The DOI matches its Crossref record; 229 of the 229 references it cites were found in a registry or an index.
Myeloperoxidase-derived oxidation: mechanisms of biological damage and its prevention
Open accessAbstract
There is considerable interest in the role that mammalian heme peroxidase enzymes, primarily myeloperoxidase, eosinophil peroxidase and lactoperoxidase, may play in a wide range of human pathologies. This has been sparked by rapid developments in our understanding of the basic biochemistry of these enzymes, a greater understanding of the basic chemistry and biochemistry of the oxidants formed by these species, the development of biomarkers that can be used damage induced by these oxidants in vivo, and the recent identification of a number of compounds that show promise as inhibitors of these enzymes. Such compounds offer the possibility of modulating damage in a number of human pathologies. This reviews recent developments in our understanding of the biochemistry of myeloperoxidase, the oxidants that this enzyme generates, and the use of inhibitors to inhibit such damage.
Overview
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
Cites
Statistics
Verification
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?
In the citing paper
“The reaction catalyzed by MPO is the oxidation of the Cl− anion by H2O2 to give hypochlorous acid HOCl, a very reactive and oxidizing agent, which can also act as a chlorinating agent and is the main strong oxidant generated by neutrophils in appreciable quantities [30].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [30]
In the citing paper
“The reaction catalyzed by MPO is the oxidation of the Cl− anion by H2O2 to give hypochlorous acid HOCl, a very reactive and oxidizing agent, which can also act as a chlorinating agent and is the main strong oxidant generated by neutrophils in appreciable quantities [30].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [30]
In the citing paper
“Hypochlorous acid HOCl and hypothiocyanous acid HOSCN synthesized through the enzyme myeloperoxidase MPO, which catalyzes the reaction between H2O2 and Cl− or SCN−, are important inorganic bactericidal molecules, effective against a wide range of microbes.”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [30]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Superoxide radical and superoxide dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455
Dietary phenolics: chemistry, bioavailability and effects on health
Crozier, A., Jaganath, I. B., & Clifford, M. N. (2009) · Natural Product Reports · doi:10.1039/b802662a · Cited by 2,062
Nitric oxide, oxidants, and protein tyrosine nitration
Radí, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307446101 · Cited by 1,477
The oxidative environment and protein damage
Davies, M. J. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.08.007 · Cited by 1,392
Self-citationDaugherty, A., Dunn, J. L., Rateri, D. L., & Heinecke, J. W. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117342 · Cited by 1,269
Phagocytes and oxidative stress
Babior, B. M. (2000) · The American Journal of Medicine · doi:10.1016/s0002-9343(00)00481-2 · Cited by 1,061
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
Myeloperoxidase-Halide-Hydrogen Peroxide Antibacterial System
Klebanoff, S. J. (1968) · Journal of Bacteriology · doi:10.1128/jb.95.6.2131-2138.1968 · Cited by 820
Pattison, D. I., & Davies, M. J. (2001) · Chemical Research in Toxicology · doi:10.1021/tx0155451 · Cited by 790
