Eosinophil peroxidase nitrates protein tyrosyl residues

Wu, Weijia; Chen, Yonghong; Hazen, Stanley L.

doi:10.1074/jbc.274.36.25933

Cited by 265Neutrophil, Myeloperoxidase and Oxidative MechanismsRedox biology and oxidative stressAntioxidant Activity and Oxidative Stress

Eosinophil peroxidase nitrates protein tyrosyl residues

Open access

Wu, Weijia, Chen, Yonghong, Hazen, Stanley L.·1999·Journal of Biological Chemistry

DOI 10.1074/jbc.274.36.25933

Open this paper in CoChat — free account

Abstract

Eosinophil peroxidase (EPO) has been implicated in promoting oxidative tissue injury in conditions ranging from asthma and other allergic inflammatory disorders to cancer and parasitic/helminthic infections. Studies thus far on this unique peroxidase have primarily focused on its unusual substrate preference for bromide (Br(-)) and the pseudohalide thiocyanate (SCN(-)) forming potent hypohalous acids as cytotoxic oxidants. However, the ability of EPO to generate reactive nitrogen species has not yet been reported. We now demonstrate that EPO readily uses nitrite (NO(2)(-)), a major end-product of nitric oxide ((.)NO) metabolism, as substrate to generate a reactive intermediate that nitrates protein tyrosyl residues in high yield. EPO-catalyzed nitration of tyrosine occurred more readily than bromination at neutral pH, plasma levels of halides, and pathophysiologically relevant concentrations of NO(2)(-). Furthermore, EPO was significantly more effective than MPO at promoting tyrosine nitration in the presence of plasma levels of halides. Whereas recent studies suggest that MPO can also promote protein nitration through indirect oxidation of NO(2)(-) with HOCl, we found no evidence that EPO can indirectly mediate protein nitration by a similar reaction between HOBr and NO(2)(-). EPO-dependent nitration of tyrosine was modulated over a physiologically relevant range of SCN(-) concentrations and was accompanied by formation of tyrosyl radical addition products (e.g. o,o'-dityrosine, pulcherosine, trityrosine). The potential role of specific antioxidants and nucleophilic scavengers on yields of tyrosine nitration and bromination by EPO are examined. Thus, EPO may contribute to nitrotyrosine formation in inflammatory conditions characterized by recruitment and activation of eosinophils.

Integrity signals

Registry

Crossref · 10.1074/jbc.274.36.25933

Cites

70 of 70 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Generation of nitrogen dioxide and subsequent protein nitration from nitrite oxidation by peroxidases and other heme proteins was appreciated many years before the biologic potential for nitrite reduction to NO was realized.
“Generation of nitrogen dioxide and subsequent protein nitration from nitrite oxidation by peroxidases such as myeloperoxidase[108], eosinophil peroxidase [109] and also other heme proteins such as cytochrome c [110], hemoglobin [111, 112] and myoglobin [112, 113] was appreciated many years before the biologic potential for nitrite-reduction to NO was realized.”
From Current perspectives and challenges in understanding the role of nitrite as an integral player in nitric oxide biology and therapy (2011) · cites this paper as [109]

A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
Markwell, M. A. K., Haas, S. M., BIEBER, L. L., & Tolbert, N. E. (1978) · Analytical Biochemistry · doi:10.1016/0003-2697(78)90586-9 · Cited by 6,460 · see citing works
Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.
Cleveland, D. W., Fischer, S. G., Kirschner, M. W., & Laemmli, U. K. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75212-0 · Cited by 5,556 · see citing works
Trace Elements in Human and Animal Nutrition
UNDERWOOD, E. J. (1963) · Soil Science · doi:10.1097/00010694-196304000-00029 · Cited by 4,511 · see citing works
Eosinophilic Inflammation in Asthma
Bousquet, J., Chanez, P., Lacoste, J. Y., Barneon, G., Ghavanian, N., Enander, I., Venge, P., Ahlstedt, S., Simony-Lafontaine, J., Godard, P., et al. (1990) · New England Journal of Medicine · doi:10.1056/nejm199010113231505 · Cited by 2,499 · see citing works
Formation 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 · see citing works
[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 · see citing works
Enthalpy of decomposition of hydrogen peroxide by catalase at 25° C (with molar extinction coefficients of H2O2 solutions in the UV)
Nelson, D. P., & Kiesow, L. A. (1972) · Analytical Biochemistry · doi:10.1016/0003-2697(72)90451-4 · Cited by 926 · see citing works
Oxygen metabolism and the toxic properties of phagocytes
KLEBANOFF, S. J. (1980) · Annals of Internal Medicine · doi:10.7326/0003-4819-93-3-480 · Cited by 868 · see citing works
3-Chlorotyrosine, a specific marker of myeloperoxidase-catalyzed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima.
Hazen, S. L., & Heinecke, J. W. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119379 · Cited by 842 · see citing works
Self-citation
Eosinophilia
Rothenberg, M. E. (1998) · New England Journal of Medicine · doi:10.1056/nejm199805283382206 · Cited by 837 · see citing works
Chlorination of Taurine by Human Neutrophils
Weiss, S. J., Klein, R., Slivka, A., & Wei, M. L. (1982) · Journal of Clinical Investigation · doi:10.1172/jci110652 · Cited by 806 · see citing works
Formation 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 · see citing works
Increased concentrations of nitrite in synovial fluid and serum samples suggest increased nitric oxide synthesis in rheumatic diseases.
Farrell, A. J., Blake, D. R., Palmer, R. M. J., & Moncada, S. (1992) · Annals of the Rheumatic Diseases · doi:10.1136/ard.51.11.1219 · Cited by 717 · see citing works
Correlation between exhaled nitric oxide, sputum eosinophils, and methacholine responsiveness in patients with mild asthma.
Jatakanon, A., Lim, S. K., Kharitonov, S. A., Chung, K. F., & Barnes, P. J. (1998) · Thorax · doi:10.1136/thx.53.2.91 · Cited by 688 · see citing works
Endogenous nitrogen oxides and bronchodilator S-nitrosothiols in human airways.
Gaston, B. M., Reilly, J., Drazen, J. M., Fackler, J. C., Ramdev, P., Arnelle, D. R., Mullins, M. E., Sugarbaker, D. J., Chee, C., Singel, D. J., et al. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.10957 · Cited by 620 · see citing works
Handbook of Analytical Derivatization Reactions
Knapp, D. R. (1979) · Andalas University Repository (Andalas University) · Cited by 610 · see citing works
Trace Elements in Human and Animal Nutrition
(1986) · Elsevier eBooks · doi:10.1016/c2009-0-02917-1 · Cited by 607 · see citing works
Myeloperoxidase-generated reactive nitrogen species convert LDL into an atherogenic form in vitro
Podrez, E. A., Schmitt, D. C., Hoff, H. F., & Hazen, S. L. (1999) · Journal of Clinical Investigation · doi:10.1172/jci5549 · Cited by 492 · see citing works
Self-citation
Formation of Nitrating and Chlorinating Species by Reaction of Nitrite with Hypochlorous Acid
Eiserich, J. P., Cross, C. E., Jones, A. D., Halliwell, B., & van der Vliet, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.32.19199 · Cited by 447 · see citing works
Increased formation of the potent oxidant peroxynitrite in the airways of asthmatic patients is associated with induction of nitric oxide synthase: effect of inhaled glucocorticoid
Saleh, D. M., Ernst, P., Lim, S., Barnes, P. J., & Giaid, A. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.11.929 · Cited by 437 · see citing works
Thiocyanate and chloride as competing substrates for myeloperoxidase
van DALEN, J. C., WHITEHOUSE, W. M., WINTERBOURN, C. C., & KETTLE, J. A. (1997) · Biochemical Journal · doi:10.1042/bj3270487 · Cited by 406 · see citing works
Brominating Oxidants Generated by Human Eosinophils
Weiss, S. J., Test, S. T., Eckmann, C. M., Roos, D., & REGIANI, S. R. (1986) · Science · doi:10.1126/science.3018933 · Cited by 360 · see citing works
[40] Preparation and characterization of chloramines
Thomas, E. L., Grisham, M. B., & Jefferson, M. M. (1986) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(86)32042-1 · Cited by 348 · see citing works
Tyrosyl radical generated by myeloperoxidase is a physiological catalyst for the initiation of lipid peroxidation in low density lipoprotein.
Savenkova, M. L., Mueller, D. M., & Heinecke, J. W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32005-7 · Cited by 339 · see citing works
Myeloperoxidase and Horseradish Peroxidase Catalyze Tyrosine Nitration in Proteins from Nitrite and Hydrogen Peroxide
Sampson, J. B., Ye, Y., Rosen, H., & Beckman, J. S. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0772 · Cited by 313 · see citing works
Structure and Function of Oxidation–Reduction Enzymes
(1972) · Elsevier eBooks · doi:10.1016/c2013-0-02487-5 · Cited by 279 · see citing works
[53] Assays for the chlorination activity of myeloperoxidase
Kettle, A. J., & Winterbourn, C. C. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(94)33056-5 · Cited by 261 · see citing works
Handbook of Analytical Derivatization Reactions
REID, E. (1980) · Biochemical Society Transactions · doi:10.1042/bst0080671a · Cited by 261 · see citing works
Human neutrophils employ chlorine gas as an oxidant during phagocytosis.
Hazen, S. L., Hsu, F., Mueller, D. M., Crowley, J., & Heinecke, J. W. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118914 · Cited by 258 · see citing works
Self-citation
Accumulation of Hypothiocyanite Ion during Peroxidase‐Catalyzed Oxidation of Thiocyanate Ion
Aune, T. M., & THOMAS, E. L. (1977) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1977.tb11873.x · Cited by 251 · see citing works
[52] Antimicrobial activity of myeloperoxidase
Klebanoff, S. J., Waltersdorph, A. M., & Rosen, H. (1984) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(84)05055-2 · Cited by 210 · see citing works
Reactive nitrogen intermediates and antimicrobial activity: Role of nitrite
Klebanoff, S. J. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90084-8 · Cited by 192 · see citing works
[19] Antibodies that recognize nitrotyrosine
Ye, Y. Z., Strong, M. J., Huang, Z., & Beckman, J. S. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)69022-3 · Cited by 189 · see citing works
Oxidation of Bromide by the Human Leukocyte Enzymes Myeloperoxidase and Eosinophil Peroxidase
Thomas, E. L., Bozeman, P. M., Jefferson, M. M., & King, C. C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.7.2906 · Cited by 186 · see citing works
3-Bromotyrosine and 3,5-Dibromotyrosine Are Major Products of Protein Oxidation by Eosinophil Peroxidase: Potential Markers for Eosinophil-Dependent Tissue Injury in Vivo
Wu, W., Chen, Y., d'Avignon, A., & Hazen, S. L. (1999) · Biochemistry · doi:10.1021/bi982401l · Cited by 181 · see citing works
Self-citation
Human eosinophil peroxidase: purification and characterization.
Carlson, M. G., Peterson, C. G. B., & Venge, P. (1985) · The Journal of Immunology · doi:10.4049/jimmunol.134.3.1875 · Cited by 172 · see citing works
Assay of the human leukocyte enzymes myeloperoxidase and eosinophil peroxidase
Bozeman, P. M., Learn, D. B., & Thomas, E. L. (1990) · Journal of Immunological Methods · doi:10.1016/0022-1759(90)90020-v · Cited by 171 · see citing works
Expired nitric oxide as a marker for childhood asthma
Nelson, B. V., Sears, S., Woods, J., Ling, C. Y., Hunt, J., Clapper, L. M., & Gaston, B. M. (1997) · The Journal of Pediatrics · doi:10.1016/s0022-3476(97)70204-x · Cited by 163 · see citing works
Chemistry and biochemistry of thiocyanic acid and its derivatives
Newman, A. A. (1975) · Medical Entomology and Zoology · Cited by 159 · see citing works
Chemistry and Biochemistry of Thiocyanic Acid and its Derivatives
Ellis, M. (1976) · Biochemical Society Transactions · doi:10.1042/bst0040540 · Cited by 159 · see citing works
Human Phagocytes Employ the Myeloperoxidase-Hydrogen Peroxide System to Synthesize Dityrosine, Trityrosine, Pulcherosine, and Isodityrosine by a Tyrosyl Radical-dependent Pathway
Jacob, J. S., Cistola, D. P., Hsu, F., Muzaffar, S., Mueller, D. M., Hazen, S. L., & Heinecke, J. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.33.19950 · Cited by 150 · see citing works
Self-citation
Eosinophils Preferentially Use Bromide to Generate Halogenating Agents
Mayeno, A. N., Curran, A. J., Roberts, R. L., & Foote, C. S. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83599-2 · Cited by 145 · see citing works
Tumor necrosis factor alpha/cachectin stimulates eosinophil oxidant production and toxicity towards human endothelium.
Slungaard, A., Vercellotti, G. M., Walker, G., Nelson, R. D., & Jacob, H. S. (1990) · The Journal of Experimental Medicine · doi:10.1084/jem.171.6.2025 · Cited by 145 · see citing works
Mass Spectrometric Quantification of 3-Chlorotyrosine in Human Tissues with Attomole Sensitivity
Hazen, S. L., Crowley, J. R., Mueller, D. M., & Heinecke, J. W. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00084-1 · Cited by 134 · see citing works
Self-citation
Oxidative metabolism of the human eosinophil
DeChatelet, L., Shirley, P., McPhail, L. C., Huntley, C., Hb, M., & Bass, D. (1977) · Blood · doi:10.1182/blood.v50.3.525.525 · Cited by 127 · see citing works
Some properties of human eosinophil peroxidase, a comparison with other peroxidases
Bolscher, B. G. J. M., Plat, H., & Wever, R. (1984) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(84)90125-0 · Cited by 124 · see citing works
Eosinophils in the 1990s: New perspectives on their role in health and disease
Wardlaw, A. J. (1994) · Postgraduate Medical Journal · doi:10.1136/pgmj.70.826.536 · Cited by 121 · see citing works
Rates of formation of N-bromo amines in aqueous solution
Wajon, J. E., & Morris, J. C. (1982) · Inorganic Chemistry · doi:10.1021/ic00142a030 · Cited by 110 · see citing works
Condensed expirate nitrite as a home marker for acute asthma
Hunt, J., Byrns, R. E., Ignarro, L., & Gaston, B. M. (1995) · The Lancet · doi:10.1016/s0140-6736(95)92947-9 · Cited by 97 · see citing works
Leukocyte Myeloperoxidase and Salivary Lactoperoxidase: Identification and Quantitation in Human Mixed Saliva
Thomas, E. L., Jefferson, M. M., Joyner, R. E., Cook, G. S., & King, C. C. (1994) · Journal of Dental Research · doi:10.1177/00220345940730021001 · Cited by 96 · see citing works
Detecting oxidative modification of biomolecules with isotope dilution mass spectrometry: Sensitive and quantitative assays for oxidized amino acids in proteins and tissues
Heinecke, J. W., Hsu, F., Crowley, J. R., Hazen, S. L., Leeuwenburgh, C., Mueller, D. M., RASMUSSEN, J. E., & TURK, J. W. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)00121-4 · Cited by 94 · see citing works
Self-citation
Differential inactivation of Escherichia coli membrane dehydrogenases by a myeloperoxidase-mediated antimicrobial system
Rakita, R. M., Michel, B. R., & Rosen, H. (1990) · Biochemistry · doi:10.1021/bi00456a033 · Cited by 88 · see citing works
Isotope Dilution Mass Spectrometric Quantification of 3-Nitrotyrosine in Proteins and Tissues Is Facilitated by Reduction to 3-Aminotyrosine
Crowley, J. R., Yarasheski, K. E., Leeuwenburgh, C., TURK, J. W., & Heinecke, J. W. (1998) · Analytical Biochemistry · doi:10.1006/abio.1998.2635 · Cited by 86 · see citing works
Relative Chlorinating, Nitrating, and Oxidizing Capabilities of Neutrophils Determined with Phagocytosable Probes
Jiang, Q., & Hurst, J. K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.52.32767 · Cited by 84 · see citing works
Modification of proteins and lipids by myeloperoxidase
Hazen, S. L., Hsu, F., Gaut, J. P., Crowley, J. R., & Heinecke, J. W. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)00117-2 · Cited by 76 · see citing works
Self-citation
Serum concentrations of nitrite in patients with HIV-1 infection.
Torre, D., Ferrario, G., Speranza, F., Orani, A., Fiori, G. P., & Zeroli, C. (1996) · Journal of Clinical Pathology · doi:10.1136/jcp.49.7.574 · Cited by 70 · see citing works
Bromide-dependent toxicity of eosinophil peroxidase for endothelium and isolated working rat hearts: a model for eosinophilic endocarditis.
Slungaard, A., & Mahoney, J. R. (1991) · The Journal of Experimental Medicine · doi:10.1084/jem.173.1.117 · Cited by 68 · see citing works
Eosinophils in Allergy and Inflammation
(2019) · CRC Press eBooks · doi:10.1201/9780367812591 · Cited by 66 · see citing works
INFLAMMATION AND ASTHMA
Horwitz, R., & Busse, W. W. (1995) · Clinics in Chest Medicine · doi:10.1016/s0272-5231(21)01165-5 · Cited by 60 · see citing works
Purification of horse eosinophil peroxidase
Jörg, A., Pasquier, J.-M., & Klebanoff, S. J. (1982) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(82)90112-1 · Cited by 59 · see citing works
Studies on Myeloperoxidase Activity. I. Spectrophotometry of the MPO-H2O2 Compound.
Agner, K., Rumley, M. K., Taniuchi, H., & Løvstad, R. A. (1963) · Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry · doi:10.3891/acta.chem.scand.17s-0332 · Cited by 55 · see citing works
Eosinophil peroxidase-dependent hydroxyl radical generation by human eosinophils.
McCormick, M. L., Roeder, T. L., Railsback, M. A., & Britigan, B. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)46874-3 · Cited by 53 · see citing works
Eosinophils and Human Disease
Gleich, G. J., Ottesen, E. A., LEIFERMAN, K. M., & Ackerman, S. J. (2009) · International Archives of Allergy and Applied Immunology · doi:10.1159/000234749 · Cited by 47 · see citing works
Comparative toxicity of the horse eosinophil peroxidase-H2O2-halide system and granule basic proteins.
Klebanoff, S. J., Agosti, J. M., Jörg, A., & Waltersdorph, A. M. (1989) · The Journal of Immunology · doi:10.4049/jimmunol.143.1.239 · Cited by 45 · see citing works
Peroxidase Antimicrobial System of Human Saliva: Requirements for Accumulation of Hypothiocyanite
Thomas, E. L., Bates, K., & Jefferson, M. M. (1981) · Journal of Dental Research · doi:10.1177/00220345810600040401 · Cited by 40 · see citing works
Some enzymatic characteristics of eosinophil peroxidase from patients with eosinophilia and from healthy donors
Bos, A., Wever, R., Hamers, M. N., & Roos, D. (1981) · Infection and Immunity · doi:10.1128/iai.32.2.427-431.1981 · Cited by 34 · see citing works
Resonance Raman characterization of the heme prosthetic group in eosinophil peroxidase
Sibbett, S. S., Klebanoff, S. J., & Hurst, J. K. (1985) · FEBS Letters · doi:10.1016/0014-5793(85)81038-3 · Cited by 19 · see citing works
Evidence that eosinophils catalyze the bromide-dependent decarboxylation of amino acids
Cramer, R., Soranzo, M., & Patriarca, P. (1981) · Blood · doi:10.1182/blood.v58.6.1112.1112 · Cited by 16 · see citing works
Characterization of the Peroxidase in Human Eosinophils
Wever, R., Hamers, M. N., de Graaf, C. J., Weening, R. S., Roos, D., & Johnston, R. B. (1982) · Advances in experimental medicine and biology · doi:10.1007/978-1-4684-8088-7_48 · Cited by 11 · see citing works
Syndromes associated with eosinopenia
Freeman, G. L. (1998) · Allergy · doi:10.1111/j.1398-9995.1998.tb03901.x · Cited by 10 · see citing works

Flagged first, then by citations

Sorted by citations

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
The eosinophil
Rothenberg, M. E., & Hogan, S. P. (2006) · Annual Review of Immunology · doi:10.1146/annurev.immunol.24.021605.090720 · Cited by 1,356 · see citing works
Nitric oxide in health and disease of the respiratory system
Ricciardolo, F. L. M., Sterk, P. J., Gaston, B., & Folkerts, G. (2004) · Physiological Reviews · doi:10.1152/physrev.00034.2003 · Cited by 903 · 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
Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease
Zheng, L., Nukuna, B. N., Brennan, M., Sun, M., Goormastic, M., Settle, M., Schmitt, D., Fu, X., Thomson, L., Fox, P. L., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21109 · Cited by 735 · see citing works
Self-citation
Biochemistry of Peroxynitrite and Protein Tyrosine Nitration
Ferrer‐Sueta, G., Campolo, N., Trujillo, M., Bartesaghi, S., Carballal, S., Romero, N., Álvarez, B., & Radí, R. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00568 · Cited by 645 · see citing works
Peroxynitrite reactions and formation in mitochondria
Radí, R., Cassina, A., Hodara, R., Quijano, C., & Castro, L. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01111-5 · Cited by 635 · see citing works
Chemical basis of inflammation-induced carcinogenesis
Ohshima, H., Tatemichi, M., & Sawa, T. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(03)00283-2 · Cited by 618 · see citing works
Novel Effects of Nitric Oxide
Davis, K. L., Martin, E., Turko, I. V., & Murad, F. (2001) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.41.1.203 · Cited by 585 · see citing works
Inducible Nitric Oxide Synthase and Inflammatory Diseases
Zamora, R., Yoram Vodovotz, B., & Billiar, T. R. (2000) · Molecular Medicine · doi:10.1007/bf03401781 · Cited by 560 · see citing works
Mammalian Heme Peroxidases: From Molecular Mechanisms to Health Implications
Davies, M. J., Hawkins, C. L., Pattison, D. I., & Rees, M. D. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1927 · Cited by 556 · see citing works
Tyrosine nitration: Localisation, quantification, consequences for protein function and signal transduction
Greenacre, S., & Ischiropoulos, H. (2001) · Free Radical Research · doi:10.1080/10715760100300471 · Cited by 500 · see citing works
Biological selectivity and functional aspects of protein tyrosine nitration
Ischiropoulos, H. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00814-3 · Cited by 500 · see citing works
A Tale of Two Controversies
Brennan, M.-L., Wu, W., Fu, X., Shen, Z., Song, W., Frost, H., Vadseth, C., Narine, L., Lenkiewicz, E., Borchers, M. T., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112400200 · Cited by 486 · see citing works
Self-citation
Mitochondrial dysfunction in cardiovascular disease
Ballinger, S. W. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.02.014 · Cited by 405 · see citing works
How biology handles nitrite
Maia, L. B., & Moura, J. J. G. (2014) · Chemical Reviews · doi:10.1021/cr400518y · Cited by 401 · see citing works
Nitric Oxide Is a Physiological Substrate for Mammalian Peroxidases
Abu‐Soud, H. M., & Hazen, S. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.48.37524 · Cited by 398 · see citing works
Self-citation
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
Biological significance of nitric oxide-mediated protein modifications
Gow, A. J., Farkouh‐Karoleski, C., Munson, D. A., Posencheg, M. A., & Ischiropoulos, H. (2004) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00295.2003 · Cited by 384 · see citing works
Protein Nitration in Cardiovascular Diseases
Turko, I. V., & Murad, F. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.4.619 · Cited by 372 · see citing works
NO-dependent protein nitration: a cell signaling event or an oxidative inflammatory response?
Schopfer, F. J. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.10.006 · Cited by 369 · see citing works
Cytochrome c Nitration by Peroxynitrite
Cassina, A. M., Hodara, R., Souza, J. M., Thomson, L., Castro, L., Ischiropoulos, H., Freeman, B. A., & Radi, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909978199 · Cited by 354 · see citing works
Chapter 3 Biology of the Eosinophil
Blanchard, C., & Rothenberg, M. E. (2009) · Advances in immunology · doi:10.1016/s0065-2776(08)01003-1 · Cited by 344 · see citing works
The cysteine proteome
Go, Y., Chandler, J. D., & Jones, D. P. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.03.022 · Cited by 343 · see citing works
Oxidative and nitrosative events in asthma
Andreadis, A. A., Hazen, S. L., Comhair, S. A. A., & Erzurum, S. C. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00278-8 · Cited by 327 · see citing works
Self-citation
Biomarkers of lipid peroxidation, airway inflammation and asthma
Wood, L. G., Gibson, P. G., & Garg, M. L. (2003) · European Respiratory Journal · doi:10.1183/09031936.03.00017003a · Cited by 321 · see citing works
Antioxidant responses to oxidant-mediated lung diseases
COMHAIR, S. A. A., & ERZURUM, S. C. (2002) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00491.2001 · Cited by 307 · see citing works
Reactive species and DNA damage in chronic inflammation: reconciling chemical mechanisms and biological fates
Lonkar, P. S., & Dedon, P. C. (2010) · International Journal of Cancer · doi:10.1002/ijc.25815 · Cited by 286 · see citing works
Eosinophils Are a Major Source of Nitric Oxide-Derived Oxidants in Severe Asthma: Characterization of Pathways Available to Eosinophils for Generating Reactive Nitrogen Species
MacPherson, J. C., COMHAIR, S. A. A., ERZURUM, S. C., Klein, D. F., Lipscomb, M. F., Kavuru, M. S., Samoszuk, M. K., & Hazen, S. L. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.9.5763 · Cited by 280 · see citing works
Self-citation
Myeloperoxidase and its contributory role in inflammatory vascular disease
Lau, D., & Baldus, S. E. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2005.06.023 · Cited by 277 · see citing works
Widespread Nitration of Pathological Inclusions in Neurodegenerative Synucleinopathies
Duda, J. E., Giasson, B. I., Chen, Q., Gur, T., Hurtig, H. I., Stern, M. B., Gollomp, S. M., Ischiropoulos, H., Lee, V. M. ‐., & Trojanowski, J. Q. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64781-5 · Cited by 276 · see citing works
Increased Nitrotyrosine in Exhaled Breath Condensate of Patients with Asthma
Hanazawa, T., Kharitonov, S. A., & Barnes, P. J. (2000) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.162.4.9912064 · Cited by 257 · see citing works
Discovery of the nitric oxide signaling pathway and targets for drug development
Nathan, S. B. (2009) · Frontiers in bioscience · doi:10.2741/3228 · Cited by 256 · see citing works
Reactive nitrogen species in the respiratory tract
Ricciardolo, F. L. M., Stefano, A. D., Sabatini, F., & Folkerts, G. (2006) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2005.12.057 · Cited by 245 · see citing works
Dose-dependent onset and cessation of action of inhaled budesonide on exhaled nitric oxide and symptoms in mild asthma
Kharitonov, S. A. (2002) · Thorax · doi:10.1136/thorax.57.10.889 · Cited by 239 · see citing works
Oxidant stress in asthma
Dworski, R. (2000) · Thorax · doi:10.1136/thorax.55.suppl_2.s51 · Cited by 209 · see citing works
Protein tyrosine nitration—An update
Ischiropoulos, H. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.10.034 · Cited by 207 · see citing works
Myeloperoxidase produces nitrating oxidants in vivo
Gaut, J. P., Byun, J., Tran, H. D., Lauber, W. M., Carroll, J. A., Hotchkiss, R. S., Belaaouaj, A., & Heinecke, J. W. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15021 · Cited by 225 · see citing works
Nitric Oxide Modulates the Catalytic Activity of Myeloperoxidase
Abu‐Soud, H. M., & Hazen, S. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5425 · Cited by 195 · see citing works
Self-citation
Nitrotyrosine Proteome Survey in Asthma Identifies Oxidative Mechanism of Catalase Inactivation
Ghosh, S., Janocha, A. J., Aronica, M. A., Swaidani, S., COMHAIR, S. A. A., Xu, W., Zheng, L., Kaveti, S., Kinter, M. T., Hazen, S. L., et al. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.9.5587 · Cited by 190 · see citing works
Self-citation
Dityrosine as a product of oxidative stress and fluorescent probe
Malencik, D. A., & Anderson, S. R. (2003) · Amino Acids · doi:10.1007/s00726-003-0014-z · Cited by 186 · see citing works
Protein nitration is mediated by heme and free metals through Fenton-type chemistry: An alternative to the NO/O\documentclass[12pt]{minimal}\usepackage{amsmath}\usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy}\usepackage{mathrsfs}\setlength{\oddsidemargin}{-69pt}\begin{document}\begin{equation*}{\mathrm{_{2}^{-}}}\end{equation*}\end{document} reaction
Thomas, D. D., Espey, M. G., Vitek, M. P., Miranda, K. M., & Wink, D. A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202312699 · Cited by 181 · see citing works
Myeloperoxidase-Generated Oxidants Modulate Left Ventricular Remodeling but Not Infarct Size After Myocardial Infarction
Vasilyev, N. V., Williams, T., Brennan, M., Unzek, S., Zhou, X., Heinecke, J. W., Spitz, D. R., Topol, E. J., Hazen, S. L., & Penn, M. S. (2005) · Circulation · doi:10.1161/circulationaha.105.542340 · Cited by 179 · see citing works
Self-citation
Role of Inducible Nitric Oxide Synthase in Pulmonary Microvascular Protein Leak in Murine Sepsis
Wang, L. F., Patel, M., Razavi, H. M., Weicker, S., JOSEPH, M. G., McCormack, D. G., & Mehta, S. (2002) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.2110017 · Cited by 172 · see citing works
Correlation of Systemic Superoxide Dismutase Deficiency to Airflow Obstruction in Asthma
COMHAIR, S. A. A., Ricci, K. S., Arroliga, M. E., Lara, A., Dweik, R. A., Song, W., Hazen, S. L., Bleecker, E. R., Busse, W. W., Chung, K. F., et al. (2005) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200502-180oc · Cited by 167 · see citing works
Self-citation
Protein tyrosine nitration in mouse peritoneal macrophages activated in vitro and in vivo: evidence against an essential role of peroxynitrite
Pfeiffer, S., Lass, A., Schmidt, K., & Mayer, B. (2001) · The FASEB Journal · doi:10.1096/fj.01-0295com · Cited by 166 · see citing works
Immunopathogenesis of Experimental Ulcerative Colitis Is Mediated by Eosinophil Peroxidase
Forbes, E., Murase, T., Yang, M., Matthaei, K. I., Lee, J. J., Lee, N. A., Foster, P. S., & Hogan, S. P. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.9.5664 · Cited by 159 · see citing works
Protein Tyrosine Nitration in Cytokine-activated Murine Macrophages
Pfeiffer, S., Lass, A., Schmidt, K., & Mayer, B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100585200 · Cited by 160 · see citing works
Dityrosine Formation Outcompetes Tyrosine Nitration at Low Steady-state Concentrations of Peroxynitrite
Pfeiffer, S., Schmidt, K., & Mayer, B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.9.6346 · Cited by 158 · see citing works
The principal eosinophil peroxidase product, HOSCN, is a uniquely potent phagocyte oxidant inducer of endothelial cell tissue factor activity: a potential mechanism for thrombosis in eosinophilic inflammatory states
Wang, J.-G., Mahmud, S. A., Thompson, J. A., Geng, J.-G., Key, N. S., & Slungaard, A. (2005) · Blood · doi:10.1182/blood-2005-05-2152 · Cited by 157 · see citing works
Role for Endothelin-1–Induced Superoxide and Peroxynitrite Production in Rebound Pulmonary Hypertension Associated With Inhaled Nitric Oxide Therapy
Wedgwood, S., McMullan, D. M., Bekker, J. M., Fineman, J. R., & Black, S. M. (2001) · Circulation Research · doi:10.1161/hh1601.094983 · Cited by 157 · see citing works
Plasma proteins modified by tyrosine nitration in acute respiratory distress syndrome
Gole, M., Souza, J. M., Choi, I. Y., Hertkorn, C., Malcolm, S., Foust, R., Finkel, B., Lanken, P. N., & Ischiropoulos, H. (2000) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2000.278.5.l961 · Cited by 152 · see citing works
Review: Oxidant—antioxidant imbalance in asthma: scientific evidence, epidemiological data and possible therapeutic options
Nadeem, A., Masood, A., & Siddiqui, N. M. (2008) · Therapeutic Advances in Respiratory Disease · doi:10.1177/1753465808094971 · Cited by 148 · see citing works
Protein oxidation at the air-lung interface
Kelly, F. J., & Mudway, I. (2003) · Amino Acids · doi:10.1007/s00726-003-0024-x · Cited by 144 · see citing works
Current analytical methods for the detection of dityrosine, a biomarker of oxidative stress, in biological samples
DiMarco, T., & Giulivi, C. (2006) · Mass Spectrometry Reviews · doi:10.1002/mas.20109 · Cited by 140 · see citing works
Eosinophils in the pathogenesis of allergic airways disease
Trivedi, S. G., & Lloyd, C. M. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-6527-y · Cited by 136 · see citing works
Reactive nitrogen and oxygen species in airway inflammation
Folkerts, G., Kloek, J., Muijsers, R. B. R., & Nijkamp, F. P. (2001) · European Journal of Pharmacology · doi:10.1016/s0014-2999(01)01324-3 · Cited by 134 · see citing works
Artifact-Free Quantification of Free 3-Chlorotyrosine, 3-Bromotyrosine, and 3-Nitrotyrosine in Human Plasma by Electron Capture–Negative Chemical Ionization Gas Chromatography Mass Spectrometry and Liquid Chromatography–Electrospray Ionization Tandem Mass Spectrometry
Gaut, J. P., Byun, J., Tran, H. D., & Heinecke, J. W. (2002) · Analytical Biochemistry · doi:10.1006/abio.2001.5469 · Cited by 133 · see citing works
Eosinophil Peroxidase Oxidation of Thiocyanate
Arlandson, M. E., Decker, T., Roongta, V. A., Bonilla, L. E., Mayo, K. H., MacPherson, J. C., Hazen, S. L., & Slungaard, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m004881200 · Cited by 130 · see citing works
Self-citation
Antioxidant and Anti-Inflammatory Effects of Resveratrol in Airway Disease
Wood, L. G., Wark, P. A. B., & Garg, M. L. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3064 · Cited by 129 · see citing works
Abnormalities in nitric oxide and its derivatives in lung cancer
Masri, F. A., Comhair, S. A. A., Koeck, T., Xu, W., Janocha, A., Ghosh, S., Dweik, R. A., Golish, J., Kinter, M., Stuehr, D. J., et al. (2005) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200411-1523oc · Cited by 128 · see citing works
On the Clinical Pharmacology of Reactive Oxygen Species
Casas, A. I., Nogales, C., Mucke, H. A., Petraina, A., Cuadrado, A., Rojo, A. I., Ghezzi, P., Jaquet, V., Augsburger, F., Dufrasne, F., et al. (2020) · Pharmacological Reviews · doi:10.1124/pr.120.019422 · Cited by 128 · see citing works
Extensive Eosinophil Degranulation and Peroxidase-Mediated Oxidation of Airway Proteins Do Not Occur in a Mouse Ovalbumin-Challenge Model of Pulmonary Inflammation
Denzler, K. L., Borchers, M. T., Crosby, J. R., Cieslewicz, G., Hines, E. M., Justice, J. P., Cormier, S. A., Lindenberger, K. A., Song, W., Wu, W., et al. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.3.1672 · Cited by 127 · see citing works
Self-citation
Nitrative and oxidative DNA damage in oral lichen planus in relation to human oral carcinogenesis
Chaiyarit, P., Ma, N., Hiraku, Y., Pinlaor, S., Yongvanit, P., Jintakanon, D., Murata, M., Oikawa, S., & Kawanishi, S. (2005) · Cancer Science · doi:10.1111/j.1349-7006.2005.00096.x · Cited by 127 · see citing works
Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromide and chloride
Senthilmohan, R., & Kettle, A. J. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.07.005 · Cited by 122 · see citing works
Oxidants, nitrosants, and the lung
van der Vliet, A., & Cross, C. E. (2000) · The American Journal of Medicine · doi:10.1016/s0002-9343(00)00479-4 · Cited by 120 · see citing works
Role of eosinophil peroxidase in host defense and disease pathology
Wang, J., & Slungaard, A. (2005) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.10.008 · Cited by 117 · see citing works
Modification of tryptophan and tryptophan residues in proteins by reactive nitrogen species
Yamakura, F., & Ikeda, K. (2005) · Nitric Oxide · doi:10.1016/j.niox.2005.07.009 · Cited by 117 · see citing works
ATS Workshop Proceedings: Exhaled Nitric Oxide and Nitric Oxide Oxidative Metabolism in Exhaled Breath Condensate
Silkoff, P. E., ERZURUM, S. C., Lundberg, J. O., George, S. C., Marczin, N., Hunt, J. F., Effros, R. M., & Horváth, I. (2006) · Proceedings of the American Thoracic Society · doi:10.1513/pats.200406-710st · Cited by 115 · see citing works
Kinetics and Thermodynamics of Halide and Nitrite Oxidation by Mammalian Heme Peroxidases
Arnhold, J., Monzani, E., Furtmüller, P. G., Zederbauer, M., Casella, L., & Obinger, C. (2006) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.200600436 · Cited by 113 · see citing works
Substrates and products of eosinophil peroxidase
van Dalen, C. J., & Kettle, A. J. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3580233 · Cited by 109 · see citing works
Eosinophil peroxidase produces hypobromous acid in the airways of stable asthmatics
Aldridge, R. E., Chan, T., van Dalen, C. J., Senthilmohan, R., WINN, M. C., Venge, P., Town, G. I., & Kettle, A. J. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00976-0 · Cited by 109 · see citing works
Nitrotyrosine and Chlorotyrosine: Clinical Significance and Biological Functions in the Vascular System
Mohiuddin, I. T., Chai, H., Lin, P. H., Lumsden, A. B., Yao, Q., & Chen, C. (2005) · Journal of Surgical Research · doi:10.1016/j.jss.2005.10.008 · Cited by 106 · see citing works
Ratiometric fluorescence imaging of cellular hypochlorous acid based on heptamethine cyanine dyes
Lou, Z., Li, P., Song, P., & Han, K. (2013) · The Analyst · doi:10.1039/c3an00198a · Cited by 104 · see citing works
Eosinophil granule proteins and their role in disease
Walsh, G. M. (2001) · Current Opinion in Hematology · doi:10.1097/00062752-200101000-00006 · Cited by 101 · see citing works
Real‐Time Amperometric Analysis of Reactive Oxygen and Nitrogen Species Released by Single Immunostimulated Macrophages
Amatore, C. A., Arbault, S., Bouton, C., Drapier, J., Ghandour, H., & Koh, A. C. W. (2008) · ChemBioChem · doi:10.1002/cbic.200700746 · Cited by 100 · see citing works
Molecular mechanisms of nitrogen dioxide induced epithelial injury in the lung.
Persinger, R. L., Poynter, M. E., Ckless, K., & Janssen-Heininger, Y. M. W. (2002) · PubMed · Cited by 99 · see citing works
Molecular mechanisms of nitrogen dioxide induced epithelial injury in the lung
Persinger, R. L., Poynter, M. E., Ckless, K., & Janssen-Heininger, Y. M. W. (2002) · Molecular and Cellular Biochemistry · doi:10.1023/a:1015973530559 · Cited by 117 · see citing works
Nitric oxide: a pro-inflammatory mediator in lung disease?
van der Vliet, A., Eiserich, J. P., & Cross, C. E. (2000) · Respiratory Research · doi:10.1186/rr14 · Cited by 92 · see citing works
Nitric Oxide and Protein Nitration are Eosinophil Dependent in Allergen-Challenged Mice
Iijima, H., Duguet, A., Eum, S., Hamid, Q. A., & Eidelman, D. H. (2001) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.163.5.2003145 · Cited by 89 · see citing works
Genetic and epigenetic damage induced by reactive nitrogen species: implications in carcinogenesis
Ohshima, H. (2003) · Toxicology Letters · doi:10.1016/s0378-4274(02)00506-4 · Cited by 89 · see citing works
Eosinophils in Infection and Intestinal Immunity
Hogan, S., Waddell, A. B., & Fulkerson, P. (2013) · Current Opinion in Gastroenterology · doi:10.1097/mog.0b013e32835ab29a · Cited by 84 · see citing works
Hemodynamics influences vascular peroxynitrite formation: Implication for low-density lipoprotein apo-B-100 nitration
Hsiai, T. K., Hwang, J., Barr, M. L., Correa, A., Hamilton, R., Alavi, M., Rouhanizadeh, M., Cadenas, E., & Hazen, S. L. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.11.017 · Cited by 87 · see citing works
Self-citation
Prevention of 1-methyl-4-phenylpyridinium- and 6-hydroxydopamine-induced nitration of tyrosine hydroxylase and neurotoxicity by EUK-134, a superoxide dismutase and catalase mimetic, in cultured dopaminergic neurons
Pong, K., Doctrow, S. R., & Baudry, M. (2000) · Brain Research · doi:10.1016/s0006-8993(00)02841-9 · Cited by 87 · see citing works
Chlorinative Stress in Age-Related Diseases: A Literature Review
Casciaro, M., Di Salvo, E., Pace, E., Ventura-Spagnolo, E., Navarra, M., & Gangemi, S. (2017) · Immunity & Ageing · doi:10.1186/s12979-017-0104-5 · Cited by 85 · 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
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
Gasotransmitter Heterocellular Signaling
Kolluru, G. K., Shen, X., Yuan, S. S., & Kevil, C. G. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6909 · Cited by 83 · see citing works
The Role of Nitric Oxide in Regulating Intestinal Redox Status and Intestinal Epithelial Cell Functionality
Mu, K., Yu, S., & Kitts, D. D. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20071755 · Cited by 83 · see citing works
Biochemical mechanisms and therapeutic potential of pseudohalide thiocyanate in human health
Chandler, J. D., & Day, B. J. (2015) · Free Radical Research · doi:10.3109/10715762.2014.1003372 · Cited by 81 · see citing works
Chromatographic and mass spectrometric methods for quantitative determination of 3-nitrotyrosine in biological samples and their application to human samples
Ryberg, H., & Caidahl, K. (2007) · Journal of Chromatography B · doi:10.1016/j.jchromb.2007.02.001 · Cited by 82 · see citing works
New Insights in Oxidant Biology in Asthma
ERZURUM, S. C. (2016) · Annals of the American Thoracic Society · doi:10.1513/annalsats.201506-385mg · Cited by 81 · see citing works
Eosinophils in Inflammatory Bowel Disease
Filippone, R. T., Sahakian, L., Apostolopoulos, V., & Nurgali, K. (2019) · Inflammatory Bowel Diseases · doi:10.1093/ibd/izz024 · Cited by 78 · see citing works
Modulation of nitric oxide pathways: Therapeutic potential in asthma and chronic obstructive pulmonary disease
Redington, A. E. (2006) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2005.12.069 · Cited by 77 · see citing works
Selective Metabolism of Hypothiocyanous Acid by Mammalian Thioredoxin Reductase Promotes Lung Innate Immunity and Antioxidant Defense
Chandler, J. D., Nichols, D. P., Nick, J. A., Hondal, R. J., & Day, B. J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.468090 · Cited by 77 · see citing works
Nitric oxide metabolism in asthma pathophysiology
Ghosh, S., & ERZURUM, S. C. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.06.009 · 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
Intramolecular Electron Transfer between Tyrosyl Radical and Cysteine Residue Inhibits Tyrosine Nitration and Induces Thiyl Radical Formation in Model Peptides Treated with Myeloperoxidase, H2O2, and NO2-
Zhang, H., Xu, Y., Joseph, J., & Kalyanaraman, B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504503200 · Cited by 76 · see citing works
Role of nitric oxide and superoxide in allergen‐induced airway hyperreactivity after the late asthmatic reaction in guinea‐pigs
de Boer, J., Meurs, H., Flendrig, L. M., Koopal, M., & Zaagsma, J. (2001) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0704191 · Cited by 73 · see citing works
Myeloperoxidase Acts as a Source of Free Iron During Steady-State Catalysis by a Feedback Inhibitory Pathway
Maitra, D., Shaeib, F., Abdulhamid, I., Abdulridha, R. M., Saed, G. M., Diamond, M. P., Pennathur, S., & Abu-Soud, H. M. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.04.009 · Cited by 64 · see citing works

3-Bromotyrosine and 3,5-Dibromotyrosine Are Major Products of Protein Oxidation by Eosinophil Peroxidase: Potential Markers for Eosinophil-Dependent Tissue Injury in Vivo
Wu, W., Chen, Y., d'Avignon, A., & Hazen, S. L. (1999) · Biochemistry · doi:10.1021/bi982401l · Cited by 181 · see citing works
Self-citation
Post-translational Tyrosine Nitration of Eosinophil Granule Toxins Mediated by Eosinophil Peroxidase
Ulrich, M., Petre, A., Youhnovski, N., Prömm, F., Schirle, M., Schumm, M., Pero, R. S., Doyle, A. D., Checkel, J. L., Kita, H., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801196200 · Cited by 46 · see citing works
Mechanism of nitrite oxidation by eosinophil peroxidase: implications for oxidant production and nitration by eosinophils
van Dalen, C. J., Winterbourn, C. C., & Kettle, A. J. (2006) · Biochemical Journal · doi:10.1042/bj20051470 · Cited by 30 · see citing works
The Potential Role of Nitric Oxide in Substrate Switching in Eosinophil Peroxidase
Galijašević, S., Proteasa, G., Abdulhamid, I. B., & Abu‐Soud, H. M. (2006) · Biochemistry · doi:10.1021/bi061177u · Cited by 10 · see citing works
Biochemical characterization of reactive nitrogen species by eosinophil peroxidase in tyrosine nitration.
Takemoto, K., Ogino, K., Wang, D.-H., Takigawa, T., Kurosawa, C. M., Kamyabashi, Y., Hibino, Y., Hitomi, Y., & Ichimura, H. (2007) · PubMed · doi:10.18926/amo/32911 · Cited by 8 · see citing works

Authors: Wu, W., Chen, Y., & Hazen, S. L.
Affiliations: Cleveland State University (US)
Corresponding author: Hazen, Stanley L.
ORCID: Wu, Weijia
Chen, Yonghong
Hazen, Stanley L.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1999-09
Volume: 274
Issue: 36
Pages: 25933-25944
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.274.36.25933
OpenAlex: W2094921988
Cited by: 265
References: 70
Citations by year: 2026: 7 · 2025: 2 · 2024: 4 · 2023: 1 · 2022: 1 · 2021: 4 · 2020: 3 · 2019: 4 · 2018: 5 · 2017: 6 · 2016: 4 · 2015: 4 · 2014: 6 · 2013: 7 · 2012: 8
FWCI: 7.75
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7707 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Heart, Lung, and Blood Institute (HL61878, HL 62526, R01HL061878, R01HL062526)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
Keywords: eosinophil peroxidase, nitrite, tyrosine nitration, reactive nitrogen species, eosinophils, myeloperoxidase, thiocyanate, bromide, hypohalous acids, nitrotyrosine, oxidative tissue injury, antioxidants, eosinophil activation
MeSH terms: Animals, Eosinophils, Inflammation, Kinetics, Nitric Oxide, Nitrites, Peroxidases, Tyrosine, Oxidative Stress, Eosinophil Peroxidase

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Eosinophil peroxidase nitrates protein tyrosyl residues

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks