The DOI matches its Crossref record; 422 of the 422 references it cites were found in a registry or an index.
Mammalian Heme Peroxidases: From Molecular Mechanisms to Health Implications
Abstract
A marked increase in interest has occurred over the last few years in the role that mammalian heme peroxidase enzymes, primarily myeloperoxidase, eosinophil peroxidase, and lactoperoxidase, may play in both disease prevention and human pathologies. This increased interest has been sparked by developments in our understanding of polymorphisms that control the levels of these enzymes, a greater understanding of the basic chemistry and biochemistry of the oxidants formed by these species, the development of specific biomarkers that can be used in vivo to detect damage induced by these oxidants, the detection of active forms of these peroxidases at most, if not all, sites of inflammation, and a correlation between the levels of these enzymes and a number of major human pathologies. This article reviews recent developments in our understanding of the enzymology, chemistry, biochemistry and biologic roles of mammalian peroxidases and the oxidants that they generate, the potential role of these oxidants in human disease, and the use of the levels of these enzymes in disease prognosis.
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Cites
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Selkoe, D. J. (1991) · Neuron · doi:10.1016/0896-6273(91)90052-2 · Cited by 2,708
Myeloperoxidase: friend and foe
Klebanoff, S. J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.1204697 · Cited by 2,282
Segal, A. W. (2005) · Annual Review of Immunology · doi:10.1146/annurev.immunol.23.021704.115653 · Cited by 1,789
Inside the Neutrophil Phagosome: Oxidants, Myeloperoxidase, and Bacterial Killing
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Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils
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Nitric oxide, oxidants, and protein tyrosine nitration
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Cited by
The basics of thiols and cysteines in redox biology and chemistry
Poole, L. B. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.11.013 · Cited by 1,031
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-citationRedox 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
Detection, identification, and quantification of oxidative protein modifications
Hawkins, C. L., & Davies, M. J. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.006217 · Cited by 426
Self-citationMyeloperoxidase-derived oxidation: Mechanisms of biological damage and its prevention
Davies, M. J. (2010) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.11-006fr · Cited by 412
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Metadata
- Authors
- Davies, M. J., Hawkins, C. L., Pattison, D. I., & Rees, M. D.
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2008-07
- Volume
- 10
- Issue
- 7
- Pages
- 1199-1234
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W1971435128
- Cited by
- 560
- References
- 422
- FWCI
- 10.17
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