Self-citationZheng, 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
Research works printed but not linked: 2
- 174 <citation><person-group person-group-type = "editor"><name><surname>Lentner</surname><given-names>C</given-names></name></person-group><source>Geigy Scientific Tables vol. 3: Physical Chemistry, Composition of Blood, Hematology, Somatometric Data</source>Basle, Ciba-Geigy Ltd, <year>1984</year></citation>
- 226 Kettle AJ, Gedye CA, Winterbourn CC. Mechanism of inactivation of myeloperoxidase by 4-aminobenzoic acid hydrazide. Biochem J 1997; 321: 503-508. · DOI
Cited by
Sorted by citations
Items 101–200 of 416
Inghardt, T., Antonsson, T., Ericsson, C., Hovdal, D., Johannesson, P., Johansson, C. A., Jurva, U., Kajanus, J., Kull, B., Michaëlsson, E., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c02141 · Cited by 46
Dexamethasone antagonizes the in vivo myotoxic and inflammatory effects of Bothrops venoms
Patrão-Neto, F. C., Tomaz, M. A., Strauch, M. A., Monteiro‐Machado, M., Rocha-Junior, J. R. D. S., Borges, P. A., Calil-Eliás, S., & Melo, P. A. (2013) · Toxicon · doi:10.1016/j.toxicon.2013.01.023 · Cited by 45
Duan, Q., Zheng, G., Li, Z., Cheng, K., Zhang, J., Yang, L., Jiang, Y., Zhang, H., He, J., & Sun, H. (2019) · Journal of Materials Chemistry B · doi:10.1039/c9tb01279f · Cited by 44
Microbial‐derived indoles inhibit neutrophil myeloperoxidase to diminish bystander tissue damage
Alexeev, E. E., Dowdell, A. S., Henen, M. A., Lanis, J. M., Lee, J. S., Cartwright, I. M., Schaefer, R. E. M., Ornelas, A., Onyiah, J. C., Vögeli, B., et al. (2021) · The FASEB Journal · doi:10.1096/fj.202100027r · Cited by 47
Ibáñez, B., Melero, A., Montoro, A., Onofre, N. S., & Soriano, J. M. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46110755 · Cited by 49
Flemmig, J., Zschaler, J., Remmler, J., & Arnhold, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.364299 · Cited by 43
Critical role for complement receptor C5aR2 in the pathogenesis of renal ischemia‐reperfusion injury
Poppelaars, F., van Werkhoven, M. B., Kotimaa, J. P., Veldhuis, Z. J., Ausema, A., Broeren, S. G. M., Damman, J. J., Hempel, J. C., Leuvenink, H. G. D., Daha, M. R., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201601218r · Cited by 43
Suzuki, T., Tanaka, R., Tahara, M., 勇有弥, NIINAE, M., Lin, L., Wang, J., Luh, J., & Coronell, O. (2016) · Water Research · doi:10.1016/j.watres.2016.04.068 · Cited by 43
Francesko, A., Rocasalbas, G., Touriño, S., Mattu, C., Gentile, P., Chiono, V., Ciardelli, G., & Tzanov, T. (2011) · Biotechnology Journal · doi:10.1002/biot.201100194 · Cited by 42
Gan, L., Fermer, M. L., Ericsson, H., Nelander, K., Lindstedt, E., Michaëlsson, E., Kjaer, M., Heijer, M., Whatling, C. A., & Fuhr, R. (2019) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.13855 · Cited by 42
Gamon, L. F., Guo, C., He, J., Hägglund, P., Hawkins, C. L., & Davies, M. J. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101586 · Cited by 42
Self-citationPatterson, E. K., Fraser, D. D., Capretta, A. A., Potter, R. F., & Cepinskas, G. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.02.020 · Cited by 41
Osburn, S., Berden, G., Oomens, J., O’Hair, R. A. J., & Ryzhov, V. (2011) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-011-0198-5 · Cited by 41
Flavonoids as promoters of the (pseudo-)halogenating activity of lactoperoxidase and myeloperoxidase
Gau, J., Furtmüller, P. G., Obinger, C., Prévost, M., Antwerpen, P. V., Arnhold, J., & Flemmig, J. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.06.026 · Cited by 41
