The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
Salen−Manganese Complexes as Catalytic Scavengers of Hydrogen Peroxide and Cytoprotective Agents: Structure−Activity Relationship Studies
Abstract
Synthetic catalytic scavengers of reactive oxygen species (ROS) may have broad clinical applicability. In previous papers, two salen-manganese complexes, EUK-8 and EUK-134, had superoxide dismutase (SOD) and catalase activities and prevented ROS-associated tissue injury. This study describes two series of salen-manganese complexes, comparing catalytic ROS scavenging properties and cytoprotective activities. The compounds vary widely in ability to scavenge hydrogen peroxide, with this activity most influenced by salen ring alkoxy substitution and aromatic bridge modifications. In contrast, all compounds show comparable SOD activities. The most active alkoxy-substituted catalase mimetics protected cultured cells from hydrogen peroxide, and a subset of these were also neuroprotective in a rodent stroke model. Thus, structural modification of the prototype EUK-8 yields compounds with enhanced catalase activity and, in turn, biological effectiveness. This supports the concept that salen-manganese complexes represent a class of SOD and, in particular, catalase mimetics potentially useful against ROS-associated diseases.
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
Free radicals in biology and medicine
(1991) · General Pharmacology: The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827
Biochemistry of Oxidative Stress
Sies, H. (1986) · Angewandte Chemie International Edition in English · doi:10.1002/anie.198610581 · Cited by 1,306
Extension of Life-Span with Superoxide Dismutase/Catalase Mimetics
Melov, S., Ravenscroft, J., Malik, S., Gill, M. S., Walker, D. W., Clayton, P. E., Wallace, D. C., Malfroy, B., Doctrow, S. R., & Lithgow, G. J. (2000) · Science · doi:10.1126/science.289.5484.1567 · Cited by 912
Self-citationChilds, R. E., & Bardsley, W. G. (1975) · Biochemical Journal · doi:10.1042/bj1450093 · Cited by 893
Carboxyfullerenes as neuroprotective agents
Dugan, L. L., Turetsky, D. M., Du, C., Lobner, D., Wheeler, M., Almli, C. R., Shen, C. K.-F., Luh, T.-Y., Choi, D. W., & Lin, T.-S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.17.9434 · Cited by 748
Oxidases and Related Redox Systems
Milazzo, G. (1975) · Bioelectrochemistry and Bioenergetics · doi:10.1016/0302-4598(75)80018-3 · Cited by 673
Biomimetic Oxidations Catalyzed by Transition Metal Complexes
Meunier, B. (2000) · IMPERIAL COLLEGE PRESS eBooks · doi:10.1142/p084 · Cited by 642
Superoxide and superoxide dismutases
Fridovich, I. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90188-z · Cited by 526
A novel neurological phenotype in mice lacking mitochondrial manganese superoxide dismutase
Melov, S., Schneider, J. A., Day, B. J., Hinerfeld, D., Coskun, P., Mirra, S. S., Crapo, J. D., & Wallace, D. C. (1998) · Nature Genetics · doi:10.1038/ng0298-159 · Cited by 489
Simándi, L. I. (1999) · Reaction Kinetics and Catalysis Letters · doi:10.1007/bf02475531 · Cited by 486
Current status of antioxidant therapy
Rice-Evans, C. A., & Diplock, A. T. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90127-g · Cited by 428
Stable Mn(III) porphyrins mimic superoxide dismutase in vitro and substitute for it in vivo.
Faulkner, K. M., Liochev, S. I., & Fridovich, I. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31540-5 · Cited by 402
Anaerobic Microbes: Oxygen Detoxification Without Superoxide Dismutase
Jenney, F. E., Verhagen, M. F. J. M., Cui, X., & Adams, M. W. W. (1999) · Science · doi:10.1126/science.286.5438.306 · Cited by 398
Baker, K., Marcus, C. B., Huffman, K., Kruk, H., Malfroy, B., & Doctrow, S. R. (1998) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)37225-8 · Cited by 335
Self-citationAntioxidants in disease mechanisms and therapy
Sies, H. (1997) · Cited by 286
Melov, S., Doctrow, S. R., Schneider, J. A., Haberson, J., Patel, M., Coskun, P. E., Huffman, K., Wallace, D. C., & Malfroy, B. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-21-08348.2001 · Cited by 277
Self-citationResponses of vomeronasal neurons to natural stimuli
Holy, T. E., Dulac, C., & Meister, M. (2000) · Science · doi:10.1126/science.289.5484.1569 · Cited by 275
Rong, Y., Doctrow, S. R., Tocco, G., & Baudry, M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.17.9897 · Cited by 266
Self-citationMetalloporphyrin class of therapeutic catalytic antioxidants
Patel, M., & Day, B. J. (1999) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(99)01336-x · Cited by 253
Inhibition of Tumor Promotion by a Biomimetic Superoxide Dismutase
Kensler, T. W., Bush, D. M., & Kozumbo, W. J. (1983) · Science · doi:10.1126/science.6857269 · Cited by 250
Ebselen as a Glutathione Peroxidase Mimic and as a Scavenger of Peroxynitrite
Sies, H., & Masumoto, H. (1996) · Advances in Pharmacology · doi:10.1016/s1054-3589(08)60986-2 · Cited by 229
Bruce, A. J., Malfroy, B., & Baudry, M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.6.2312 · Cited by 216
Self-citationSalen-Manganese Complexes Are Superoxide Dismutase-Mimics
Baudry, M., Etienne, S., Bruce, A., Palucki, M., Jacobsen, E., & Malfroy, B. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.1509 · Cited by 207
Self-citationInactivation of catecholamines by superoxide gives new insights on the pathogenesis of septic shock
Macarthur, H., Westfall, T. C., Riley, D. P., Misko, T. P., & Salvemini, D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.17.9753 · Cited by 205
The characteristics of the ‘peroxidatic’ reaction of catalase in ethanol oxidation
Oshino, N., Oshino, R., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1310555 · Cited by 200
Jung, C., Rong, Y., Doctrow, S., Baudry, M., Malfroy, B., & Xu, Z. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)01784-0 · Cited by 177
Self-citationSHARPE, M. A., OLLOSSON, R., STEWART, V. C., & CLARK, J. B. (2002) · Biochemical Journal · doi:10.1042/bj20020154 · Cited by 164
Manganese macrocyclic ligand complexes as mimics of superoxide dismutase
Riley, D. P., & Weiss, R. H. (1994) · Journal of the American Chemical Society · doi:10.1021/ja00080a051 · Cited by 163
Neuroprotection from Delayed Postischemic Administration of a Metalloporphyrin Catalytic Antioxidant
Mackensen, G. B., Patel, M., Sheng, H., Calvi, C. L., Batinic̈‐Haberle, I., Day, B. J., Liang, L., Fridovich, I., Crapo, J. D., Pearlstein, R. D., et al. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-13-04582.2001 · Cited by 157
Dix, T. A., & Marnett, L. J. (1983) · Science · doi:10.1126/science.6304879 · Cited by 156
Doctrow, S. R., Huffman, K. D., Marcus, C. B., Musleh, W., Bruce‐Keller, A. J., Baudry, M., & Malfroy, B. (1996) · Advances in pharmacology · doi:10.1016/s1054-3589(08)60987-4 · Cited by 142
Self-citationGonzalez, P. K., Zhuang, J. C., Doctrow, S. R., Malfroy, B., Benson, P. F., Menconi, M. J., & Fink, M. (1995) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)12131-9 · Cited by 136
Self-citationWeiss, R. H., Flickinger, A. G., Rivers, W. J., Hardy, M. M., Aston, K. W., Ryan, U. S., & Riley, D. P. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49423-4 · Cited by 101
A mimic of superoxide dismutase activity based upon desferrioxamine B and manganese(IV)
Darr, D. J., Zarilla, K. A., & Fridovich, I. (1987) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(87)90354-7 · Cited by 99
Pong, K., Doctrow, S. R., Huffman, K. D., Adinolfi, C. A., & Baudry, M. (2001) · Experimental Neurology · doi:10.1006/exnr.2001.7747 · Cited by 90
Self-citationMalfroy, B., Doctrow, S. R., Orr, P. L., Tocco, G., Fedoseyeva, E. V., & Bénichou, G. (1997) · Cellular Immunology · doi:10.1006/cimm.1997.1091 · Cited by 86
Self-citationA Metalloporphyrin Superoxide Dismutase Mimetic Protects against Paraquat-Induced Lung Injuryin Vivo
Day, B. J., & Crapo, J. D. (1996) · Toxicology and Applied Pharmacology · doi:10.1006/taap.1996.0201 · Cited by 85
Cutler, R. G., & Rodriguez, H. (2002) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789812775733 · Cited by 84
Peroxynitrite scavenging by metalloporphyrins and thiolates
Crow, J. P. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00249-5 · Cited by 84
Poduslo, J. F., Whelan, S. L., Curran, G. L., & Wengenack, T. M. (2000) · Annals of Neurology · doi:10.1002/1531-8249(200012)48:6<943::aid-ana18>3.0.co;2-1 · Cited by 40
A nonpeptidyl mimic of superoxide dismutase with therapeutic activity in rats
Rotella, D. P., Wang, Z.-Z., Zweier, J. L., et al. (2000) · Chemtracts · Cited by 17
Cited by
Crans, D. C., Smee, J. J., Gaidamauskas, E., & Yang, L. (2004) · Chemical Reviews · doi:10.1021/cr020607t · Cited by 1,364
Superoxide Dismutase Mimics: Chemistry, Pharmacology, and Therapeutic Potential
Batinić-Haberle, I., Rebouças, J. S., & Spasojević, I. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2876 · Cited by 531
Redox-Directed Cancer Therapeutics: Molecular Mechanisms and Opportunities
Wondrak, G. T. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2541 · Cited by 462
Catechol oxidase and phenoxazinone synthase: Biomimetic functional models and mechanistic studies
Dey, S. K., & Mukherjee, A. (2016) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2015.11.002 · Cited by 286
Cancer chemoprevention by the antioxidant tempol in Atm-deficient mice
Schubert, R. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh189 · Cited by 139
Metadata
- Authors
- Doctrow, S. R., Huffman, K., Marcus, C. B., Tocco, G., Malfroy, E., Adinolfi, C. A., Kruk, H., Baker, K., Lazarowych, N., Mascarenhas, J., & Malfroy, B.
- Venue
- Journal of Medicinal Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-08-28
- Volume
- 45
- Issue
- 20
- Pages
- 4549-4558
- ISSN
- 0022-2623 (ISSN-L)
- 1520-4804
- OpenAlex
- W2048246398
- Cited by
- 274
- References
- 42
- FWCI
- 5.93
- 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.
