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Long-lived reactive species on free-radical-damaged proteins
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We have demonstrated two novel reactive species on radical-modified proteins which are relatively long-lived, one oxidizing and one reducing. The two species are reactive with critical biological components, and so may be of physiological and pathological importance. The oxidizing species, which have been identified as protein hydroperoxides, can consume key cellular reductants, such as ascorbate and glutathione. The reducing species can act on both free and metalloprotein forms of copper and iron ions, which participate in radical generation. These findings suggest that proteins may act as traps for the chemical energy released by free radicals, with the capacity to pass it on to other molecules. The long-lived nature of both the reactive moieties indicates that they may be able to diffuse and transfer damaging reactions to distant sites.
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“Under normal circumstances, the biological system releases an enzyme, superoxide dismutase SOD, which specifically maintains the O2 concentration at an optimal level of 10–10 M [68].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [68]
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Cites
Oxygen toxicity, oxygen radicals, transition metals and disease
Halliwell, B., & Gutteridge, J. M. C. (1984) · Biochemical Journal · doi:10.1042/bj2190001 · Cited by 5,330
Free Radicals in Biology and Medicine
Land, E. J. (1990) · International Journal of Radiation Biology · doi:10.1080/09553009014552071 · Cited by 4,871
The Chemical Basis of Radiation Biology
O'Neill, P. (1987) · International Journal of Radiation Biology and Related Studies in Physics Chemistry and Medicine · doi:10.1080/09553008714552571 · Cited by 1,849
Free Radical Mechanisms in Tissue Injury
Slater, T. F. (1988) · Springer eBooks · doi:10.1007/978-1-4613-0813-3_18 · Cited by 1,555
Wolff, S. P., & Dean, R. T. (1987) · Biochemical Journal · doi:10.1042/bj2450243 · Cited by 1,272
Self-citationWayner, D. D. M., Burton, G. W., Ingold, K. U., Barclay, L. R. C., & Locke, S. J. (1987) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(87)90155-3 · Cited by 872
Oliver, C., Starke-Reed, P. E., Stadtman, E. R., Liu, G. J., Carney, J. M., & Floyd, R. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.13.5144 · Cited by 771
Novel thioether bond revealed by a 1.7 Å crystal structure of galactose oxidase
Ito, N., Phillips, S. E. V., Stevens, C., Ogel, Z. B., McPherson, M. J., Keen, J. N., Yadav, K. D. S., & Knowles, P. F. (1991) · Nature · doi:10.1038/350087a0 · Cited by 763
Transition metals as catalysts of “autoxidation” reactions
Miller, D. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90148-c · Cited by 739
Davies, K. J. A., & Delsignore, M. E. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48020-9 · Cited by 576
Research works printed but not linked: 2
- Oliver, C. N., Starke-Reed, P. E., Stadtman, E. R., Liu, G. J., Carney, J. M. & Floyd, R. A. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 5144-5147
- Okada, S. (1958) in Organic Peroxides in Radiobiology (Latarjet, R., ed.), pp. 47-49, Pergamon Press, London
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Nimse, S. B., & Pal, D. (2015) · RSC Advances · doi:10.1039/c4ra13315c · Cited by 2,084
Biochemistry and pathology of radical-mediated protein oxidation
Dean, R. T., Fu, S., Stocker, R., & Davies, M. J. (1997) · Biochemical Journal · doi:10.1042/bj3240001 · Cited by 1,678
Self-citationThe 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
Protein oxidation and peroxidation
Davies, M. J. (2016) · Biochemical Journal · doi:10.1042/bj20151227 · Cited by 952
Generation and propagation of radical reactions on proteins
Hawkins, C. L., & Davies, M. J. (2001) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00252-8 · Cited by 763
QUANTIFICATION AND SIGNIFICANCE OF PROTEIN OXIDATION IN BIOLOGICAL SAMPLES*
Shacter, E. B. (2000) · Drug Metabolism Reviews · doi:10.1081/dmr-100102336 · Cited by 748
Shacter, E. B., Williams, J. A., Lim, M., & Levine, R. L. (1994) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)90169-4 · Cited by 466
Stable markers of oxidant damage to proteins and their application in the study of human disease
Davies, M. J., Fu, S., Wang, H., & Dean, R. T. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00206-3 · Cited by 461
Self-citationJoe, B., & Lokesh, B. R. (1994) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(94)90198-8 · Cited by 396
Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity
Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031841 · Cited by 342
Formation of peroxides in amino acids and proteins exposed to oxygen free radicals
Gebicki, S., & Gebicki, J. M. (1993) · Biochemical Journal · doi:10.1042/bj2890743 · Cited by 305
Self-citationFree Radicals Generated during the Glycation Reaction of Amino Acids by Methylglyoxal
Yim, H., Kang, S., Hah, Y.-C., Chock, P. B., & Yim, M. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.47.28228 · Cited by 260
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Du, J., & Gebicki, J. M. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.05.012 · Cited by 258
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Evidence for roles of radicals in protein oxidation in advanced human atherosclerotic plaque
Fu, S., Davies, M. J., Stocker, R., & Dean, R. T. (1998) · Biochemical Journal · doi:10.1042/bj3330519 · Cited by 256
Self-citationReactive species and their accumulation on radical-damaged proteins
Dean, R. T., Gieseg, S. P., & Davies, M. J. (1993) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(93)90145-d · Cited by 252
Self-citationProtein hydroperoxides can give rise to reactive free radicals
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Self-citationGieseg, S. P., Simpson, J. A., Charlton, T., Duncan, M. W., & Dean, R. T. (1993) · Biochemistry · doi:10.1021/bi00069a012 · Cited by 191
Self-citationKuhn, D. M., Arthur, R. E., Thomas, D. M., & Elferink, L. A. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0731309.x · Cited by 184
Total Hydroperoxide and Advanced Oxidation Protein Products in Preterm Hypoxic Babies
Buonocore, G., Perrone, S., Longini, M., Terzuoli, L., & Bracci, R. (2000) · Pediatric Research · doi:10.1203/00006450-200002000-00012 · Cited by 169
Radical-induced chain oxidation of proteins and its inhibition by chain-breaking antioxidants
Neužil, J., Gebicki, J. M., & Stocker, R. (1993) · Biochemical Journal · doi:10.1042/bj2930601 · Cited by 168
Self-citationBabizhayev, M. A., Strokov, I. A., Nosikov, V. V., Savel'yeva, E. L., Sitnikov, V. F., Yegorov, Y. E., & Lankin, V. Z. (2014) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-014-0365-y · Cited by 154
Linton, S. M., Davies, M. J., & Dean, R. T. (2001) · Experimental Gerontology · doi:10.1016/s0531-5565(01)00136-x · Cited by 145
Self-citationSaeed, S., & Howell, N. K. (2002) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.1080 · Cited by 143
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Termini, J. S. (2000) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(00)00019-1 · Cited by 141
Possible Atherogenic Effects of Hypoxia During Obstructive Sleep Apnea
Dean, R. T., & Wilcox, I. (1993) · SLEEP · doi:10.1093/sleep/16.suppl_8.s15 · Cited by 142
Self-citationCrosslinking of DNA and proteins induced by protein hydroperoxides
Gebicki, S., & Gebicki, J. M. (1999) · Biochemical Journal · doi:10.1042/bj3380629 · Cited by 127
Self-citationOxidative modification of fibrinogen inhibits thrombin-catalyzed clot formation
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Zubair, H., Khan, H. Y., Sohail, A., Azim, S., Ullah, M. F., Ahmad, A., Sarkar, F. H., & Hadi, S. M. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.172 · Cited by 126
Oxidative stress, free radicals and protein peroxides
Gebicki, J. M. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.10.021 · Cited by 121
Self-citationProtein hydroperoxides as new reactive oxygen species
Gebicki, J. M. (1997) · Redox Report · doi:10.1080/13510002.1997.11747096 · Cited by 121
Self-citationBenderitter, M., Vincent-Genod, L., Pouget, J., & Voisin, P. (2003) · Radiation Research · doi:10.1667/0033-7587(2003)159[0471:tcmaab]2.0.co;2 · Cited by 120
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Jessup, W., Dean, R. T., & Gebicki, J. M. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(94)33032-8 · Cited by 113
Self-citationPark, D., & Xiong, Y. L. (2006) · Food Chemistry · doi:10.1016/j.foodchem.2006.09.004 · Cited by 113
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Costantini, D. (2016) · Behavioral Ecology and Sociobiology · doi:10.1007/s00265-016-2091-5 · Cited by 108
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Self-citationReduction of protein radicals by GSH and ascorbate: potential biological significance
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Farahmand, S. K., Samini, F., Samini, M., & Samarghandian, S. (2012) · Biogerontology · doi:10.1007/s10522-012-9409-0 · Cited by 96
Farhan, M., Khan, H. Y., Oves, M., Al‐Harrasi, A., Rehmani, N., Arif, H., Hadi, S. M., & Ahmad, A. (2016) · Toxins · doi:10.3390/toxins8020037 · Cited by 92
Schild, L., Reinheckel, T., Wiswedel, I., & AUGUSTIN, W. (1997) · Biochemical Journal · doi:10.1042/bj3280205 · Cited by 91
Morgan, P. E., Dean, R. T., & Davies, M. J. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.02845.x · Cited by 89
Self-citationBiological fate of amino acid, peptide and protein hydroperoxides
Fu, S., Gebicki, S., Jessup, W., Gebicki, J. M., & Dean, R. T. (1995) · Biochemical Journal · doi:10.1042/bj3110821 · Cited by 88
Self-citationHeadlam, H. A., & Davies, M. J. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00814-6 · Cited by 83
Mitochondrial oxidative alterations following partial hepatectomy
GUERRIERI, F., Vendemiale, G., Grattagliano, I., Cocco, T., Pellecchia, G., & Altomare, E. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00145-2 · Cited by 83
Photo-oxidation of cells generates long-lived intracellular protein peroxides
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Self-citationRadicals Derived from Histone Hydroperoxides Damage Nucleobases in RNA and DNA
Luxford, C., Dean, R. T., & Davies, M. J. (2000) · Chemical Research in Toxicology · doi:10.1021/tx000053u · Cited by 81
Self-citationThe kinetics of oxidation of GSH by protein radicals
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Self-citationEffect of Antioxidants on the Oxidative Stability of Chicken Breast Meat in a Dispersion System
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Fu, S., Hick, L. A., Sheil, M. M., & Dean, R. T. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)00021-o · Cited by 77
Self-citationLuxford, C., Morin, B., Dean, R. T., & Davies, M. J. (1999) · Biochemical Journal · doi:10.1042/bj3440125 · Cited by 76
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Self-citationSamarghandian, S., Afshari, R., & Farkhondeh, T. (2014) · Europe PMC (PubMed Central) · Cited by 79
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Srinivasan, S., & Hultin, H. O. (1994) · Journal of Food Biochemistry · doi:10.1111/j.1745-4514.1994.tb00513.x · Cited by 75
Østdal, H., Skibsted, L. H., & Andersen, H. J. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00023-3 · Cited by 73
Fu, S., Fu, M.-X., BAYNES, W. J., THORPE, R. S., & Dean, R. T. (1998) · Biochemical Journal · doi:10.1042/bj3300233 · Cited by 73
Self-citationEfficient repair of protein radicals by ascorbate
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Age-dependent modifications in rat hepatocyte antioxidant defense systems
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Cold atmospheric-pressure plasma induces DNA–protein crosslinks through protein oxidation
Guo, L., Zhao, Y., Liu, D., Liu, Z., Chen, C., Xu, R., Tian, M., Wang, X., Chen, H., & Kong, M. G. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1471476 · Cited by 67
Mutual interaction between glycation and oxidation during non-enzymatic protein modification
Traverso, N., Menini, S., Cottalasso, D., Odetti, P. R., Marinari, U. M., & Pronzato, M. A. (1997) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(97)00052-4 · Cited by 67
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Silvester, J. A., Timmins, G. S., & Davies, M. J. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00327-4 · Cited by 62
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Self-citationŻbikowska, H. M., Nowak, P., & Wachowicz, B. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.09.012 · Cited by 53
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Kunz, L., Zeidler, U., Haegele, K. D., Przybylski, M., & Stark, G. (1995) · Biochemistry · doi:10.1021/bi00037a030 · Cited by 48
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Kuhn, D. M., & Arthur, R. E. (1999) · Molecular Brain Research · doi:10.1016/s0169-328x(99)00238-7 · Cited by 44
Gebicki, J. M., Du, J., Collins, J., & Tweeddale, H. J. (2000) · Acta Biochimica Polonica · doi:10.18388/abp.2000_3945 · Cited by 44
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Self-citationAntosiewicz, J., Popinigis, J., Woźniak, M., Damiani, E., Carloni, P., & Greci, L. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)00196-q · Cited by 43
Macrophage antioxidant protection within atherosclerotic plaques
Steven, P. G. (2009) · Frontiers in bioscience · doi:10.2741/3305 · Cited by 42
Metadata
- Authors
- Simpson, J. A., Narita, S., Gieseg, S., Gebicki, S., Gebicki, J. M., & Dean, R. T.
- Affiliations
- The Heart Research Institute (AU)
- Macquarie University (AU)
- Corresponding author
- Gieseg, S
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1992-03-15
- Volume
- 282
- Issue
- 3
- Pages
- 621-624
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1130831
- OpenAlex
- W2404844012
- Cited by
- 225
- References
- 23
- Citations by year
- 2026: 2 · 2025: 4 · 2023: 5 · 2021: 6 · 2019: 5 · 2018: 2 · 2017: 5 · 2016: 7 · 2015: 4 · 2014: 7 · 2013: 8 · 2012: 9
- FWCI
- 4.10
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Heart Research Institute
- Medical Research Council
- Australian Research Council
- National Health and Medical Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Keywords
- reactive oxygen species, vitamin C, glutathione, copper ions, iron ions, metalloproteins, free radical generation, energy transfer, protein oxidation
- MeSH terms
- Amino Acids, Free Radicals, Metals, Oxidation-Reduction, Peroxides, Proteins
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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.
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