The science of licking your wounds: Function of oxidants in the innate immune system
Day, B. J. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.03.013 · Cited by 39
Formation of Oxidatively Modified Lipids as the Basis for a Cellular Epilipidome
Spickett, C. M. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.602771 · Cited by 41
Soni, D., Duvva, N., Badgurjar, D., Roy, T. K., Nimesh, S., Arya, G., Giribabu, L., & Chitta, R. K. (2018) · Chemistry - An Asian Journal · doi:10.1002/asia.201800349 · Cited by 38
Andrés, C. M. C., de la Lastra, J. M. P., Andrés, C., Plou, F. J., & Pérez‐Lebeña, E. (2023) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23455 · Cited by 44
Kajer, T., Fairfull‐Smith, K. E., Yamasaki, T., Yamada, K., Fu, S., Bottle, S. E., Hawkins, C. L., & Davies, M. J. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.02.011 · Cited by 38
Self-citationPaiva, D. C. C., dos Santos, C. A., Diniz, J. C., Viana, F. A., Thomazzi, S. M., & Falcão, D. A. (2013) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2013.06.012 · Cited by 37
Moldogazieva, N. T., Mokhosoev, I. M., Melnikova, T. I., Zavadskiy, S. P., Kuzmenko, A. N., & Terentiev, A. A. (2020) · Biochemistry (Moscow) · doi:10.1134/s0006297920140047 · Cited by 35
Zhao, H., Yang, L., Chen, X., Sheng, M., Cao, G., Cai, L., Meng, S., & Tang, C. Y. (2021) · Environmental Science & Technology · doi:10.1021/acs.est.1c00206 · Cited by 34
Pinz, M. P., Medeiros, I., Carvalho, L. A. D. C., & Meotti, F. C. (2025) · Redox Report · doi:10.1080/13510002.2025.2498105 · Cited by 38
N-chlorination mediates protective and immunomodulatory effects of oxidized human plasma proteins
Ulfig, A., Schulz, A. V., Müller, A., Lupilov, N., & Leichert, L. I. O. (2019) · eLife · doi:10.7554/elife.47395 · Cited by 30
Mitochondria-targeted fluorescent probes for oxidative stress imaging
Niu, H., Chen, K., Xu, J., Zhu, X., Cao, W., Wang, Z., Ye, Y., & Zhao, Y. (2019) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2019.126938 · Cited by 34
Tùng, Q. N., Busche, T., Loi, V. V., Kalinowski, J., & Antelmann, H. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.12.032 · Cited by 34
Imaging of innate immunity activation in vivo with a redox-tuned PET reporter
Pisaneschi, F., Gammon, S. T., Paolillo, V., Qureshy, S. A., & Piwnica-Worms, D. R. (2022) · Nature Biotechnology · doi:10.1038/s41587-021-01169-y · Cited by 34
Xie, Y., Xu, W., Jin, Z., & Zhao, K. (2023) · Materials Today Bio · doi:10.1016/j.mtbio.2023.100617 · Cited by 33
Neutrophils and Neutrophil-Based Drug Delivery Systems in Anti-Cancer Therapy
Wahnou, H., El Kebbaj, R., Hba, S., Ouadghiri, Z., El Faqer, O., Pinon, A., Liagre, B., Limami, Y., & Duval, R. E. (2025) · Cancers · doi:10.3390/cancers17071232 · Cited by 35
Hillion, M., Imber, M., Pedre, B., Bernhardt, J., Saleh, M., Loi, V. V., Maaß, S., Becher, D., Rosado, L. A., Adrian, L., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-05206-2 · Cited by 33
Electrochemical Assays and Immunoassays of the Myeloperoxidase/SCN–/H2O2 System
Bekhit, M., & Górski, W. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.8b05855 · Cited by 33
Singlet‐Oxygen Generation by Peroxidases and Peroxygenases for Chemoenzymatic Synthesis
Ingenbosch, K. N., Quint, S., Dyllick‐Brenzinger, M., Wunschik, D. S., Kiebist, J., Süss, P., Liebelt, U., Zuhse, R., Menyes, U., Scheibner, K., et al. (2020) · ChemBioChem · doi:10.1002/cbic.202000326 · Cited by 33
Ulfig, A., Bader, V., Varatnitskaya, M., Lupilov, N., Winklhofer, K. F., & Leichert, L. I. O. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101981 · Cited by 34
Wang, C., & Qian, Y. (2019) · Journal of Luminescence · doi:10.1016/j.jlumin.2019.02.044 · Cited by 32
You, Y., Cheng, S., Zhang, L., Zhu, Y., Zhang, C., & Xian, Y. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b05468 · Cited by 32
Franck, T. J., Mouithys-Mickalad, A. A., Robert, T., Ghitti, G., Deby-Dupont, G. P., Neven, P., & Serteyn, D. A. (2013) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2013.09.009 · Cited by 32
Mancini, S., Mariani, F., Sena, P., Benincasa, M., & Roncucci, L. (2017) · Redox Report · doi:10.1080/13510002.2016.1277049 · Cited by 32
Bushueva, O. Y., Solodilova, M. A., Ivanov, V. P., & Polonikov, A. (2015) · Journal of the American Society of Hypertension · doi:10.1016/j.jash.2015.08.006 · Cited by 31
Mechanisms and consequences of acquired brain injury during development
Morrison, G. C., Fraser, D. D., & Cepinskas, G. (2012) · Pathophysiology · doi:10.1016/j.pathophys.2012.02.006 · Cited by 31
Delgado, A., Stewart, S. M., Urroz, M., Rodríguez, A., Borobia, A. M., Akatbach-Bousaid, I., González-Muñoz, M., & Ramı́rez, E. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10194432 · Cited by 31
Li, J., He, Y., Ke, H., Jin, Y., Jiang, Z., & Zhong, G. (2017) · Clinical Cardiology · doi:10.1002/clc.22633 · Cited by 31
Gandhi, K., Goda, J. S., Gandhi, V. V., Sadanpurwala, A., Jain, V. K., Joshi, K., Epari, S., Rane, S. U., Mohanty, B., Chaudhari, P. R., et al. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.09.009 · Cited by 31
Singh, E., Gupta, A., Singh, P., Jain, M., Muthukumaran, J., Singh, R. P., & Singh, A. K. (2024) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2024.110155 · Cited by 32
TNF-α Blockade Efficiently Reduced Severe Intestinal Damage in Necrotizing Enterocolitis
Tayman, C., Aydemir, S., Yakut, I., Serkant, U., Çiftçi, A., Arslan, E., & Koç, O. (2016) · Journal of Investigative Surgery · doi:10.3109/08941939.2015.1127449 · Cited by 30
Villamena, F. A. (2013) · Wiley eBooks · doi:10.1002/9781118355886.ch1 · Cited by 31
Abd‐Nikfarjam, B., Hajiali, F., Adineh, M., & Nassiri‐Asl, M. (2017) · Europe PMC (PubMed Central) · doi:10.3831/kpi.2017.20.017 · Cited by 29
Interaction kinetics of selenium-containing compounds with oxidants
Carroll, L., Gardiner, K. A., Ignasiak, M. T., Holmehave, J., Shimodaira, S., Breitenbach, T., Iwaoka, M., Ogilby, P. R., Pattison, D. I., & Davies, M. J. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.05.007 · Cited by 30
Self-citationMarsche, G., Stadler, J. T., Kargl, J., & Holzer, M. (2022) · Antioxidants · doi:10.3390/antiox11030556 · Cited by 30
Souza‐Neto, F. V., Islas, F., Jiménez‐González, S., Luaces, M., Ramchandani, B., Romero‐Miranda, A., Delgado‐Valero, B., Roldán, E. M., Saiz‐Pardo, M., Cerón-Nieto, M. Á., et al. (2022) · Antioxidants · doi:10.3390/antiox11071232 · Cited by 29
Ferreres, G., Pérez‐Rafael, S., Palacios, Ò., Todorova, K. S., Hinojosa-Caballero, D., Torrent‐Burgués, J., & Tzanov, T. (2024) · Chemical Engineering Journal · doi:10.1016/j.cej.2024.153064 · Cited by 28
Gas-phase reactivity of sulfur-based radical ions of cysteine derivatives and small peptides
Osburn, S., O’Hair, R. A. J., & Ryzhov, V. (2011) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2011.12.001 · Cited by 28
