Cited by 333Neutrophil, Myeloperoxidase and Oxidative MechanismsRedox biology and oxidative stressNitric Oxide and Endothelin Effects

The DOI matches its Crossref record; 308 of the 308 references it cites were found in a registry or an index.

The Role of Myeloperoxidase in Biomolecule Modification, Chronic Inflammation, and Disease

Open access

Davies, Michael J., Hawkins, Clare L.·2020·Antioxidants & Redox Signaling

DOI 10.1089/ars.2020.8030

Open this paper in CoChat — free account Open PDF

Abstract

Significance: The release of myeloperoxidase (MPO) by activated leukocytes is critical in innate immune responses. MPO produces hypochlorous acid (HOCl) and other strong oxidants, which kill bacteria and other invading pathogens. However, MPO also drives the development of numerous chronic inflammatory pathologies, including atherosclerosis, neurodegenerative disease, lung disease, arthritis, cancer, and kidney disease, which are globally responsible for significant patient mortality and morbidity. Recent Advances: The development of imaging approaches to precisely identify the localization of MPO and the molecular targets of HOCl in vivo is an important advance, as typically the involvement of MPO in inflammatory disease has been inferred by its presence, together with the detection of biomarkers of HOCl, in biological fluids or diseased tissues. This will provide valuable information in regard to the cell types responsible for releasing MPO in vivo , together with new insight into potential therapeutic opportunities. Critical Issues: Although there is little doubt as to the value of MPO inhibition as a protective strategy to mitigate tissue damage during chronic inflammation in experimental models, the impact of long-term inhibition of MPO as a therapeutic strategy for human disease remains uncertain, in light of the potential effects on innate immunity. Future Directions: The development of more targeted MPO inhibitors or a treatment regimen designed to reduce MPO-associated host tissue damage without compromising pathogen killing by the innate immune system is therefore an important future direction. Similarly, a partial MPO inhibition strategy may be sufficient to maintain adequate bacterial activity while decreasing the propagation of inflammatory pathologies.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1089/ars.2020.8030

