The DOI matches its Crossref record; 66 of the 66 references it cites were found in a registry or an index.
Redefining Oxidative Stress
Abstract
Oxidative stress is often defined as an imbalance of pro-oxidants and antioxidants, which can be quantified in humans as the redox state of plasma GSH/GSSG. Plasma GSH redox in humans becomes oxidized with age, in response to oxidative stress (chemotherapy, smoking), and in common diseases (type 2 diabetes, cardiovascular disease). However, data also show that redox of plasma GSH/GSSG is not equilibrated with the larger plasma cysteine/cystine (Cys/CySS) pool, indicating that the "balance" of pro-oxidants and antioxidants cannot be defined by a single entity. The major cellular thiol/disulfide systems, including GSH/GSSG, thioredoxin- 1 (-SH(2)/-SS-), and Cys/CySS, are not in redox equilibrium and respond differently to chemical toxicants and physiologic stimuli. Individual signaling and control events occur through discrete redox pathways rather than through mechanisms that are directly responsive to a global thiol/disulfide balance such as that conceptualized in the common definition of oxidative stress. Thus, from a mechanistic standpoint, oxidative stress may be better defined as a disruption of redox signaling and control. Adoption of such a definition could redirect research to identify key perturbations of redox signaling and control and lead to new treatments for oxidative stress-related disease processes.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
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?
In the citing paper
“Wick et al. [137] demonstrated the size-dependent transport of fluorescent polystyrene particles with diameters of 50, 80, and 240 nm (but not 500 nm) across human placental explants into the fetal circuit.”
From Air pollution and children’s health—a review of adverse effects associated with prenatal exposure from fine to ultrafine particulate matter (2021) · cites this paper as [137]
In the citing paper
“Since the enhanced antioxidant status has not been shown to be effective in the alleviation of oxidative stress, a new approach based on the thiol redox pool has been proposed (Jones 2006).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Jones 2006
In the citing paper
“In view of this, a more complex definition of oxidative stress, based on the disruption of redox signaling has been proposed (Jones 2006).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Jones 2006
Citations
Cites
[49] Determination of carbonyl content in oxidatively modified proteins
Levine, R. L., Garland, D. L., Oliver, C. N., Amici, A., Climent, I., Lenz, A.-G., Ahn, B. W., Shaltiel, S., & Stadtman, E. R. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)86141-h · Cited by 5,895
Role of Oxidative Modifications in Atherosclerosis
Stocker, R., & Keaney, J. F. (2004) · Physiological Reviews · doi:10.1152/physrev.00047.2003 · Cited by 2,651
Oxidative Stress and Vascular Disease
Madamanchi, N. R., Vendrov, A., & Runge, M. S. (2005) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000150649.39934.13 · Cited by 1,618 · cited 1×
“titative measures of disease outcome (11, 14, 19, 41, 42, 49 55, 62, 67).”
Omenn, G. S., Goodman, G. E., Thornquist, M. D., Balmes, J., Cullen, M. R., Glass, A., Keogh, J. P., Meyskens, F. L., Valanis, B., Williams, J. H., et al. (1996) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/88.21.1550 · Cited by 1,255
(2005) · JAMA · doi:10.1001/jama.293.11.1338 · Cited by 1,209 · cited 1×
“titative measures of disease outcome (11, 14, 19, 41, 42, 49 55, 62, 67).”
Oxidative Stress: Introductory Remarks
Sies, H. (1985) · Elsevier eBooks · doi:10.1016/b978-0-12-642760-8.50005-3 · Cited by 1,037
[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
Self-citationFong, K.-L., McCay, P. B., Poyer, J. L., Keele, B. B., & Misra, H. P. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43258-4 · Cited by 650
Distinct Roles of Thioredoxin in the Cytoplasm and in the Nucleus
Hirota, K., Murata, M., Sachi, Y., Nakamura, H., Takeuchi, J. S., Mori, K., & Yodoi, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.39.27891 · Cited by 615
Flagged first, then by citations
Research works printed but not linked: 2
- Jiang S, 2002, Invest Ophthalmol Vis Sci, 43, 2546
- Nelson KC, 2002, Invest Ophthalmol Vis Sci, 43, 3550
Cited by
Sorted by citations
Sies, H., Berndt, C., & Jones, D. P. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045037 · Cited by 3,520
Self-citationOxidative stress: a concept in redox biology and medicine
Sies, H. (2015) · Redox Biology · doi:10.1016/j.redox.2015.01.002 · Cited by 3,187
The role of antioxidants in the chemistry of oxidative stress: A review
Pisoschi, A. M., & Pop, A. (2015) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2015.04.040 · Cited by 2,963
Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging
Jomova, K., Raptova, R., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03562-9 · Cited by 2,638
Exercise-Induced Oxidative Stress: Cellular Mechanisms and Impact on Muscle Force Production
Powers, S. K., & Jackson, M. J. (2008) · Physiological Reviews · doi:10.1152/physrev.00031.2007 · Cited by 2,459
Oxidative Stress, Synaptic Dysfunction, and Alzheimer’s Disease
Tönnies, E., & Trushina, E. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161088 · Cited by 1,750
Graves, D. B. (2012) · Journal of Physics D Applied Physics · doi:10.1088/0022-3727/45/26/263001 · Cited by 1,534
Understanding Oxidative Stress and Antioxidant Functions to Enhance Photosynthesis
Foyer, C. H., & Shigeoka, S. (2010) · PLANT PHYSIOLOGY · doi:10.1104/pp.110.166181 · Cited by 1,222
Radical-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
Self-citationDoes the Interdependence between Oxidative Stress and Inflammation Explain the Antioxidant Paradox?
Biswas, S. K. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/5698931 · Cited by 1,235
Glutathione dysregulation and the etiology and progression of human diseases
Ballatori, N., Krance, S. M., Notenboom, S., Shi, S., Tieu, K., & Hammond, C. L. (2009) · Biological Chemistry · doi:10.1515/bc.2009.033 · Cited by 1,145
The basics of thiols and cysteines in redox biology and chemistry
Poole, L. B. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.11.013 · Cited by 1,031
Iron homeostasis and oxidative stress: An intimate relationship
Galaris, D., Barbouti, A., & Pantopoulos, K. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118535 · Cited by 960
Real-time imaging of the intracellular glutathione redox potential
Gutscher, M., Pauleau, A.-L., Marty, L., Brach, T., Wabnitz, G. H., Samstag, Y., Meyer, A. J., & Dick, T. P. (2008) · Nature Methods · doi:10.1038/nmeth.1212 · Cited by 894
ROS and p53: A versatile partnership
Liu, B., Chen, Y., & Clair, D. K. S. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.01.011 · Cited by 842
Stress-activated cap’n’collar transcription factors in aging and human disease
Sykiotis, G. P., & Bohmann, D. (2010) · Science Signaling · doi:10.1126/scisignal.3112re3 · Cited by 776
López‐Alarcón, C., & Denicola, A. (2012) · Analytica Chimica Acta · doi:10.1016/j.aca.2012.11.051 · Cited by 802
Apoptosis and glutathione: beyond an antioxidant
Franco, R., & Cidlowski, J. A. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.107 · Cited by 761
Mitochondrial Energetics and Therapeutics
Wallace, D. C., Fan, W., & Procaccio, V. (2010) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092314 · Cited by 747
History and progress of hypotheses and clinical trials for Alzheimer’s disease
Liu, P.-P., Xie, Y., Meng, X.-Y., & Kang, J.-S. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0063-8 · Cited by 723
Reactive Oxygen Species Signaling and Oxidative Stress: Transcriptional Regulation and Evolution
Hong, Y., Boiti, A., Vallone, D., & Foulkes, N. S. (2024) · Antioxidants · doi:10.3390/antiox13030312 · Cited by 775
The thiol pool in human plasma: The central contribution of albumin to redox processes
Turell, L., Radí, R., & Álvarez, B. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.050 · Cited by 712
Hanschmann, E.-M., Godoy, J. R., Berndt, C., Hudemann, C., & Lillig, C. H. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4599 · Cited by 694
Reactive oxygen species, aging and articular cartilage homeostasis
Bolduc, J. A., Collins, J. A., & Loeser, R. F. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.08.038 · Cited by 671
Exercise-induced oxidative stress: Friend or foe?
Powers, S. K., Deminice, R., Ozdemir, M., Yoshihara, T., Bomkamp, M. P., & Hyatt, H. (2020) · Journal of Sport and Health Science · doi:10.1016/j.jshs.2020.04.001 · Cited by 655
Redox compartmentalization in eukaryotic cells
Go, Y., & Jones, D. P. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.01.011 · Cited by 645
Self-citationRadak, Z. O., Zhao, Z., Koltai, E., Ohno, H., & Atalay, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4498 · Cited by 643
Glutathione levels in human tumors
Gamcsik, M. P., Kasibhatla, M. S., Teeter, S. D., & Colvin, O. M. (2012) · Biomarkers · doi:10.3109/1354750x.2012.715672 · Cited by 608
Oxidative Stress as Key Player in Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) Infection
Delgado-Roche, L., & Mesta, F. (2020) · Archives of Medical Research · doi:10.1016/j.arcmed.2020.04.019 · Cited by 612
Sleep Loss Can Cause Death through Accumulation of Reactive Oxygen Species in the Gut
Vaccaro, A., Kaplan Dor, Y., Nambara, K., Pollina, E. A., Lin, C., Greenberg, M. E., & Rogulja, D. (2020) · Cell · doi:10.1016/j.cell.2020.04.049 · Cited by 541
Kemp, M. L., Go, Y., & Jones, D. P. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.11.008 · Cited by 573
Self-citationMetcalfe, N. B., & Alonso‐Álvarez, C. (2010) · Functional Ecology · doi:10.1111/j.1365-2435.2010.01750.x · Cited by 559
Chemistry and biochemistry of lipid peroxidation products
Guéraud, F., Atalay, M., Bresgen, N., Gašparović, A. Č., Eckl, P., Laurence Therese, H. U. C., Jouanin, I., Siems, W., & Uchida, K. (2010) · Free Radical Research · doi:10.3109/10715762.2010.498477 · Cited by 570
Consequences of oxidative stress in age-related macular degeneration
Jarrett, S. G., & Boulton, M. E. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.03.009 · Cited by 549
The central role of glutathione in the pathophysiology of human diseases
Franco, R., Schoneveld, O., Pappa, A., & Panayiotidis, M. I. (2007) · Archives of Physiology and Biochemistry · doi:10.1080/13813450701661198 · Cited by 554
The Keap1-Nrf2 System: A Mediator between Oxidative Stress and Aging
Yu, C., & Xiao, J.-H. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6635460 · Cited by 537
Diabetes, oxidative stress and therapeutic strategies
Rochette, L., Zeller, M., Cottin, Y., & Vergely, C. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.05.017 · Cited by 543
Chakraborty, S., Kaur, S., Guha, S., & Batra, S. K. (2012) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2012.03.008 · Cited by 503
Energetics, epigenetics, mitochondrial genetics
Wallace, D. C., & Fan, W. (2009) · Mitochondrion · doi:10.1016/j.mito.2009.09.006 · Cited by 519
S-glutathionylation in protein redox regulation
Dalle‐Donne, I., Rossi, R., Giustarini, D., Colombo, R., & Milzani, A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.06.014 · Cited by 506
The redox stress hypothesis of aging
Sohal, R. S., & Orr, W. C. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.445 · Cited by 473
Battin, E. E., & Brumaghim, J. L. (2009) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-009-9054-7 · Cited by 479
Evolution of Catalases from Bacteria to Humans
Zámocký, M., Furtmüller, P. G., & Obinger, C. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2046 · Cited by 467
Rochette, L., Lorin, J., Zeller, M., Guilland, J.-C., Lorgis, L., Cottin, Y., & Vergely, C. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.07.004 · Cited by 456
Reactive Oxygen Species: Impact on Skeletal Muscle
Powers, S. K., Ji, L. L., Kavazis, A. N., & Jackson, M. J. (2011) · Comprehensive physiology · doi:10.1002/cphy.c100054 · Cited by 532
Oxidative Stress, Redox Signaling, and Autophagy: Cell Death Versus Survival
Navarro-Yepes, J., Burns, M., Anandhan, A., Khalimonchuk, O., Razo, L. M. D., Quintanilla‐Vega, B., Pappa, A., Panayiotidis, M. I., & Franco, R. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5837 · Cited by 467
McMahon, M. J., Lamont, D. J., Beattie, K. A., & Hayes, J. D. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1007387107 · Cited by 445
Reactive Oxygen Species Are Signalling Molecules for Skeletal Muscle Adaptation
Powers, S. K., Duarte, J., Kavazis, A. N., & Talbert, E. E. (2010) · Experimental Physiology · doi:10.1113/expphysiol.2009.050526 · Cited by 440
Exercise-induced oxidative stress in humans: cause and consequences
Powers, S. K., Nelson, W. B., & Hudson, M. B. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.12.009 · Cited by 441
Effects of oxidative stress on embryonic development
Dennery, P. A. (2007) · Birth Defects Research Part C Embryo Today Reviews · doi:10.1002/bdrc.20098 · Cited by 428
Oxidative Stress and Antioxidants in Disease and Cancer: A Review
Gupta, R. K., Patel, A., Shah, N., Chaudhary, A. K., Jha, U. K., Yadav, U. C., Gupta, P. K., & Pakuwal, U. (2014) · Asian Pacific Journal of Cancer Prevention · doi:10.7314/apjcp.2014.15.11.4405 · Cited by 432
Allen, D. G., Whitehead, N. P., & Froehner, S. C. (2015) · Physiological Reviews · doi:10.1152/physrev.00007.2015 · Cited by 446
Roles of Reactive Oxygen Species and Antioxidants in Ovarian Toxicity1
Devine, P. J., Perreault, S. D., & Luderer, U. (2011) · Biology of Reproduction · doi:10.1095/biolreprod.111.095224 · Cited by 422
Amado, L. L., Garcia, M. L., Ramos, P. B., Freitas, R. F., Zafalon, B., Ferreira, J. L. R., Yunes, J. S., & Monserrat, J. M. (2008) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2008.11.038 · Cited by 415
Resveratrol: Its Biologic Targets and Functional Activity
Pervaiz, S., & Holme, A. L. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2412 · Cited by 415
Hypoxia-induced reactive oxygen species formation in skeletal muscle
Clanton, T. L. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01298.2006 · Cited by 401
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 406
Self-citationObesity ‑ a risk factor for increased COVID‑19 prevalence, severity and lethality (Review)
Petrakis, D., Margina, D. M., Tsarouhas, K., Tekos, F., Stan, M., Nikitovic, D., Kouretas, D., Spandidos, D. A., & Tsatsakis, A. M. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11127 · Cited by 396
Creasy, D. M., & Chapin, R. E. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-415759-0.00059-5 · Cited by 387
Dikalov, S., Dikalova, A., Bikineyeva, A. T., Schmidt, H. H. H. W., Harrison, D. G., & Griendling, K. K. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.08.013 · Cited by 391
Molecular mechanisms underlying chemical liver injury
Gu, X., & Manautou, J. E. (2012) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399411002110 · Cited by 405
Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme
Toppo, S., Flohé, L., Ursini, F., Vanin, S., & Maiorino, M. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.04.007 · Cited by 368
Cortese-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 371
The cell cycle is a redox cycle: Linking phase-specific targets to cell fate
Burhans, W. C., & Heintz, N. H. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.05.026 · Cited by 368
Redox Signaling Mediated by Thioredoxin and Glutathione Systems in the Central Nervous System
Ren, X., Zou, L., Zhang, X., Branco, V., Wang, J., Carvalho, C. M. L., Holmgren, A., & Lu, J. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6925 · Cited by 376
Oxidative Stress and Iron Homeostasis: Mechanistic and Health Aspects
Galaris, D., & Pantopoulos, K. (2008) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360701713104 · Cited by 352
Recent progress in the development of fluorescent probes for imaging pathological oxidative stress
Geng, Y., Wang, Z., Zhou, J., Zhu, M., Liu, J., & James, T. D. (2023) · Chemical Society Reviews · doi:10.1039/d2cs00172a · Cited by 361
Exercise‐induced oxidative stress: past, present and future
Powers, S. K., Radak, Z. O., & Ji, L. L. (2016) · The Journal of Physiology · doi:10.1113/jp270646 · Cited by 373
Johnson, N. M., Hoffmann, A. R., Behlen, J. C., Lau, C., Pendleton, D., Harvey, N., Shore, R., Li, Y., Chen, J., Tian, Y., et al. (2021) · Environmental Health and Preventive Medicine · doi:10.1186/s12199-021-00995-5 · Cited by 339
“[137] demonstrated the size-dependent transport of fluorescent polystyrene particles with diameters of 50, 80, and 240 nm (but not 500 nm) across human placental explants into the fetal circuit.”
BackgroundReactive oxygen and nitrogen species as intracellular signals in skeletal muscle
Powers, S. K., Talbert, E. E., & Adhihetty, P. J. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2010.201327 · Cited by 349
Go, Y., Chandler, J. D., & Jones, D. P. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.03.022 · Cited by 360
Self-citationMeasuring 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
Self-citationAntioxidants in Foods: State of the Science Important to the Food Industry
Finley, J. W., Kong, A. T., Hintze, K. J., Jeffery, E. H., Ji, L. L., & Lei, X. G. (2011) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf2013875 · Cited by 345
Intestinal redox biology and oxidative stress
Circu, M. L., & Aw, T. Y. (2012) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2012.03.014 · Cited by 332
Oxidative Stress and Human Hypertension: Vascular Mechanisms, Biomarkers, and Novel Therapies
Montezano, A. C. I., Dulak-Lis, M. G., Tsiropoulou, S., Harvey, A., Briones, A. M., & Touyz, R. M. (2015) · Canadian Journal of Cardiology · doi:10.1016/j.cjca.2015.02.008 · Cited by 324
Chemotherapy-Induced Weakness and Fatigue in Skeletal Muscle: The Role of Oxidative Stress
Gilliam, L. A. A., & Clair, D. K. S. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3965 · Cited by 338
Oxidative stress generation by microcystins in aquatic animals: Why and how
Amado, L. L., & Monserrat, J. M. (2009) · Environment International · doi:10.1016/j.envint.2009.10.010 · Cited by 315
Targeting Oxidative Stress in Central Nervous System Disorders
Patel, M. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.06.007 · Cited by 312
Antioxidant Supplementation during Exercise Training: Beneficial or Detrimental?
Peternelj, T.-T., & Coombes, J. S. (2011) · Sports Medicine · doi:10.2165/11594400-000000000-00000 · Cited by 314
PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria
Lo, S.-C., & Hannink, M. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.02.014 · Cited by 300
Cervantes-Gracia, K., Llanas-Cornejo, D., & Husi, H. (2017) · Journal of Clinical Medicine · doi:10.3390/jcm6020022 · Cited by 320
Antioxidant Capacity Determination in Plants and Plant‐Derived Products: A Review
Pisoschi, A. M., Pop, A., Cimpeanu, C. L., & Predoi, G. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/9130976 · Cited by 329
Direct and indirect antioxidant properties of α‐lipoic acid and therapeutic potential
Rochette, L., Ghibu, S., Richard, C., Zeller, M., Cottin, Y., & Vergely, C. (2013) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201200608 · Cited by 297
Molecular 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 301
The biology of ergothioneine, an antioxidant nutraceutical
Borodina, I., Kenny, L. C., McCarthy, C. M., Paramasivan, K., Pretorius, E., Roberts, T. J., van der Hoek, S. A., & Kell, D. B. (2020) · Nutrition Research Reviews · doi:10.1017/s0954422419000301 · Cited by 296
Oxidative Damage Increases and Antioxidant Gene Expression Decreases with Aging in the Mouse Ovary
Lim, J., & Luderer, U. (2010) · Biology of Reproduction · doi:10.1095/biolreprod.110.088583 · Cited by 298
Krifka, S., Spagnuolo, G., Schmalz, G., & Schweikl, H. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.03.019 · Cited by 297
Redox signaling and cancer: The role of “labile” iron
Galaris, D., Skiada, V., & Barbouti, A. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.02.038 · Cited by 284
Noble, E. E., Billington, C. J., Kotz, C. M., & Wang, C. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00776.2010 · Cited by 284
On the history of oxidative stress: Concept and some aspects of current development
Sies, H. (2018) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2018.01.002 · Cited by 285
Oliveira, J. H. M., Goncalves, R. L. S., Lara, F. A., Dias, F. A., Gandara, A. C. P., Menna‐Barreto, R. F. S., Edwards, M. C., Laurindo, F. R. M., Silva-Neto, M. A. C., Sorgine, M. H. F., et al. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1001320 · Cited by 282
A nuclear glutathione cycle within the cell cycle
Díaz‐Vivancos, P., Wolff, T., Marković, J., Pallardó, F. V., & Foyer, C. H. (2010) · Biochemical Journal · doi:10.1042/bj20100409 · Cited by 280
Redox signaling in the gastrointestinal tract
Pérez, S., Taléns‐Visconti, R., Rius‐Pérez, S., Finamor, I., & Sastre, J. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.12.048 · Cited by 276
Oxidative stress and liver disease
Zhu, R., Wang, Y., Zhang, L., & Guo, Q. (2012) · Hepatology Research · doi:10.1111/j.1872-034x.2012.00996.x · Cited by 267
Wang, L., Chen, Y., Sternberg, P., & Cai, J. (2008) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.07-1099 · Cited by 271
Commensal bacteria modulate cullin‐dependent signaling via generation of reactive oxygen species
Kumar, A., Wu, H., Collier-Hyams, L. S., Hansen, J. M., Li, T., Yamoah, K., Pan, Z., Jones, D. P., & Neish, A. S. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601867 · Cited by 268
Self-citationThe mitochondrial carnitine/acylcarnitine carrier: Function, structure and physiopathology
Indiveri, C., Iacobazzi, V., Tonazzi, A., Giangregorio, N., Infantino, V., Convertini, P., Console, L., & Palmieri, F. (2011) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2011.10.008 · Cited by 265
Polycystic ovary syndrome and mitochondrial dysfunction
Zhang, J., Bao, Y.-G., Zhou, X., & Zheng, L. (2019) · Reproductive Biology and Endocrinology · doi:10.1186/s12958-019-0509-4 · Cited by 273
Redox properties of serum albumin
Anraku, M., Chuang, V. T. G., Maruyama, T., & Otagiri, M. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.04.036 · Cited by 258
Protein disulfide isomerase in redox cell signaling and homeostasis
Laurindo, F. R. M., Pescatore, L. A., & Fernandes, D. C. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.037 · Cited by 258
Metadata
- Authors
- Jones, D. P.
- Affiliations
- Emory University (US)
- Corresponding author
- Jones, Dean P.
- ORCID
- Jones, Dean P.
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2006-09
- Volume
- 8
- Issue
- 9-10
- Pages
- 1865-1879
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W1970240791
- Semantic Scholar
- 21aa29343a7c35ad93ce5d00685d8074eb1f4efa
- Cited by
- 1,726
- References
- 66
- Citations by year
- 2026: 94 · 2025: 51 · 2024: 84 · 2023: 92 · 2022: 96 · 2021: 109 · 2020: 97 · 2019: 87 · 2018: 100 · 2017: 87 · 2016: 105 · 2015: 90 · 2014: 109 · 2013: 89 · 2012: 109
- FWCI
- 4.16
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Antioxidants and Redox Signaling (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Environmental Health Sciences (R01ES009047, R01-ES-09047, R01ES011195)
- National Center for Research Resources (M01-RR00039, M01RR000039)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Keywords
- oxidative stress, redox signaling, glutathione, glutathione disulfide, thioredoxin, thiol-disulfide balance, redox equilibria, redox regulation
- MeSH terms
- Animals, Cysteine, Cystine, Glutathione, Humans, Models, Biological, Oxidation-Reduction, Signal Transduction, 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