Coutinho, D. D. S., Pires, J., Gomes, H. D. S., Pohlmann, A. R., Guterres, S. S., Silva, P., Martins, M. A., Ferrarini, S. R., & Bernardi, A. (2020) · Pharmaceutics · doi:10.3390/pharmaceutics12111075 · Cited by 29
S-to-αC Radical Migration in the Radical Cations of Gly-Cys and Cys-Gly
Osburn, S., Berden, G., Oomens, J., O’Hair, R. A. J., & Ryzhov, V. (2012) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-012-0356-4 · Cited by 28
Misztal, T., Gołaszewska, A., Tomasiak, M. M., Iwanicka, M., Marcińczyk, N., Leszczynska, A., Chabielska, E., & Rusak, T. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.07.003 · Cited by 28
Wierdak, M., Surmiak, M., Milian-Ciesielska, K., Rubinkiewicz, M., Rzepa, A., Wysocki, M., Major, P., Kłęk, S., & Pędziwiatr, M. (2021) · Cancers · doi:10.3390/cancers13061444 · Cited by 27
Li, Z., Huang, S., He, Y., Duan, Q., Zheng, G., Jiang, Y., Cai, L., Jia, Y., Zhang, H., & Ho, D. L. (2020) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2020.118073 · Cited by 27
Cook, N. L., Pattison, D. I., & Davies, M. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.033 · Cited by 26
Self-citationWitaicenis, A., de Oliveira, E. C. S., Tanimoto, A., Zorzella-Pezavento, S. F. G., de Oliveira, S. L., Sartori, A., & Stasi, L. C. D. (2017) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2017.12.006 · Cited by 26
Li, M., Du, F., Xue, P., Tan, X., Liu, S., Zhou, Y., Chen, J., & Bai, L. (2019) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2019.117760 · Cited by 26
Huang, Z.-W., Liu, N., Li, D., Zhang, H.-Y., Wang, Y., Liu, Y., Zhang, L.-L., & Ju, X.-L. (2017) · Yonsei Medical Journal · doi:10.3349/ymj.2017.58.1.206 · Cited by 25
de Oliveira, M. T. P., Coutinho, D. D. S., Guterres, S. S., Pohlmann, A. R., Silva, P., Martins, M. A., & Bernardi, A. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13050683 · Cited by 25
Liu, X., Chang, R., Zhou, Z., Ren, Q., Shen, C., Lan, Y., Cao, X., & Mao, J. (2023) · Journal of Functional Foods · doi:10.1016/j.jff.2023.105722 · Cited by 25
HO-1 and CD39: It Takes Two to Protect the Realm
Lee, G. R., Shaefi, S., & Otterbein, L. E. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01765 · Cited by 24
Borek-Dorosz, A., Grosicki, M., Dybaś, J., Matuszyk, E., Rodewald, M., Meyer, T., Popp, J., Małek, K., & Barańśka, M. (2020) · Cells · doi:10.3390/cells9092041 · Cited by 24
Sultana, S., LeDoux, K., Crompton, M. E., Jankiewicz, O., Morales, G. H., Johnson, C., Horbach, E., Hoffmann, K. P., Kr, P., Shah, R., et al. (2022) · mBio · doi:10.1128/mbio.01926-22 · Cited by 25
Yang, T., An, K., Zhang, S., & Han, Y. (2023) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2023.122655 · Cited by 24
Chapple, I., Matthews, J. B., Wright, H. J., Scott, A. E., Griffiths, H. R., & Grant, M. M. (2012) · Innate Immunity · doi:10.1177/1753425912455207 · Cited by 24
ROS-induced lipid transformations without oxygen participation
Шадыро, О. И., & Lisouskaya, A. (2019) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2019.03.013 · Cited by 24
Ameliorative effect of gallic acid on doxorubicin-induced cardiac dysfunction in rats
Omóbòwálé, T. O., Oyagbemi, A. A., Folasire, A., Ajibade, T. O., Asenuga, E. R., Adejumobi, O. A., Ola‐Davies, O. E., Orotusin, O., James, G., Adedapo, A. A., et al. (2017) · Journal of Basic and Clinical Physiology and Pharmacology · doi:10.1515/jbcpp-2016-0194 · Cited by 23
Promutagenicity of 8-Chloroguanine, A Major Inflammation-Induced Halogenated DNA Lesion
Kou, Y., Koag, M., & Lee, S. (2019) · Molecules · doi:10.3390/molecules24193507 · Cited by 23
Baruah, M., Jana, A., Ali, M., Mapa, K., & Samanta, A. (2022) · Journal of Materials Chemistry B · doi:10.1039/d2tb00356b · Cited by 23
da Fonseca, L. J. S., Nunes-Souza, V., Guedes, G. D. S., Schettino-Silva, G., Gomes, M. A. M., & Rabelo, L. A. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/898501 · Cited by 23
Talib, J., Kwan, J., Rahmanto, A. S., Witting, P. K., & Davies, M. J. (2013) · Biochemical Journal · doi:10.1042/bj20131135 · Cited by 23
Self-citationNguyen, T. M., Mandiki, S. N. M., Gense, C., Tran, T. N. T., Nguyen, T. H., & Kestemont, P. (2019) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2019.103488 · Cited by 25
Singh, S., Ahmad, T., Sharma, J., & Chakrabarti, R. (2020) · Fish Physiology and Biochemistry · doi:10.1007/s10695-020-00896-4 · Cited by 22
Gan, Q., Chi, H., Dalmo, R. A., Meng, X., Tang, X., Xing, J., Sheng, X., & Zhan, W. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1124813 · Cited by 22
Hussain, R. M., Razak, Z. N. R. B. A., Saad, W. M. M., & Mustakim, M. (2017) · Asian Pacific Journal of Tropical Medicine · doi:10.1016/j.apjtm.2017.07.009 · Cited by 21
Mannino, M. H., Patel, R. S., Eccardt, A. M., Perez-Magnelli, R., Robinson, C. L. C., Janowiak, B. E., Warren, D. E., & Fisher, J. S. (2019) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2019.04.005 · Cited by 24
Liu, J., Chi, C., Zheng, X., Xu, C., Zhang, C., Ye, M.-W., & Liu, W. (2019) · Aquaculture Reports · doi:10.1016/j.aqrep.2019.100217 · Cited by 22
Ali, F. E. M., Hassanein, E. H. M., El‐Ghafar, O. A. M. A., Rashwan, E. K., Saleh, F. M., & Atwa, A. M. (2023) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23309 · Cited by 21
Salivary Alterations of Myeloperoxidase in Patients with Systemic Diseases: A Systematic Review
Nijakowski, K., Jankowski, J., Gruszczyński, D., & Surdacka, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512078 · Cited by 24
Aldib, I., Gelbcke, M., Soubhye, J., Prévost, M., Furtmüller, P. G., Obinger, C., Elfving, B., Alard, I. C., Roos, G., Delporte, C., et al. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.07.053 · Cited by 21
Hanifeh, M., Sankari, S., Rajamäki, M. M., Syrjä, P., Kilpinen, S., Suchodolski, J. S., Heilmann, R. M., Guadiano, P., Lidbury, J. A., Steiner, J. M., et al. (2018) · BMC Veterinary Research · doi:10.1186/s12917-018-1441-0 · Cited by 21
Niu, H., Duan, Y., Zhang, Y., Hua, X., Xu, C. S., Li, Z., Ma, J., Qin, F., Zhai, Y., Ye, Y., et al. (2022) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2022.112441 · Cited by 21
Akduman, H., Tayman, C., Korkmaz, V., Akduman, F., Fettah, N. D., Kaya, B., Türkmenoğlu, T. T., & Çağlayan, M. (2021) · American Journal of Perinatology · doi:10.1055/s-0041-1727156 · Cited by 20
Clemen, R., Dethloff, W., Berner, J., Schulan, P., Martinet, A., Weltmann, K. D., von Woedtke, T., Grune, T., Wende, K., & Bekeschus, S. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103372 · Cited by 20
Disruption of heme-peptide covalent cross-linking in mammalian peroxidases by hypochlorous acid
Abu‐Soud, H. M., Maitra, D., Shaeib, F., Khan, S., Byun, J., Abdulhamid, I. B., Yang, Z., Saed, G. M., Diamond, M. P., Andreana, P. R., et al. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.06.018 · Cited by 20
Chlorinated Flavonoids Modulate the Inflammatory Process in Human Blood
Proença, C., Ribeiro, D., Soares, T., Tomé, S. M., Silva, A. M. S., Lima, J. L. F. C., Fernandes, E. G. R., & Freitas, M. (2017) · Inflammation · doi:10.1007/s10753-017-0559-8 · Cited by 20