Cites

308 of 308 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

1 retracted

Myeloperoxidase Deletion Prevents High-Fat Diet–Induced Obesity and Insulin Resistance
Wang, Q., Xie, Z., Zhang, W., Zhou, J., Wu, Y., Zhang, M., Zhu, H., & Zou, M. (2014) · Diabetes · doi:10.2337/db14-0026 · Cited by 97
Retracted
Novel cell death program leads to neutrophil extracellular traps
Fuchs, T. A., Abed, U., Goosmann, C., Hurwitz, R., Schulze, I., Wahn, V., Weinrauch, Y., Brinkmann, V., & Zychlinsky, A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200606027 · Cited by 3,197
Myeloperoxidase: friend and foe
Klebanoff, S. J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.1204697 · Cited by 2,282
Neutrophil Extracellular Traps Contain Calprotectin, a Cytosolic Protein Complex Involved in Host Defense against Candida albicans
Urban, C. F., Ermert, D., Schmid, M., Abed, U. A., Goosmann, C., Nacken, W. K. F., Brinkmann, V., Jungblut, P. R., & Zychlinsky, A. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000639 · Cited by 1,720
Inside the Neutrophil Phagosome: Oxidants, Myeloperoxidase, and Bacterial Killing
Hampton, M. B., Kettle, A. J., & Winterbourn, C. C. (1998) · Blood · doi:10.1182/blood.v92.9.3007.421k47_3007_3017 · Cited by 1,665
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
The antioxidants of human extracellular fluids
Halliwell, B. B., & Gutteridge, J. M. C. (1990) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(90)90510-6 · Cited by 1,351
Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions.
Daugherty, A., Dunn, J. L., Rateri, D. L., & Heinecke, J. W. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117342 · Cited by 1,269
Prognostic Value of Myeloperoxidase in Patients with Chest Pain
Brennan, M., Penn, M. S., Lente, F. V., Nambi, V., Shishehbor, M. H., Aviles, R. J., Goormastic, M., Pepoy, M. L., McErlean, E. S., Topol, E. J., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa035003 · Cited by 1,071
Myeloperoxidase Serum Levels Predict Risk in Patients With Acute Coronary Syndromes
Baldus, S. E., Heeschen, C., Meinertz, T., Zeiher, A. M., Eiserich, J. P., Münzel, T. F., Simoons, M. L., & Hamm, C. W. (2003) · Circulation · doi:10.1161/01.cir.0000090690.67322.51 · Cited by 1,007
Beneficial suicide: why neutrophils die to make NETs
Brinkmann, V., & Zychlinsky, A. (2007) · Nature Reviews Microbiology · doi:10.1038/nrmicro1710 · Cited by 937
The Acid Ionization Constant of HOCl from 5 to 35°
Morris, J. C. (1966) · The Journal of Physical Chemistry · doi:10.1021/j100884a007 · Cited by 927
Association Between Myeloperoxidase Levels and Risk of Coronary Artery Disease
Zhang, R. (2001) · JAMA · doi:10.1001/jama.286.17.2136 · Cited by 919
Neutrophilic Inflammation in Severe Persistent Asthma
Jatakanon, A., Uasuf, C. G., Maziak, W., Lim, S., Chung, K. F., & Barnes, P. J. (1999) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.160.5.9806170 · Cited by 845
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
Myeloperoxidase is required for neutrophil extracellular trap formation: implications for innate immunity
Metzler, K. D., Fuchs, T. A., Nauseef, W. M., Reumaux, D., Roesler, J., Schulze, I., Wahn, V., Papayannopoulos, V., & Zychlinsky, A. (2010) · Blood · doi:10.1182/blood-2010-06-290171 · Cited by 802
Absolute Rate Constants for the Reaction of Hypochlorous Acid with Protein Side Chains and Peptide Bonds
Pattison, D. I., & Davies, M. J. (2001) · Chemical Research in Toxicology · doi:10.1021/tx0155451 · Cited by 790
Self-citation
Redox-based regulation of signal transduction: principles, pitfalls, and promises
Janssen-Heininger, Y. M. W., Mossman, B. T., Heintz, N. H., Forman, H. J., Kalyanaraman, B., Finkel, T., Stamler, J. S., Rhee, S. G., & van der Vliet, A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.011 · Cited by 784
Inflammation and cancer: role of phagocyte-generated oxidants in carcinogenesis
Weitzman, S., & Gordon, L. I. (1990) · Blood · doi:10.1182/blood.v76.4.655.655 · Cited by 761
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
Protein carbamylation links inflammation, smoking, uremia and atherogenesis
Wang, Z., Nicholls, S. J., Rodríguez, E. R., Kummu, O., Hörkkö, S., Barnard, J., Reynolds, W. F., Topol, E. J., DiDonato, J. A., & Hazen, S. L. (2007) · Nature Medicine · doi:10.1038/nm1637 · Cited by 722
Macrophage Myeloperoxidase Regulation by Granulocyte Macrophage Colony-Stimulating Factor in Human Atherosclerosis and Implications in Acute Coronary Syndromes
Sugiyama, S., Okada, Y., Sukhova, G. K., Virmani, R., Heinecke, J. W., & Libby, P. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64036-9 · Cited by 699
Myeloperoxidase, a Leukocyte-Derived Vascular NO Oxidase
Eiserich, J. P., Baldus, S. E., Brennan, M., Ma, W., Zhang, C., Tousson, A., Castro, L., Lusis, A. J., Nauseef, W. M., White, C. R., et al. (2002) · Science · doi:10.1126/science.1106830 · Cited by 685
Myeloperoxidase: a key regulator of neutrophil oxidant production
Kettle, A. J., & Winterbourn, C. C. (1997) · Redox Report · doi:10.1080/13510002.1997.11747085 · Cited by 671
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 653
Modeling the Reactions of Superoxide and Myeloperoxidase in the Neutrophil Phagosome
Winterbourn, C. C., Hampton, M. B., Livesey, J. H., & Kettle, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605898200 · Cited by 633
Hypochlorite-induced oxidation of amino acids, peptides and proteins
Hawkins, C. L., Pattison, D. I., & Davies, M. J. (2003) · Amino Acids · doi:10.1007/s00726-003-0016-x · Cited by 600
Self-citation
Presence of hypochlorite-modified proteins in human atherosclerotic lesions.
Hazell, L. J., Arnold, L., Flowers, D., Waeg, G., Malle, E., & Stocker, R. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118576 · Cited by 592
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 559
Self-citation
Taurine and Inflammatory Diseases
Marcinkiewicz, J., & Kontny, E. (2014) · Amino Acids · doi:10.1007/s00726-012-1361-4 · Cited by 531
Myeloperoxidase: Molecular Mechanisms of Action and Their Relevance to Human Health and Disease
van der Veen, B. S., de Winther, M. P. J., & Heeringa, P. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2538 · Cited by 530
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
Hypochlorous Acid Oxygenates the Cysteine Switch Domain of Pro-matrilysin (MMP-7)
Fu, X., Kassim, S. Y., Parks, W. C., & Heinecke, J. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106958200 · Cited by 482
Redox Reactions and Microbial Killing in the Neutrophil Phagosome
Winterbourn, C. C., & Kettle, A. J. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4827 · Cited by 468
Comparative reactivities of various biological compounds with myeloperoxidase-hydrogen peroxide-chloride, and similarity of oxidant to hypochlorite
Winterbourn, C. C. (1985) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(85)90120-5 · Cited by 463
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
Biological reactivity of hypochlorous acid: implications for microbicidal mechanisms of leukocyte myeloperoxidase.
Albrich, J. M., McCarthy, C. A., & Hurst, J. K. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.1.210 · Cited by 442
Hypochlorous Acid, a Macrophage Product, Induces Endothelial Apoptosis and Tissue Factor Expression
Sugiyama, S., Kugiyama, K., Aikawa, M., Nakamura, S., Ogawa, H., & Libby, P. (2004) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000131784.50633.4f · Cited by 415
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
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 399
Protease-Antiprotease Imbalance in the Lungs of Children with Cystic Fibrosis
Birrer, P., McElvaney, N. G., Rüdeberg, A., Sommer, C. W., Liechti‐Gallati, S., Kraemer, R., Hubbard, R. C., & Crystal, R. G. (1994) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.150.1.7912987 · Cited by 381
