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Factors Determining the Selectivity of Protein Tyrosine Nitration
Open accessAbstract
Tyrosine nitration is a covalent posttranslational protein modification derived from the reaction of proteins with nitrating agents. Protein nitration appears to be a selective process since not all tyrosine residues in proteins or all proteins are nitrated in vivo. To investigate factors that may determine the biological selectivity of protein tyrosine nitration, we developed an in vitro model consisting of three proteins with similar size but different three-dimensional structure and tyrosine content. Exposure of ribonuclease A to putative in vivo nitrating agents revealed preferential nitration of tyrosine residue Y(115). Tyrosine residue Y(23) and to a lesser extent residue Y(20) were preferentially nitrated in lysozyme, whereas tyrosine Y(102) was the only residue modified by nitration in phospholipase A(2). Tyrosine Y(115) was the residue modified by nitration after exposure of ribonuclease A to different nitrating agents: chemically synthesized peroxynitrite, nitric oxide, and superoxide generated by SIN-1 or myeloperoxidase (MPO)/H(2)O(2) plus nitrite (NO(-2)) in the presence of bicarbonate/CO(2). The nature of the nitrating agent determined in part the protein that would be predominantly modified by nitration in a mixture of all three proteins. Ribonuclease A was preferentially nitrated upon exposure to MPO/H(2)O(2)/NO(-2), whereas phospholipase A(2) was the primary target for nitration upon exposure to peroxynitrite. The data also suggest that the exposure of the aromatic ring to the surface of the protein, the location of the tyrosine on a loop structure, and its association with a neighboring negative charge are some of the factors determining the selectivity of tyrosine nitration in proteins.
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“The results of different studies are contradictory, with examples of improved outcomes for NOX1 deficient mice subjected to high fat diet (854) and diabetic mouse models (380), whereas in other cases, NOX1 deletion did not seem to have an effect (875).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [875]
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Cites
The interpretation of protein structures: Estimation of static accessibility
Lee, B., & Richards, F. M. (1971) · Journal of Molecular Biology · doi:10.1016/0022-2836(71)90324-x · Cited by 5,884
Proteins: Structures and Molecular Properties
Creighton, T. E. (1986) · Medical Entomology and Zoology · Cited by 2,645
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 2,492
Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase
Ischiropoulos, H., Zhu, L., Chen, J., Tsai, M., Martin, J. C., Smith, C. D. L., & Beckman, J. S. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90431-u · Cited by 1,499
Self-citationFormation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils
Eiserich, J. P., Hristova, M., Cross, C. E., Jones, A. D., Freeman, B. A., Halliwell, B., & van der Vliet, A. (1998) · Nature · doi:10.1038/34923 · Cited by 1,496
Ischiropoulos, H. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0755 · Cited by 1,025
Self-citationOxidative Damage and Tyrosine Nitration from Peroxynitrite
Beckman, J. S. (1996) · Chemical Research in Toxicology · doi:10.1021/tx9501445 · Cited by 993
[23] Oxidative chemistry of peroxynitrite
Beckman, J. S., Chen, J., Ischiropoulos, H., & Crow, J. P. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(94)33026-3 · Cited by 973
Self-citationFormation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite
van der Vliet, A., Eiserich, J. P., Halliwell, B., & Cross, C. E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.12.7617 · Cited by 780
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 769
Flagged first, then by citations
Research works printed but not linked: 3
- Zou, 1997, Biochem. J., 378, 707
- Huttner, 1987, TIBS, 12, 361
- Kemp, 1990, TIBS, 15, 342
Cited by
Sorted by citations
Items 101–200 of 315
NO sparks off chromatin: Tales of a multifaceted epigenetic regulator
Illi, B., Colussi, C., Grasselli, A., Farsetti, A., Capogrossi, M. C., & Gaetano, C. (2009) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2009.05.003 · Cited by 74
Komeima, K., Usui, S., Shen, J., Rogers, B. S., & Campochiaro, P. A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.06.020 · Cited by 74
Fries, D. M., Paxinou, E., Themistocleous, M. S., Swanberg, E., Griendling, K. K., Salvemini, D., Slot, J. W., Heijnen, H. F. G., Hazen, S. L., & Ischiropoulos, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210806200 · Cited by 72