Wang, H., Zhou, L., Yang, M. G., Luo, X., Li, Y., & Dan, X. (2017) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2017.10.063 · Cited by 20
Iodide modulates protein damage induced by the inflammation-associated heme enzyme myeloperoxidase
Gamon, L. F., Dieterich, S., Ignasiak, M. T., Schrameyer, V., & Davies, M. J. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101331 · Cited by 20
Self-citationLuo, Y., Pang, X.-X., Ansari, A. R., Wu, X., Li, H., Zhang, Z.-W., & Song, H. (2019) · Inflammation · doi:10.1007/s10753-019-01100-3 · Cited by 20
Yanamala, N., Kapralov, A. A., Djukic, M., Peterson, J., Mao, G., Klein-Seetharaman, J., Stoyanovsky, D. A., Stursa, J., Neuzil, J., & Kagan, V. E. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.601377 · Cited by 19
Osburn, S., Burgie, T., Berden, G., Oomens, J., O’Hair, R. A. J., & Ryzhov, V. (2012) · The Journal of Physical Chemistry A · doi:10.1021/jp304769y · Cited by 19
Mishra, O. P., Popov, A. V., Pietrofesa, R. A., Nakamaru‐Ogiso, E., Andrake, M., & Christofidou‐Solomidou, M. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.03.003 · Cited by 19
Some of the effective factors in the pathogenesis of gastro‐oesophageal reflux disease
Pish‐Kenari, F. N., Qujeq, D., & Maghsoudi, H. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13939 · Cited by 20
Skoie, I. M., Dalen, I., Omdal, R., & Jonsson, G. (2019) · Archives of Dermatological Research · doi:10.1007/s00403-019-01903-2 · Cited by 19
Villamena, F. A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-420017-3.00005-0 · Cited by 19
Oxidized Proteins Differentially Affect Maturation and Activation of Human Monocyte-Derived Cells
Clemen, R., Arlt, K., Miebach, L., von Woedtke, T., & Bekeschus, S. (2022) · Cells · doi:10.3390/cells11223659 · Cited by 18
Expression of RcrB confers resistance to hypochlorous acid in uropathogenic Escherichia coli
Crompton, M. E., Gaessler, L. F., Tawiah, P. O., Polzer, L. K., Camfield, S. K., Jacobson, G. D., Naudszus, M. K., Johnson, C., Meurer, K., Bennis, M., et al. (2023) · Journal of Bacteriology · doi:10.1128/jb.00064-23 · Cited by 19
Yang, B., Qu, W., Lu, J., Wu, Z., Li, Y., Yao, R., Wang, J., Li, Y., Lü, Z., Geng, Z., et al. (2025) · Analytica Chimica Acta · doi:10.1016/j.aca.2025.344140 · Cited by 18
Metadata
- Authors
- Davies, M. J.
- Affiliations
- The University of Sydney (AU)
- Corresponding author
- Davies, Michael J.
- ORCID
- Davies, Michael J.
- Venue
- Journal of Clinical Biochemistry and Nutrition
- Published
- 2010
- Volume
- 48
- Issue
- 1
- Pages
- 8-19
- ISSN
- 0912-0009 (ISSN-L)
- 1880-5086
- PMC
- PMC3022070
- OpenAlex
- W2028031080
- Cited by
- 412
- References
- 227
- Citations by year
- 2026: 18 · 2025: 15 · 2024: 31 · 2023: 30 · 2022: 34 · 2021: 40 · 2020: 41 · 2019: 37 · 2018: 27 · 2017: 29 · 2016: 23 · 2015: 21 · 2014: 19 · 2013: 16 · 2012: 24
- FWCI
- 6.45
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Biochemistry and Nutrition (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Fondation pour la Recherche Médicale
- Medical Research Council
- Australian Research Council (CE0561607, DP0988311)
- National Health and Medical Research Council (570829)
- 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 (medical) › Antioxidant Activity and Oxidative Stress
- Keywords
- myeloperoxidase, heme peroxidase, eosinophil peroxidase, lactoperoxidase, oxidative damage, oxidative damage biomarkers, enzyme inhibitors
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