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
Items 201–229 of 229
8-Chloroadenine: a novel product formed from hypochlorous acid-induced damage to calf thymus DNA
WHITEMAN, A. J. M. (1999) · Biomarkers · doi:10.1080/135475099230831 · Cited by 40
Lactoperoxidase-catalyzed incorporation of thiocyanate ion into a protein substrate
Aune, T. M., Thomas, E. L., & Morrison, M. (1977) · Biochemistry · doi:10.1021/bi00640a013 · Cited by 39
Peroxynitrite efficiently mediates the interconversion of redox intermediates of myeloperoxidase
Furtmüller, P. G., Jantschko, W., Zederbauer, M., Schwanninger, M., Jakopitsch, C., Herold, S., Koppenol, W. H., & Obinger, C. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.09.138 · Cited by 39
Park, Y. S., Suzuki, K., Mumby, S. E., Taniguchi, N., & Gutteridge, J. M. C. (2000) · Free Radical Research · doi:10.1080/10715760000301421 · Cited by 39
Potential role of tryptophan and chloride in the inhibition of human myeloperoxidase
Galijašević, S., Abdulhamid, I. B., & Abu‐Soud, H. M. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.01.003 · Cited by 39
Jantschko, W., Furtmüller, P. G., Zederbauer, M., Lanz, M., Jakopitsch, C., & Obinger, C. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.10.117 · Cited by 38
Paracetamol Catalyzes Myeloperoxidase-Initiated Lipid Oxidation in LDL
Kapiotis, S., Sengoelge, G., Hermann, M., Held, I., Seelos, C., & Gmeiner, B. M. K. (1997) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.17.11.2855 · Cited by 38
Siraki, A. G., Bonini, M. G., Jiang, J., Ehrenshaft, M., & Mason, R. P. (2007) · Chemical Research in Toxicology · doi:10.1021/tx6003562 · Cited by 37
van Zyl, J. M., Basson, K., Uebel, R. A., & van der Walt, B. J. (1989) · Biochemical Pharmacology · doi:10.1016/0006-2952(89)90477-2 · Cited by 37
Green, S. P., Baker, M. S., & Lowther, D. A. (1990) · PubMed · Cited by 36
Current concepts of the actions of paracetamol (acetaminophen) and NSAIDs
Graham, G. G., Day, R. O., Milligan, M. K., Ziegler, J. B., & Kettle, A. J. (1999) · Inflammopharmacology · doi:10.1007/s10787-999-0008-x · Cited by 36
Analysis of the mechanism by which tryptophan analogs inhibit human myeloperoxidase
Sliskovic, I., Abdulhamid, I. B., Sharma, M., & Abu‐Soud, H. M. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.07.007 · Cited by 36
Carboxyhaemoglobin and plasma thiocyanate: complementary indicators of smoking behaviour?
Saloojee, Y., VESEY, C. J., Cole, P. V., & Russell, M. A. (1982) · Thorax · doi:10.1136/thx.37.7.521 · Cited by 35
A study of ligand binding to spleen myeloperoxidase
Ikeda‐Saito, M. (1987) · Biochemistry · doi:10.1021/bi00388a024 · Cited by 35
Myeloperoxidase Potentiates Nitric Oxide-mediated Nitrosation
Lakshmi, V. M., Nauseef, W. M., & Zenser, T. V. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411263200 · Cited by 35
Reactions of superoxide with the myoglobin tyrosyl radical
Das, A. B., Nagy, P., Abbott, H. F., Winterbourn, C. C., & Kettle, A. J. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.02.039 · Cited by 34
Horseradish Peroxidase Mutants That Autocatalytically Modify Their Prosthetic Heme Group
Colas, C., & de Montellano, P. R. O. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401687200 · Cited by 33
Chen, H. C., Row, S.-W., & Hong, C.-L. (2002) · Chemical Research in Toxicology · doi:10.1021/tx015578g · Cited by 33
Gould, J. (1984) · Water Research · doi:10.1016/0043-1354(84)90250-1 · Cited by 32
Myeloperoxidase Metabolizes Thiocyanate in a Reaction Driven by Nitric Oxide
Galijašević, S., Saed, G. M., Hazen, S. L., & Abu‐Soud, H. M. (2006) · Biochemistry · doi:10.1021/bi051438k · Cited by 30
Marquez‐Curtis, L. A., & Dunford, H. B. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1440 · Cited by 29
Neutrophil-mediated oxidation of enkephalins via myeloperoxidase-dependent addition of superoxide
Nagy, P., Kettle, A. J., & Winterbourn, C. C. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.05.033 · Cited by 24
Inhibition of hypochlorous acid-induced oxidative reactions by nitrite: is nitrite an antioxidant?
Whiteman, M., Rose, P. E., & Halliwell, B. B. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00503-5 · Cited by 23
Oxidative metabolism of amsacrine by the neutrophil enzyme myeloperoxidase
Kettle, A. J., Robertson, I. G. C., Palmer, B. D., Anderson, R. F., Patel, K. B., & Winterbourn, C. C. (1992) · Biochemical Pharmacology · doi:10.1016/0006-2952(92)90066-r · Cited by 22
Bouriche, H., Salavei, P., Leßig, J., & Arnhold, J. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2006.10.030 · Cited by 22
Aromatic hydroxylation during the myeloperoxidase-oxidase oxidation of hydrazines
van der Walt, B. J., van Zyl, J. M., & Kriegler, A. (1994) · Biochemical Pharmacology · doi:10.1016/0006-2952(94)90415-4 · Cited by 20
Burner, U., Krapfenbauer, G., Furtmüller, P. G., Regelsberger, G., & Obinger, C. (2000) · Redox Report · doi:10.1179/135100000101535735 · Cited by 17
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
Dusting, G. J., Tan, C., Jiang, F., Datla, S. R., Chan, E. C., Hickey, H. M., Sobey, C. G., & Drummond, G. R. (2006) · Acta Pharmacologica Sinica · Cited by 1
Flagged first, then by citations
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
Cavallo, G., Metrangolo, P., Milani, R., Pilati, T., Priimägi, A., Resnati, G., & Terraneo, G. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00484 · Cited by 4,124
Excited-state intramolecular proton-transfer (ESIPT) based fluorescence sensors and imaging agents
Sedgwick, A. C., Wu, L., Han, H., Bull, S. D., He, X., James, T. D., Sessler, J. L., Tang, B. Z., Tian, H., & Yoon, J. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00185e · Cited by 1,589
Cysteine-Mediated Redox Signaling: Chemistry, Biology, and Tools for Discovery
Paulsen, C. E., & Carroll, K. S. (2013) · Chemical Reviews · doi:10.1021/cr300163e · Cited by 1,313
The Neutrophil’s Role During Health and Disease
Liew, P. X., & Kubes, P. (2019) · Physiological Reviews · doi:10.1152/physrev.00012.2018 · Cited by 1,237
Graham, G. G., Davies, M. J., Day, R. O., Mohamudally, A., & Scott, K. F. (2013) · Inflammopharmacology · doi:10.1007/s10787-013-0172-x · Cited by 671
Self-citation
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
