The DOI matches its Crossref record.
Free Radicals in Biology and Medicine
Abstract
The new edition of this well-established book is thoroughly revised and gives a comprehensive account of the role of free radicals, other reactive species (RS), and antioxidants in life, health, and disease. Chapter 1 reviews how oxygen (O2) is used by living organisms, why it can be toxic, and introduces the concept of oxygen radicals and other RS; their chemistry is detailed in Chapter 2, especially for superoxide, hydroxyl radical (including Fenton chemistry), peroxynitrite, nitric oxide, ozone, and singlet O2, with emphasis on their redox properties. Subsequent chapters detail what antioxidants can be made in vivo (e.g. superoxide dismutases, peroxiredoxins) and which can come from diet (e.g. vitamins E and C, carotenoids, and polyphenols such as the flavonoids) and how they work in vivo. The role of RS in cell proliferation, senescence, and death (e.g. by apoptosis, necrosis, or intermediate forms) is presented. Methods for measuring RS are described in detail, including electron paramagnetic resonance and biomarker determination. Useful roles for RS (e.g. cell signalling, phagocyte action), as well as systems in which they cause particular problems (e.g. premature babies, the eye, the ear) are presented. Acute and chronic inflammation are used to illustrate both roles There is a comprehensive description of the role of RS in human diseases, from cancer to heart disease to dementia, in the ageing process, and in the toxicity of many agents, from ethanol to carbon tetrachloride to paraquat. Therapeutic agents active against RS are reviewed in detail, including NADPH oxidase inhibitors, N-acetylcysteine, and Ebselen.
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?
Diabetes causes oxidative stress, which may contribute to the increased tendency for Alzheimer disease in diabetes.
“Diabetes also leads to oxidative stress (ref8, also see later discussion), which may make a contribution to its propensity to favour AD development9.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
In preclinical Alzheimer disease and Alzheimer disease brains, oxidative damage to many molecules is elevated.
“In the brains of subjects with PCAD and AD, levels of oxidative damage to a wide range of molecules are increased8–19.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
Oxidative damage is a central component of Alzheimer disease pathogenesis.
“but oxidative damage is a key component.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
Oxidative stress contributes substantially to the development and progression of Alzheimer disease.
“has been shown in a wide range of studies to contribute significantly to the pathogenesis and progression of AD2,8–19.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
Loss of ion gradients allows extracellular calcium to enter, raising intracellular free calcium and stimulating calcium-dependent endonuclease, phospholipase, and proteinase activities, contributing to synaptic dysfunction and neuronal death.
“Moreover, loss of ion gradients can allow extracellular Ca2+ to enter, which can further raise intracellular free Ca2+ levels, stimulating Ca2+-dependent endonuclease, phospholipase, and proteinase activities8, contributing to synaptic dysfunction and eventual neuronal death.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
Inefficient glucose use and impaired ATP production are closely related to oxidative damage.
“Research from our laboratories11,12,34 and many others2,4,8,10 has shown that inefficient glucose utilization (and thus impaired ATP production) and oxidative damage are intimately related.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
Oxidative stress raises intracellular free calcium levels, which can lead to several harmful effects.
“because oxidative stress is well known to raise intracellular free Ca2+ levels, from which several deleterious consequences can follow8.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
Lipid peroxidation is increased in Alzheimer disease and amnestic mild cognitive impairment brain or cerebrospinal fluid and in preclinical Alzheimer disease hippocampus, as shown by elevated protein-conjugated HNE, F2-isoprostanes, and F4-isoprostanes.
“Increased lipid peroxidation (a term explained in Table 1) in AD and aMCI brains or CSF and in PCAD hippocampus is further evidenced by rises in the levels of protein-conjugated HNE, F2-isoprostanes, and F4-isoprostanes8,11,12,13,15,16,19–23.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
Protein carbonyls are significantly elevated in brain or cerebrospinal fluid from patients with amnestic mild cognitive impairment.
“Even in aMCI patients, oxidative damage is already significantly increased: PC are significantly elevated in aMCI brain or cerebrospinal fluid (CSF)8,14,20.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
Proteostasis dysfunction contributes to neuronal damage and death through mechanisms including ER stress and accumulation of oxidatively damaged proteins.
“This dysfunction contributes to neuronal damage and death by several mechanisms, including ER stress and the accumulation of oxidatively damaged proteins, which in the normal brain are usually degraded by the UPS and autophagy to keep their levels low8,50,53,55.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
This hormetic response often raises levels of antioxidants such as GSH and HO-1, mediated by activation of Nrf-2.
“This often leads to rises in the levels of antioxidants such as GSH and HO-1, mediated by activation of the transcription factor Nrf-2, (nuclear factor erythroid 2-related factor 2)8,89.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
Because oxidative damage is central to aMCI, PCAD, and AD pathology, blocking it ought to help therapeutically.
“The key role of oxidative damage in the pathology of aMCI, PCAD and AD suggests that inhibiting it should have therapeutic benefit8,11.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
Trials of antioxidants like vitamin E in aMCI and AD have mostly been disappointing.
“It is therefore surprising that the results of clinical trials in aMCI and AD involving antioxidant therapies (such as vitamin E) have been largely disappointing2,8,70,78,80.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
Nrf2 is widely expressed in animal tissues but is mostly kept inactive in the cytosol by binding to Keap1, which also promotes its rapid proteasomal degradation.
“Nrf2 is widely expressed in animal tissues but most of it is kept in an inactive form, largely in the cytosol, by binding to the Keap1 (Kelch-like erythroid cell-derived protein with CNC-homology associated protein 1) protein, which also promotes its rapid degradation by the proteasome8,89.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
Many preclinical models of aMCI and AD, such as neuronal cell cultures or transgenic mice, have shown significant protective effects of antioxidant treatment.
“Consistent with this view, many preclinical models of aMCI and AD, such as neuronal cell cultures or transgenic mice, have shown significant protective effects of antioxidant treatment (e.g. refs 2, 8, 77–79).”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
Curcumin is a weak antioxidant in vitro and degrades readily, including in cell culture, into various active products.
“But, curcumin is actually a poor antioxidant in vitro8 and readily breaks down, for example in cell culture91, to a range of biologically active products.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
Extra vitamin E has not been shown to work well as an antioxidant in living humans.
“administering extra vitamin E has not proved particularly effective as an antioxidant in humans in vivo8.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
Clinical trials in aMCI and AD using antioxidants have been disappointing.
“Clinical trials in both conditions using antioxidants have been disappointing”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
HO-1 oxidizes heme to produce biliverdin, which is reduced by BVR-A to bilirubin, a scavenger of ROS/RNS.
“The enzyme heme oxygenase 1 (HO-1) oxidizes heme (a pro-oxidant)8 to produce biliverdin, which is reduced by a biliverdin reductase-A (BVR-A) enzyme to bilirubin (a scavenger of ROS/RNS8,101).”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
Evidence that oxidative damage is a critical part of AD pathology and progression is compelling.
“The evidence for oxidative damage being a critical component of the pathology and progression of AD is compelling8,11,115.”
From Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease (2019) · cites this paper as [8]
Tyrosine nitration inhibits tyrosine phosphorylation by tyrosine kinases due to steric interference of the NO2 group with the active site of the enzyme.
“With the NO2 functionality on Tyr, tyrosine phosphorylation by tyrosine kinases, including receptor tyrosine kinases, is inhibited due to steric interference of the NO2 group with the active site of the enzyme.”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [13]
H2O2 can be decomposed to hydroxyl anion and the highly reactive hydroxyl free radical by Fe2+ or Cu+ in Fenton chemistry.
“In that case, H2O2, which has zero dipole moments and is therefore neutral and can diffuse into or through bilayers, can be decomposed to hydroxyl anion and the highly reactive hydroxyl free radical by Fe2+ or Cu+ in a process known as Fenton chemistry [8,13].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [13]
OH-mediated allylic hydrogen atom abstraction from unsaturated lipid acyl chains initiates lipid peroxidation, leading to highly reactive nucleophilic unsaturated aldehydes such as 4-hydroxynonenal.
“while OH-mediated allylic hydrogen atom abstraction from unsaturated lipid acyl chains initiates the processes of lipid peroxidation, leading to highly reactive nucleophilic unsaturated aldehydes such as 4-hydroxynonenal (HNE) (Figure 2A) [8,13,25,26,27].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [13]
ROS are extremely reactive with half-life times in the nano-second range.
“In addition, criticism arises due to the fact that ROS are extremely reactive with half-life times in the nano-second range [63]”
From The Sixth Edition of the WHO Manual for Human Semen Analysis: A Critical Review and SWOT Analysis (2021) · cites this paper as [63]
Antioxidants reduce oxidative stress, play a key role in immunity, and may improve recovery following exercise.
“Antioxidants reduce OS, play a key role in immunity and may improve recovery following exercise [58,59].”
From Sleep and Nutrition Interactions: Implications for Athletes (2019) · cites this paper as [58]
The most frequently occurring free radicals and reactive molecules in biological systems are derived from oxygen (ROS) and nitrogen (RNS).
“The most frequently occurring free radicals and reactive molecules in biological systems are derived from oxygen (reactive oxygen species, ROS) and nitrogen (Reactive Nitrogen Species, RNS).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Halliwell and Gutteridge 2015
Free radicals contain at least one unpaired electron in the outer shell, which usually gives them high reactivity.
“Free radicals are chemical entities containing at least one unpaired electron in the outer shell which usually gives them high reactivity.”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Halliwell and Gutteridge 2015
ROS/RNS are formed during electron transfer reactions by losing or accepting electrons.
“ROS or RNS are formed during electron transfer reactions, by losing or accepting electron(s) (Halliwell and Gutteridge 2015).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Halliwell and Gutteridge 2015
The interaction (oxidation) of biomolecules with molecular dioxygen is spin restricted and therefore rather slow.
“Since chemical bonds of biomolecules are formed by two antiparallel electrons (↑↓), their interaction (oxidation) with molecular dioxygen (containing two parallel electrons) is spin restricted and therefore rather slow.”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Halliwell and Gutteridge 2015
Molecular oxygen in a triplet state contains two unpaired electrons with parallel spin states in antibonding π* orbitals and is a biradical.
“Molecular oxygen in a triplet state contains two unpaired electrons with parallel spin states (↑↑) in antibonding π* orbitals and therefore is a biradical.”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Halliwell and Gutteridge 2015
Oxidative stress has been related to many pathological states of an organism.
“Oxidative stress has been related to many pathological states of an organism (Halliwell and Gutteridge 2015).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Halliwell and Gutteridge 2015
Citations
Cited by
Sorted by citations
Reactive oxygen species (ROS) as pleiotropic physiological signalling agents
Sies, H., & Jones, D. P. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0230-3 · Cited by 5,335
Neurodegenerative diseases and oxidative stress
Barnham, K. J., Masters, C. L., & Bush, A. I. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1330 · Cited by 3,683
ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
D'Autréaux, B., & Toledano, M. B. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2256 · Cited by 3,642
Sies, H., Berndt, C., & Jones, D. P. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045037 · Cited by 3,520
Free Radicals: Properties, Sources, Targets, and Their Implication in Various Diseases
Phaniendra, A., Jestadi, D. B., & Periyasamy, L. (2015) · Indian Journal of Clinical Biochemistry · doi:10.1007/s12291-014-0446-0 · Cited by 2,886
Hayes, J. D., Dinkova-Kostova, A. T., & Tew, K. D. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.06.001 · Cited by 2,654
Oxidative stress and neurodegeneration: where are we now?
Halliwell, B. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03907.x · Cited by 2,614
Self-citationReactive 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
Reconciling the chemistry and biology of reactive oxygen species
Winterbourn, C. C. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.85 · Cited by 2,504
Halliwell, B., & Whiteman, M. (2004) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705776 · Cited by 2,238
Self-citationOxidative stress, dysfunctional glucose metabolism and Alzheimer disease
Butterfield, D. A., & Halliwell, B. (2019) · Nature Reviews Neuroscience · doi:10.1038/s41583-019-0132-6 · Cited by 1,954
Self-citationAlgae as nutritional and functional food sources: revisiting our understanding.
Wells, M. L., Potin, P., Craigie, J. S., Raven, J. A., Merchant, S. S., Helliwell, K. E., Smith, A. G., Camire, M. E., & Brawley, S. H. (2017) · Journal of Applied Phycology · doi:10.1007/s10811-016-0974-5 · Cited by 1,562
Molecular Mechanisms of Ultraviolet Radiation‐Induced DNA Damage and Repair
Rastogi, R. P., Richa, Kumar, A., Tyagi, M. B., & Sinha, R. P. (2010) · Journal of Nucleic Acids · doi:10.4061/2010/592980 · Cited by 1,329
Zhang, W., Wang, T., Pei, Z., Miller, D. S., Wu, X., Block, M. L., Wilson, B., Zhang, W., Zhou, Y., Hong, J.-S., et al. (2005) · The FASEB Journal · doi:10.1096/fj.04-2751com · Cited by 1,265
Potential toxicity of superparamagnetic iron oxide nanoparticles (SPION)
Singh, N., Jenkins, G. J. S., Asadi, R., & Doak, S. H. (2010) · Nano Reviews · doi:10.3402/nano.v1i0.5358 · Cited by 1,112
Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease
Ngo, V., & Duennwald, M. L. (2022) · Antioxidants · doi:10.3390/antiox11122345 · Cited by 1,130
Heilbronn, L. K., de Jonge, L., Frisard, M. I., DeLany, J. P., Larson-Meyer, D. E., Rood, J., Nguyen, T., Martin, C. K., Volaufova, J., Most, M. M., et al. (2006) · JAMA · doi:10.1001/jama.295.13.1539 · Cited by 969
Microalgae for High-Value Products Towards Human Health and Nutrition
Barkia, I., Saari, N., & Manning, S. R. (2019) · Marine Drugs · doi:10.3390/md17050304 · Cited by 719
Antioxidants in wild mushrooms
Ferreira, I., Barros, L., & Abreu, R. (2009) · Current Medicinal Chemistry · doi:10.2174/092986709787909587 · Cited by 670
Placental oxidative stress: from miscarriage to preeclampsia
Burton, G. J., & Jauniaux, E. (2004) · Journal of the Society for Gynecologic Investigation · doi:10.1016/j.jsgi.2004.03.003 · Cited by 673
A signalling role for 4‐hydroxy‐2‐nonenal in regulation of mitochondrial uncoupling
Echtay, K. S., Esteves, T. C., Pakay, J. L., Jekabsons, M. B., Lambert, A. J., Portero‐Otín, M., Pamplona, R., Vidal‐Puig, A. J., Wang, S., Roebuck, S. J., et al. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg412 · Cited by 597
Role of iron in carcinogenesis: cancer as a ferrotoxic disease
Toyokuni, S. (2009) · Cancer Science · doi:10.1111/j.1349-7006.2008.01001.x · Cited by 552
Mitohormesis: Promoting Health and Lifespan by Increased Levels of Reactive Oxygen Species (ROS)
Ristow, M., & Schmeisser, K. (2014) · Dose-Response · doi:10.2203/dose-response.13-035.ristow · Cited by 534
Terman, A., Kurz, T., Navratil, M., Arriaga, E. A., & Brunk, U. T. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2598 · Cited by 490
Redox Reactions and Microbial Killing in the Neutrophil Phagosome
Winterbourn, C. C., & Kettle, A. J. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4827 · Cited by 468
Oxidative Stress, Chronic Disease, and Muscle Wasting
Moylan, J. S., & Reid, M. B. (2007) · Muscle & Nerve · doi:10.1002/mus.20743 · Cited by 416
Diet-Derived Phenols in Plasma and Tissues and their Implications for Health
Clifford, M. N. (2004) · Planta Medica · doi:10.1055/s-2004-835835 · Cited by 410
Fukuto, J. M., Carrington, S. J., Tantillo, D. J., Harrison, J. G., Ignarro, L. J., Freeman, B. A., Chen, A., & Wink, D. A. (2012) · Chemical Research in Toxicology · doi:10.1021/tx2005234 · Cited by 389
Kell, D. B. (2010) · Archives of Toxicology · doi:10.1007/s00204-010-0577-x · Cited by 361
Antioxidant activity of medicinal and aromatic plants. A review.
Miguel, M. G. (2010) · Flavour and Fragrance Journal · doi:10.1002/ffj.1961 · Cited by 323
The antioxidant paradox: less paradoxical now?
Halliwell, B. (2013) · British Journal of Clinical Pharmacology · doi:10.1111/j.1365-2125.2012.04272.x · Cited by 318
Self-citationRecent advances in biorefinery of astaxanthin from Haematococcus pluvialis
Khoo, K. S., Lee, S. Y., Ooi, C. W., Fu, X., Miao, X., Ling, T. C., & Show, P. L. (2019) · Bioresource Technology · doi:10.1016/j.biortech.2019.121606 · Cited by 318
Management of oxidative stress and other pathologies in Alzheimer’s disease
Simunkova, M., Alwasel, S. H., Alhazza, I. M., Jomova, K., Kollar, V., Rusko, M., & Valko, M. (2019) · Archives of Toxicology · doi:10.1007/s00204-019-02538-y · Cited by 303
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
Skeletal muscle insulin resistance: role of mitochondria and other ROS sources
Di Meo, S., Iossa, S., & Venditti, P. (2017) · Journal of Endocrinology · doi:10.1530/joe-16-0598 · Cited by 282
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
Gordon, L. A., Morrison, E. Y., McGrowder, D. A., Young, R., Fraser, Y. T. P., Zamora, E. M., Alexander-Lindo, R. L., & Irving, R. R. (2008) · BMC Complementary and Alternative Medicine · doi:10.1186/1472-6882-8-21 · Cited by 275
The Sixth Edition of the WHO Manual for Human Semen Analysis: A Critical Review and SWOT Analysis
Boitrelle, F., Shah, R., Saleh, R., Henkel, R., Kandil, H., Chung, E., Vogiatzi, P., Zini, A., Arafa, M., & Agarwal, A. (2021) · Life · doi:10.3390/life11121368 · Cited by 271
Oxidative stress in chronic venous leg ulcers
Wlaschek, M., & Scharffetter‐Kochanek, K. (2005) · Wound Repair and Regeneration · doi:10.1111/j.1067-1927.2005.00065.x · Cited by 241
Cannito, S., Novo, E., di Bonzo, L. V., Busletta, C., Colombatto, S., & Parola, M. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2737 · Cited by 239
Perluigi, M., Coccia, R., & Butterfield, D. A. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4406 · Cited by 229
Andrés, C. M. C., Pérez de la Lastra, J. M., Juan, C. A., Plou, F. J., & Pérez-Lebeña, E. (2022) · Stresses · doi:10.3390/stresses2030019 · Cited by 218
A design of fluorescent probes for superoxide based on a nonredox mechanism
Maeda, H., Yamamoto, K., Nomura, Y., Kohno, I., Hafsi, L., Ueda, N., Yoshida, S., Fukuda, M., Fukuyasu, Y., Yamauchi, Y., et al. (2005) · Journal of the American Chemical Society · doi:10.1021/ja047018k · Cited by 196
Mitochondrial iron metabolism and its role in neurodegeneration
Horowitz, M. P., & Greenamyre, J. T. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100354 · Cited by 195
Sleep and Nutrition Interactions: Implications for Athletes
Doherty, R., Madigan, S., Warrington, G., & Ellis, J. (2019) · Nutrients · doi:10.3390/nu11040822 · Cited by 186
“Antioxidants are any substance that significantly delay or prevent oxidative damage of a target molecule [58].”
BackgroundThe Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms
Reeder, B. J. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2974 · Cited by 189
Sakellariou, G. K., Jackson, M. J., & Vasilaki, A. (2014) · Free Radical Research · doi:10.3109/10715762.2013.830718 · Cited by 184
Kanti Das, T., Wati, M. R., & Fatima-Shad, K. (2014) · Archives of Neuroscience · doi:10.5812/archneurosci.20078 · Cited by 177
Air pollution and circulating biomarkers of oxidative stress
Delfino, R. J., Staimer, N., & Vaziri, N. D. (2011) · Air Quality, Atmosphere & Health · doi:10.1007/s11869-010-0095-2 · Cited by 181
Do polyphenols enter the brain and does it matter? Some theoretical and practical considerations
Schaffer, S., & Halliwell, B. (2012) · Genes & Nutrition · doi:10.1007/s12263-011-0255-5 · Cited by 178
Self-citationOxidative Stress Regulation of Stem and Progenitor Cells
Pervaiz, S., Taneja, R., & Ghaffari, S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2804 · Cited by 176
Chemistry and analysis of HNE and other prominent carbonyl-containing lipid oxidation compounds
Sousa, B. C., Pitt, A. R., & Spickett, C. M. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.02.003 · Cited by 172
Trace elements as an activator of antioxidant enzymes
Wołonciej, M., Milewska, E., & Roszkowska-Jakimiec, W. (2016) · Postępy Higieny i Medycyny Doświadczalnej · doi:10.5604/17322693.1229074 · Cited by 171
ROS-induced ROS release in vascular biology: redox-redox signaling
Zinkevich, N. S., & Gutterman, D. D. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01271.2010 · Cited by 163
Morphological and Chemical Mechanisms of Elongated Mineral Particle Toxicities
Aust, A. E., Cook, P. M., & Dodson, R. F. (2011) · Journal of Toxicology and Environmental Health, Part B · doi:10.1080/10937404.2011.556046 · Cited by 155
Sun, Y., Zhang, H., Zhang, X., Wang, W., Chen, Y., Cai, Z., Wang, Q., Wang, J., & Shi, Y. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102690 · Cited by 151
Panis, C., Victorino, V. J., Herrera, A. C. S. A., Freitas, L. F., De Rossi, T., Campos, F. C., Simão, A. N. C., Barbosa, D. S., Pinge-Filho, P., Cecchini, R., et al. (2012) · Breast Cancer Research and Treatment · doi:10.1007/s10549-011-1851-1 · Cited by 138
Antioxidants, Food Processing and Health
Poljsak, B., Kovač, V., & Milisav, I. (2021) · Antioxidants · doi:10.3390/antiox10030433 · Cited by 133
Grape seed oil: A potential functional food?
SHINAGAWA, F. B., SANTANA, F. C. D., TORRES, L. R. O., & MANCINI-FILHO, J. (2015) · Food Science and Technology · doi:10.1590/1678-457x.6826 · Cited by 125
Correlation of oxidant status with oxidative tissue damage in patients with rheumatoid arthritis
Datta, S., Kundu, S., Ghosh, P., De, S., Ghosh, A., & Chatterjee, M. (2014) · Clinical Rheumatology · doi:10.1007/s10067-014-2597-z · Cited by 123
Ergothioneine, an adaptive antioxidant for the protection of injured tissues? A hypothesis
Halliwell, B., Cheah, I. K., & Drum, C. L. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.12.124 · Cited by 123
Self-citationRauen, U., Springer, A., Weisheit, D., Petrat, F., Korth, H., de Groot, H., & Sustmann, R. (2007) · ChemBioChem · doi:10.1002/cbic.200600311 · Cited by 121
Young, M. L., & Franklin, J. L. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.103409 · Cited by 120
A neuro-immune model of myalgic encephalomyelitis/chronic fatigue syndrome
Morris, G., & Maes, M. (2013) · Metabolic Brain Disease · doi:10.1007/s11011-012-9324-8 · Cited by 117
Toyokuni, S. (2016) · Pathology International · doi:10.1111/pin.12396 · Cited by 111
Lifespan and mitochondrial control of neurodegeneration
Wright, A. F., Jacobson, S. G., Cideciyan, A. V., Roman, A. J., Shu, X., Vlachantoni, D., McInnes, R. R., & Riemersma, R. A. (2004) · Nature Genetics · doi:10.1038/ng1448 · Cited by 111
Does oxidative stress contribute to the pathology of Friedreich's ataxia? A radical question
Armstrong, J. S., Khdour, O., & Hecht, S. M. (2010) · The FASEB Journal · doi:10.1096/fj.09-143222 · Cited by 107
Does exercise reduce brain oxidative stress? A systematic review
Camiletti‐Moirón, D., Aparicio, V. A., Aranda, P., & Radak, Z. (2013) · Scandinavian Journal of Medicine & Science in Sports · doi:10.1111/sms.12065 · Cited by 104
Akatsuka, S., Yamashita, Y., Ohara, H., Liu, Y.-T., Izumiya, M., Abe, K., Ochiai, M., Jiang, L., Nagai, H., Okazaki, Y., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043403 · Cited by 102
Lampe, K. J., Namba, R. M., Silverman, T. R., Bjugstad, K. B., & Mahoney, M. J. (2009) · Biotechnology and Bioengineering · doi:10.1002/bit.22352 · Cited by 98
Metformin induces oxidative stress in white adipocytes and raises uncoupling protein 2 levels
Anedda, A., Rial, E., & González-Barroso, M. M. (2008) · Journal of Endocrinology · doi:10.1677/joe-08-0278 · Cited by 98
Schmidt, M. C., Askew, E. W., Roberts, D. E., Prior, R. L., Ensign Jr, W. Y., & Hesslink Jr, R. E. (2002) · Wilderness & Environmental Medicine · doi:10.1580/1080-6032(2002)013[0094:osihti]2.0.co;2 · Cited by 97
Briels, N., Ciesielski, T. M., Herzke, D., & Jaspers, V. L. B. (2018) · Environmental Science & Technology · doi:10.1021/acs.est.8b04749 · Cited by 93
Kinetic Analysis of Intracellular Concentrations of Reactive Nitrogen Species
Lim, C. H., Dedon, P. C., & Deen, W. M. (2008) · Chemical Research in Toxicology · doi:10.1021/tx800213b · Cited by 93
The Plasma Membrane: A Platform for Intra- and Intercellular Redox Signaling
Nordzieke, D. E., & Medraño-Fernandez, I. (2018) · Antioxidants · doi:10.3390/antiox7110168 · Cited by 90
Mitochondrial Dysfunctions: A Red Thread across Neurodegenerative Diseases
Stanga, S., Caretto, A., Boido, M., & Vercelli, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103719 · Cited by 90
Inactivity‐induced oxidative stress: A central role in age‐related sarcopenia?
Derbré, F., Gratas‐Delamarche, A., Gómez‐Cabrera, M. C., & Viña, J. (2014) · European Journal of Sport Science · doi:10.1080/17461391.2011.654268 · Cited by 89
Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease
Butterfield, D. A., & Boyd-Kimball, D. (2020) · Antioxidants · doi:10.3390/antiox9090818 · Cited by 85
Halliwell, B. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.08.098 · Cited by 87
Self-citationBakuradze, T., Lang, R., Hofmann, T., Stiebitz, H., Bytof, G., Lantz, I., Baum, M., Eisenbrand, G., & Janzowski, C. (2010) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201000147 · Cited by 87
Maeda, H., Yamamoto, K., Kohno, I., Hafsi, L., Itoh, N., Nakagawa, S., Kanagawa, N., Suzuki, K., & Uno, T. (2007) · Chemistry – A European Journal · doi:10.1002/chem.200600522 · Cited by 85
Hypocholesterolaemic and antioxidant effects of kombucha tea in high-cholesterol fed mice
Yang, Z., Ji, B., Zhou, F., Li, B., Luo, Y., Yang, L., & Li, T. (2009) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.3422 · Cited by 84
Antioxidants in Personalized Nutrition and Exercise
Margaritelis, N. V., Paschalis, V., Theodorou, A. A., Kyparos, A., & Nikolaidis, M. G. (2018) · Advances in Nutrition · doi:10.1093/advances/nmy052 · Cited by 84
Arunachalam, K., Yang, X., & San, T. T. (2022) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2021.114540 · Cited by 82
Brezova, V., Valko, M., Breza, M., Morris, H., Telser, J., Dvoranova, D., Kaiserova, K., Varecka, L., Mazur, M., & Leibfritz, D. (2003) · The Journal of Physical Chemistry B · doi:10.1021/jp027743m · Cited by 80
Heart Disease Link to Fetal Hypoxia and Oxidative Stress
Giussani, D. A., Niu, Y., Herrera, E. A., Richter, H. G., Camm, E. J., Thakor, A. S., Kane, A. D., Hansell, J. A., Brain, K. L., Skeffington, K. L., et al. (2014) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4939-1031-1_7 · Cited by 81
Body iron store as a predictor of oxidative DNA damage in healthy men and women
Hori, A., Mizoue, T., Kasai, H., Kawai, K., Matsushita, Y., Nanri, A., Sato, M., & Ohta, M. (2010) · Cancer Science · doi:10.1111/j.1349-7006.2009.01394.x · Cited by 72
Wlaschek, M., Singh, K., Sindrilaru, A., Crisan, D., & Scharffetter-Kochanek, K. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.036 · Cited by 76
“As stated by Halliwell and Gutteridge [33], interfering with transition metals induced oxidative stress helps to address the redox state of metals, reduces the concentration of accessible metals, and/or quenches generated ROS.”
BackgroundReflections of an aging free radical
Halliwell, B. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.10.010 · Cited by 75
Self-citationBendova, P., Mackova, E., Haskova, P., Vavrova, A., Jirkovsky, E., Sterba, M., Popelova, O., Kalinowski, D. S., Kovarikova, P., Vavrova, K., et al. (2010) · Chemical Research in Toxicology · doi:10.1021/tx100125t · Cited by 73
Haack, F., Lemcke, H., Ewald, R., Rharass, T., & Uhrmacher, A. M. (2015) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1004106 · Cited by 66
Vitamin C Deficiency Causes Muscle Atrophy and a Deterioration in Physical Performance
Takisawa, S., Funakoshi, T., Yatsu, T., Nagata, K., Aigaki, T., Machida, S., & Ishigami, A. (2019) · Scientific Reports · doi:10.1038/s41598-019-41229-7 · Cited by 63
Peñas, E., Frias, J., Sidro, B., & Vidal-Valverde, C. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf903739a · Cited by 58
Vincent, A., Thauvin, M., Quévrain, E., Mathieu, E., Layani, S., Seksik, P., Batinic-Haberle, I., Vriz, S., Policar, C., & Delsuc, N. (2021) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2021.111431 · Cited by 58
Capitani, C. D., Carvalho, A. C. L., Rivelli, D. P., Barros, S. B. M., & Castro, I. A. (2009) · European Journal of Lipid Science and Technology · doi:10.1002/ejlt.200800215 · Cited by 53
Superoxide dismutase 1 knockdown induces oxidative stress and DNA methylation loss in the prostate
Bhusari, S. S., Dobosy, J. R., Fu, V., Almassi, N., Oberley, T., & Jarrard, D. F. (2010) · Epigenetics · doi:10.4161/epi.5.5.11853 · Cited by 50
Involvement of NRF2 in Breast Cancer and Possible Therapeutical Role of Polyphenols and Melatonin
Tascioglu Aliyev, A., Panieri, E., Stepanić, V., Gurer-Orhan, H., & Saso, L. (2021) · Molecules · doi:10.3390/molecules26071853 · Cited by 50
Plant polyphenols and human skin: Friends or foes
Korkina, L., De Luca, C., & Pastore, S. (2012) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2012.06510.x · Cited by 47
Role of glutathione in the oxidative stress response in the fungal pathogen Candida glabrata
Gutiérrez-Escobedo, G., Orta-Zavalza, E., Castaño, I., & De Las Peñas, A. (2013) · Current Genetics · doi:10.1007/s00294-013-0390-1 · Cited by 47
Petrović, J., Stanić, D., Dmitrašinović, G., Plećaš-Solarović, B., Ignjatović, S., Batinić, B., Popović, D., & Pešić, V. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/2019643 · Cited by 45
Metadata
- Authors
- Halliwell, B., & Gutteridge, J. M. C.
- ORCID
- Halliwell, Barry
- Venue
- Oxford University Press eBooks
- Publisher
- Oxford University Press
- Published
- 2015-08-01
- OpenAlex
- W4300198507
- Cited by
- 8,990
- References
- 0
- Citations by year
- 2026: 311 · 2025: 396 · 2024: 508 · 2023: 497 · 2022: 549 · 2021: 578 · 2020: 544 · 2019: 476 · 2018: 444 · 2017: 462 · 2016: 386 · 2015: 357
- FWCI
- 41.27
- Type
- book
- Language
- en
- Open access
- closed
- Locations
- Oxford University Press eBooks (publishedVersion)
- Topics
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
- Keywords
- free radicals, reactive species, antioxidants, oxygen toxicity, superoxide, hydroxyl radicals, Fenton reaction, peroxynitrite, nitric oxide, singlet oxygen, superoxide dismutase, peroxiredoxin, carotenoids, polyphenols, flavonoids, apoptosis, cellular senescence, cell death, electron spin resonance, biomarkers, signal transduction, phagocytes, preterm birth, inflammation, cancer, heart disease, dementia, aging, chemical toxicity, NADPH oxidase inhibitors, N-acetylcysteine, ebselen
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
