Tyrosine-nitrated proteins: Proteomic and bioanalytical aspects

Batthyány, Carlos; Bartesaghi, Silvina; Mastrogiovanni, Mauricio; Lima, Analía; Demicheli, Verónica; Radi, Rafael

doi:10.1089/ars.2016.6787

Cited by 86Redox biology and oxidative stressAdvanced Proteomics Techniques and ApplicationsMass Spectrometry Techniques and Applications

Tyrosine-nitrated proteins: Proteomic and bioanalytical aspects

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Batthyány, Carlos, Bartesaghi, Silvina, Mastrogiovanni, Mauricio, Lima, Analía, Demicheli, Verónica, Radi, Rafael·2017·Antioxidants & Redox Signaling

DOI 10.1089/ars.2016.6787PMC PMC5326983

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Abstract

SIGNIFICANCE: "Nitroproteomic" is under active development, as 3-nitrotyrosine in proteins constitutes a footprint left by the reactions of nitric oxide-derived oxidants that are usually associated to oxidative stress conditions. Moreover, protein tyrosine nitration can cause structural and functional changes, which may be of pathophysiological relevance for human disease conditions. Biological protein tyrosine nitration is a free radical process involving the intermediacy of tyrosyl radicals; in spite of being a nonenzymatic process, nitration is selectively directed toward a limited subset of tyrosine residues. Precise identification and quantitation of 3-nitrotyrosine in proteins has represented a "tour de force" for researchers. Recent Advances: A small number of proteins are preferential targets of nitration (usually less than 100 proteins per proteome), contrasting with the large number of proteins modified by other post-translational modifications such as phosphorylation, acetylation, and, notably, S-nitrosation. Proteomic approaches have revealed key features of tyrosine nitration both in vivo and in vitro, including selectivity, site specificity, and effects in protein structure and function. CRITICAL ISSUES: Identification of 3-nitrotyrosine-containing proteins and mapping nitrated residues is challenging, due to low abundance of this oxidative modification in biological samples and its unfriendly behavior in mass spectrometry (MS)-based technologies, that is, MALDI, electrospray ionization, and collision-induced dissociation. FUTURE DIRECTIONS: The use of (i) classical two-dimensional electrophoresis with immunochemical detection of nitrated proteins followed by protein ID by regular MS/MS in combination with (ii) immuno-enrichment of tyrosine-nitrated peptides and (iii) identification of nitrated peptides by a MIDAS™ experiment is arising as a potent methodology to unambiguously map and quantitate tyrosine-nitrated proteins in vivo. Antioxid. Redox Signal. 26, 313-328.