X-ray Crystal Structure and Characterization of Halide-binding Sites of Human Myeloperoxidase at 1.8 Å Resolution
Fiedler, T. J., Davey, C. A., & Fenna, R. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.16.11964 · Cited by 374
An abundant dysfunctional apolipoprotein A1 in human atheroma
Huang, Y. R., DiDonato, J. A., Levison, B. S., Schmitt, D., Li, L., Wu, Y., Buffa, J. A., Kim, T., Gerstenecker, G. S., Gu, X., et al. (2014) · Nature Medicine · doi:10.1038/nm.3459 · Cited by 369
Serum Myeloperoxidase Levels Independently Predict Endothelial Dysfunction in Humans
Vita, J. A., Brennan, M., Gokce, N., Mann, S. A., Goormastic, M., Shishehbor, M. H., Penn, M. S., Keaney, J. F., & Hazen, S. L. (2004) · Circulation · doi:10.1161/01.cir.0000140262.20831.8f · Cited by 369
Reactions of Myeloperoxidase-Derived Oxidants with Biological Substrates:Gaining Chemical Insight into Human Inflammatory Diseases
Pattison, D. I., & Davies, M. J. (2006) · Current Medicinal Chemistry · doi:10.2174/092986706778773095 · Cited by 361
Self-citation
Kinetics and Mechanisms of Hypochlorous Acid Reactions
Folkes, L. K., Candeias, L. P., & Wardman, P. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.0017 · Cited by 358
Active site structure and catalytic mechanisms of human peroxidases
Furtmüller, P. G., Zederbauer, M., Jantschko, W., Helm, J., Bogner, M., Jakopitsch, C., & Obinger, C. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.09.017 · Cited by 358
Tyrosyl radical generated by myeloperoxidase catalyzes the oxidative cross-linking of proteins.
Heinecke, J. W., Li, W., Francis, G. A., & Goldstein, J. A. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116531 · Cited by 354
Myeloperoxidase in kidney disease
Malle, E., Buch, T., & Gröne, H. (2003) · Kidney International · doi:10.1046/j.1523-1755.2003.00336.x · Cited by 353
Myeloperoxidase acts as a profibrotic mediator of atrial fibrillation
Rudolph, V., Andrié, R., Rudolph, T. K., Friedrichs, K. P., Klinke, A., Hirsch-Hoffmann, B., Schwoerer, A. P., Lau, D., Fu, X., Klingel, K., et al. (2010) · Nature Medicine · doi:10.1038/nm.2124 · Cited by 352
Myeloperoxidase associated with neutrophil extracellular traps is active and mediates bacterial killing in the presence of hydrogen peroxide
Parker, H. A., Albrett, A. M., Kettle, A. J., & Winterbourn, C. C. (2011) · Journal of Leukocyte Biology · doi:10.1189/jlb.0711387 · Cited by 349
[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 344
Plasma Concentrations of Myeloperoxidase Predict Mortality After Myocardial Infarction
Mocatta, T. J., Pilbrow, A. P., Cameron, V. A., Senthilmohan, R., Frampton, C. M., Richards, M., & Winterbourn, C. C. (2007) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2007.02.040 · Cited by 344
Evidence for Rapid Inter- and Intramolecular Chlorine Transfer Reactions of Histamine and Carnosine Chloramines: Implications for the Prevention of Hypochlorous-Acid-Mediated Damage
Pattison, D. I., & Davies, M. J. (2006) · Biochemistry · doi:10.1021/bi060348s · Cited by 338
Self-citation
Neuronal expression of myeloperoxidase is increased in Alzheimer's disease
Green, P. S., Mendez, A. J., Jacob, J. S., Crowley, J. R., Growdon, W., Hyman, B. T., & Heinecke, J. W. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02527.x · Cited by 337
Kinetics of the reactions of hypochlorous acid and amino acid chloramines with thiols, methionine, and ascorbate
Peskin, A. V., & Winterbourn, C. C. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00506-2 · Cited by 335
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 333
Endothelial transcytosis of myeloperoxidase confers specificity to vascular ECM proteins as targets of tyrosine nitration
Baldus, S. E., Eiserich, J. P., Mani, A. R., Castro, L., Figueroa, M., Chumley, P. H., Ma, W., Tousson, A., White, C. R., Bullard, D. C., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci12617 · Cited by 332
Hypochlorous Acid Interactions with Thiols, Nucleotides, DNA, and Other Biological Substrates
Prütz, W. A. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0322 · Cited by 327
Myeloperoxidase Polymorphism Is Associated with Gender Specific Risk for Alzheimer's Disease
Reynolds, W. F., Rhees, J., Maciejewski, D. F., Paladino, T., Sieburg, H. B., Maki, R. A., & Masliah, E. (1999) · Experimental Neurology · doi:10.1006/exnr.1998.6977 · Cited by 321
Oxidation of low-density lipoprotein with hypochlorite causes transformation of the lipoprotein into a high-uptake form for macrophages
Hazell, L. J., & Stocker, R. (1993) · Biochemical Journal · doi:10.1042/bj2900165 · Cited by 311
X-ray crystal structure of canine myeloperoxidase at 3 Å resolution
Zeng, J., & Fenna, R. E. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90133-5 · Cited by 310
Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation
Hawkins, C. L., & Davies, M. J. (1998) · Biochemical Journal · doi:10.1042/bj3320617 · Cited by 305
Self-citation
Ablation of the Inflammatory Enzyme Myeloperoxidase Mitigates Features of Parkinson's Disease in Mice
Choi, D., Pennathur, S., Perier, C., Tieu, K., Teismann, P., Wu, D.-C., Jackson-Lewis, V. R., Vila, M., Vonsattel, J., Heinecke, J. W., et al. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0970-05.2005 · Cited by 286
Myeloperoxidase in the inflamed colon: A novel target for treating inflammatory bowel disease
Chami, B., Martin, N., Dennis, J. M., & Witting, P. K. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.03.012 · Cited by 285
Immunohistochemical and genetic evidence of myeloperoxidase involvement in multiple sclerosis
Nagra, R. M., Becher, B., Tourtellotte, W. W., Antel, J. P., Gold, D. P., Paladino, T., Smith, R. A., Nelson, J. R., & Reynolds, W. F. (1997) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(97)00089-1 · Cited by 284
Myeloperoxidase in human neutrophil host defence
Nauseef, W. M. (2014) · Cellular Microbiology · doi:10.1111/cmi.12312 · Cited by 283
Endothelial transcytosis of myeloperoxidase confers specificity to vascular ECM proteins as targets of tyrosine nitration
Baldus, S. E., Eiserich, J. P., Mani, A. R., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci200112617 · Cited by 281
Modification of High Density Lipoprotein by Myeloperoxidase Generates a Pro-inflammatory Particle
Undurti, A., Huang, Y. R., Lupica, J. A., Smith, J. D., DiDonato, J. A., & Hazen, S. L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.047605 · Cited by 267
Human Atherosclerotic Intima and Blood of Patients with Established Coronary Artery Disease Contain High Density Lipoprotein Damaged by Reactive Nitrogen Species
Pennathur, S., Bergt, C., Shao, B., Byun, J., Kassim, S. Y., Singh, P., Green, P. S., McDonald, T. O., Brunzell, J. D., Chait, A., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406762200 · Cited by 263
Biological reactivity and biomarkers of the neutrophil oxidant, hypochlorous acid
Winterbourn, C. C. (2002) · Toxicology · doi:10.1016/s0300-483x(02)00286-x · Cited by 247
Mechanism of inactivation of myeloperoxidase by 4-aminobenzoic acid hydrazide
Kettle, A. J., Gedye, C. A., & Winterbourn, C. C. (1997) · Biochemical Journal · doi:10.1042/bj3210503 · Cited by 245
Myeloperoxidase: A new player in autoimmunity
Strzępa, A., Pritchard, K. A., & Dittel, B. N. (2017) · Cellular Immunology · doi:10.1016/j.cellimm.2017.05.002 · Cited by 244
Kinetics of Oxidation of Tyrosine and Dityrosine by Myeloperoxidase Compounds I and II
Marquez‐Curtis, L. A., & Dunford, H. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.51.30434 · Cited by 237
Leukocytic Oxygen Activation and Microbicidal Oxidative Toxin
Hurst, J. K., & Barrette, W. C. (1989) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238909082555 · Cited by 227
Nitric oxide suppresses NADPH oxidase-dependent superoxide production by S-nitrosylation in human endothelial cells
Selemidis, S., Dusting, G. J., Peshavariya, H., Kemp‐Harper, B. K., & Drummond, G. R. (2007) · Cardiovascular Research · doi:10.1016/j.cardiores.2007.03.030 · Cited by 226
Myeloperoxidase and oxidative stress in rheumatoid arthritis
Stamp, L. K., Khalilova, I. S., Tarr, J. M., Senthilmohan, R., Turner, R., Haigh, R. C., Winyard, P. G., & Kettle, A. J. (2012) · Lara D. Veeken · doi:10.1093/rheumatology/kes193 · Cited by 215
Free Hydroxyl Radicals are Formed on Reaction Between the Neutrophil-Derived Species Superoxide Anion and Hypochlorous Acid
Candeias, L. P., Patel, K. B., Stratford, M. R. L., & Wardman, P. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80394-a · Cited by 212
Myeloperoxidase, modified lipoproteins, and atherogenesis
Nicholls, S. J., & Hazen, S. L. (2008) · Journal of Lipid Research · doi:10.1194/jlr.r800086-jlr200 · Cited by 211
Kinetic Analysis of the Reactions of Hypobromous Acid with Protein Components: Implications for Cellular Damage and Use of 3-Bromotyrosine as a Marker of Oxidative Stress
Pattison, D. I., & Davies, M. J. (2004) · Biochemistry · doi:10.1021/bi035946a · Cited by 209
Self-citation
Cytotoxicity mechanisms of sodium hypochlorite in cultured human dermal fibroblasts and its bactericidal effectiveness
Hidalgo, E., Bartolomé, R. M., & Domı́nguez, C. (2002) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00003-0 · Cited by 209
Hypochlorite-Induced Damage to DNA, RNA, and Polynucleotides: Formation of Chloramines and Nitrogen-Centered Radicals
Hawkins, C. L., & Davies, M. J. (2002) · Chemical Research in Toxicology · doi:10.1021/tx015548d · Cited by 208
Self-citation
Myeloperoxidase and protein oxidation in cystic fibrosis
van der Vliet, A., Nguyen, M. N., Shigenaga, M. K., Eiserich, J. P., Marelich, G. P., & Cross, C. E. (2000) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2000.279.3.l537 · Cited by 203
Myeloperoxidase: A Leukocyte-Derived Protagonist of Inflammation and Cardiovascular Disease
Nußbaum, C., Klinke, A., Adam, M., Baldus, S. E., & Sperandio, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4783 · Cited by 199
Heparins Increase Endothelial Nitric Oxide Bioavailability by Liberating Vessel-Immobilized Myeloperoxidase
Baldus, S. E., Rudolph, V., Roiss, M., Ito, W. D., Rudolph, T. K., Eiserich, J. P., Sydow, K., Lau, D., Szöcs, K., Klinke, A., et al. (2006) · Circulation · doi:10.1161/circulationaha.105.590083 · Cited by 198
The roles of myeloperoxidase in coronary artery disease and its potential implication in plaque rupture
Teng, N., Maghzal, G. J., Talib, J., Rashid, I., Lau, A. K., & Stocker, R. (2016) · Redox Report · doi:10.1080/13510002.2016.1256119 · Cited by 198
Modification of low-density lipoprotein by myeloperoxidase-derived oxidants and reagent hypochlorous acid
Malle, E., Marsche, G., Arnhold, J., & Davies, M. J. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2006.03.024 · Cited by 184
Self-citation
Reactions and reactivity of myeloperoxidase-derived oxidants: Differential biological effects of hypochlorous and hypothiocyanous acids
Pattison, D. I., Davies, M. J., & Hawkins, C. L. (2012) · Free Radical Research · doi:10.3109/10715762.2012.667566 · Cited by 183
Self-citation
Elevated Activity and Microglial Expression of Myeloperoxidase in Demyelinated Cerebral Cortex in Multiple Sclerosis
Gray, E., Thomas, T. L., Betmouni, S., Scolding, N. J., & Love, S. (2007) · Brain Pathology · doi:10.1111/j.1750-3639.2007.00110.x · Cited by 175
Reactivity of disulfide bonds is markedly affected by structure and environment: implications for protein modification and stability
Karimi, M., Ignasiak, M. T., Chan, B., Croft, A. K., Radom, L., Schiesser, C. H., Pattison, D. I., & Davies, M. J. (2016) · Scientific Reports · doi:10.1038/srep38572 · Cited by 175
Self-citation
Expression of Human Myeloperoxidase by Macrophages Promotes Atherosclerosis in Mice
McMillen, T. S., Heinecke, J. W., & LeBoeuf, R. C. (2005) · Circulation · doi:10.1161/circulationaha.104.516278 · Cited by 168
Hypochlorous Acid-Induced Base Modifications in Isolated Calf Thymus DNA
Whiteman, M., Jenner, A. M., & Halliwell, B. B. (1997) · Chemical Research in Toxicology · doi:10.1021/tx970086i · Cited by 167
Reevaluation of the rate constants for the reaction of hypochlorous acid (HOCl) with cysteine, methionine, and peptide derivatives using a new competition kinetic approach
Storkey, C., Davies, M. J., & Pattison, D. I. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.04.024 · Cited by 165
Self-citation
Enzyme-Sensitive Magnetic Resonance Imaging Targeting Myeloperoxidase Identifies Active Inflammation in Experimental Rabbit Atherosclerotic Plaques
Ronald, J. A., Chen, J. W., Chen, Y., Hamilton, A. M., Rodríguez, E., Reynolds, F., Hegele, R. A., Rogers, K. A., Querol, M., Bogdanov, A. A., Jr., et al. (2009) · Circulation · doi:10.1161/circulationaha.108.813998 · Cited by 164
2-Thioxanthines Are Mechanism-based Inactivators of Myeloperoxidase That Block Oxidative Stress during Inflammation
Tiden, A. K., Sjögren, T., Svensson, M., Bernlind, A., Senthilmohan, R., Auchère, F., Norman, H. L., Markgren, P.-O., Gustavsson, S., Schmidt, S., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.266981 · Cited by 163
Oxidants and asthma
Caramori, G. (2004) · Thorax · doi:10.1136/thorax.2002.002477 · Cited by 162
Hypochlorous acid induces apoptosis of cultured cortical neurons through activation of calpains and rupture of lysosomes
Yap, Y. W., Whiteman, M., Bay, B., Li, Y., Sheu, F., Qi, R. Z., Tan, C. H., & Cheung, N. S. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03996.x · Cited by 161
Renal participation of myeloperoxidase in antineutrophil cytoplasmic antibody (ANCA)-associated glomerulonephritis
O’Sullivan, K. M., Lo, C. Y.-W., Summers, S. A., Elgass, K., McMillan, P. J., Longano, A., Ford, S. L., Gan, P., Kerr, P. G., Kitching, A. R., et al. (2015) · Kidney International · doi:10.1038/ki.2015.202 · Cited by 159
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 159
The Pathophysiological Role of Neutrophil Extracellular Traps in Inflammatory Diseases
Bonaventura, A., Liberale, L., Carbone, F., Vecchié, A., Díaz-Cañestro, C., Camici, G. G., Montecucco, F., & Dallegri, F. (2018) · Thrombosis and Haemostasis · doi:10.1160/th17-09-0630 · Cited by 157
Human Myeloperoxidase: Structure of a Cyanide Complex and Its Interaction with Bromide and Thiocyanate Substrates at 1.9 Å Resolution
Blair-Johnson, M., Fiedler, T. J., & Fenna, R. E. (2001) · Biochemistry · doi:10.1021/bi0111808 · Cited by 154
Myeloperoxidase and Protein Oxidation in the Airways of Young Children with Cystic Fibrosis
Kettle, A. J., Chan, T., Osberg, I. M., Senthilmohan, R., Chapman, A., Mocatta, T. J., & Wagener, J. S. (2004) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200311-1516oc · Cited by 148
Effects of native and myeloperoxidase-modified apolipoprotein A-I on reverse cholesterol transport and atherosclerosis in mice
Hewing, B., Parathath, S., Barrett, T. J., Chung, W. K. K., Astudillo, Y., Hamada, T., Ramkhelawon, B., Tallant, T. C., Yusufishaq, M., DiDonato, J., et al. (2014) · Arteriosclerosis, Thrombosis and Vascular Biology · doi:10.1161/atvbaha.113.303044 · Cited by 147
Chlorination of Guanosine and Other Nucleosides by Hypochlorous Acid and Myeloperoxidase of Activated Human Neutrophils
Masuda, M., Suzuki, T., Friesen, M. D., Ravanat, J.-L., Cadet, J., Pignatelli, B., Nishino, H., & Ohshima, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102700200 · Cited by 144
Phagocytes Produce 5-Chlorouracil and 5-Bromouracil, Two Mutagenic Products of Myeloperoxidase, in Human Inflammatory Tissue
Henderson, J. P., Byun, J., Takeshita, J., & Heinecke, J. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303928200 · Cited by 141
Hypochlorous Acid-Mediated Oxidation of Lipid Components and Antioxidants Present in Low-Density Lipoproteins: Absolute Rate Constants, Product Analysis, and Computational Modeling
Pattison, D. I., Hawkins, C. L., & Davies, M. J. (2003) · Chemical Research in Toxicology · doi:10.1021/tx025670s · Cited by 139
Self-citation
Nitrite as a Substrate and Inhibitor of Myeloperoxidase
van Dalen, C. J., Winterbourn, C. C., Senthilmohan, R., & Kettle, A. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.16.11638 · Cited by 139
Myeloperoxidase-immunoreactive cells are significantly increased in brain areas affected by neurodegeneration in Parkinson’s and Alzheimer’s disease
Gellhaar, S., Sunnemark, D., Eriksson, H., Olson, L., & Galter, D. (2017) · Cell and Tissue Research · doi:10.1007/s00441-017-2626-8 · Cited by 139
The antioxidant role of thiocyanate in the pathogenesis of cystic fibrosis and other inflammation-related diseases
Xu, Y., Szép, S., & Lü, Z. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911412106 · Cited by 136
Myeloperoxidase Inactivates TIMP-1 by Oxidizing Its N-terminal Cysteine Residue
Wang, Y., Rosen, H., Madtes, D. K., Shao, B., Martin, T. R., Heinecke, J. W., & Fu, X. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704894200 · Cited by 132
Oxidation of intracellular glutathione after exposure of human red blood cells to hypochlorous acid
Vissers, M. C. M., & Winterbourn, C. C. (1995) · Biochemical Journal · doi:10.1042/bj3070057 · Cited by 130
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
Hypothiocyanous acid reactivity with low-molecular-mass and protein thiols: absolute rate constants and assessment of biological relevance
Skaff, O., Pattison, D. I., & Davies, M. J. (2009) · Biochemical Journal · doi:10.1042/bj20090276 · Cited by 130
Self-citation
Thiocyanate is the major substrate for eosinophil peroxidase in physiologic fluids. Implications for cytotoxicity.
Slungaard, A., & Mahoney, J. R. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67734-3 · Cited by 129
Dietary quercetin attenuates oxidant-induced endothelial dysfunction and atherosclerosis in apolipoprotein E knockout mice fed a high-fat diet: A critical role for heme oxygenase-1
Shen, Y., Ward, N. C., Hodgson, J. M., Puddey, I. B., Wang, Y., Zhang, D., Maghzal, G. J., Stocker, R., & Croft, K. D. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.08.185 · Cited by 129
Flavonoids as Substrates and Inhibitors of Myeloperoxidase: Molecular Actions of Aglycone and Metabolites
Shiba, Y., Kinoshita, T., Chuman, H., Taketani, Y., Takeda, E., Kato, Y., Naito, M., Kawabata, K., Ishisaka, A., Terao, J., et al. (2008) · Chemical Research in Toxicology · doi:10.1021/tx8000835 · Cited by 129
Biological hydroperoxides and singlet molecular oxygen generation
Miyamoto, S., Ronsein, G. E., Prado, F. M., Uemi, M., Corrêa, T. C., Toma, I. N., Bertolucci, A., de Oliveira, M. C. B., Motta, F. D., de Medeiros, M. H. G., et al. (2007) · IUBMB Life · doi:10.1080/15216540701242508 · Cited by 127
Aberrant Expression of Myeloperoxidase in Astrocytes Promotes Phospholipid Oxidation and Memory Deficits in a Mouse Model of Alzheimer Disease
Maki, R. A., Tyurin, V. A., Lyon, R. C., Hamilton, R. L., DeKosky, S. T., Kagan, V. E., & Reynolds, W. F. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807731200 · Cited by 127
Chlorination of taurine by myeloperoxidase. Kinetic evidence for an enzyme-bound intermediate.
Marquez‐Curtis, L. A., & Dunford, H. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37143-0 · Cited by 126
Elevated myeloperoxidase activity in white matter in multiple sclerosis
Gray, E., Thomas, T. L., Betmouni, S., Scolding, N. J., & Love, S. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.08.035 · Cited by 125
Nitrogen dioxide radical generated by the myeloperoxidase‐hydrogen peroxide‐nitrite system promotes lipid peroxidation of low density lipoprotein
Byun, J., Mueller, D. M., Fabjan, J. S., & Heinecke, J. W. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00893-5 · Cited by 125
What Are the Plasma Targets of the Oxidant Hypochlorous Acid? A Kinetic Modeling Approach
Pattison, D. I., Hawkins, C. L., & Davies, M. J. (2009) · Chemical Research in Toxicology · doi:10.1021/tx800372d · Cited by 123
Self-citation
Lysine Residues Direct the Chlorination of Tyrosines in YXXK Motifs of Apolipoprotein A-I When Hypochlorous Acid Oxidizes High Density Lipoprotein
Bergt, C., Fu, X., Saifee, N. H., Kao, J. L.-F., & Heinecke, J. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309046200 · Cited by 123
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
Hypochlorous Acid-Mediated Protein Oxidation: How Important Are Chloramine Transfer Reactions and Protein Tertiary Structure?
Pattison, D. I., Hawkins, C. L., & Davies, M. J. (2007) · Biochemistry · doi:10.1021/bi7008294 · Cited by 122
Self-citation
A kinetic study of the reaction between human myeloperoxidase, hydroperoxides and cyanide inhibition by chloride and thiocyanate
Bolscher, B. G. J. M., & Wever, R. (1984) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(84)90290-5 · Cited by 121
Interactions of Hypochlorous Acid with Pyrimidine Nucleotides, and Secondary Reactions of Chlorinated Pyrimidines with GSH, NADH, and Other Substrates
Prütz, W. A. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0440 · Cited by 121
[41] Cytotoxicity 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)32043-3 · Cited by 121
Myeloperoxidase: Bridging the gap in neurodegeneration
Ray, R. S., & Katyal, A. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.06.031 · Cited by 120
Myeloperoxidase is a potential molecular imaging and therapeutic target for the identification and stabilization of high-risk atherosclerotic plaque
Rashid, I., Maghzal, G. J., Chen, Y., Cheng, D., Talib, J., Newington, D. L., Minqin, R., Vajandar, S. K., Searle, A. K., Maluenda, A. C., et al. (2018) · European Heart Journal · doi:10.1093/eurheartj/ehy419 · Cited by 119
Neutrophil-derived myeloperoxidase aggravates non-alcoholic steatohepatitis in low-density lipoprotein receptor-deficient mice
Rensen, S. S., Bieghs, V., Xanthoulea, S., Arfianti, E., Bakker, J. A., Shiri-Sverdlov, R., Hofker, M. H., Greve, J. W., & Buurman, W. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052411 · Cited by 116
Comparative reactivity of myeloperoxidase-derived oxidants with mammalian cells
Rayner, B. S., Love, D. T., & Hawkins, C. L. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.004 · Cited by 114
Self-citation
Microglia and myeloperoxidase: A deadly partnership in neurodegenerative disease
Lefkowitz, D. L., & Lefkowitz, S. S. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.05.021 · Cited by 113
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
Reaction of HOCl with amino acids and peptides: EPR evidence for rapid rearrangement and fragmentation reactions of nitrogen-centred radicals
Hawkins, C. L., & Davies, M. J. (1998) · Journal of the Chemical Society Perkin Transactions 2 · doi:10.1039/a802949k · Cited by 113
Self-citation
Redox Buffering of Hypochlorous Acid by Thiocyanate in Physiologic Fluids
Ashby, M. T., Carlson, A. C., & Scott, M. J. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0438361 · Cited by 113
Biochemical requirements for singlet oxygen production by purified human myeloperoxidase.
Kanofsky, J. R., Wright, J., Miles-Richardson, G. E., & Tauber, A. I. (1984) · Journal of Clinical Investigation · doi:10.1172/jci111562 · Cited by 111
Oxidative Biomarkers in the Diagnosis and Prognosis of Cardiovascular Disease
Tsimikas, S. (2006) · The American Journal of Cardiology · doi:10.1016/j.amjcard.2006.09.015 · Cited by 111
Kinetics and Mechanisms of the Reaction of Hypothiocyanous Acid with 5-Thio-2-nitrobenzoic Acid and Reduced Glutathione
Nagy, P., Jameson, G. N. L., & Winterbourn, C. C. (2009) · Chemical Research in Toxicology · doi:10.1021/tx900249d · Cited by 111
Inactivation of Protease Inhibitors and Lysozyme by Hypochlorous Acid: Role of Side-Chain Oxidation and Protein Unfolding in Loss of Biological Function
Hawkins, C. L., & Davies, M. J. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050207b · Cited by 110
Self-citation
Low-Density Lipoprotein Modified by Myeloperoxidase in Inflammatory Pathways and Clinical Studies
Delporte, C., Antwerpen, P. V., Vanhamme, L., Roumeguère, T., & Boudjeltia, K. Z. (2013) · Mediators of Inflammation · doi:10.1155/2013/971579 · Cited by 109
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
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
2-Chlorohexadecanal Derived From Hypochlorite-Modified High-Density Lipoprotein–Associated Plasmalogen Is a Natural Inhibitor of Endothelial Nitric Oxide Biosynthesis
Marsche, G., Heller, R., Fauler, G., Kovacevic, A., Nuszkowski, A., Graier, W. F., Sattler, W., & Malle, E. (2004) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000148703.43429.25 · Cited by 108
Hypochlorite-modified Low Density Lipoprotein Inhibits Nitric Oxide Synthesis in Endothelial Cells via an Intracellular Dislocalization of Endothelial Nitric-oxide Synthase
Nuszkowski, A., Gräbner, R., Marsche, G., Unbehaun, A., Malle, E., & Heller, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007659200 · Cited by 106
Heme to protein linkages in mammalian peroxidases: impact on spectroscopic, redox and catalytic properties
Zederbauer, M., Furtmüller, P. G., Brogioni, S., Jakopitsch, C., Smulevich, G., & Obinger, C. (2007) · Natural Product Reports · doi:10.1039/b604178g · Cited by 106
Comparison of human red cell lysis by hypochlorous and hypobromous acids: insights into the mechanism of lysis
VISSERS, C. M. M., Carr, A. C., & Chapman, L. (1998) · Biochemical Journal · doi:10.1042/bj3300131 · Cited by 103
Inhibition of myeloperoxidase oxidant production by N-acetyl lysyltyrosylcysteine amide reduces brain damage in a murine model of stroke
Yu, G., Liang, Y. S., Huang, Z., Jones, D. W., Pritchard, K. A., & Zhang, H. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0583-x · Cited by 103
Leukocyte-Derived Myeloperoxidase Amplifies High-Glucose—Induced Endothelial Dysfunction Through Interaction With High-Glucose—Stimulated, Vascular Non—Leukocyte-Derived Reactive Oxygen Species
Zhang, C., Yang, J., & Jennings, L. K. (2004) · Diabetes · doi:10.2337/diabetes.53.11.2950 · Cited by 101
Role of Myeloperoxidase in Patients with Chronic Kidney Disease
Kisić, B., Miric, D. J., Dragojević, I. M., Rašić, J., & Popović, L. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1069743 · Cited by 101
Reactions of Superoxide with Myeloperoxidase
Kettle, A. J., Anderson, R. F., Hampton, M. B., & Winterbourn, C. C. (2007) · Biochemistry · doi:10.1021/bi602587k · Cited by 99
Taurine chloramine is more selective than hypochlorous acid at targeting critical cysteines and inactivating creatine kinase and glyceraldehyde-3-phosphate dehydrogenase
Peskin, A. V., & Winterbourn, C. C. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.08.019 · Cited by 98
Redox Intermediates of Plant and Mammalian Peroxidases: A Comparative Transient-Kinetic Study of Their Reactivity Toward Indole Derivatives
Jantschko, W., Furtmüller, P. G., Allegra, M., Livrea, M. A., Jakopitsch, C., Regelsberger, G., & Obinger, C. (2002) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2674 · Cited by 98
Demyelinating Diseases: Myeloperoxidase as an Imaging Biomarker and Therapeutic Target
Forghani, R., Wojtkiewicz, G. R., Zhang, Y., Seeburg, D. P., Bautz, B. R. M., Pulli, B., Milewski, A., Atkinson, W. L., Iwamoto, Y., Zhang, E. R., et al. (2012) · Radiology · doi:10.1148/radiol.12111593 · Cited by 97
Growing Significance of Myeloperoxidase in Non-infectious Diseases
Hoy, A., Leininger‐Muller, B., Kutter, D., Siest, G., & Visvikis‐Siest, S. (2002) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2002.002 · Cited by 96
Defects in leukocyte-mediated initiation of lipid peroxidation in plasma as studied in myeloperoxidase-deficient subjects: systematic identification of multiple endogenous diffusible substrates for myeloperoxidase in plasma
Zhang, R., Shen, Z., Nauseef, W. M., & Hazen, S. L. (2002) · Blood · doi:10.1182/blood.v99.5.1802.h8001802_1802_1810 · Cited by 95
Hypochlorous acid causes caspase activation and apoptosis or growth arrest in human endothelial cells
Vissers, M. C. M., Pullar, J. M., & Hampton, M. B. (1999) · Biochemical Journal · doi:10.1042/bj3440443 · Cited by 95
Myeloperoxidase Generates 5-Chlorouracil in Human Atherosclerotic Tissue
Takeshita, J., Byun, J., Nhan, T. Q., Pritchard, D. K., Pennathur, S., Schwartz, S. M., Chait, A., & Heinecke, J. W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509236200 · Cited by 95
Myeloperoxidase Inhibitors as Potential Drugs
Pašti, T. D. L., Leskovac, A. R., & Vasić, V. (2015) · Current Drug Metabolism · doi:10.2174/138920021603150812120640 · Cited by 95
Superoxide is an antagonist of anti-inflammatory drugs that inhibit hypochlorous acid production by myeloperoxidase
Kettle, A. J., Gedye, C. A., & Winterbourn, C. C. (1993) · Biochemical Pharmacology · doi:10.1016/0006-2952(93)90010-t · Cited by 94
A Kinetic Analysis of the Catalase Activity of Myeloperoxidase
Kettle, A. J., & Winterbourn, C. C. (2001) · Biochemistry · doi:10.1021/bi010940b · Cited by 94
MPO (Myeloperoxidase) Reduces Endothelial Glycocalyx Thickness Dependent on Its Cationic Charge
Manchanda, K., Kolářová, H., Kerkenpaß, C., Mollenhauer, M., Víteček, J., Rudolph, V., Kubala, L., Baldus, S. E., Adam, M., & Klinke, A. (2018) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.118.311143 · Cited by 94
Identifying peroxidases and their oxidants in the early pathology of cystic fibrosis
Thomson, E., Brennan, S., Senthilmohan, R., Gangell, C. L., Chapman, A., Sly, P. D., & Kettle, A. J. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.07.010 · Cited by 93
Oxidative Modification and Nitration of Human Low-Density Lipoproteins by the Reaction of Hypochlorous Acid with Nitrite
Panasenko, O. M., Briviba, K., Klotz, L., & Sies, H. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0171 · Cited by 93
Dose-dependent transitions in Nrf2-mediated adaptive response and related stress responses to hypochlorous acid in mouse macrophages
Woods, C. G., Fu, J., Xue, P., Hou, Y., Pluta, L., Yang, L., Zhang, Q., Thomas, R. S., Andersen, M. E., & Pi, J. (2009) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.04.007 · Cited by 92
Hypothiocyanous Acid: Benign or Deadly?
Barrett, T. J., & Hawkins, C. L. (2011) · Chemical Research in Toxicology · doi:10.1021/tx200219s · Cited by 91
Self-citation
Myeloperoxidase and Neurological Disorder: A Crosstalk
Pravalika, K., Sarmah, D., Kaur, H., Wanve, M., Saraf, J., Kalia, K., Borah, A., Yavagal, D. R., Dave, K. R., & Bhattacharya, P. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00462 · Cited by 91
Hypochlorous Acid Stimulation of the Mitogen-Activated Protein Kinase Pathway Enhances Cell Survival
Midwinter, R. G., Vissers, M. C. M., & Winterbourn, C. C. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2530 · Cited by 90
The Role of Neutrophil Myeloperoxidase in Models of Lung Tumor Development
Rymaszewski, A. L., Tate, E. R., Yimbesalu, J., Gelman, A. E., Jarzembowski, J. A., Zhang, H., Pritchard, K. A., & Vikis, H. G. (2014) · Cancers · doi:10.3390/cancers6021111 · Cited by 89
The Myeloperoxidase-Derived Oxidant HOSCN Inhibits Protein Tyrosine Phosphatases and Modulates Cell Signalling via the Mitogen-Activated Protein Kinase (MAPK) Pathway in Macrophages
Lane, A. E., Tan, J. T. M., Hawkins, C. L., Heather, A. K., & Davies, M. J. (2010) · Biochemical Journal · doi:10.1042/bj20100082 · Cited by 86
Self-citation
Production of glutathione sulfonamide and dehydroglutathione from GSH by myeloperoxidase-derived oxidants and detection using a novel LC–MS/MS method
Harwood, D. T., Kettle, A. J., & Winterbourn, C. C. (2006) · Biochemical Journal · doi:10.1042/bj20060978 · Cited by 85
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
Hypochlorous Acid Impairs Endothelium-Derived Nitric Oxide Bioactivity Through a Superoxide-Dependent Mechanism
Stocker, R., Huang, A., Jeranian, E., Hou, J. Y., Wu, T. T., Thomas, S. R., & Keaney, J. F. (2004) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000143388.20994.fa · Cited by 84
Myeloperoxidase Propagates Damage and is a Potential Therapeutic Target for Subacute Stroke
Forghani, R., Kim, H. J., Wojtkiewicz, G. R., Buré, L., Wu, Y., Hayase, M., Wei, Y., Zheng, Y. Z., Moskowitz, M. A., & Chen, J. W. (2014) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2014.222 · Cited by 83
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 83
Inhibition of myeloperoxidase-mediated hypochlorous acid production by nitroxides
Rees, M. D., Bottle, S. E., Fairfull‐Smith, K. E., Malle, E., Whitelock, J. M., & Davies, M. J. (2009) · Biochemical Journal · doi:10.1042/bj20090309 · Cited by 83
Self-citation
Myeloperoxidase-derived Reactive Chlorinating Species from Human Monocytes Target Plasmalogens in Low Density Lipoprotein
Thukkani, A. K., Albert, C. J., Wildsmith, K. R., Messner, M. C., Martinson, B. D., Hsu, F., & Ford, D. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305449200 · Cited by 81
Selenium-containing amino acids are targets for myeloperoxidase-derived hypothiocyanous acid: determination of absolute rate constants and implications for biological damage
Skaff, O., Pattison, D. I., Morgan, P. E., Bachana, R., Jain, V. K., Priyadarsini, K. I., & Davies, M. J. (2011) · Biochemical Journal · doi:10.1042/bj20101762 · Cited by 79
Self-citation
Hypothiocyanous acid is a more potent inducer of apoptosis and protein thiol depletion in murine macrophage cells than hypochlorous acid or hypobromous acid
Lloyd, M. M., van Reyk, D. M., Davies, M. J., & Hawkins, C. L. (2008) · Biochemical Journal · doi:10.1042/bj20080468 · Cited by 79
Self-citation
Inhibition of myeloperoxidase at the peak of experimental autoimmune encephalomyelitis restores blood–brain barrier integrity and ameliorates disease severity
Zhang, H., Ray, A., Miller, N. M., Hartwig, D., Pritchard, K. A., & Dittel, B. N. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13426 · Cited by 79
Intrinsic mutagenic properties of 5-chlorocytosine: A mechanistic connection between chronic inflammation and cancer
Fedeles, B. I., Freudenthal, B., Yau, E., Singh, V., Chang, S.-C., Li, D., Delaney, J. C., Wilson, S. H., & Essigmann, J. M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1507709112 · Cited by 79
Correlation between intima-to-media ratio, apolipoprotein B-100, myeloperoxidase, and hypochlorite-oxidized proteins in human atherosclerosis
Hazell, L., Baernthaler, G., & Stocker, R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00717-1 · Cited by 78
Pathways for oxidation of low density lipoprotein by myeloperoxidase: tyrosyl radical, reactive aldehydes, hypochlorous acid and molecular chlorine
Heinecke, J. W. (1997) · BioFactors · doi:10.1002/biof.5520060208 · Cited by 78
Hypochlorous acid inhibits Ca2+-ATPase from skeletal muscle sarcoplasmic reticulum
Favero, T. G., Colter, D. C., Hooper, P. F., & Abramson, J. J. (1998) · Journal of Applied Physiology · doi:10.1152/jappl.1998.84.2.425 · Cited by 78
Activation of Nrf2-mediated oxidative stress response in macrophages by hypochlorous acid
Pi, J., Zhang, Q., Woods, C. G., Wong, V. A., Collins, S., & Andersen, M. E. (2007) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2007.09.016 · Cited by 77
Substrates and products of eosinophil peroxidase
van DALEN, C. J., & Kettle, A. J. (2001) · Biochemical Journal · doi:10.1042/bj3580233 · Cited by 77
High plasma thiocyanate levels in smokers are a key determinant of thiol oxidation induced by myeloperoxidase
Morgan, P. E., Pattison, D. I., Talib, J., Summers, F. A., Harmer, J. A., Celermajer, D. S., Hawkins, C. L., & Davies, M. J. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.08.008 · Cited by 76
Self-citation
Increased Myeloperoxidase Plasma Levels in Patients with Alzheimer's Disease
Tzikas, S., Schlak, D., Sopova, K., Gatsiou, A., Stakos, D., Stamatelopoulos, K. S., Stellos, K., & Laske, C. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131469 · Cited by 75
The action of hypochlorous acid on phosphatidylcholine liposomes in dependence on the content of double bonds. Stoichiometry and NMR analysis
Arnhold, J., Panasenko, O. M., Schiller, J., IuA, V., & Arnold, K. (1995) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(95)02484-z · Cited by 75
Myeloperoxidase-mediated lipoprotein carbamylation as a mechanistic pathway for atherosclerotic vascular disease
Sirpal, S. (2009) · Clinical Science · doi:10.1042/cs20080322 · Cited by 74
Oxidation contributes to low glutathione in the airways of children with cystic fibrosis
Kettle, A. J., Turner, R., Gangell, C. L., Harwood, D. T., Khalilova, I. S., Chapman, A., Winterbourn, C. C., & Sly, P. D. (2014) · European Respiratory Journal · doi:10.1183/09031936.00170213 · Cited by 74
Impact of myeloperoxidase-LDL interactions on enzyme activity and subsequent posttranslational oxidative modifications of apoB-100
Delporte, C., Boudjeltia, K. Z., Noyon, C., Furtmüller, P. G., Nuyens, V., Slomianny, M., Madhoun, P., Desmet, J.-M., Raynal, P., Dufour, D., et al. (2014) · Journal of Lipid Research · doi:10.1194/jlr.m047449 · Cited by 74
The pro-inflammatory oxidant hypochlorous acid induces Bax-dependent mitochondrial permeabilisation and cell death through AIF-/EndoG-dependent pathways
Whiteman, M., Chu, S. H., Siau, J. L., Rose, P. E., Sabapathy, K., Schantz, J., Cheung, N. S., Spencer, J. P. E., & Armstrong, J. S. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.08.019 · Cited by 72
Hypertonic saline increases lung epithelial lining fluid glutathione and thiocyanate: two protective CFTR-dependent thiols against oxidative injury
Gould, N. S., Gauthier, S., Kariya, C. T., Min, E., Huang, J., & Day, B. J. (2010) · Respiratory Research · doi:10.1186/1465-9921-11-119 · Cited by 72
Role of hypochlorous acid (HOCl) and other inflammatory mediators in the induction of macrophage extracellular trap formation
Rayner, B. S., Zhang, Y., Brown, B. E., Reyes, L., Cogger, V. C., & Hawkins, C. L. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.001 · Cited by 72
Self-citation
Class B Scavenger Receptors CD36 and SR-BI Are Receptors for Hypochlorite-modified Low Density Lipoprotein
Marsche, G., Zimmermann, R., Horiuchi, S., Tandon, N. N., Sattler, W., & Malle, E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308428200 · Cited by 71
The Vinyl Ether Linkages of Plasmalogens Are Favored Targets for Myeloperoxidase-Derived Oxidants: A Kinetic Study
Skaff, O., Pattison, D. I., & Davies, M. J. (2008) · Biochemistry · doi:10.1021/bi800786q · Cited by 71
Self-citation
Myeloperoxidase aggravates pulmonary arterial hypertension by activation of vascular Rho-kinase
Klinke, A., Berghausen, E. M., Friedrichs, K. P., Molz, S., Lau, D., Remane, L., Berlin, M., Kaltwasser, C., Adam, M., Mehrkens, D., et al. (2018) · JCI Insight · doi:10.1172/jci.insight.97530 · Cited by 71
Association of myeloperoxidase with heparin: Oxidative inactivation of proteins on the surface of endothelial cells by the bound enzyme
Daphna, E.-M., Sharabani, M., Eynat, P., Aviram, I., & Sara, R. (1998) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006848730927 · Cited by 70
Regulation of Apoptosis by Vitamin C
Vissers, M. C. M., Lee, W.-G., & Hampton, M. B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107664200 · Cited by 70

Flagged first, then by citations

Research works printed but not linked: 9

Cojocaru IM, , Cojocaru M, , Iliescu I, , Botnaru L, , Gurban CV, , Sfrijan F, , and Tanasescu R. Plasma myeloperoxidase levels in patients with acute ischemic stroke. Rom J Intern Med, 48: 101–104, 2010.
10.1021/bi052339 · DOI
10.1182/blood.V92.9.3007 · DOI
Hawkins CL, , Pattison DI, , Whiteman M, , and Davies MJ. Chlorination and nitration of DNA and nucleic acid components. In: Oxidative Damage to DNA, edited by Evans MD and Cooke MS. Austin, TX: Landes Bioscience and Springer Science, 2006, pp. 14–39.
Panasenko OM, , Arnhold J, , and Schiller J. Hypochlorite reacts with organic hydroperoxides forming free radicals, but not singlet oxygen, and thus initiates lipid peroxidation. Biochemistry (Mosc), 62: 951–959, 1997.
Pullar JM, , Winterbourn CC, , and Vissers MCM. Loss of GSH and thiol enzymes in endothelial cells exposed to sublethal concentrations of hypochlorous acid. Am J Physiol, 277: H1505–H1512, 1999.
Tay A, , Tamam Y, , Yokus B, , Ustundag M, , and Orak M. Serum myeloperoxidase levels in predicting the severity of stroke and mortality in acute ischemic stroke patients. Eur Rev Med Pharmacol Sci, 19: 1983–1988, 2015.
Zhang C, , Patel R, , Eiserich JP, , Zhou F, , Kelpke S, , Ma W, , Parks DA, , Darley Usmar V, , and White CR. Endothelial dysfunction is induced by proinflammatory oxidant HOCl. Am J Physiol, 281: H1469–H1475, 2001.
10.1172/JCI200421109 · DOI

Sorted by citations

Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging
Jomova, K., Raptova, R., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03562-9 · Cited by 2,638
Oxidative Stress: Concept and Some Practical Aspects
Sies, H. (2020) · Antioxidants · doi:10.3390/antiox9090852 · Cited by 652
Oxidative Stress and Inflammation in Acute and Chronic Lung Injuries
Bezerra, F. S., Lanzetti, M., Nesi, R. T., Nagato, A. C., Silva, C. P. E., Kennedy-Feitosa, E., Melo, A. C., Cattani‐Cavalieri, I., Pôrto, L. C., & Valença, S. S. (2023) · Antioxidants · doi:10.3390/antiox12030548 · Cited by 373
Overview of the Mechanisms of Oxidative Stress: Impact in Inflammation of the Airway Diseases
Albano, G. D., Gagliardo, R. P., Montalbano, A. M., & Profita, M. (2022) · Antioxidants · doi:10.3390/antiox11112237 · Cited by 284
The Roles of Neutrophil-Derived Myeloperoxidase (MPO) in Diseases: The New Progress
Lin, W. C., Chen, H., Chen, X., & Guo, C. (2024) · Antioxidants · doi:10.3390/antiox13010132 · Cited by 290

See all 333

Authors: Davies, M. J., & Hawkins, C. L.
Affiliations: University of Copenhagen (DK)
Corresponding author: Hawkins, Clare L.
ORCID: Davies, Michael J.
Hawkins, Clare L.
Venue: Antioxidants & Redox Signaling
Publisher: SAGE Publications
Published: 2020-03-24
Volume: 32
Issue: 13
Pages: 957-981
ISSN: 1523-0864 (ISSN-L)
1557-7716
DOI: 10.1089/ars.2020.8030
OpenAlex: W3003715287
Cited by: 332
References: 306
Citations by year: 2026: 46 · 2025: 56 · 2024: 61 · 2023: 64 · 2022: 54 · 2021: 33 · 2020: 17
FWCI: 4.13
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: journals.sagepub.com/page/policies/text-and-data-mining-license (tdm)
Locations: Antioxidants and Redox Signaling (publishedVersion)
PubMed (publishedVersion)
Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
Funders: Novo Nordisk Fonden (NNF17OC0028990, NNF13OC0004294)
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 › Physiology (medical) › Nitric Oxide and Endothelin Effects
Keywords: myeloperoxidase, hypochlorous acid, biomolecule modification, chronic inflammation, innate immunity, MPO inhibitors, atherosclerosis, neurodegenerative diseases, lung disease, arthritis, cancer, kidney disease, host tissue damage, bacterial killing
MeSH terms: Animals, Arthritis, Enzyme Inhibitors, Humans, Hypochlorous Acid, Inflammation, Kidney Diseases, Lung Diseases, Peroxidase, Neoplasms, Neurodegenerative Diseases, Atherosclerosis

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

The Role of Myeloperoxidase in Biomolecule Modification, Chronic Inflammation, and Disease

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks