Redox analysis of human plasma allows separation of pro-oxidant events of aging from decline in antioxidant defenses
Abstract
Oxidative stress is a component of diseases and degenerative processes associated with aging. However, no means are available to assess causative oxidative events separately from decline in function of protective antioxidant systems. Previous studies show that ongoing oxidative processes maintain plasma cysteine/cystine redox at a value that is more oxidized than the antioxidant glutathione/glutathione disulfide (GSH/GSSG) system, suggesting that redox analysis of these plasma thiols could allow separate evaluation of an increase in oxidative events from a decline in antioxidant function. The present study uses measurement of cysteine/cystine and GSH/GSSG redox in plasma of 122 healthy individuals aged 19-85 years to determine whether thiol-disulfide redox changes occur with age. The results show a linear oxidation of cysteine/cystine redox state with age at a rate of 0.16 mV/year over the entire age span. In contrast, GSH/GSSG redox was not oxidized prior to 45 years and subsequently was oxidized at a nearly linear rate of 0.7 mV/year. These data suggest that there is a continuous, linear increase in oxidative events throughout adult life but that the capacity of the GSH antioxidant system is maintained until 45 years and then declines rapidly. The data further suggest that redox states of cysteine/cystine and GSH/GSSG provide an approach to clinically distinguish between increased causative oxidative events and decreased GSH antioxidant function. In principle, such analyses can be used to assess efficacy of intervention strategies against oxidative stress prior to or early after onset of clinical symptoms in aging and age-related disease.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
The Cys/CySS ratio tends to become more oxidized with aging, smoking, diabetes, and obesity.
“The Cys/CySS ratio tends to become even more oxidized with aging, smoking, diabetes, and obesity (198, 302).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [198]
Cites
The Free Radical Theory of Aging Matures
BECKMAN, K. B., & AMES, B. N. (1998) · Physiological Reviews · doi:10.1152/physrev.1998.78.2.547 · Cited by 3,879 · see citing works
Oxidative stress and gene regulation
Allen, R. G., & Tresini, M. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00242-7 · Cited by 1,297 · see citing works
Redox Regulation of Cellular Signalling
Kamata, H., & Hirata, H. (1999) · Cellular Signalling · doi:10.1016/s0898-6568(98)00037-0 · Cited by 1,150 · see citing works
Oxidation-reduction potentials of organic systems
(1960) · Journal of the Franklin Institute · doi:10.1016/0016-0032(60)90644-x · Cited by 889 · see citing works
[11] Redox potential of GSH/GSSG couple: Assay and biological significance
Jones, D. P. (2002) · Methods in Enzymology · doi:10.1016/s0076-6879(02)48630-2 · Cited by 812 · see citing works
Self-citationLevine, R. L. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00765-7 · Cited by 657 · see citing works
Oxidative damage and protection of the RPE
Cai, J., Nelson, K. C., Wu, M., Sternberg, P., & Jones, D. P. (2000) · Progress in Retinal and Eye Research · doi:10.1016/s1350-9462(99)00009-9 · Cited by 628 · see citing works
Self-citationRedox state of glutathione in human plasma
Jones, D. P., Carlson, J. L., Mody, V. C., Cai, J., Lynn, M., & Sternberg, P. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00275-0 · Cited by 587 · see citing works
Self-citationSamiec, P. S., Drews‐Botsch, C., Flagg, E. W., Kurtz, J. C., Sternberg, P., Reed, R. L., & Jones, D. P. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00286-4 · Cited by 493 · see citing works
Self-citationGlutathione measurement in human plasma
Jones, D. P., Carlson, J. L., Samiec, P. S., Sternberg, P., Mody, V. C., Reed, R. L., & Brown, L. A. S. (1998) · Clinica Chimica Acta · doi:10.1016/s0009-8981(98)00089-8 · Cited by 485 · see citing works
Self-citationOxidative modification of proteins during aging
Levine, R. L., & Stadtman, E. R. (2001) · Experimental Gerontology · doi:10.1016/s0531-5565(01)00135-8 · Cited by 466 · see citing works
Properties and Biological Activities of Thioredoxins
Powis, G., & Montfort, W. R. (2001) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.41.1.261 · Cited by 451 · see citing works
Age-related accumulation and spatial distribution of lipofuscin in RPE of normal subjects.
Delori, F. C., Goger, D. G., & Dorey, C. K. (2001) · PubMed · Cited by 424 · see citing works
Human studies related to protein oxidation: protein carbonyl content as a marker of damage.
Chevion, M., Berenshtein, E., & Stadtman, E. R. (2000) · PubMed · Cited by 400 · see citing works
Manganese superoxide dismutase in disease
MacMillan-Crow, L. A., & Cruthirds, D. L. (2001) · Free Radical Research · doi:10.1080/10715760100300281 · Cited by 371 · see citing works
Glutathione redox potential in response to differentiation and enzyme inducers
Kirlin, W. G., Cai, J., Thompson, S. A., Dı́az, D., Kavanagh, T. J., & Jones, D. P. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00145-8 · Cited by 359 · see citing works
Self-citationFunctions of Glutathione in Liver and Kidney
Sies, H., & Wendel, A. (1978) · Proceedings in life sciences · doi:10.1007/978-3-642-67132-6 · Cited by 351 · see citing works
Plasma antioxidants and longevity: a study on healthy centenarians
Mecocci, P., Polidori, M. C., Troiano, L., Cherubini, A., Cecchetti, R., Pini, G., Straatman, M., Monti, D., Stahl, W., Sies, H., et al. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00246-x · Cited by 306 · see citing works
Mechanisms of L-Cysteine Neurotoxicity
Janáky, R., Varga, V., Hermann, A., Saransaari, P., & Oja, S. S. (2000) · Neurochemical Research · doi:10.1023/a:1007616817499 · Cited by 292 · see citing works
Protein disulfide isomerase: The multifunctional redox chaperone of the endoplasmic reticulum
Noiva, R. (1999) · Seminars in Cell and Developmental Biology · doi:10.1006/scdb.1999.0319 · Cited by 279 · see citing works
Role of the Liver in Interorgan Homeostasis of Glutathione and Cyst(e)ine
Ookhtens, M., & Kaplowitz, N. (1998) · Seminars in Liver Disease · doi:10.1055/s-2007-1007167 · Cited by 211 · see citing works
A Mitochondrial Paradigm for Degenerative Diseases and Ageing
Wallace, D. C. (2001) · Novartis Foundation symposium · doi:10.1002/0470868694.ch20 · Cited by 210 · see citing works
Antioxidant regulation of genes encoding enzymes that detoxify xenobiotics and carcinogens
Dhakshinamoorthy, S., Long, D. J., & Jaiswal, A. K. (2001) · Current topics in cellular regulation · doi:10.1016/s0070-2137(01)80009-1 · Cited by 203 · see citing works
Distribution of oxidized and reduced forms of glutathione and cysteine in rat plasma
Lash, L. H., & Jones, D. P. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90065-7 · Cited by 193 · see citing works
Self-citationReduction-potential of Glutathione
Rost, J., & Rapoport, S. M. (1964) · Nature · doi:10.1038/201185a0 · Cited by 172 · see citing works
Jonas, C. R., Puckett, A. B., Jones, D. P., Griffith, D. P., Szeszycki, E. E., Bergman, G. F., Furr, C. E., Tyre, C., Carlson, J. L., Galloway, J. R., et al. (2000) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/72.1.181 · Cited by 168 · see citing works
Self-citationRedox modulation of the NMDA receptor
Choi, Y., & Lipton, S. A. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000638 · Cited by 165 · see citing works
Immunohistochemical and ELISA Assays for Biomarkers of Oxidative Stress in Aging and Diseasea
Onorato, J. M., Thorpe, S. R., & Baynes, J. (1998) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1998.tb09909.x · Cited by 141 · see citing works
Glutathione Therapy: From Prodrugs to Genes
Anderson, M. E., & Luo, J. (1998) · Seminars in Liver Disease · doi:10.1055/s-2007-1007174 · Cited by 140 · see citing works
Age-related changes in oxidative damage to lipids and DNA in rat skin
Tahara, S., Matsuo, M., & Kaneko, T. (2001) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(00)00257-8 · Cited by 78 · see citing works
Epidermal growth factor receptor is modulated by redox through multiple mechanisms
Kamata, H., Shibukawa, Y., Oka, S., & Hirata, H. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01194.x · Cited by 75 · see citing works
Lenton, K. J., Therriault, H., Cantin, A. M., Fülöp, T., Payette, H., & Wagner, J. R. (2000) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/71.5.1194 · Cited by 67 · see citing works
The reductive capacity index of saliva obtained from donors of various ages
Kohen, R., Tirosh, O., & Kopolovich, K. (1992) · Experimental Gerontology · doi:10.1016/0531-5565(92)90040-7 · Cited by 50 · see citing works
Bauman, P. F., Smith, T. K., & Bray, T. Μ. (1988) · Journal of Nutrition · doi:10.1093/jn/118.8.1048 · Cited by 48 · see citing works
Solberg, H. E. (1986) · PubMed · Cited by 31 · see citing works
Depletion of circulating cyst(e)ine by oral and intravenous mesna
Stofer-Vogel, B., Cerny, T., Kupfer, A., Junker, E., & Lauterburg, B. H. (1993) · British Journal of Cancer · doi:10.1038/bjc.1993.391 · Cited by 30 · see citing works
The Role of the Cystathionine Pathway in Glutathione Regulation by Isolated Hepatocytes
Reed, D. J., & Beatty, P. W. (1978) · Proceedings in life sciences · doi:10.1007/978-3-642-67132-6_3 · Cited by 25 · see citing works
Petzki, K. J. (1980) · Food / Nahrung · doi:10.1002/food.19800240632 · Cited by 14 · see citing works
Darley-Usmar, V. M., & Starke-Reed, P. E. (2000) · Antioxidants and Redox Signaling · doi:10.1089/15230860050192143 · Cited by 11 · see citing works
Flagged first, then by citations
2 of the 41 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
The importance of glutathione in human disease
Townsend, D. M., Tew, K. D., & Tapiero, H. (2003) · Biomedicine & Pharmacotherapy · doi:10.1016/s0753-3322(03)00043-x · Cited by 2,009 · see citing works
Jones, D. P. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.1865 · Cited by 1,726 · see citing works
Self-citationRadical-free biology of oxidative stress
Jones, D. P. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00283.2008 · Cited by 1,213 · see citing works
Self-citationSULFUR AMINO ACID METABOLISM: Pathways for Production and Removal of Homocysteine and Cysteine
Stipanuk, M. H. (2004) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.24.012003.132418 · Cited by 997 · see citing works
Jones, D. P., & Sies, H. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2015.6247 · Cited by 647 · see citing works
Self-citationRedox compartmentalization in eukaryotic cells.
Go, Y., & Jones, D. P. (2008) · Biochimica et Biophysica Acta · doi:10.1016/j.bbagen.2008.01.011 · Cited by 635 · see citing works
Self-citationRedox regulation of mitochondrial function
Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works
Kemp, M. L., Go, Y., & Jones, D. P. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.11.008 · Cited by 568 · see citing works
Self-citationPolyphenols and glutathione synthesis regulation
Moskaug, J. Ø., Carlsen, H., Myhrstad, M. C. W., & Blomhoff, R. (2005) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/81.1.277s · Cited by 495 · see citing works
Cysteine/cystine redox signaling in cardiovascular disease
Go, Y.-M., & Jones, D. P. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.11.029 · Cited by 447 · see citing works
Self-citationThe effects of stress and aging on glutathione metabolism
Maher, P. A. (2005) · Ageing Research Reviews · doi:10.1016/j.arr.2005.02.005 · Cited by 426 · see citing works
Established and Emerging Plasma Biomarkers in the Prediction of First Atherothrombotic Events
Ridker, P. M., Brown, N. J., Vaughan, D. E., Harrison, D. G., & Mehta, J. L. (2004) · Circulation · doi:10.1161/01.cir.0000133444.17867.56 · Cited by 418 · see citing works
Redox imbalance in cystine/glutamate transporter-deficient mice
Sato, H., Shiiya, A., Kimata, M., Maebara, K., Tamba, M., Sakakura, Y., Makino, N., Sugiyama, F., Yagami, K.-I., Moriguchi, T., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506439200 · Cited by 422 · see citing works
NUCLEAR AND MITOCHONDRIAL COMPARTMENTATION OF OXIDATIVE STRESS AND REDOX SIGNALING
Hansen, J. M., Go, Y., & Jones, D. P. (2005) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.46.120604.141122 · Cited by 401 · see citing works
Self-citationEXTRACELLULAR THIOLS AND THIOL/DISULFIDE REDOX IN METABOLISM
Moriarty-Craige, S. E., & Jones, D. P. (2004) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.24.012003.132208 · Cited by 390 · see citing works
Self-citationCortese-Krott, M. M., Koning, A. M., Kuhnle, G., Nagy, P., Bianco, C. L., Pasch, A., Wink, D. A., Fukuto, J. M., Jackson, A. A., van Goor, H., et al. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7083 · Cited by 363 · see citing works
Oettl, K., & Stauber, R. E. (2007) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707251 · Cited by 359 · see citing works
Measuring the poise of thiol/disulfide couples in vivo
Jones, D. P., & Liang, Y. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.08.021 · Cited by 338 · see citing works
Self-citationAnalysis of GSH and GSSG after derivatization with N-ethylmaleimide
Giustarini, D., Dalle‐Donne, I., Milzani, A., Fanti, P., & Rossi, R. (2013) · Nature Protocols · doi:10.1038/nprot.2013.095 · Cited by 335 · see citing works
Glutathione: Antioxidant Properties Dedicated to Nanotechnologies
Gaucher, C., Boudier, A., Bonetti, J., Clarot, I., Leroy, P., & Parent, M. (2018) · Antioxidants · doi:10.3390/antiox7050062 · Cited by 332 · see citing works
Jones, D. P., Go, Y., Anderson, C. L., Ziegler, T. R., Kinkade, J. M., & Kirlin, W. G. (2004) · The FASEB Journal · doi:10.1096/fj.03-0971fje · Cited by 302 · see citing works
Self-citationMolecular Mechanisms and Potential Clinical Significance of S -Glutathionylation
Dalle‐Donne, I., Milzani, A., Gagliano, N., Colombo, R., Giustarini, D., & Rossi, R. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1716 · Cited by 296 · see citing works
Redox imbalance links COVID-19 and myalgic encephalomyelitis/chronic fatigue syndrome
Paul, B. D., Lemle, M. D., Komaroff, A. L., & Snyder, S. H. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2024358118 · Cited by 271 · see citing works
Protein damage, repair and proteolysis
Chondrogianni, N., Petropoulos, I., Grimm, S., Georgila, K., Catalgol, B., Friguet, B., Grune, T., & Gonos, E. S. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.09.001 · Cited by 254 · see citing works
Clinical trials of antioxidants as cancer prevention agents: Past, present, and future
Goodman, M. G., Bostick, R. M., Küçük, Ö., & Jones, D. P. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.05.018 · Cited by 255 · see citing works
Self-citationRedox compartmentalization and cellular stress
Jones, D. P., & Go, Y.-M. (2010) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2010.01266.x · Cited by 246 · see citing works
Self-citationAge-associated analysis of oxidative stress parameters in human plasma and erythrocytes
Gil, L., Siems, W., Mazurek, B., Gross, J., Schroeder, P., Voss, P., & Grune, T. (2006) · Free Radical Research · doi:10.1080/10715760600592962 · Cited by 242 · see citing works
Extracellular Redox State: Refining the Definition of Oxidative Stress in Aging
Jones, D. P. (2006) · Rejuvenation Research · doi:10.1089/rej.2006.9.169 · Cited by 241 · see citing works
Self-citationThiol/disulfide redox states in signaling and sensing
Go, Y.-M., & Jones, D. P. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.764840 · Cited by 241 · see citing works
Self-citationGlutathione and glutathione-dependent enzymes: From biochemistry to gerontology and successful aging
Lapenna, D. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102066 · Cited by 239 · see citing works
Cellular Senescence: Molecular Mechanisms, In Vivo Significance, and Redox Considerations
Müller, M. K. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2104 · Cited by 237 · see citing works
Li, Y., Zou, Q., Yuan, C., Li, S., Xing, R., & Yan, X. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201810087 · Cited by 236 · see citing works
Ashfaq, S., Abramson, J. L., Jones, D. P., Rhodes, S. D., Weintraub, W. S., Hooper, W. C., Vaccarino, V., Harrison, D. G., & Quyyumi, A. A. (2006) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2005.09.063 · Cited by 227 · see citing works
Self-citationOxidative Stress Markers Are Associated with Persistent Atrial Fibrillation
Neuman, R. B., Bloom, H. L., Shukrullah, I., Darrow, L. A., Kleinbaum, D. G., Jones, D. P., & Dudley, S. C. (2007) · Clinical Chemistry · doi:10.1373/clinchem.2006.083923 · Cited by 218 · see citing works
Self-citationChandrasekharan, B. P., Anitha, M., Blatt, R., Shahnavaz, N., Kooby, D. A., Staley, C. A., Mwangi, S. M., Jones, D. P., Sitaraman, S. V., & Srinivasan, S. (2010) · Neurogastroenterology & Motility · doi:10.1111/j.1365-2982.2010.01611.x · Cited by 211 · see citing works
Self-citationSchmitt, B., Vicenzi, M., Garrel, C., & Denis, F. M. (2015) · Redox Biology · doi:10.1016/j.redox.2015.07.012 · Cited by 208 · see citing works
Redox outside the Box: Linking Extracellular Redox Remodeling with Intracellular Redox Metabolism
Banerjee, R. V. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.287995 · Cited by 204 · see citing works
Oxidation of glutathione and cysteine in human plasma associated with smoking
Moriarty, S. E., Shah, J. H., Lynn, M., Jiang, S., Openo, K., Jones, D. P., & Sternberg, P. (2003) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2003.09.006 · Cited by 193 · see citing works
Self-citationFranzoni, F., Ghiadoni, L., Galetta, F., PLANTINGA, Y., Lubrano, V., Huang, Y., Salvetti, G., Regoli, F., Taddei, S., & Santoro, G. (2005) · American Journal of Hypertension · doi:10.1016/j.amjhyper.2004.11.006 · Cited by 193 · see citing works
Diurnal variation in glutathione and cysteine redox states in human plasma
Blanco, R. A., Ziegler, T. R., Carlson, B. A., Cheng, P., Park, Y. H., Cotsonis, G., Accardi, C. J., & Jones, D. P. (2007) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/86.4.1016 · Cited by 192 · see citing works
Self-citationDisulfide-containing parenteral delivery systems and their redox-biological fate
Brülisauer, L., Gauthier, M. A., & Leroux, J. (2014) · Journal of Controlled Release · doi:10.1016/j.jconrel.2014.06.012 · Cited by 190 · see citing works
Wang, C., Xu, Y., Wang, X., Guo, C., Wang, T., & Wang, Z. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7440 · Cited by 189 · see citing works
Fitzpatrick, A. M., Teague, W. G., Holguín, F., Yeh, M. Y., & Brown, L. A. S. (2009) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2008.10.047 · Cited by 182 · see citing works
Cheng, X., Siow, R. C. M., & Mann, G. E. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3283 · Cited by 181 · see citing works
Current trends in redox polymers for energy and medicine
Casado, N., Hernández, G., Sardón, H., & Mecerreyes, D. (2015) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2015.08.003 · Cited by 179 · see citing works
Cytoplasmic and Mitochondrial NADPH-Coupled Redox Systems in the Regulation of Aging
Bradshaw, P. C. (2019) · Nutrients · doi:10.3390/nu11030504 · Cited by 178 · see citing works
Disruption of mitochondrial redox circuitry in oxidative stress
Jones, D. P. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2006.07.008 · Cited by 176 · see citing works
Self-citationRedox theory of aging: implications for health and disease
Go, Y., & Jones, D. P. (2017) · Clinical Science · doi:10.1042/cs20160897 · Cited by 173 · see citing works
Self-citationMan, A. W. C., Li, H., & Xia, N. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/1496462 · Cited by 173 · see citing works
Bermejo‐Bescós, P., Martín‐Aragón, S., Benedı́, J., Susín, C., Felici, E., Gil, P., Ribera, J. M., & Villar, Á. (2008) · Free Radical Research · doi:10.1080/10715760701861373 · Cited by 167 · see citing works
Giustarini, D., Tsikas, D., Colombo, G., Milzani, A., Dalle‐Donne, I., Fanti, P., & Rossi, R. (2016) · Journal of Chromatography B · doi:10.1016/j.jchromb.2016.02.015 · Cited by 163 · see citing works
Low-Molecular-Weight Thiols in Thiol–Disulfide Exchange
Laer, K. V., Hamilton, C. J., & Messens, J. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4964 · Cited by 159 · see citing works
Go, Y., & Jones, D. P. (2005) · Circulation · doi:10.1161/circulationaha.104.515155 · Cited by 153 · see citing works
Self-citationRedox Regulation in the Extracellular Environment
Ottaviano, F. G., Handy, D. E., & Loscalzo, J. (2007) · Circulation Journal · doi:10.1253/circj.72.1 · Cited by 155 · see citing works
Age-Related Influence on Thiol, Disulfide, and Protein-Mixed Disulfide Levels in Human Plasma
Giustarini, D., Dalle‐Donne, I., Lorenzini, S., Milzani, A., & Rossi, R. (2006) · The Journals of Gerontology Series A · doi:10.1093/gerona/61.10.1030 · Cited by 143 · see citing works
Sies, H., & Jones, D. P. (2007) · Elsevier eBooks · doi:10.1016/b978-012373947-6.00285-3 · Cited by 142 · see citing works
Self-citationRedox Mechanisms in Neurodegeneration: From Disease Outcomes to Therapeutic Opportunities
Sbodio, J. I., Snyder, S. H., & Paul, B. D. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7321 · Cited by 143 · see citing works
Transcription factor NRF2 as a promising therapeutic target for Alzheimer’s disease
Qu, Z., Sun, J., Zhang, W., Yu, J., & Zhuang, C. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.06.028 · Cited by 140 · see citing works
Leydig cell aging and hypogonadism
Beattie, M. C., Adekola, L., Papadopoulos, V., Chen, H., & Zirkin, B. R. (2015) · Experimental Gerontology · doi:10.1016/j.exger.2015.02.014 · Cited by 139 · see citing works
A Microfabricated PDMS Microbial Fuel Cell
Siu, C.-P.-B., & Chiao, M. (2008) · Journal of Microelectromechanical Systems · doi:10.1109/jmems.2008.2006816 · Cited by 136 · see citing works
Oxidative stress is associated with impaired arterial elasticity
Patel, R. S., Mheid, I. A., Morris, A. A., Ahmed, Y. A., Kavtaradze, N., Ali, S., Dabhadkar, K. C., Brigham, K. L., Hooper, W. C., Alexander, R. W., et al. (2011) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2011.04.033 · Cited by 135 · see citing works
Self-citationClinical oxidation parameters of aging
Voß, P., & Siems, W. (2006) · Free Radical Research · doi:10.1080/10715760600953859 · Cited by 134 · see citing works
Erythrocyte Plasma Membrane Redox System in Human Aging
Rizvi, S. I., Jha, R., & Maurya, P. K. (2006) · Rejuvenation Research · doi:10.1089/rej.2006.9.470 · Cited by 134 · see citing works
Amino acids in the regulation of aging and aging-related diseases
Canfield, C.-A. E., & Bradshaw, P. C. (2019) · Translational Medicine of Aging · doi:10.1016/j.tma.2019.09.001 · Cited by 133 · see citing works
Maciel-Barón, L. A., Morales-Rosales, S. L., Aquino-Cruz, A. A., Triana-Martínez, F., Galván-Arzate, S., Luna-López, A., González-Puertos, V. Y., López-Díazguerrero, N. E., Torres, C., & Königsberg, M. (2016) · AGE · doi:10.1007/s11357-016-9886-1 · Cited by 128 · see citing works
Implications of plasma thiol redox in disease
Oliveira, P. V. S., & Laurindo, F. R. M. (2018) · Clinical Science · doi:10.1042/cs20180157 · Cited by 127 · see citing works
Glutathione during embryonic development
Hansen, J. M., & Harris, C. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.12.001 · Cited by 127 · see citing works
Ayer, A., Gourlay, C. W., & Dawes, I. W. (2014) · FEMS Yeast Research · doi:10.1111/1567-1364.12114 · Cited by 125 · see citing works
Murashima, M., Watanabe, S., Zhuo, X., Uehara, M., & Kurashige, A. (2004) · BioFactors · doi:10.1002/biof.5520220154 · Cited by 122 · see citing works
Redox State of Human Serum Albumin in Terms of Cysteine-34 in Health and Disease
Oettl, K., & Marsche, G. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)74011-8 · Cited by 121 · see citing works
Atherothrombosis and Oxidative Stress: Mechanisms and Management in Elderly
Violi, F., Loffredo, L., Carnevale, R., Pignatelli, P., & Pastori, D. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6963 · Cited by 121 · see citing works
Aging-Related Oxidative Stress in Healthy Humans
Mendoza-Núñez, V. M., Ruíz-Ramos, M., Sánchez-Rodrı́guez, M. A., Retana-Ugalde, R., & Muñoz-Sánchez, J. L. (2007) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.213.261 · Cited by 116 · see citing works
Extracellular/Microenvironmental Redox State
Chaiswing, L., & Oberley, T. D. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3020 · Cited by 114 · see citing works
Ginsenoside-Rd attenuates oxidative damage related to aging in senescence-accelerated mice
Yokozawa, T., Satoh, A., & Cho, E. J. (2004) · Journal of Pharmacy and Pharmacology · doi:10.1211/0022357022449 · Cited by 114 · see citing works
Cysteinylation and homocysteinylation of plasma protein thiols during ageing of healthy human beings
Rossi, R., Giustarini, D., Milzani, A., & Dalle‐Donne, I. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00417.x · Cited by 112 · see citing works
Vučetić, M., Cormerais, Y., Parks, S. K., & Pouysségur, J. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00319 · Cited by 113 · see citing works
Zhang, P., Wu, J., Xiao, F., Zhao, D., & Luan, Y. (2018) · Medicinal Research Reviews · doi:10.1002/med.21485 · Cited by 108 · see citing works
Redox-related biomarkers in human cardiovascular disease - classical footprints and beyond
Daiber, A., Hahad, O., Andreadou, I., Steven, S., Daub, S., & Münzel, T. F. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101875 · Cited by 107 · see citing works
Glutathione availability modulates alveolar macrophage function in the chronic ethanol-fed rat
Brown, L. A. S., Ping, X., Harris, F. L., & Gauthier, T. W. (2006) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00346.2006 · Cited by 106 · see citing works
Jiang, S., Moriarty-Craige, S. E., Orr, M. L., Cai, J., Sternberg, P., & Jones, D. P. (2005) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.04-0949 · Cited by 106 · see citing works
Self-citationThiol–Disulfide Exchange Reactions in the Mammalian Extracellular Environment
Yi, M. C., & Khosla, C. (2016) · Annual Review of Chemical and Biomolecular Engineering · doi:10.1146/annurev-chembioeng-080615-033553 · Cited by 104 · see citing works
A key role for mitochondria in endothelial signaling by plasma cysteine/cystine redox potential
Go, Y.-M., Park, H., Koval, M., Orr, M., Reed, M., Liang, Y., Smith, D., Pohl, J., & Jones, D. P. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.10.050 · Cited by 103 · see citing works
Self-citationA reducing redox environment promotes C2C12 myogenesis: Implications for regeneration in aged muscle
Hansen, J. M., Klass, M., Harris, C., & CSETE, M. E. (2006) · Cell Biology International · doi:10.1016/j.cellbi.2006.11.027 · Cited by 100 · see citing works
Ferguson, G., & Bridge, W. J. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.01.017 · Cited by 99 · see citing works
Glutathione Redox Control of Asthma: From Molecular Mechanisms to Therapeutic Opportunities
Fitzpatrick, A. M., Jones, D. P., & Brown, L. A. S. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4198 · Cited by 99 · see citing works
Self-citationCysteine Redox Potential Determines Pro-Inflammatory IL-1β Levels
Iyer, S. S., Accardi, C. J., Ziegler, T. R., Blanco, R. A., Ritzenthaler, J. D., Rojas, M., Roman, J., & Jones, D. P. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005017 · Cited by 96 · see citing works
Self-citationAgeing‐Associated Oxidative Stress and Inflammation Are Alleviated by Products from Grapes
Petersen-Ross, K. S., & Smith, C. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/6236309 · Cited by 95 · see citing works
Extracellular redox status regulates Nrf2 activation through mitochondrial reactive oxygen species
Imhoff, B. R., & Hansen, J. M. (2009) · Biochemical Journal · doi:10.1042/bj20091286 · Cited by 92 · see citing works
Rosa, A. R., Singh, N., Whitaker, E., de Brito, M., Lewis, A. M., Vieta, E., Churchill, G. C., Geddes, J. R., & Goodwin, G. M. (2014) · Psychological Medicine · doi:10.1017/s0033291714000014 · Cited by 91 · see citing works
Gale, E. M., Mukherjee, S., Liu, C., Loving, G. S., & Caravan, P. D. (2014) · Inorganic Chemistry · doi:10.1021/ic502005u · Cited by 90 · see citing works
Kleinhenz, J., Kleinhenz, D. J., You, S., Ritzenthaler, J. D., Hansen, J. M., Archer, D. R., Sutliff, R. L., & Hart, C. M. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00148.2009 · Cited by 91 · see citing works
Red blood cells as a physiological source of glutathione for extracellular fluids
Giustarini, D., Milzani, A., Dalle‐Donne, I., & Rossi, R. (2007) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2007.09.001 · Cited by 89 · see citing works
Age‐related anabolic resistance after endurance‐type exercise in healthy humans
Durham, W. J., Casperson, S. L., Dillon, E. L., Keske, M. A., Paddon‐Jones, D., Sanford, A. P., Hickner, R. C., Grady, J. J., & Sheffield‐Moore, M. (2010) · The FASEB Journal · doi:10.1096/fj.09-150177 · Cited by 88 · see citing works
Oxidation of extracellular cysteine/cystine redox state in bleomycin-induced lung fibrosis
Iyer, S. S., Ramirez, A. M., Ritzenthaler, J. D., Torres-González, E., Roser‐Page, S., Mora, A. L., Brigham, K. L., Jones, D. P., Roman, J., & Rojas, M. (2008) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.90401.2008 · Cited by 88 · see citing works
Self-citationLee, B., Li, Z., Clemens, D. L., Dillon, B. J., Hwang, A., Zink, J. I., & Horwitz, M. A. (2016) · Small · doi:10.1002/smll.201600892 · Cited by 87 · see citing works
Chronic Alcoholism Alters Systemic and Pulmonary Glutathione Redox Status
Yeh, M. Y., Burnham, E. L., Moss, M., & Brown, L. A. S. (2007) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200611-1722oc · Cited by 86 · see citing works
Carlson, D. A., SMITH, A. R. W., Fischer, S. J., Young, K. L., & Packer, L. (2007) · PubMed · Cited by 86 · see citing works
Oxidative stress in aging: Theoretical outcomes and clinical evidences in humans
del Valle, L. G. (2011) · Biomedicine & Aging Pathology · doi:10.1016/j.biomag.2011.03.001 · Cited by 85 · see citing works
Redox control of teratogenesis
Hansen, J. M., & Harris, C. (2012) · Reproductive Toxicology · doi:10.1016/j.reprotox.2012.09.004 · Cited by 84 · see citing works
Endothelial Function and Aminothiol Biomarkers of Oxidative Stress in Healthy Adults
Ashfaq, S., Abramson, J. L., Jones, D. P., Rhodes, S. D., Weintraub, W. S., Hooper, W. C., Vaccarino, V., Alexander, R. W., Harrison, D. G., & Quyyumi, A. A. (2008) · Hypertension · doi:10.1161/hypertensionaha.107.097386 · Cited by 84 · see citing works
Self-citation
- Authors
- Jones, D. P., Mody, V. C., Carlson, J. L., Lynn, M. J., & Sternberg, P.
- Affiliations
- Emory University (US)
- Corresponding author
- Jones, Dean P
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2002-11
- Volume
- 33
- Issue
- 9
- Pages
- 1290-1300
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W2067305246
- Cited by
- 392
- References
- 41
- Citations by year
- 2026: 6 · 2025: 9 · 2024: 9 · 2023: 7 · 2022: 18 · 2021: 12 · 2020: 17 · 2019: 21 · 2018: 18 · 2017: 17 · 2016: 20 · 2015: 23 · 2014: 23 · 2013: 14 · 2012: 25
- FWCI
- 3.59
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Eye Institute (EY07892, EY0 6360, P30EY006360)
- National Institute of Environmental Health Sciences (ES09047, R01ES009047)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Keywords
- oxidative stress, aging, antioxidant defense, age-related diseases
- MeSH terms
- Adolescent, Adult, Aged, Aged, 80 and over, Aging, Cysteine, Disulfides, Female, Glutathione, Humans, Kinetics, Male, Middle Aged, Models, Chemical, Oxidation-Reduction, Reference Values, Sulfhydryl Compounds, Age Distribution, Sex Distribution, Oxidative Stress, Glutathione Disulfide
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