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Tyrosine nitration inhibits tyrosine phosphorylation by tyrosine kinases due to steric interference of the NO2 group with the active site of the enzyme.
“With the NO2 functionality on Tyr, tyrosine phosphorylation by tyrosine kinases, including receptor tyrosine kinases, is inhibited due to steric interference of the NO2 group with the active site of the enzyme.”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [30]
The Introduction says that adding a bulky NO2 group to a relevant tyrosine residue can impose steric restrictions and inhibit tyrosine phosphorylation. It does not specifically say that the inhibition results from interference with a tyrosine kinase’s active site, or identify receptor tyrosine kinases in this account. (LLM, conf=0.86)
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Shao, B., Tang, C., Heinecke, J. W., & Oram, J. F. (2010) · Journal of Lipid Research · doi:10.1194/jlr.m004085 · Cited by 94 · see citing works
A sensitive mass spectrometric method for hypothesis-driven detection of peptide post-translational modifications: multiple reaction monitoring-initiated detection and sequencing (MIDAS)
Unwin, R. D., Griffiths, J. R., & Whetton, A. D. (2009) · Nature Protocols · doi:10.1038/nprot.2009.57 · Cited by 92 · see citing works
Formation of Protein Tyrosine ortho-Semiquinone Radical and Nitrotyrosine from Cytochrome c-derived Tyrosyl Radical
Chen, Y.-R., Chen, C. L., Chen, W., Zweier, J. L., Augusto, O., Radí, R., & Mason, R. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307706200 · Cited by 89 · see citing works
Site-Specific Incorporation of 3-Nitrotyrosine as a Probe of pKa Perturbation of Redox-Active Tyrosines in Ribonucleotide Reductase
Yokoyama, K., Uhlin, U., & Stubbe, J. (2010) · Journal of the American Chemical Society · doi:10.1021/ja101097p · Cited by 85 · see citing works
Diffusion of Nitric Oxide into Low Density Lipoprotein
Denicola, A., Batthyány, C., Lissi, E. A., Freeman, B. Α., Rubbo, H., & Radí, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106589200 · Cited by 85 · see citing works
Self-citation
Cytochrome c: a catalyst and target of nitrite-hydrogen peroxide-dependent protein nitration
Castro, L., Eiserich, J. P., Sweeney, S., Radi, R., & Freeman, B. A. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.08.033 · Cited by 84 · see citing works
Prevalence of anti-3-nitrotyrosine antibodies in the joint synovial fluid of patients with rheumatoid arthritis, osteoarthritis and systemic lupus erythematosus
Khan, F., & Siddiqui, A. A. (2006) · Clinica Chimica Acta · doi:10.1016/j.cca.2006.01.020 · Cited by 82 · see citing works
Mechanistic Studies of Peroxynitrite-Mediated Tyrosine Nitration in Membranes Using the Hydrophobic Probe N-t- BOC- <scp>l</scp> -tyrosine tert -Butyl Ester
Bartesaghi, 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
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Nitration and Oxidation of a Hydrophobic Tyrosine Probe by Peroxynitrite in Membranes: Comparison with Nitration and Oxidation of Tyrosine by Peroxynitrite in Aqueous Solution
Zhang, H., Joseph, J., Feix, J. B., Hogg, N., & Kalyanaraman, B. (2001) · Biochemistry · doi:10.1021/bi002958c · Cited by 77 · see citing works
Mass spectrometry and 3‐nitrotyrosine: Strategies, controversies, and our current perspective
Tsikas, D., & Duncan, M. W. (2014) · Mass Spectrometry Reviews · doi:10.1002/mas.21396 · Cited by 76 · see citing works
Site-Selective Nitration of Tyrosine in Human Serum Albumin by Peroxynitrite
Jiao, K., Mandapati, S., Skipper, P. L., Tannenbaum, S. R., & Wishnok, J. S. (2001) · Analytical Biochemistry · doi:10.1006/abio.2001.5118 · Cited by 76 · 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
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Intragastric nitration by dietary nitrite: implications for modulation of protein and lipid signaling
Rocha, B. S., Gago, B., Barbosa, R. M., Lundberg, J. O., Radi, R., & Laranjinha, J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.11.011 · Cited by 74 · see citing works
Kinetics 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
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Cyclosporine A-induced nitration of tyrosine 34 MnSOD in endothelial cells: role of mitochondrial superoxide
Redondo‐Horcajo, M., Romero, N., Martínez-Acedo, P., Martı́nez-Ruiz, A., Quijano, C., Lourenço, C. F., Movilla, N., Enrı́quez, J. A., Rodríguez‐Pascual, F., Rial, E., et al. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq028 · Cited by 74 · see citing works
3‐Nitrotyrosine as a spectroscopic probe for investigating protein–protein interactions
Filippis, V. D., Frasson, R., & Fontana, A. (2006) · Protein Science · doi:10.1110/ps.051957006 · Cited by 72 · see citing works
Immunoaffinity liquid chromatography–tandem mass spectrometry detection of nitrotyrosine in biological fluids: Development of a clinically translatable biomarker
Radabaugh, M. R., Nemirovskiy, O. V., Misko, T. P., Aggarwal, P., & Mathews, W. R. (2008) · Analytical Biochemistry · doi:10.1016/j.ab.2008.05.019 · Cited by 70 · see citing works
Inflammatory and oxidative markers in atherosclerosis: Relationship to outcome
Shishehbor, M. H., & Hazen, S. L. (2004) · Current Atherosclerosis Reports · doi:10.1007/s11883-004-0038-1 · Cited by 69 · see citing works
Identification of a Denitrase Activity against Calmodulin in Activated Macrophages Using High-Field Liquid Chromatography−FTICR Mass Spectrometry
Smallwood, H. S., Lourette, N. M., Boschek, C. B., Bigelow, D. J., Smith, R. D., Paša‐Tolić, L., & Squier, T. C. (2007) · Biochemistry · doi:10.1021/bi7009713 · Cited by 67 · see citing works
Leghemoglobin is nitrated in functional legume nodules in a tyrosine residue within the heme cavity by a nitrite/peroxide‐dependent mechanism
Sainz, M., Calvo-Beguería, L., Pérez‐Rontomé, C., Wienkoop, S., Abián, J., Staudinger, C., Bartesaghi, S., Radí, R., & Becana, M. (2015) · The Plant Journal · doi:10.1111/tpj.12762 · Cited by 67 · see citing works
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Enhanced Nitrosative Stress during Trypanosoma cruzi Infection Causes Nitrotyrosine Modification of Host Proteins
Dhiman, M., Nakayasu, E. S., Hosakote, Y. M., Reynolds, B. K., Wen, J.-J., de Almeida, I. C., & Garg, N. J. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.080047 · Cited by 66 · see citing works
pTcINDEX: a stable tetracycline-regulated expression vector for Trypanosoma cruzi.
Taylor, M. C., & Kelly, J. M. (2006) · BMC Biotechnology · doi:10.1186/1472-6750-6-32 · Cited by 66 · see citing works
l-arginine metabolism during interaction of Trypanosoma cruzi with host cells
Peluffo, G., Piacenza, L., Irigoı́n, F., Álvarez, M. N., & Radí, R. (2004) · Trends in Parasitology · doi:10.1016/j.pt.2004.05.010 · Cited by 65 · see citing works
Structural and Molecular Basis of the Peroxynitrite-mediated Nitration and Inactivation of Trypanosoma cruzi Iron-Superoxide Dismutases (Fe-SODs) A and B
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
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Mass spectrometry analysis of nitrotyrosine‐containing proteins
Zhan, X., Wang, X., & Desiderio, D. M. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21413 · Cited by 57 · see citing works
Exploring the molecular basis of human manganese superoxide dismutase inactivation mediated by tyrosine 34 nitration
Moreno, D. M., Marti, M. A., Biase, P. M. D., Estrin, D. A., Demicheli, V., Radí, R., & Boechi, L. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.12.011 · Cited by 53 · see citing works
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S-Nitroso-Proteome in Poplar Leaves in Response to Acute Ozone Stress
Vanzo, E. M., Ghirardo, A., Merl‐Pham, J., Lindermayr, C., Heller, W. E., Hauck, S. M., Durner, J., & Schnitzler, J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0106886 · Cited by 50 · see citing works
Serine/threonine protein kinase PrkA of the human pathogen Listeria monocytogenes: biochemical characterization and identification of interacting partners through proteomic approaches.
Lima, A., Durán, R., Schujman, G., Marchissio, M. J., Portela, M. M., Obal, G., Pritsch, O., de Mendoza, D., & Červeñanský, C. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.03.005 · Cited by 50 · see citing works
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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
Peroxynitrite transforms nerve growth factor into an apoptotic factor for motor neurons
Pehar, M., Vargas, M. R., Robinson, K. M., Cassina, P., England, P., Beckman, J. S., Alzari, P. M., & Barbeito, L. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.08.010 · Cited by 48 · see citing works
Nitration Transforms a Sensitive Peroxiredoxin 2 into a More Active and Robust Peroxidase
Randall, L. M., Manta, B., Hugo, M., Gil, M., Batthyány, C., Trujillo, M., Poole, L. B., & Denicola, A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.539213 · Cited by 48 · see citing works
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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
Antibodies against Nitric Oxide Damaged Poly L-Tyrosine and 3-Nitrotyrosine Levels in Systemic Lupus Erythematosus
Khan, F., & Ali, R. (2006) · BMB Reports · doi:10.5483/bmbrep.2006.39.2.189 · Cited by 45 · see citing works
Mechanism of the Reaction of Human Manganese Superoxide Dismutase with Peroxynitrite: Nitration of Critical Tyrosine 34
Demicheli, V., Moreno, D. M., Jara, G. E., Lima, A. E., Carballal, S., Ríos, N., Batthyány, C., Ferrer‐Sueta, G., Quijano, C., Estrin, D. A., et al. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00045 · Cited by 43 · see citing works
Self-citation
Peroxynitrous acid induces structural and functional modifications to basement membranes and its key component, laminin
Degendorfer, G., Chuang, C. Y., Hammer, A., Malle, E., & Davies, M. J. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.09.018 · Cited by 42 · see citing works
Nitroproteins in Human Astrocytomas Discovered by Gel Electrophoresis and Tandem Mass Spectrometry
Peng, F., Li, J., Guo, T., Yang, H., Li, M., Sang, S., Li, X., Desiderio, D. M., & Zhan, X. (2015) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-015-1270-3 · Cited by 42 · see citing works
A novel mixed-mode solid phase extraction coupled with LC–MS/MS for the re-evaluation of free 3-nitrotyrosine in human plasma as an oxidative stress biomarker
Li, X., Li, S., & Kellermann, G. H. (2015) · Talanta · doi:10.1016/j.talanta.2015.02.053 · Cited by 35 · see citing works
Sensitive and accurate analyses of free 3-nitrotyrosine in exhaled breath condensate by LC–MS/MS
Göen, T., Müller-Lux, A., Dewes, P., Musiol, A., & Kraus, T. (2005) · Journal of Chromatography B · doi:10.1016/j.jchromb.2005.08.001 · Cited by 34 · see citing works
Pepsin is nitrated in the rat stomach, acquiring antiulcerogenic activity: A novel interaction between dietary nitrate and gut proteins
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
Nitration of Specific Tyrosine Residues of Cytochrome c Is Associated with Caspase-Cascade Inactivation
Nakagawa, H., Komai, N., Takusagawa, M., Miura, Y., Toda, T., Miyata, N., Ozawa, T., & Ikota, N. (2007) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.30.15 · Cited by 33 · see citing works
Nitrocytochrome c: Synthesis, Purification, and Functional Studies
Souza, J. M., Castro, L., Cassina, A., Batthyány, C., & Radí, R. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)01211-1 · Cited by 32 · see citing works
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Detection and Characterization of Peroxynitrite-Induced Modifications of Tyrosine, Tryptophan, and Methionine Residues by Tandem Mass Spectrometry
Rebrin, I., Brégère, C., Gallaher, T. K., & Sohal, R. S. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)01215-9 · Cited by 30 · see citing works
Mass spectrometric identification of tryptophan nitration sites on proteins in peroxynitrite-treated lysates from PC12 cells
Kawasaki, H., Ikeda, K., Shigenaga, A., Baba, T., Takamori, K., Ogawa, H., & Yamakura, F. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.10.688 · Cited by 30 · see citing works
Quantification of 3‐Nitrotyrosine Levels Using a Benchtop Ion Trap Mass Spectrometry Method
Nicholls, S. J., Shen, Z., Fu, X., Levison, B. S., & Hazen, S. L. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)96022-9 · Cited by 25 · see citing works
A simple and robust LC‐MS/MS method for quantification of free 3‐nitrotyrosine in human plasma from patients receiving on‐pump CABG surgery
Yu, H., Wong, M., Zhao, S. S., Love, J. A., Ansley, D. M., & Chen, D. D. Y. (2012) · Electrophoresis · doi:10.1002/elps.201100368 · Cited by 20 · see citing works
Incorporation of the Hydrophobic Probe N-t-BOC- l -tyrosine tert-Butyl Ester to Red Blood Cell Membranes To Study Peroxynitrite-Dependent Reactions
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-citation
Nitration of tryptophan in ribosomal proteins is a novel post-translational modification of differentiated and naïve PC12 cells
Kawasaki, H., Shigenaga, A., Uda, M., Baba, T., Ogawa, H., Takamori, K., & Yamakura, F. (2011) · Nitric Oxide · doi:10.1016/j.niox.2011.05.005 · Cited by 14 · see citing works
Tyrosine Nitration, Dimerization, and Hydroxylation by Peroxynitrite in Membranes as Studied by the Hydrophobic Probe N-t-BOC-l-tyrosine tert-Butyl Ester
Bartesaghi, S., Peluffo, G., Zhang, H., Joseph, J., Kalyanaraman, B., & Radí, R. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)01212-3 · Cited by 12 · see citing works
Self-citation
Tailored 96-well μElution solid-phase extraction combined with UFLC-MS/MS: a significantly improved approach for determination of free 3-nitrotyrosine in human urine
Li, X., Li, S., & Kellermann, G. H. (2015) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-015-8934-5 · Cited by 8 · see citing works
Hydrophobic Tyrosyl Probes for Monitoring Nitration Reactions in Membranes
Zhang, H., Joseph, J., & Kalyanaraman, B. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)96018-7 · Cited by 4 · see citing works

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Oxygen radicals, nitric oxide, and peroxynitrite: Redox pathways in molecular medicine
Radi, R. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1804932115 · Cited by 1,142 · see citing works
Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
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Fundamentals on the biochemistry of peroxynitrite and protein tyrosine nitration
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ROS and RNS signalling: adaptive redox switches through oxidative/nitrosative protein modifications
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Detection and quantification of nitric oxide–derived oxidants in biological systems
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Nitric oxide and hydrogen sulfide: an indispensable combination for plant functioning
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Myeloid-derived suppressor cells inhibit T cell activation through nitrating LCK in mouse cancers
Feng, S., Cheng, X., Zhang, L., Lu, X., Chaudhary, S., Teng, R., Frederickson, C. E., Champion, M. M., Zhao, R., Liang Cheng, C., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1800695115 · Cited by 154 · see citing works
Fluorescence and chemiluminescence approaches for peroxynitrite detection
Prolo, C., Ríos, N., Piacenza, L., Álvarez, M. N., & Radí, R. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.02.017 · Cited by 106 · see citing works
Peroxynitrite: a multifaceted oxidizing and nitrating metabolite
Prolo, C., Piacenza, L., & Radí, R. (2024) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2024.102459 · Cited by 95 · see citing works
Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease
Butterfield, D. A., & Boyd-Kimball, D. (2020) · Antioxidants · doi:10.3390/antiox9090818 · Cited by 85 · see citing works
“This modification can provide detrimental consequences for cell survival [8,13,29,30].”
Background
Oxidative Stress
Sies, H. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813146-6.00013-8 · Cited by 88 · see citing works
3-Nitrotyrosine and related derivatives in proteins: precursors, radical intermediates and impact in function
Campolo, N., Issoglio, F. M., Estrin, D. A., Bartesaghi, S., & Radí, R. (2020) · Essays in Biochemistry · doi:10.1042/ebc20190052 · Cited by 85 · see citing works
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Glutathione and Nitric Oxide: Key Team Players in Use and Disuse of Skeletal Muscle
Baldelli, S., Ciccarone, F., Limongi, D., Checconi, P., Palamara, A. T., & Ciriolo, M. R. (2019) · Nutrients · doi:10.3390/nu11102318 · Cited by 83 · see citing works
Nitric oxide and hydrogen sulfide modulate the NADPH-generating enzymatic system in higher plants
Corpas, F. J., González‐Gordo, S., & Palma, J. M. (2020) · Journal of Experimental Botany · doi:10.1093/jxb/eraa440 · Cited by 76 · see citing works
Impact of Reactive Species on Amino Acids—Biological Relevance in Proteins and Induced Pathologies
Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214049 · Cited by 71 · see citing works
Oxidative Modification of Proteins: From Damage to Catalysis, Signaling, and Beyond
Demasi, M., Augusto, O., Bechara, E. J. H., Bicev, R. N., Cerqueira, F. M., da Cunha, F. M., Denicola, A., Gomes, F., Miyamoto, S., Netto, L. E. S., et al. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8176 · Cited by 68 · see citing works
The mitochondrial thioredoxin reductase system (TrxR2) in vascular endothelium controls peroxynitrite levels and tissue integrity
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Linking biomarkers of oxidative stress and disease with flavonoid consumption: From experimental models to humans
Oteiza, P. I., Fraga, C. G., & Galleano, M. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101914 · Cited by 61 · see citing works
Regulation of Chemokine Function: The Roles of GAG-Binding and Post-Translational Nitration
Thompson, S., Martínez‐Burgo, B., Sepuru, K. M., Rajarathnam, K., Kirby, J. A., Sheerin, N., & Ali, S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18081692 · Cited by 49 · see citing works
Detection of ROS Induced Proteomic Signatures by Mass Spectrometry
McDonagh, B. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00470 · Cited by 42 · see citing works
Glutamine synthetase as a central element in hepatic glutamine and ammonia metabolism: novel aspects
Frieg, B., Görg, B., Gohlke, H., & Häussinger, D. (2021) · Biological Chemistry · doi:10.1515/hsz-2021-0166 · Cited by 42 · see citing works
Peroxynitrite nitrates adenine nucleotide translocase and voltage-dependent anion channel 1 and alters their interactions and association with hexokinase II in mitochondria
Yang, M., Xu, Y., Heisner, J. S., Sun, J., Stowe, D. F., Kwok, W., & Camara, A. K. S. (2018) · Mitochondrion · doi:10.1016/j.mito.2018.10.002 · Cited by 38 · see citing works
Nitrative Modification of Caveolin-3: A Novel Mechanism of Cardiac Insulin Resistance and a Potential Therapeutic Target Against Ischemic Heart Failure in Prediabetic Animals
Meng, Z., Zhang, Z., Zhao, J., Liu, C., Yao, P., Zhang, L., Xie, D., Lau, W. B., Tsukuda, J., Christopher, T. A., et al. (2023) · Circulation · doi:10.1161/circulationaha.122.063073 · Cited by 37 · see citing works
The challenge of detecting modifications on proteins
Smith, L. E., & Rogowska-Wrzesińska, A. (2020) · Essays in Biochemistry · doi:10.1042/ebc20190055 · Cited by 37 · see citing works
Combined chronic copper exposure and aging lead to neurotoxicity in vivo
González-Alcocer, A., Gopar‐Cuevas, Y., Soto‐Domínguez, A., Castillo-Velázquez, U., Loera‐Arias, M. D. J., Cárdenas, O. S., Montes‐de‐Oca‐Luna, R., García‐García, A., & Rodríguez‐Rocha, H. (2023) · NeuroToxicology · doi:10.1016/j.neuro.2023.02.002 · Cited by 32 · see citing works
Human Mn-superoxide dismutase inactivation by peroxynitrite: a paradigm of metal-catalyzed tyrosine nitration in vitro and in vivo
Demicheli, V., Moreno, D. M., & Radí, R. (2018) · Metallomics · doi:10.1039/c7mt00348j · Cited by 29 · see citing works
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Proteomic strategies to unravel age-related redox signalling defects in skeletal muscle
Cobley, J. N., Sakellariou, G. K., Husi, H., & McDonagh, B. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.012 · Cited by 29 · see citing works
The Hypoxia Tolerance of the Goldfish (Carassius auratus) Heart: The NOS/NO System and Beyond
Filice, M., Mazza, R., Leo, S., Gattuso, A., Cerra, M. C., & Imbrogno, S. (2020) · Antioxidants · doi:10.3390/antiox9060555 · Cited by 22 · see citing works
Role of papillary thyroid carcinoma patients with Hashimoto thyroiditis: evaluation of oxidative stress and inflammatory markers
Lopes, N. M. D., Lens, H. H. M., Brito, W. A. D. S., Bianchi, J. K., Marinello, P. C., Cecchini, R., Armani, A., & Cecchini, A. L. (2022) · Clinical & Translational Oncology · doi:10.1007/s12094-022-02891-y · Cited by 21 · see citing works
Uncommon posttranslational modifications in proteomics: ADP‐ribosylation, tyrosine nitration, and tyrosine sulfation
Bashyal, A., & Brodbelt, J. S. (2022) · Mass Spectrometry Reviews · doi:10.1002/mas.21811 · Cited by 22 · see citing works
Neuronal Parasitism, Early Myenteric Neurons Depopulation and Continuous Axonal Networking Damage as Underlying Mechanisms of the Experimental Intestinal Chagas' Disease
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Authors: Batthyány, C., Bartesaghi, S., Mastrogiovanni, M., Lima, A., Demicheli, V., & Radi, R.
Affiliations: Universidad de la República de Uruguay (UY)
Unidad de Bioquímica y Proteómica Analíticas, Institut Pasteur de Montevideo, Montevideo, Uruguay.
Departamento de Bioquímica, Facultad de Medicina, Universidad de la República, Montevideo, Uruguay.
ORCID: Batthyány, Carlos
Bartesaghi, Silvina
Mastrogiovanni, Mauricio
Venue: Antioxidants & Redox Signaling
Publisher: SAGE Publications
Published: 2017-03
Volume: 26
Issue: 7
Pages: 313-328
ISSN: 1523-0864 (ISSN-L)
1557-7716
DOI: 10.1089/ars.2016.6787
PMC: PMC5326983
OpenAlex: W2500532125
Cited by: 86
References: 124
Citations by year: 2026: 5 · 2025: 4 · 2024: 5 · 2023: 7 · 2022: 14 · 2021: 10 · 2020: 9 · 2019: 12 · 2018: 13 · 2017: 7
FWCI: 0.97
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Antioxidants and Redox Signaling (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion)
Funders: Institut Pasteur de Montevideo
National Institutes of Health
National Institute of Allergy and Infectious Diseases (R01AI095173)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
Keywords: tyrosine nitration, nitrotyrosine, oxidative stress, tyrosyl radical, post-translational modification, MIDAS, protein structure-function relationship
MeSH terms: Animals, Humans, Nitrates, Protein Processing, Post-Translational, Proteins, Sensitivity and Specificity, Mass Spectrometry, Tyrosine, Nitrosation, Proteome, Proteomics

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Tyrosine-nitrated proteins: Proteomic and bioanalytical aspects

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