The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Myeloperoxidase, a Leukocyte-Derived Vascular NO Oxidase
Abstract
Myeloperoxidase (MPO) is an abundant mammalian phagocyte hemoprotein thought to primarily mediate host defense reactions. Although its microbicidal functions are well established in vitro, humans deficient in MPO are not at unusual risk of infection. MPO was observed herein to modulate the vascular signaling and vasodilatory functions of nitric oxide (NO) during acute inflammation. After leukocyte degranulation, MPO localized in and around vascular endothelial cells in a rodent model of acute endotoxemia and impaired endothelium-dependent relaxant responses, to which MPO-deficient mice were resistant. Altered vascular responsiveness was due to catalytic consumption of NO by substrate radicals generated by MPO. Thus MPO can directly modulate vascular inflammatory responses by regulating NO bioavailability.
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.
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
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
Self-citationPrevention of lung reperfusion injury in rabbits by a monoclonal antibody against interleukin-8
Sekido, N., Mukaida, N., Harada, A., Nakanishi, I., Watanabe, Y., & Matsushima, K. (1993) · Nature · doi:10.1038/365654a0 · Cited by 514
Nitric Oxide Is a Physiological Substrate for Mammalian Peroxidases
Abu-Soud, H. M., & Hazen, S. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.48.37524 · Cited by 398
Baldus, S., Eiserich, J. P., Mani, A., Castro, L., Figueroa, M., Chumley, P., Ma, W., Tousson, A., White, C. R., Bullard, D. C., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci12617 · Cited by 333
Self-citationIncreased atherosclerosis in myeloperoxidase-deficient mice
Brennan, M.-L., Anderson, M. M., Shih, D. M., Qu, X.-D., Wang, X., Mehta, A. C., Lim, L. L., Shi, W., Hazen, S. L., Jacob, J. S., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci8797 · Cited by 323
Self-citationWinterbourn, C. C., Vissers, M. C., & Kettle, A. J. (2000) · Current Opinion in Hematology · doi:10.1097/00062752-200001000-00010 · Cited by 269
Heparin in Inflammation: Potential Therapeutic Applications beyond Anticoagulation
Tyrrell, D. J., Horne, A. P., Holme, K. R., Preuss, J. M. H., & Page, C. P. (1999) · Advances in Pharmacology · doi:10.1016/s1054-3589(08)60471-8 · Cited by 245
Kinetics of Oxidation of Tyrosine and Dityrosine by Myeloperoxidase Compounds I and II
Marquez, L. A., & Dunford, H. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.51.30434 · Cited by 236
Nitric Oxide Modulates the Catalytic Activity of Myeloperoxidase
Abu-Soud, H. M., & Hazen, S. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5425 · Cited by 195
Clinical manifestation of myeloperoxidase deficiency
Lanza, F. (1998) · Journal of Molecular Medicine · doi:10.1007/s001090050267 · Cited by 187
Nitric Oxide Reaction with Lipid Peroxyl Radicals Spares α-Tocopherol during Lipid Peroxidation
Rubbo, H., Radi, R., Anselmi, D., Kirk, M., Barnes, S., Butler, J., Eiserich, J. P., & Freeman, B. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.15.10812 · Cited by 182
Self-citationNitric oxide rapidly scavenges tyrosine and tryptophan radicals
Eiserich, J. P., Butler, J., van der Vliet, A., Cross, C. E., & Halliwell, B. B. (1995) · Biochemical Journal · doi:10.1042/bj3100745 · Cited by 150
Self-citationHeinecke, J. W. (1999) · Journal of Laboratory and Clinical Medicine · doi:10.1016/s0022-2143(99)90061-6 · Cited by 149
Hereditary myeloperoxidase deficiency due to a missense mutation of arginine 569 to tryptophan.
Nauseef, W. M., Brigham, S. C., & Cogley, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42244-7 · Cited by 87
Self-citationNeutrophil myeloperoxidase revisited: it's role in health and disease
Deby-Dupont, G. P., Deby, C. M. T., & Lamy, M. (1999) · Intensivmedizin und Notfallmedizin · doi:10.1007/s003900050270 · Cited by 84
Effect of the R569W Missense Mutation on the Biosynthesis of Myeloperoxidase
Nauseef, W. M., Cogley, M., & McCormick, S. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.16.9546 · Cited by 71
Self-citationANCA antigens, proteinase 3 and myeloperoxidase, are not expreΔed in endothelial cells
Pendergraft, W. F., Alcorta, D. A., Segelmark, M., Jia, Y., Tuttle, R., Jennette, J. C., Falk, R. J., & Preston, G. A. (2000) · Kidney International · doi:10.1046/j.1523-1755.2000.00048.x · Cited by 51
Oxidation of Clozapine and Ascorbate by Myeloperoxidase
Hsuanyu, Y., & Dunford, H. B. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1328 · Cited by 49
The Reaction Rates of NO with Horseradish Peroxidase Compounds I and II
Glover, R. E., Koshkin, V., Dunford, H. B., & Mason, R. P. (1999) · Nitric Oxide · doi:10.1006/niox.1999.0256 · Cited by 47
Nitric Oxide and Septic Vascular Dysfunction
Murray, P. T., Wylam, M. E., & Umans, J. G. (2000) · Anesthesia & Analgesia · doi:10.1097/00000539-200001000-00021 · Cited by 42
Pathophysiology of ischaemia-reperfusion injury
Carden, D. L., & Granger, D. N. (2000) · The Journal of Pathology · doi:10.1002/(sici)1096-9896(200002)190:3 · Cited by 5
Cited by
Role of Oxidative Modifications in Atherosclerosis
Stocker, R., & Keaney, J. F. (2004) · Physiological Reviews · doi:10.1152/physrev.00047.2003 · Cited by 2,624
Myeloperoxidase: friend and foe
Klebanoff, S. J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.1204697 · Cited by 2,282
Antimicrobial reactive oxygen and nitrogen species: concepts and controversies
Fang, F. C. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro1004 · Cited by 1,676
Oxidant signals and oxidative stress
Finkel, T. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00002-4 · Cited by 1,393
Prognostic Value of Myeloperoxidase in Patients with Chest Pain
Brennan, M.-L., Penn, M. S., Van Lente, F., 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 1,070
Self-citation
Metadata
- Authors
- Eiserich, J. P., Baldus, S., Brennan, M.-L., Ma, W., Zhang, C., Tousson, A., Castro, L., Lusis, A. J., Nauseef, W. M., White, C. R., & Freeman, B. A.
- Venue
- Science
- Published
- 2002-06-28
- Volume
- 296
- Issue
- 5577
- Pages
- 2391-2394
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2137623306
- Cited by
- 685
- References
- 21
- FWCI
- 13.33
- Type
- journal article
- Language
- en
- Open access
- closed
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
Data sources
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.