Self-citationInactivation and Reactivation of the Mitochondrial α-Ketoglutarate Dehydrogenase Complex
Shi, Q., Xu, H., Yu, H., Zhang, N., Ye, Y., Estévez, Á. G., Deng, H., & Gibson, G. E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.203018 · Cited by 72
Watabe, M., & Nakaki, T. (2008) · Molecular Pharmacology · doi:10.1124/mol.108.048546 · Cited by 71
Wong, P., Eiserich, J. P., Reddy, S., López, C. L., Cross, C. E., & van der Vliet, A. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2532 · Cited by 72
Peroxynitrite formation from biochemical and cellular fluxes of nitric oxide and superoxide
Álvarez, M. N., Trujillo, M., & Radí, R. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)59198-9 · Cited by 69
Tyrosine Nitration Impairs Mammalian Aldolase A Activity
Koeck, T., Levison, B. S., Hazen, S. L., Crabb, J. W., Stuehr, D. J., & Aulak, K. S. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m300141-mcp200 · Cited by 68
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 71
Kuhn, D. M., Sakowski, S. A., Sadidi, M., & Geddes, T. J. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02346.x · Cited by 66
Veiga‐Lopez, A., Pennathur, S., Kannan, K., Patisaul, H. B., Dolinoy, D. C., Zeng, L., & Padmanabhan, V. (2015) · Endocrinology · doi:10.1210/en.2014-1863 · Cited by 68
Monteiro, H. P. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00893-6 · Cited by 63
Tcyganov, E. N., Sanseviero, E., Marvel, D., Beer, T., Tang, H., Hembach, P., Speicher, D. W., Zhang, Q., Donthireddy, L., Ali, M., et al. (2022) · Cancer Cell · doi:10.1016/j.ccell.2022.09.001 · Cited by 64
Mass spectrometric analysis of protein tyrosine nitration in aging and neurodegenerative diseases
Yeo, W., Kim, Y. J., Kabir, M. H., Kang, J. W., & Kim, K. P. (2015) · Mass Spectrometry Reviews · doi:10.1002/mas.21429 · Cited by 61
Matalon, S., Shrestha, K., KIRK, M. C., Waldheuser, S., McDonald, B., Smith, K., Gao, Z., Belaaouaj, A., & Crouch, E. C. (2009) · The FASEB Journal · doi:10.1096/fj.08-120568 · Cited by 61
Functional Roles of Protein Nitration in Acute and Chronic Liver Diseases
Abdelmegeed, M. A., & Song, B. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/149627 · Cited by 62
Lanone, S., Manivet, P., Callebert, J., Launay, J., Payen, D. M., Aubier, M., Boczkowski, J., & Mebazaa, A. (2002) · Biochemical Journal · doi:10.1042/bj20020339 · Cited by 61
Oxidative hotspots on actin promote skeletal muscle weakness in rheumatoid arthritis
Steinz, M. M., Persson, M., Aresh, B., Olsson, K., Cheng, A. J., Ahlstrand, E., Lilja, M. R., Lundberg, T. R., Rullman, E., Möller, K. Ä., et al. (2019) · JCI Insight · doi:10.1172/jci.insight.126347 · Cited by 61
Zhang, Y., Yang, H., & Pöschl, U. (2010) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-010-4280-9 · Cited by 59
Inhibition of Arabidopsis O-Acetylserine(thiol)lyase A1 by Tyrosine Nitration
Álvarez, C., Lozano‐Juste, J., Romero, L. C., García, I., Gotor, C., & León, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.147678 · Cited by 62
Protein tyrosine nitration in cellular signal transduction pathways
Yakovlev, V. A., & Mikkelsen, R. B. (2010) · Journal of Receptors and Signal Transduction · doi:10.3109/10799893.2010.513991 · Cited by 59
Venkatesan, A., Uzasci, L., Chen, Z., Rajbhandari, L., Anderson, C. F., Lee, M. H., Bianchet, M. A., Cotter, R. J., Song, H., & Nath, A. (2011) · Molecular Brain · doi:10.1186/1756-6606-4-28 · Cited by 60
Peroxynitrite: From interception to signaling
Speckmann, B., Steinbrenner, H., Grune, T., & Klotz, L. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.06.022 · Cited by 59
Zhang, Y. J., Xu, Y. F., Chen, X., Wang, X. C., & Wang, J. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.03.041 · Cited by 58
Buchczyk, D. P., Briviba, K., Hartl, F. U., & Sies, H. (2000) · Biological Chemistry · doi:10.1515/bc.2000.017 · Cited by 58
Nitro-Oxidative Stress after Neuronal Ischemia Induces Protein Nitrotyrosination and Cell Death
Tajes, M., ILL‐Raga, G., Palomer, E., Ramos‐Fernández, E., Guix, F. X., Bosch-Morató, M., Guivernau, B., Jiménez-Conde, J., Ois, Á., Pérez-Asensio, F. J., et al. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/826143 · Cited by 57
Transmembrane Nitration of Hydrophobic Tyrosyl Peptides
Zhang, H., Bhargava, K., Keszler, Á., Feix, J. B., Hogg, N., Joseph, J., & Kalyanaraman, B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211561200 · Cited by 56
Daiber, A., Daub, S., Bachschmid, M. M., Schildknecht, S., Oelze, M. W., Steven, S., Schmidt, P., Megner, A., Wada, M., Tanabe, T., et al. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14047542 · Cited by 58
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Jacques, S., Ghesquière, B., Breusegem, F. V., & Gevaert, K. (2012) · PROTEOMICS · doi:10.1002/pmic.201200237 · Cited by 61
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Hurst, J. K. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215816 · Cited by 56
Proteomic Modification by Nitric Oxide
Bian, K., Ke, Y., Kamisaki, Y., & Murad, F. (2006) · Journal of Pharmacological Sciences · doi:10.1254/jphs.crj06009x · Cited by 55
Tajes, M., Eraso‐Pichot, A., Rubio-Moscardó, F., Guivernau, B., Bosch-Morató, M., Valls-Comamala, V., & Muñoz, F. J. (2014) · Neuroscience Letters · doi:10.1016/j.neulet.2014.07.047 · Cited by 53
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Self-citationThe impact of metal catalysis on protein tyrosine nitration by peroxynitrite
Daiber, A., Bachschmid, M. M., Beckman, J. S., Münzel, T. F., & Ullrich, V. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.03.122 · Cited by 51
Tyrosine nitration as mediator of cell death
Franco, M. C., & Estévez, Á. G. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1662-8 · Cited by 50
Vaz, S. M., & Augusto, O. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708211105 · Cited by 49
Factors influencing protein tyrosine nitration—structure-based predictive models
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Pietraforte, D., Salzano, A. M., Marino, G., & Minetti, M. (2003) · Amino Acids · doi:10.1007/s00726-003-0021-0 · Cited by 48
Chemical labeling and enrichment of nitrotyrosine-containing peptides
Abello, N., Barroso, B., Kerstjens, H. A. M., Postma, D. S., & Bischoff, R. (2009) · Talanta · doi:10.1016/j.talanta.2009.02.002 · Cited by 47
Peroxynitrite-induced protein nitration contributes to liver mitochondrial damage in diabetic rats
Ren, X., Li, Y., Qi, J., & Niu, T. (2008) · Journal of Diabetes and its Complications · doi:10.1016/j.jdiacomp.2007.06.013 · Cited by 47
Selective tau tyrosine nitration in non-AD tauopathies
Reyes, J. F., Geula, C., Vana, L., & Binder, L. I. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0898-8 · Cited by 46
Peroxynitrite-Induced Nitrative and Oxidative Modifications Alter Tau Filament Formation
Vana, L., Kanaan, N. M., Hakala, K. W., Weintraub, S. T., & Binder, L. I. (2011) · Biochemistry · doi:10.1021/bi101735m · Cited by 45
Tedeschi, G., Cappelletti, G., Negri, A. L., Pagliato, L., Maggioni, M. G., Maci, R., & Ronchi, S. (2005) · PROTEOMICS · doi:10.1002/pmic.200401208 · Cited by 45
Trostchansky, A., O’Donnell, V. B., Goodwin, D. C., Landino, L. M., Marnett, L. J., Radí, R., & Rubbo, H. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.01.009 · Cited by 45
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Barreiro, E. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21394 · Cited by 46
Tajes, M., Eraso‐Pichot, A., Rubio-Moscardó, F., Guivernau, B., Ramos‐Fernández, E., Bosch-Morató, M., Guix, F. X., Clarimón, J., Miscione, G. P., Boada, M., et al. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131685 · Cited by 43
Nitrotyrosine and protein carbonyls are equally distributed in HT22 cells after nitrosative stress
Jung, T., Engels, M., Klotz, L., Kröncke, K., & Grune, T. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.11.029 · Cited by 44
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Liu, H., Gaza‐Bulseco, G., Chumsae, C. M., & Radziejewski, C. H. (2007) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.3322 · Cited by 41
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White, P. J., Charbonneau, A., Cooney, G. J., & Marette, A. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00510.2010 · Cited by 49
Takahashi, T., Yamashita, H., Nagano, Y., Nakamura, T., Ohmori, H., Avraham, H. K., Avraham, S., Yasuda, M., & Matsumoto, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213217200 · Cited by 40
Lin, H.-L., Myshkin, E., Waskell, L. A., & Hollenberg, P. F. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700220e · Cited by 39
Hasan, M. M., Khatun, M. S., Mollah, M. N. H., Yong, C., & Guo, D. (2018) · Molecules · doi:10.3390/molecules23071667 · Cited by 38
Zhang, Q., Zhang, N., Long, Y., Qian, X. H., & Yang, Y. (2015) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.5b00396 · Cited by 37
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Newman, D. K., Hoffman, S. M., Kotamraju, S., Zhao, T., Wakim, B. T., Kalyanaraman, B., & Newman, P. J. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02060-0 · Cited by 37
Tyrosine nitration as a key event of signal transduction that regulates functional state of the cell
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Elsasser, T. H., Li, C., Caperna, T. J., Kahl, S., & Schmidt, W. (2007) · Endocrinology · doi:10.1210/en.2006-1736 · Cited by 35
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Knight, A. R., Taylor, E., Lukaszewski, R. A., Jensen, K. T., Jones, H., Carré, J. E., Isupov, M. N., Littlechild, J. A., Bailey, S. J., Brewer, E., et al. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.03.026 · Cited by 34
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Goryacheva, A. V., Круглов, С. В., Pshennikova, M. G., Smirin, B. V., Malyshev, I. Y., Barskov, I. V., Викторов, И. В., Downey, H. F., & Manukhina, E. B. (2010) · Nitric Oxide · doi:10.1016/j.niox.2010.08.005 · Cited by 34
Erdal, N., Gürgül, S., Tamer, L., & Ayaz, L. (2008) · Journal of Radiation Research · doi:10.1269/jrr.07070 · Cited by 33
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Østerholt, H. C. D., Dannevig, I., Wyckoff, M. H., Liao, J., Akgul, Y., Ramgopal, M., Mija, D., Cheong, N., Longoria, C., Mahendroo, M., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038839 · Cited by 32
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Dixit, K., Khan, M. A., Sharma, Y. D., Moinuddin, M., & Alam, K. (2009) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2009.10.009 · Cited by 32
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
Wang, Y., Peng, F., Tong, W., Sun, H., Xu, N., & Liu, S. (2010) · Journal of Proteome Research · doi:10.1021/pr100349g · Cited by 30
Zhang, F., Chen, L., Liu, C., Qiu, P., Wang, A., Li, L., & Wang, H. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.03.016 · Cited by 31
Elsasser, T. H., Kahl, S., Li, C., Sartin, J. L., Garrett, W. M., & Rodrigo, J. (2007) · Endocrinology · doi:10.1210/en.2006-1737 · Cited by 30
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Chatterjee, S., Lardinois, O. M., Bonini, M. G., Bhattacharjee, S., Stadler, K., Corbett, J. T., Deterding, L. J., Tomer, K. B., Kadiiska, M. B., & Mason, R. P. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900593 · Cited by 28
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Petre, B. A., Ulrich, M., Stumbaum, M., Bernevic, B., Moise, A., Döring, G., & Przybylski, M. (2012) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-012-0461-4 · Cited by 26
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Heck, D. E. (2001) · Antioxidants and Redox Signaling · doi:10.1089/152308601300185205 · Cited by 26
Zhang, 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
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Zhu, X., Heunks, L. M. A., Versteeg, E. M. M., van der Heijden, E. H. F. M., Ennen, L., Kuppevelt, T. H. V., Viña, J., & Dekhuijzen, P. N. R. (2004) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00412.2003 · Cited by 26
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Metadata
- Authors
- Souza, J. M., Daikhin, E., Yudkoff, M., Raman, C. S., & Ischiropoulos, H.
- Affiliations
- Children's Hospital of Philadelphia (US)
- Corresponding author
- Ischiropoulos, Harry
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 1999-11
- Volume
- 371
- Issue
- 2
- Pages
- 169-178
- ISSN
- 0003-9861 (ISSN-L)
- OpenAlex
- W2054336997
- Cited by
- 315
- References
- 30
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 4 · 2023: 9 · 2022: 8 · 2021: 3 · 2020: 8 · 2019: 8 · 2018: 12 · 2017: 6 · 2016: 6 · 2015: 6 · 2014: 14 · 2013: 12 · 2012: 17
- FWCI
- 5.98
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Archives of Biochemistry and Biophysics (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- American Heart Association
- University of Pennsylvania
- National Institutes of Health (1r03ag016987-01)
- National Institute on Aging (AG 13966, R01AG013966, AG 16987)
- National Heart, Lung, and Blood Institute (HL54926, R01HL054926)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- tyrosine nitration, nitration selectivity, post-translational modification, peroxynitrite, nitric oxide, superoxide, myeloperoxidase, ribonuclease A, lysozyme, phospholipase A2, tyrosine residues, nitrating agents
- MeSH terms
- Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Muramidase, Nitrates, Nitric Oxide, Phospholipases A, Protein Processing, Post-Translational, Ribonuclease, Pancreatic, Superoxides, Tyrosine, Protein Structure, Secondary, Sequence Analysis, Protein
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