Rubbo, H., KIRK, M. C., Barnes, S., Freeman, B. Α., & Radí, R. (1996) · Chemical Research in Toxicology · doi:10.1021/tx950133b · Cited by 259 · see citing works
Pryor, W. A., & Lightsey, J. W. (1981) · Science · doi:10.1126/science.214.4519.435 · Cited by 255 · see citing works
Kinetics of Peroxynitrite Reaction with Amino Acids and Human Serum Albumin
Álvarez, B., Ferrer‐Sueta, G., Freeman, B. Α., & Radí, R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.2.842 · Cited by 253 · see citing works
Ford, E., Hughes, M., & Wardman, P. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00850-x · Cited by 229 · see citing works
Shao, B., Bergt, C., Fu, X., Green, P., Voss, J. C., Oda, M. N., Oram, J. F., & Heinecke, J. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411484200 · Cited by 227 · see citing works
Reaction of Peroxynitrite with Mn-Superoxide Dismutase
Quijano, C., Hernández-Saavedra, D., Castro, L., McCord, J. M., Freeman, B. Α., & Radí, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009429200 · Cited by 185 · see citing works
Trujillo, M., & Radí, R. (2002) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2619 · Cited by 180 · see citing works
Peroxynitrite Mediated Oxidation of Purine Bases of Nucleosides and Isolated DNA
Douki, T., & Cadet, J. (1996) · Free Radical Research · doi:10.3109/10715769609088035 · Cited by 178 · see citing works
Peroxynitrite Reactions and Diffusion in Biology
Radí, R. (1998) · Chemical Research in Toxicology · doi:10.1021/tx980096z · Cited by 172 · see citing works
Quantitation of 8-Oxoguanine and Strand Breaks Produced by Four Oxidizing Agents
Kennedy, L. J., Moore, K., Caulfield, J. L., Tannenbaum, S. R., & Dedon, P. C. (1997) · Chemical Research in Toxicology · doi:10.1021/tx960102w · Cited by 169 · see citing works
Kinetic and mechanistic considerations to assess the biological fate of peroxynitrite
Carballal, S., Bartesaghi, S., & Radí, R. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.07.005 · Cited by 160 · see citing works
Self-citationThe effect of oxygen, antioxidants, and superoxide radical on tyrosine phenoxyl radical dimerization
Hunter, E. P. L., Desrosiers, M. F., & Simic, M. G. (1989) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(89)90064-6 · Cited by 153 · see citing works
Dang, P. M., Cross, A. R., Quinn, M. T., & BABIOR, B. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.072345299 · Cited by 149 · see citing works
Möller, M. N., Botti, H., Batthyány, C., Rubbo, H., Radí, R., & Denicola, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413699200 · Cited by 145 · see citing works
The Role of Oxidative Stress in Amyotrophic Lateral Sclerosis and Parkinson’s Disease
Baillet, A. C., Chanteperdrix, V., Trocmé, C., Casez, P., Garrel, C., & Besson, G. (2010) · Neurochemical Research · doi:10.1007/s11064-010-0212-5 · Cited by 143 · see citing works
One- and two-electron oxidation of thiols: mechanisms, kinetics and biological fates
Trujillo, M., Alvarez, B., & Radi, R. (2016) · Free Radical Research · doi:10.3109/10715762.2015.1089988 · Cited by 142 · see citing works
CO2-Catalyzed One-Electron Oxidations by Peroxynitrite: Properties of the Reactive Intermediate
Lymar, S. V., & Hurst, J. K. (1998) · Inorganic Chemistry · doi:10.1021/ic970946i · Cited by 141 · see citing works
Kinetics of Peroxiredoxins and their Role in the Decomposition of Peroxynitrite
Trujillo, M., Ferrer‐Sueta, G., Thomson, L., Flohé, L., & Radí, R. (2007) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4020-6051-9_5 · Cited by 140 · see citing works
Reactions of Nitric Oxide with Metalloproteins
Radí, R. (1996) · Chemical Research in Toxicology · doi:10.1021/tx950176s · Cited by 139 · see citing works
Protein tyrosine nitration in hydrophilic and hydrophobic environments
Bartesaghi, S., Ferrer‐Sueta, G., Peluffo, G., Valez, V., Zhang, H., Kalyanaraman, B., & Radí, R. (2006) · Amino Acids · doi:10.1007/s00726-006-0425-8 · Cited by 130 · see citing works
Self-citationThe Biological Chemistry of Peroxynitrite
Radí, R., Denicola, A., Álvarez, B., Ferrer‐Sueta, G., & Rubbo, H. (2000) · Elsevier eBooks · doi:10.1016/b978-012370420-7/50005-8 · Cited by 115 · see citing works
Time Course and Site(s) of Cytochrome <i>c</i> Tyrosine Nitration by Peroxynitrite
Batthyány, C., Souza, J. M., Durán, R., Cassina, A., Cerveñansky, C., & Radi, R. (2005) · Biochemistry · doi:10.1021/bi0474620 · Cited by 112 · see citing works
Self-citationOn the limited ability of superoxide to release iron from ferritin
Bolann, B. J., & Ulvik, R. J. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19415.x · Cited by 111 · see citing works
[37] Peroxynitrite reactions with carbon dioxide-bicarbonate
Radí, R., Denicola, A., & Freeman, B. Α. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)01099-x · Cited by 103 · see citing works
Reduction of protein radicals by GSH and ascorbate: potential biological significance
Gebicki, J. M., Nauser, T., Domazou, A. S., Steinmann, D., Bounds, P. L., & Koppenol, W. H. (2010) · Amino Acids · doi:10.1007/s00726-010-0610-7 · Cited by 100 · see citing works
Abriata, L. A., Cassina, A., Tórtora, V., Marı́n, M., Souza, J. M., Castro, L., Vila, A. J., & Radí, R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807203200 · Cited by 100 · see citing works
Tyrosine-nitrated proteins: Proteomic and bioanalytical aspects
Batthyány, C., Bartesaghi, S., Mastrogiovanni, M., Lima, A., Demicheli, V., & Radi, R. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6787 · Cited by 86 · see citing works
Self-citationBartesaghi, S., Valez, V., Trujillo, M., Peluffo, G., Romero, N., Zhang, H., Kalyanaraman, B., & Radi, R. (2006) · Biochemistry · doi:10.1021/bi060363x · Cited by 78 · see citing works
Self-citationKinetic Studies on Peroxynitrite Reduction by Peroxiredoxins
Trujillo, M., Ferrer‐Sueta, G., & Radí, R. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)01210-x · Cited by 77 · see citing works
Lipid Peroxyl Radicals Mediate Tyrosine Dimerization and Nitration in Membranes
Bartesaghi, S., Wenzel, J., Trujillo, M., López, M., Joseph, J., Kalyanaraman, B., & Radi, R. (2010) · Chemical Research in Toxicology · doi:10.1021/tx900446r · Cited by 76 · see citing works
Self-citationKinetics of reduction of tyrosine phenoxyl radicals by glutathione
Folkes, L. K., Trujillo, M., Bartesaghi, S., Radí, R., & Wardman, P. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.12.006 · Cited by 74 · see citing works
Self-citation[33] Kinetic analysis of reactivity of peroxynitrite with biomolecules
Radí, R. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)69036-3 · Cited by 69 · see citing works
S. Rocha, B., Gago, B., Pereira, C., M. Barbosa, R., Bartesaghi, S., O. Lundberg, J., Radi, R., & Laranjinha, J. (2011) · Current Drug Targets · doi:10.2174/138945011796150334 · Cited by 64 · see citing works
Self-citationThe Effect of Bicarbonate on Oxidation by Peroxynitrite: Implication for Its Biological Activity
Goldstein, S., & Czapski, G. (1997) · Inorganic Chemistry · doi:10.1021/ic970471v · Cited by 61 · see citing works
Oxidative Damage of Biomolecules by the Environmental Pollutants NO 2 • and NO 3 •
Gamon, L. F., & Wille, U. (2016) · Accounts of Chemical Research · doi:10.1021/acs.accounts.6b00219 · Cited by 61 · see citing works
Martínez, A., Peluffo, G., Petruk, A. A., Hugo, M., Piñeyro, M. D., Demicheli, V., Moreno, D. M., Lima, A. E., Batthyány, C., Durán, R., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.545590 · Cited by 60 · see citing works
Kennett, E. C., & Davies, M. J. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.05.002 · Cited by 59 · see citing works
Metal-catalyzed protein tyrosine nitration in biological systems
Campolo, N., Bartesaghi, S., & Radí, R. (2014) · Redox Report · doi:10.1179/1351000214y.0000000099 · Cited by 55 · see citing works
Self-citationNagy, P., Kettle, A. J., & Winterbourn, C. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809396200 · Cited by 53 · see citing works
Nitrogen dioxide solubility and permeation in lipid membranes
Signorelli, S., Möller, M. N., Coitiño, E. L., & Denicola, A. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.06.003 · Cited by 49 · see citing works
Kennett, E. C., Rees, M. D., Malle, E., Hammer, A., Whitelock, J. M., & Davies, M. J. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.04.018 · Cited by 48 · see citing works
Factors influencing protein tyrosine nitration—structure-based predictive models
Bayden, A. S., Yakovlev, V. A., Graves, P. R., Mikkelsen, R. B., & Kellogg, G. E. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.12.016 · Cited by 48 · see citing works
Kinetics of the oxidation of nitric oxide by chlorine and oxygen in nonaqueous media
Nottingham, W. C., & Sutter, J. R. (1986) · International Journal of Chemical Kinetics · doi:10.1002/kin.550181107 · Cited by 44 · see citing works
Rocha, B. S., Gago, B., Barbosa, R. M., Lundberg, J. O., Mann, G. E., Radí, R., & Laranjinha, J. A. N. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.12.017 · Cited by 34 · see citing works
Petruk, A. A., Bartesaghi, S., Trujillo, M., Estrin, D. A., Murgida, D. H., Kalyanaraman, B., Marti, M. A., & Radí, R. (2012) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2012.05.012 · Cited by 32 · see citing works
Self-citationZhang, H., Zielonka, J., Sikora, A., Joseph, J., Xu, Y., & Kalyanaraman, B. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.11.018 · Cited by 26 · see citing works
Biochemistry of Nitric Oxide and Peroxynitrite: Sources, Targets and Biological Implications
Aicardo, A., Martinez, D. M., Campolo, N., Bartesaghi, S., & Radí, R. (2016) · Springer eBooks · doi:10.1007/978-3-319-45865-6_5 · Cited by 21 · see citing works
Self-citationKinetics of oxidation of tyrosine by a model alkoxyl radical
Folkes, L. K., Bartesaghi, S., Trujillo, M., Radí, R., & Wardman, P. (2012) · Free Radical Research · doi:10.3109/10715762.2012.695868 · Cited by 19 · see citing works
Self-citationBiological Antioxidant Defenses
Radí, R. (1993) · Toxicology and Industrial Health · doi:10.1177/0748233793009001-206 · Cited by 19 · see citing works
The Interaction of Reactive Oxygen and Nitrogen Species with Membranes
Möller, M. N., Lancaster, J. R., & Denicola, A. (2008) · Cited by 19 · see citing works
Tyrosine oxidation and nitration in transmembrane peptides is connected to lipid peroxidation
Bartesaghi, S., Herrera, D., Martinez, D. M., Petruk, A., Demicheli, V., Trujillo, M., Martí, M. A., Estrín, D. A., & Radi, R. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.04.006 · Cited by 18 · see citing works
Self-citationZeida, A., Reyes, A. M., Lichtig, P., et al. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00758 · Cited by 17 · see citing works
Romero, N., Peluffo, G., Bartesaghi, S., Zhang, H., Joseph, J., Kalyanaraman, B., & Radí, R. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700142a · Cited by 15 · see citing works
Self-citationOxidative Inactivation of Nitric Oxide and Peroxynitrite Formation in the Vasculature
Subelzú, N., Bartesaghi, S., Bem, A. F. D., & Radí, R. (2015) · ACS symposium series · doi:10.1021/bk-2015-1200.ch004 · Cited by 12 · see citing works
Self-citation"Aerosolized deferoxamine prevents lung and systemic injury caused by smoke inhalation"
Crapo, J. D. (1994) · Journal of Applied Physiology · doi:10.1152/jappl.1994.77.5.2055 · Cited by 6 · see citing works
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Reactive oxygen species (ROS) as pleiotropic physiological signalling agents
Sies, H., & Jones, D. P. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0230-3 · Cited by 5,335 · see citing works
Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging
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Jomova, K., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2024) · Archives of Toxicology · doi:10.1007/s00204-024-03696-4 · Cited by 1,445 · see citing works
Janaszak-Jasiecka, A., Płoska, A., Wierońska, J. M., Dobrucki, L. W., & Kalinowski, L. (2023) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-023-00423-2 · Cited by 358 · see citing works
Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases
Kehm, R., Baldensperger, T., Raupbach, J., & Höhn, A. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101901 · Cited by 348 · see citing works
“The irreversible modification 3-nitrotyrosine (3-NT) is formed by nitration of tyrosine via attack of the nitrogen dioxide radical at the ortho-position of the aromatic ring [74].”
BackgroundThe biology of ergothioneine, an antioxidant nutraceutical
Borodina, I., Kenny, L. C., McCarthy, C. M., Paramasivan, K., Pretorius, E., Roberts, T. J., van der Hoek, S. A., & Kell, D. B. (2020) · Nutrition Research Reviews · doi:10.1017/s0954422419000301 · Cited by 296 · see citing works
Self-defense of macrophages against oxidative injury: Fighting for their own survival
Virág, L., Jaén, R. I., Regdon, Z., Boscá, L., & Prieto, P. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101261 · Cited by 121 · see citing works
Niki, E., & Noguchi, N. (2021) · Free Radical Research · doi:10.1080/10715762.2020.1866181 · Cited by 47 · see citing works
Tramutola, A., Abate, G., Lanzillotta, C., Triani, F., Barone, E., Iavarone, F., Vincenzoni, F., Castagnola, M., Marziano, M., Memo, M., et al. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.414 · Cited by 26 · see citing works
- Authors
- Bartesaghi, S., & Radi, R.
- Affiliations
- Universidad de la República de Uruguay (UY)
- Corresponding author
- Bartesaghi, Silvina
- ORCID
- Bartesaghi, Silvina
- Venue
- Redox Biology
- Publisher
- Elsevier BV
- Published
- 2018-04
- Volume
- 14
- Pages
- 618-625
- ISSN
- 2213-2317 (ISSN-L)
- PMC
- PMC5694970
- OpenAlex
- W2756324351
- Cited by
- 485
- References
- 98
- Citations by year
- 2026: 38 · 2025: 66 · 2024: 63 · 2023: 48 · 2022: 61 · 2021: 71 · 2020: 63 · 2019: 52 · 2018: 22
- FWCI
- 3.50
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Redox Biology (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Agencia Nacional de Investigación e Innovación (FCE_2014_104233)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- peroxynitrite, tyrosine nitration, superoxide, nitric oxide, superoxide dismutase, guanylate cyclase, secondary radicals, homolysis, oxidative damage biomarkers, lipid peroxidation, membrane proteins, lipoproteins, cytotoxicity
- MeSH terms
- Animals, Humans, Models, Molecular, Nitric Oxide, Proteins, Superoxides, Tyrosine, Oxidative Stress, Peroxynitrous Acid
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.
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