Cited by 220Redox biology and oxidative stressAntioxidant Activity and Oxidative StressFree Radicals and Antioxidants

The DOI matches its Crossref record; 125 of the 125 references it cites were found in a registry or an index.

The Importance of Proteins in Defense Against Oxidation

Bourdon, Emmanuel, Blache, Denis·2001·Antioxidants & Redox Signaling

Open this paper in CoChat — free account

Abstract

Free radicals are a normal feature of cellular oxygen metabolism. However, free radical-associated damage is an important factor in many pathological and toxicological processes. For a long time, lipid peroxidation, mediated by oxygen-derived free radicals, was probably the most extensively investigated process. From more recent studies, it has become evident that proteins are also the targets of free radicals, and this has important implication for their activity, unfolding, and degradation, as well as in cell functioning. After giving a brief overview of the key role of proteins in the overall antioxidant defense, this review examines their role as targets of oxidation reactions, taking into account the reactivity of amino acid residues and some of their oxidation products. In light of recent data, we then consider the specific role of sulfur-containing amino acids in protein degradation and their possible interplay with the reversal of limited oxidative lesions. The participation of proteins in the overall antioxidant defense is also discussed, specifically the role of metallothionein as an intracellular antioxidant and that of albumin as a circulating antioxidant.

Integrity signals

Registry

Crossref · 10.1089/152308601300185241

Cites

125 of 125 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Tissue sulfhydryl groups
Ellman, G. L. (1959) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(59)90090-6 · Cited by 26,824
Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
Esterbauer, H., Schaur, R. J., & Zollner, H. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90192-6 · Cited by 6,672
A Quantitative Assessment of Plasma Homocysteine as a Risk Factor for Vascular Disease
Boushey, C. J. (1995) · JAMA · doi:10.1001/jama.1995.03530130055028 · Cited by 3,708
Superoxide radical and superoxide dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455
Protein Oxidation in Aging, Disease, and Oxidative Stress
Berlett, B. S., & Stadtman, E. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.33.20313 · Cited by 3,379
A Novel Method for Measuring Antioxidant Capacity and its Application to Monitoring the Antioxidant Status in Premature Neonates
Miller, N. J., Rice-Evans, C. A., Davies, M. J., Gopinathan, V., & Milner, A. D. (1993) · Clinical Science · doi:10.1042/cs0840407 · Cited by 3,108
All About Albumin: Biochemistry, Genetics, and Medical Applications
Peters, T. (1995) · Thammasat University Digital Collections · Cited by 3,089
Advanced Glycosylation End Products in Tissue and the Biochemical Basis of Diabetic Complications
Flier, J. S., Underhill, L. H., Brownlee, M., Cerami, A., & Vlassara, H. (1988) · New England Journal of Medicine · doi:10.1056/nejm198805193182007 · Cited by 2,512
The role of lipid peroxidation and antioxidants in oxidative modification of LDL
Esterbauer, H., Gebicki, J. M., Puhl, H., & Jürgens, G. (1992) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(92)90181-f · Cited by 2,307
Antioxidants in Human Health and Disease
Halliwell, B. B. (1996) · Annual Review of Nutrition · doi:10.1146/annurev.nu.16.070196.000341 · Cited by 1,852
Plasma homocysteine as a risk factor for vascular disease. The European Concerted Action Project.
Graham, I. M., Daly, L. E., Refsum, H. M., Robinson, K., Brattström, L. E., Ueland, P. M., Palma-Reis, R. J., Boers, G. H., Sheahan, R. G., Israelsson, B., et al. (1997) · PubMed · doi:10.1001/jama.1997.03540460039030 · Cited by 1,738
Free radicals, oxidative stress, and antioxidants in human health and disease
Aruoma, O. I. (1998) · Journal of the American Oil Chemists' Society · doi:10.1007/s11746-998-0032-9 · Cited by 1,682
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
Free-Radical Chemistry of Cigarette Smoke and Its Toxicological Implications
CHURCH, D. F., & PRYOR, W. A. (1985) · Environmental Health Perspectives · doi:10.1289/ehp.8564111 · Cited by 1,442
OXIDATION OF FREE AMINO ACIDS AND AMINO ACID RESIDUES IN PROTEINS BY RADIOLYSIS AND BY METAL-CATALYZED REACTIONS
Stadtman, E. R. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.004053 · Cited by 1,408
Oxidants in Cigarette Smoke Radicals, Hydrogen Peroxide, Peroxynitrate, and Peroxynitritea
Pryor, W. A., & Stone, K. (1993) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1993.tb39148.x · Cited by 1,179
Oxidative stress: the paradox of aerobic life
Davies, K. J. A. (1995) · Biochemical Society Symposia · doi:10.1042/bss0610001 · Cited by 1,150
Methionine residues as endogenous antioxidants in proteins
Levine, R. L., Mosoni, L., Berlett, B. S., & Stadtman, E. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.26.15036 · Cited by 1,041
[23] Oxidative chemistry of peroxynitrite
Beckman, J. S., Chen, J., Ischiropoulos, H., & Crow, J. P. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(94)33026-3 · Cited by 973
Comparison of different analytical methods for assessing total antioxidant capacity of human serum
Cao, G., & Prior, R. L. (1998) · Clinical Chemistry · doi:10.1093/clinchem/44.6.1309 · Cited by 904
Protein glycation and oxidative stress in diabetes mellitus and ageing
Wolff, S. P., Jiang, Z. Y., & Hunt, J. V. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90040-a · Cited by 886
Oxidation of methionyl residues in proteins: Tools, targets, and reversal
Vogt, W. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)00158-g · Cited by 883
Oxygen free radicals and metallothionein
Sato, M., & Bremner, I. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90029-t · Cited by 855
Biomarkers of free radical damage
de Zwart, L. L., Meerman, J. H. N., Commandeur, J. N. M., & Vermeulen, N. P. E. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00196-8 · Cited by 854
Functional food science and defence against reactive oxidative species
Diplock, A. T., Charuleux, J.-L., Crozier, G. L., Kok, F. J., Rice-Evans, C. A., Roberfroid, M. B., Stahl, W., & Viña, J. (1998) · British Journal Of Nutrition · doi:10.1079/bjn19980106 · Cited by 818
A quantitative assessment of plasma homocysteine as a risk factor for vascular disease. Probable benefits of increasing folic acid intakes
Boushey, C. J. (1995) · JAMA · doi:10.1001/jama.274.13.1049 · Cited by 771
Lewis A. Conner Memorial Lecture
Steinberg, D. H. (1997) · Circulation · doi:10.1161/01.cir.95.4.1062 · Cited by 749
Association of serum albumin and mortality risk
Goldwasser, P., & Feldman, J. G. (1997) · Journal of Clinical Epidemiology · doi:10.1016/s0895-4356(97)00015-2 · Cited by 716
The Yin and Yang of Oxidation in the Development of the Fatty Streak
Navab, M., Berliner, J. A., Watson, A. D., Hama, S. Y., Territo, M., Lusis, A. J., Shih, D. M., Lenten, B. J. V., Frank, J. S., Demer, L. L., et al. (1996) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.16.7.831 · Cited by 699
Albumin—An important extracellular antioxidant?
Halliwell, B. B. (1988) · Biochemical Pharmacology · doi:10.1016/0006-2952(88)90126-8 · Cited by 648
Oxygen-derived species: their relation to human disease and environmental stress.
Halliwell, B. B., & Cross, C. E. (1994) · Environmental Health Perspectives · doi:10.1289/ehp.94102s105 · Cited by 644
Quantitative measurement of the total, peroxyl radical‐trapping antioxidant capability of human blood plasma by controlled peroxidation
Wayner, D. D. M., Burton, G. W., Ingold, K. U., & Locke, S. J. (1985) · FEBS Letters · doi:10.1016/0014-5793(85)81208-4 · Cited by 634
Protein-bound acrolein: Potential markers for oxidative stress
Uchida, K., Kanematsu, M., Sakai, K., Matsuda, T., Hattori, N., Mizuno, Y., Suzuki, D., Miyata, T., Noguchi, N., Niki, E., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.9.4882 · Cited by 632
Commentary Oxidative Stress, Nutrition and Health. Experimental Strategies for Optimization of Nutritional Antioxidant Intake in Humans
Halliwell, B. B. (1996) · Free Radical Research · doi:10.3109/10715769609145656 · Cited by 576
Nutrition and health aspects of free radicals and antioxidants
Aruoma, O. I. (1994) · Food and Chemical Toxicology · doi:10.1016/0278-6915(94)90011-6 · Cited by 572
Protein damage and degradation by oxygen radicals. IV. Degradation of denatured protein.
Davies, K. J. A., Lin, S. W., & Pacifici, R. E. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48021-0 · Cited by 480
Regulation of antioxidant enzymes 1
Harris, E. D. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.9.1612291 · Cited by 462
Reactive Nitrogen Intermediates Promote Low Density Lipoprotein Oxidation in Human Atherosclerotic Intima
Leeuwenburgh, C., Hardy, M. M., Hazen, S. L., Wagner, P. D., Oh‐ishi, S., Steinbrecher, U. P., & Heinecke, J. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.3.1433 · Cited by 461
ASSOCIATION BETWEEN SERUM ALBUMIN AND MORTALITY FROM CARDIOVASCULAR DISEASE, CANCER, AND OTHER CAUSES
Phillips, A. N., Shaper, A. G., & Whincup, P. H. (1989) · The Lancet · doi:10.1016/s0140-6736(89)92042-4 · Cited by 434
A new role for phospholipase A2: protection of membranes from lipid peroxidation damage
van Kuijk, F. J. G. M., Sevanian, A., Handelman, G. J., & Dratz, E. A. (1987) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(87)90014-4 · Cited by 428
Metallothioneins: new functional and structural insights
Vašák, M. (2000) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00082-x · Cited by 417
Nonenzymatic glycosylation of human serum albumin alters its conformation and function.
Shaklai, N., Garlick, R., & Bunn, H. F. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43168-1 · Cited by 416
Protein, Lipid and DNA Repair Systems in Oxidative Stress: The Free-Radical Theory of Aging Revisited
Pacifici, R. E., & Davies, K. J. A. (2009) · Gerontology · doi:10.1159/000213257 · Cited by 411
Plasma homocysteine as a risk factor for vascular disease. The European Concerted Action Project
Graham, I. M. (1997) · JAMA · doi:10.1001/jama.277.22.1775 · Cited by 409
Effect of platelet activating factor-acetylhydrolase on the formation and action of minimally oxidized low density lipoprotein.
Watson, A. D., Navab, M., Hama, S. Y., Sevanian, A., Prescott, S. M., Stafforini, D. M., McIntyre, T. M., Du, B. N. L., Fogelman, A. M., & Berliner, J. A. (1995) · Journal of Clinical Investigation · doi:10.1172/jci117726 · Cited by 403
Protein Sulfhydryls and Their Role in the Antioxidant Function of Protein S-Thiolation
Thomas, J. A., Poland, B. W., & Honzatko, R. B. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1261 · Cited by 399
Automated assay of oxygen radical absorbance capacity with the COBAS FARA II
Cao, G., Verdon, C. P., Wu, A. H., Wang, H., & Prior, R. L. (1995) · Clinical Chemistry · doi:10.1093/clinchem/41.12.1738 · Cited by 386
Hyperhomocysteinemia, Atherosclerosis and Thrombosis
Cattaneo, M. (1999) · Thrombosis and Haemostasis · doi:10.1055/s-0037-1614438 · Cited by 360
Enzymatic reduction of protein-bound methionine sulfoxide.
Brot, N., Weissbach, L., Werth, J. L., & Weissbach, H. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.4.2155 · Cited by 359
Blood Radicals: Reactive Nitrogen Species, Reactive Oxygen Species, Transition Metal Ions, and the Vascular System
Darley-Usmar, V. M., & Halliwell, B. B. (1996) · Pharmaceutical Research · doi:10.1023/a:1016079012214 · Cited by 314
High-affinity-receptor-mediated uptake and degradation of glucose-modified proteins: a potential mechanism for the removal of senescent macromolecules.
Vlassara, H., Brownlee, M., & Cerami, A. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.17.5588 · Cited by 310
Inactivation of Glutathione Peroxidase by Nitric Oxide
Asahi, M., Fujii, J., Suzuki, K., Seo, H. G., Kuzuya, T., Hori, M., Tada, M., Fujii, S., & Taniguchi, N. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.36.21035 · Cited by 309
Glucose and free radicals impair the antioxidant properties of serum albumin
Bourdon, E., Loreau, N., & Blache, D. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.2.233 · Cited by 307
Self-citation
Thioltransferase is a specific glutathionyl mixed-disulfide oxidoreductase
Gravina, S. A., & Mieyal, J. J. (1993) · Biochemistry · doi:10.1021/bi00064a021 · Cited by 306
Biochemistry and physiological role of methionine sulfoxide residues in proteins
Brot, N., & Weissbach, H. (1983) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(83)90592-1 · Cited by 298
Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress
Moskovitz, J., Flescher, E., Berlett, B. S., Azare, J., Poston, J. M., & Stadtman, E. R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.24.14071 · Cited by 281
Oxidative stress associated with exercise, psychological stress and life-style factors
Møller, P., Wallin, H., & Knudsen, L. E. (1996) · Chemico-Biological Interactions · doi:10.1016/0009-2797(96)03729-5 · Cited by 270
Apolipoproteins, membrane cholesterol domains, and the regulation of cholesterol efflux.
Rothblat, G. H., Mahlberg, F. H., Johnson, W., & Phillips, M. C. (1992) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)40761-8 · Cited by 266
Metallothionein protects against the cytotoxic and DNA-damaging effects of nitric oxide.
Schwarz, M. A., Lazo, J. S., Yalowich, J. C., Allen, W. P., Whitmore, M., Bergonia, H. A., Tzeng, E., Billiar, T., Robbins, P. D., & Lancaster, J. R. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.10.4452 · Cited by 244
The multicatalytic proteinase of mammalian cells
Rivett, A. J. (1989) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(89)90558-4 · Cited by 242
Superoxide dismutase undergoes proteolysis and fragmentation following oxidative modification and inactivation.
Salo, D. C., Pacifici, R. E., Lin, S. W., Giulivi, C., & Davies, K. J. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38488-1 · Cited by 237
Cloning the expression of a mammalian gene involved in the reduction of methionine sulfoxide residues in proteins.
Moskovitz, J., Weissbach, H., & Brot, N. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.5.2095 · Cited by 219
Free-Radical Chemistry of Cigarette Smoke and Its Toxicological Implications
Church, D. F., & Pryor, W. A. (1985) · Environmental Health Perspectives · doi:10.2307/3430003 · Cited by 219
Acute methionine load‐induced hyperhomocysteinemia enhances platelet aggregation, thromboxane biosynthesis, and macrophage‐derived tissue factor activity in rats
Durand, P., Lussier‐Cacan, S., & Blache, D. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.13.9367351 · Cited by 214
Self-citation
Advanced Glycation End-products and Atherosclerosis
Vlassara, H. (1996) · Annals of Medicine · doi:10.3109/07853899608999102 · Cited by 209
Lipid Abnormalities in the Nephrotic Syndrome: Causes, Consequences, and Treatment
Wheeler, D. C., & Bernard, D. B. (1994) · American Journal of Kidney Diseases · doi:10.1016/s0272-6386(12)80994-2 · Cited by 186
Free radical damage to proteins: The influence of the relative localization of radical generation, antioxidants, and target proteins
Dean, R. T., Hunt, J. V., Grant, A. J., Yamamoto, Y., & Niki, E. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90167-2 · Cited by 179
Homocysteine metabolism and the oxidative modification of proteins and lipids
Olszewski, A. J., & McCully, K. S. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90151-j · Cited by 168
Cytoplasmic metallothionein overexpression protects NIH 3T3 cells from tert-butyl hydroperoxide toxicity.
Schwarz, M. A., Lazo, J. S., Yalowich, J. C., Reynolds, I. J., Kagan, V. E., Tyurin, V. A., Kim, Y. M., Watkins, S. C., & Pitt, B. R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36597-3 · Cited by 164
Administration of albumin to patients with sepsis syndrome: a possible beneficial role in plasma thiol repletion
Quinlan, G. J., Margarson, M., Mumby, S. E., Evans, T. W., & Gutteridge, J. M. C. (1998) · Clinical Science · doi:10.1042/cs0950459 · Cited by 160
S-thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes.
Ravichandran, V., Seres, T., Moriguchi, T., Thomas, J. A., & Johnston, R. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31491-6 · Cited by 156
Age-related change in redox state of human serum albumin
Era, S., Kuwata, K., Imai, H., Nakamura, K., Hayashi, T., & Sogami, M. (1995) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(94)00166-e · Cited by 156
[3] Toxicological significance of metallothionein
Templeton, D. M., & Cherian, M. G. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)05079-b · Cited by 148
Inactivation of glutathione reductase by 4-hydroxynonenal and other endogenous aldehydes
Jagt, D. L. V., Hunsaker, L. A., Jagt, T. J. V., Gomez, M. S., Gonzales, D. M., Deck, L. M., & Royer, R. E. (1997) · Biochemical Pharmacology · doi:10.1016/s0006-2952(97)00090-7 · Cited by 146
Direct Reaction of H2O2with Sulfhydryl Groups in HL-60 Cells: Zinc-Metallothionein and Other Sites
Quesada, A. R., Byrnes, R. W., Krezoski, S. O., & Petering, D. H. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0452 · Cited by 141
Pro-thrombotic effects of a folic acid deficient diet in rat platelets and macrophages related to elevated homocysteine and decreased n-3 polyunsaturated fatty acids
Durand, P., Prost, M., & Blache, D. (1996) · Atherosclerosis · doi:10.1016/0021-9150(95)06724-8 · Cited by 140
Self-citation
Oxygen-Derived Species: Their Relation to Human Disease and Environmental Stress
Halliwell, B. B., & Cross, C. E. (1994) · Environmental Health Perspectives · doi:10.2307/3432205 · Cited by 134
Oxidative modification of fibrinogen inhibits thrombin-catalyzed clot formation
Shacter, E. B., Williams, J. A., & Levine, R. L. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)93872-4 · Cited by 126
Metallothioneins and Cell Death by Anticancer Drugs
Lazo, J. S., & Pitt, B. R. (1995) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.35.040195.003223 · Cited by 123
Effect of a two-year supplementation with low doses of antioxidant vitamins and/or minerals in elderly subjects on levels of nutrients and antioxidant defense parameters.
Girodon, F., Blache, D., Monget, A. L., Lombart, M., Brunet-Lecompte, P., Arnaud, J., Richard, M., & Galan, P. (1997) · Journal of the American College of Nutrition · doi:10.1080/07315724.1997.10718698 · Cited by 122
Self-citation
Tyrosyl radicals and their role in hydroperoxide-dependent activation and inactivation of prostaglandin endoperoxide synthase
Smith, W. L., Eling, T. E., Kulmacz, R. J., Marnett, L. J., & Tsai, A.-L. (1992) · Biochemistry · doi:10.1021/bi00116a001 · Cited by 122
Effect of oxidation on the properties of apolipoproteins A-I and A-II.
Anantharamaiah, G. M., Hughes, T. A., Iqbal, M., Gawish, A., Neame, P. J., Medley, M. F., & Segrest, J. P. (1988) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)38529-1 · Cited by 121
Mechanism of action of a mammalian DNA repair endonuclease
Doetsch, P. W., Helland, D. E., & Haseltine, W. A. (1986) · Biochemistry · doi:10.1021/bi00356a054 · Cited by 120
Effect of B-group vitamins and antioxidant vitamins on hyperhomocysteinemia: a double-blind, randomized, factorial-design, controlled trial
Woodside, J. V., Yarnell, J., McMaster, D., Young, I. S., Harmon, D., McCrum, E. E., Patterson, C., GEY, K. F., Whitehead, A. S., & Evans, A. (1998) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/67.5.858 · Cited by 118
Oxidative dissociation of human alpha 2-macroglobulin tetramers into dysfunctional dimers.
Reddy, V. Y., Desorchers, P. E., Pizzo, S. V., Gonias, S. L., Sahakian, J. A., Levine, R. L., & Weiss, S. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41830-8 · Cited by 112
Extrarenal Complications of the Nephrotic Syndrome
Harris, R. C., & Ismail, N. (1994) · American Journal of Kidney Diseases · doi:10.1016/s0272-6386(12)80369-6 · Cited by 109
Glucose induces lipid peroxidation and inactivation of membrane‐associated ion‐transport enzymes in human erythrocytes in vivo and in vitro
Pichika, R., Natarajan, R. D., Nadler, J. L., Kumar, D., & Kalra, V. K. (1991) · Journal of Cellular Physiology · doi:10.1002/jcp.1041490113 · Cited by 96
Myoglobin-Induced Oxidative Damage: Evidence for Radical Transfer from Oxidized Myoglobin to Other Proteins and Antioxidants
Irwin, J. A., Østdal, H., & Davies, M. J. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0987 · Cited by 96
Detecting oxidative modification of biomolecules with isotope dilution mass spectrometry: Sensitive and quantitative assays for oxidized amino acids in proteins and tissues
Heinecke, J. W., Hsu, F., Crowley, J. R., Hazen, S. L., Leeuwenburgh, C., Mueller, D. M., RASMUSSEN, J. E., & TURK, J. W. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)00121-4 · Cited by 94
Prostaglandin endoperoxide‐dependent vasospasm in bovine coronary arteries after nitration of prostacyclin synthase
Zou, M., Jendral, M. J., & Ullrich, V. (1999) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0702434 · Cited by 93
Decrease in Accessible Thiols as an Index of Oxidative Damage to Membrane Proteins
Soszyński, M., & Bartosz, G. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00117-2 · Cited by 88
Oxidation of the methionine residues of Escherichia coli ribosomal protein L12 decreases the protein's biological activity.
Caldwell, P., Luk, D. C., Weissbach, H., & Brot, N. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.11.5349 · Cited by 85
Deletion in Human Chromosome Region 12q13-15 by Integration of Human Papillomavirus DNA in a Cervical Carcinoma Cell Line
Gallego, M. I., & Lazo, P. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.41.24321 · Cited by 79
Acute influence of smoking on platelet behaviour, endothelium and plasma lipids and normalization by aspirin
Blache, D., Bouthillier, D., & Davignon, J. (1992) · Atherosclerosis · doi:10.1016/0021-9150(92)90254-e · Cited by 77
Self-citation
α‐Tocopherol does not inhibit hypochlorite‐induced oxidation of apolipoprotein B‐100 of low‐density lipoprotein
Hazell, L. J., & Stocker, R. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01066-1 · Cited by 77
Cloning, sequencing, and expression of the Escherichia coli peptide methionine sulfoxide reductase gene.
Rahman, M. A., Nelson, H. R., Weissbach, H., & Brot, N. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49570-7 · Cited by 75
Oxidation of methionine residues in proteins of activated human neutrophils.
Fliss, H., Weissbach, H., & Brot, N. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.23.7160 · Cited by 73
Molecular mechanisms of damage by excess nitrogen oxides: Nitration of tyrosine by gas‐phase cigarette smoke
Eiserich, J. P., Vossen, V., O’neill, C. A., Halliwell, B. B., Cross, C. E., & van der Vliet, A. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01011-0 · Cited by 71
High serum alpha‐tocopherol, albumin, selenium and cholesterol, and low mortality from coronary heart disease in northern Finland*
Luoma, P. V., Näyhä, S., Sikkilä, K., & Hassi, J. (1995) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.1995.tb01139.x · Cited by 69
Redox Regulation of Copper–Metallothionein
Fabisiak, J. P., Tyurin, V. A., Tyurina, Y. Y., Borisenko, G. G., Korotaeva, A., Pitt, B. R., Lazo, J. S., & Kagan, V. E. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.1077 · Cited by 66
Regulation of voltage‐dependent K+ channels by methionine oxidation: effect of nitric oxide and vitamin C
Ciorba, M. A., Heinemann, S. H., Weissbach, H., Brot, N., & Hoshi, T. (1999) · FEBS Letters · doi:10.1016/s0014-5793(98)01616-0 · Cited by 65
Apolipoprotein B of oxidized LDL accumulates in the lysosomes of macrophages
Mander, E. L., Dean, R. T., Stanley, K. K., & Jessup, W. (1994) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(94)90192-9 · Cited by 63
Administration of albumin to patients with sepsis syndrome: a possible beneficial role in plasma thiol repletion
Quinlan, G. J., MARGARSON, M. P., Mumby, S. E., et al. (1998) · Clinical Science · doi:10.1042/cs19980191 · Cited by 62
Radical-Induced Damage to Bovine Serum Albumin: Role of the Cysteine Residue
Davies, M. J., Gilbert, B. C., & Haywood, R. M. (1993) · Free Radical Research Communications · doi:10.3109/10715769309147502 · Cited by 60
Phagocytosis and stimulation of the respiratory burst by phorbol diester initiate S-thiolation of specific proteins in macrophages
Rokutan, K., Thomas, J. A., & Johnston, R. B. (1991) · The Journal of Immunology · doi:10.4049/jimmunol.147.1.260 · Cited by 59
Accelerated endocytosis and incomplete catabolism of radical-damaged protein
Grant, A. J., Jessup, W., & Dean, R. T. (1992) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(92)90177-d · Cited by 56
Oxidative damage of bovine serum albumin and other enzyme proteins by iron-chelate complexes
Ogino, T., & Okada, S. (1995) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(95)00101-8 · Cited by 53
Age-related changes in the composition of proteins in the trabecular meshwork of the human eye
HORSTMANN, H., Rohen, J. W., & Sames, K. (1983) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(83)90069-6 · Cited by 47
Antioxidant Capacity in Different Tissues of Young and Old Rats
Cao, G., Giovanoni, M., & Prior, R. L. (1996) · Experimental Biology and Medicine · doi:10.3181/00379727-211-43981 · Cited by 46
Analbuminemia: Report of a Case and Review of the Literature1
Dammacco, F., Miglietta, A. S., D’Addabbo, A., Fratello, A., Moschetta, R., & Bonomo, L. (1980) · Vox Sanguinis · doi:10.1111/j.1423-0410.1980.tb01851.x · Cited by 42
Identification of a peptide methionine sulphoxide reductase gene in an oleosin promoter from Brassica napus‡
Sadanandom, A., Piffanelli, P., Knott, T. G., Robinson, C., Sharpe, A., Lydiate, D. J., Murphy, D. J., & Fairbairn, D. J. (1996) · The Plant Journal · doi:10.1046/j.1365-313x.1996.10020235.x · Cited by 42
Folic Acid Deficiency Enhances Oral Contraceptive-Induced Platelet Hyperactivity
Durand, P., Prost, M., & Blache, D. (1997) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.17.10.1939 · Cited by 41
Self-citation
Modulation of the sarcolemmal L-type current by alteration in SR Ca2+release
Balog, E. M., & Gallant, E. M. (1999) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1999.276.1.c128 · Cited by 39
Characterization of the adduct formed from the reaction between homocysteine thiolactone and low-density lipoprotein: antioxidant implications
Ferguson, E. G., Hogg, N., Antholine, W. E., Joseph, J., Singh, R. J., Parthasarathy, S., & Kalyanaraman, B. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00287-1 · Cited by 35
Impaired Cellular Cholesterol Efflux By Oxysterol-Enriched High Density Lipoproteins
Gesquiere, L. R., Loreau, N., & Blache, D. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00114-7 · Cited by 34
Self-citation
Folate Deficiencies and Cardiovascular Pathologies
Durand, P., Prost, M., & Blache, D. (1998) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.1998.072 · Cited by 33
Self-citation
Enhanced platelet thromboxane synthesis and reduced macrophage-dependent fibrinolytic activity related to oxidative stress in oral contraceptive-treated female rats
Durand, P., & Blache, D. (1996) · Atherosclerosis · doi:10.1016/0021-9150(95)05720-x · Cited by 28
Self-citation
Zinc prevents the structural and functional properties of free radical treated-insulin
Faure, P., Lafond, J.-L., Coudray, C., Rossini, E., Halimi, S., Favier, A. E., & Blache, D. (1994) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(94)90194-5 · Cited by 27
Self-citation
Inactivation of xanthine oxidase by hydrogen peroxide involves site-directed hydroxyl radical formation
Terada, L. S., Leff, J. A., Guidot, D. M., Willingham, I. R., & Repine, J. E. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90022-u · Cited by 26
Inactivation of Rabbit Red Blood Cell Hexokinase Activity Promoted in Vitro by an Oxygen-Radical-Generating System
Stocchi, V., Biagiarelli, B., Fiorani, M., Palma, F., Piccoli, G., Cucchiarini, L., & Dachà, M. (1994) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1994.1221 · Cited by 25
Blood lipoperoxidation and antioxidant enzymes inhealthy individuals: Relation to age, sex, habits, lifestyle and environment
Aslan, R., Şekeroğlu, M. R., Gültekin, F., & Bayıroğlu, F. (1997) · Journal of Environmental Science and Health Part A Environmental Science and Engineering and Toxicology · doi:10.1080/10934529709376670 · Cited by 22
Ozone Exposure and Blood Antioxidants: A Study in a Periurban Area in Southern France
Saintot, M., Bernard, N., Astre, C., Gerber, M., & Inserm-crlc (1999) · Archives of Environmental Health An International Journal · doi:10.1080/00039899909602234 · Cited by 16
[45] Escherichia coli peptide methionine sulfoxide reductase: Cloning, high expression, and purification
Brot, N., Rahman, M. A., Moskovitz, J., & Weissbach, H. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)51150-4 · Cited by 8
Determination of 2-oxohistidine by amino acid analysis
Lewisch, S. A., & Levine, R. L. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)00120-2 · Cited by 7
Fibrinogen Proteolysis and Coagulation System Activation during Thrombolytic Therapy
Owen, J. D., Grossman, B. A., Sobel, J., & Kudryk, B. J. (1990) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-3806-6_43 · Cited by 3

Research works printed but not linked: 7

Ciorba MA, 1999, Proc Natl Acad Sci U S A, 93, 15306
Evans MD, 1994, Am J Physiol, 266, L593
McCully KS, 1983, Atheroscler Rev, 11, 157
Montgomery DAD, 1962, Clin Sci, 22, 141
Pitt BR, 1997, Am J Physiol, 273, L856
Rosenblatt DS, 1995, New York, 3111
Stafforini DM, 1994, J Lipid Mediat, 10, 53

Sorted by citations

Human serum albumin: From bench to bedside
Fanali, G., di Masi, A., Trezza, V., Marino, M., Fasano, M., & Ascenzi, P. (2011) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2011.12.002 · Cited by 2,008
Redox regulation of cell survival
Trachootham, D., Lu, W., Ogasawara, M. A., Valle, N. R.-D., & Huang, P. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1957 · Cited by 1,781
Hypoalbuminemia: Pathogenesis and Clinical Significance
Soeters, P. B., Wolfe, R. R., & Shenkin, A. (2019) · Journal of Parenteral and Enteral Nutrition · doi:10.1002/jpen.1451 · Cited by 1,448
The antioxidant properties of serum albumin
Roche, M., Rondeau, P., Singh, N. R., Tarnus, E., & Bourdon, E. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.04.057 · Cited by 1,255
Self-citation
Antioxidant Activity/Capacity Measurement. 1. Classification, Physicochemical Principles, Mechanisms, and Electron Transfer (ET)-Based Assays
Apak, R., Özyürek, M., Güçlü, K., & Çapanoğlu, E. (2016) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5b04739 · Cited by 988

See all 220

Authors: Bourdon, E., & Blache, D.
Affiliations: Inserm (FR)
ORCID: Bourdon, Emmanuel
Venue: Antioxidants & Redox Signaling
Publisher: SAGE Publications
Published: 2001-04
Volume: 3
Issue: 2
Pages: 293-311
ISSN: 1523-0864 (ISSN-L)
1557-7716
DOI: 10.1089/152308601300185241
OpenAlex: W1611625030
Cited by: 220
References: 124
Citations by year: 2026: 5 · 2025: 8 · 2024: 9 · 2023: 12 · 2022: 9 · 2021: 13 · 2020: 12 · 2019: 6 · 2018: 18 · 2017: 6 · 2016: 15 · 2015: 13 · 2014: 14 · 2013: 13 · 2012: 8
FWCI: 1.28
Type: journal article
Language: en
Open access: closed
Locations: Antioxidants and Redox Signaling (publishedVersion)
PubMed (publishedVersion)
Funders: Institut National de la Santé et de la Recherche Médicale
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
Keywords: protein oxidation, antioxidant defense, free radicals, lipid peroxidation, protein unfolding, protein degradation, sulfur-containing amino acids, metallothionein, albumin, oxidative damage
MeSH terms: Animals, Antioxidants, Oxidation-Reduction, Proteins

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

The Importance of Proteins in Defense Against Oxidation

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks