During my long career in the field of redox biology, I met many inspiring people, especially Lester Packer.
Recent Advances:
This special issue of Antioxidants & Redox Signaling is dedicated to Lester Packer.
Critical Issues:
In this short review, I explore how Lester and other pioneers helped to develop the redox biology field and how I interacted with them.
Future Directions:
In our research to advance the field of redox biology, we stand on the shoulders of giants, including Lester Packer. Antioxid. Redox Signal. 38, 792–802.
Get full access to this article
View all access options for this article.
References
1.
AlamZI, JennerA, DanielSE, LeesAJ, CairnsN, MarsdenCD, JennerP, and HalliwellB. Oxidative DNA damage in the Parkinsonian brain: an apparent selective increase in 8-hydroxyguanine levels in substantia nigra. J Neurochem, 69: 1196–1203, 1997.
2.
AlamZI, DanielSE, LeesAJ, MarsdenDC, JennerP, and HalliwellB. A generalised increase in protein carbonyls in the brain in Parkinson's but not incidental Lewy body disease. J Neurochem, 69: 1326–1329, 1997.
3.
AntoineJM and DiplockAT. Validation of markers for their relevance to health and disease. Free Radic Res, 33: S117–S120, 2000.
4.
ArmstrongNC, PagangaG, BrunnerE, MillerNJ, NanchahalK, ShipleyM, Rice-EvansCA, MarmotMG, and DiplockAT. Reference values for α-tocopherol and β-carotene in the Whitehall II Study. Free Radic Res, 27: 207–219, 1997.
5.
AruomaOI, HalliwellB, and DizdarogluM. Iron ion-dependent modification of bases in DNA by the superoxide radical-generating system hypoxanthine/xanthine oxidase. J Biol Chem, 264: 13024–13028, 1989.
6.
AruomaOI, HalliwellB, GajewskiE, and DizdarogluM. Copper-ion-dependent damage to the bases in DNA in the presence of hydrogen peroxide. Biochem J, 273: 601–604, 1991.
7.
AruomaOI, HalliwellB, GajewskiE, and DizdarogluM. Damage to the bases in DNA induced by hydrogen peroxide and ferric ion chelates. J Biol Chem, 264: 20509–20512, 1989.
8.
AruomaOI, HalliwellB, HoeyBM, and ButlerJ. The antioxidant action of N-acetylcysteine: its reaction with hydrogen peroxide, hydroxyl radical, superoxide, and hypochlorous acid. Free Radic Biol Med, 6: 593–597, 1989.
9.
AruomaOI, SpencerJPE, ButlerJ, and HalliwellB. Commentary: reaction of plant-derived and synthetic antioxidants with trichloromethylperoxyl radicals. Free Radic Res, 22: 187–190, 1995.
10.
AruomaOI, WasilM, HalliwellB, HoeyBM, and ButlerJ. The scavenging of oxidants by sulphasalazine and its metabolites. A possible contribution to their anti-inflammatory effects?. Biochem Pharmacol, 36: 3739–3742, 1987.
11.
BlakeDR, HallND, BaconPA, DieppePA, HalliwellB, and GutteridgeJM. Effect of a specific iron chelating agent on animal models of inflammation. Ann Rheum Dis, 42: 89–93, 1983.
12.
BlakeDR, HallND, BaconPA, DieppePA, HalliwellB, and GutteridgeJMC. The importance of iron in rheumatoid disease. Lancet, 318: 1142–1144, 1981.
13.
BorceaV, Nourooz-ZadehJ, WolffSP, KlevesathM, HofmannM, UrichH, WahlP, ZieglerR, TritschlerH, HalliwellB, and NawrothPP. α-Lipoic acid decreases oxidative stress even in diabetic patients with poor glycemic control and albuminuria. Free Radic Biol Med, 26: 1495–1500, 1999.
14.
ButlerJ and HalliwellB. Reaction of iron-EDTA chelates with the superoxide radical. Arch Biochem Biophys, 218: 174–178, 1982.
15.
BuzadžićB, SpasicM, SaičićZS, RadojičićR, HalliwellB, and PetrovićVM. Antioxidant defenses in the ground squirrel Citellus citellus 1. A comparison with the rat. Free Radic Biol Med, 9: 401–406, 1990.
16.
BuzadžićB, SpasićM, SaičićZS, RadojičićR, PetrovićVM, and HalliwellB. Antioxidant defenses in the ground squirrel Citellus citellus 2. The effect of hibernation. Free Radic Biol Med, 9: 407–413, 1990.
17.
CecchiniR, AruomaOI, and HalliwellB. The action of hydrogen peroxide on the formation of thiobarbituric acid-reactive material from microsomes, liposomes or fromDNA damaged by bleomycin or phenanthroline. Artefacts in the thiobarbituric acid test. Free Radic Res, 10: 245–258, 1990.
ClementMV, LongLH, RamalingamJ, and HalliwellB. The cytotoxicity of dopamine may be an artefact of cell culture. J Neurochem, 81: 414–421, 2002.
20.
CoghlanJG, FlitterWD, HolleyAE, NorellM, MitchellAG, IlsleyCD, and SlaterTF. Detection of free radicals and cholesterol hydroperoxides in blood taken from the coronary sinus of man during percutaneous transluminal coronary angioplasty. Free Radic Res, 14: 409–417, 1991.
21.
CoghlanJG, FlitterWD, PaulVE, MitchellAG, SlaterTF, and IlsleyCDJ. Direct relationship between ischaemic burden and myocardial release of products of lipid peroxidation in patients undergoing percutaneous transluminal coronary angioplasty. Coron Artery Dis, 5: 961–970, 1994.
22.
CrossAR, HigsonFK, JonesOT, HarperAM, and SegalAW. The enzymic reduction and kinetics of oxidation of cytochrome b-245 of neutrophils. Biochem J, 204: 479–485, 1982.
23.
CrossCE, HalliwellB, BorishET, PryorWA, AmesBN, SaulRL, McCordJM and HarmanD. Oxygen radicals and human disease. Ann Intern Med, 107: 526–545, 1987.
24.
CrossCE and HalliwellB. Evaluation of biomolecular damage by ozone. Methods Enzymol, 234: 252–256, 1994.
25.
CrossCE and HalliwellB. Nutrition and human disease: how much extra vitamin C might smokers need?. Lancet, 341: 1091, 1993.
26.
CrossCE, HalliwellB, and AllenA. Antioxidant protection: a function of tracheobronchial and gastrointestinal mucus. Lancet, 323: 1328–1330, 1984.
27.
CrossCE, MotchnikPA, BruenerBA, JonesDA, KaurH, AmesBN, and HalliwellB. Oxidative damage to plasma constituents by ozone. FEBS Lett, 298: 269–272, 1992.
28.
CrossCE, ReznickAZ, PackerL, DavisPA, SuzukiYJ, and HalliwellB. Oxidative damage to human plasma proteins by ozone. Free Radic Res, 15: 347–352, 1992.
29.
CrossCE, Van der VlietA, LouieS, ThieleJJ, and HalliwellB. Oxidative stress and antioxidants at biosurfaces: plants, skin, and respiratory tract surfaces. Environ Health Perspect, 106: 1241–1251, 1998.
30.
DaviesKJA, QuintanilhaAT, BrooksGA, and PackerL. Free radicals and tissue damage produced by exercise. Biochem Biophys Res Commun, 107: 1198–1205, 1982.
31.
DaviesMJ, ForniLG, and WillsonRL. Vitamin E analogue TroloxC. E.s.r. and pulse-radiolysis studies of free-radical reactions. Biochem J, 255: 513–522, 1988.
32.
DaviesMJ and SlaterTF. Studies on the metal-ion and lipoxygenase-catalysed breakdown of hydroperoxides using electron-spin-resonance spectroscopy. Biochem J, 245: 167–173, 1987.
33.
DaviesMJ and SlaterTF. Studies on the photolytic breakdown of hydroperoxides and peroxidized fatty acids by using electron spin resonance spectroscopy. Spin trapping of alkoxyl and peroxyl radicals in organic solvents. Biochem J, 240: 789–795, 1986.
34.
DaviesMJ and SlaterTF. Electron spin resonance spin trapping studies on the photolytic generation of halocarbon radicals. Chem Biol Interact, 58: 137–147, 1986.
35.
DaviesMJ and SlaterTF. The use of electron-spin-resonance techniques to detect free-radical formation and tissue damage. Proc Nutr Soc, 47: 397–405, 1988.
36.
DexterDT, HolleyAE, FlitterWD, SlaterTF, WellsFR, DanielSE, LeesAJ, JennerP, and MarsdenCD. Increased levels of lipid hydroperoxides in the parkinsonian substantia nigra: an HPLC andESR. study. Mov Disord, 9: 92–97, 1994.
37.
DexterDT and JennerP. Parkinson disease: from pathology to molecular disease mechanisms. Free Radic Biol Med, 62: 132–144, 2013.
38.
DiplockAT. Erratum: will the “good fairies” please prove to us that vitamin E lessens human degenerative disease? (Free Radical Research 26. (565–583)). Free Radic Res, 27: 511–532, 1997.
39.
EiserichJP, ButlerJ, Van der VlietA, CrossCE, and HalliwellB. Nitric oxide rapidly scavenges tyrosine and tryptophan radicals. Biochem J, 310: 745–749, 1995.
40.
EiserichJP, Van der VlietA, HalliwellB, and CrossCE. Interactions of diesel engine emissions with extracellular biological fluids. Biochem Soc Trans, 23: 238S, 1995.
41.
EiserichJP, CrossCE, JonesAD, HalliwellB, and Van der VlietA. Formation of nitrating and chlorinating species by reaction of nitrite with hypochlorous acid. A novel mechanism for nitric oxide-mediated protein modification. J Biol Chem, 271: 19199–19208, 1996.
42.
EiserichJP, HristovaM, CrossCE, JonesAD, FreemanBA, HalliwellB, and Van Der VlietA. Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils. Nature, 391: 393–397, 1998.
43.
EiserichJP, Van Der VlietA, HandelmanGJ, HalliwellB, and CrossCE. Dietary antioxidants and cigarette smoke-induced biomolecular damage: a complex interaction. Am J Clin Nutr, 62: 1490S–1500S, 1995.
44.
EnglandTG, JennerA, AruomaOI, and HalliwellB. Determination of oxidativeDNA base damage by gas chromatography-mass spectrometry. Effect of derivatization conditions on artifactual formation of certain base oxidation products. Free Radic Res, 29: 321–330, 1998.
45.
EverettSA, DennisMF, PatelKB, MaddixS, KunduSC, and WillsonRL. Scavenging of nitrogen dioxide, thiyl, and sulfonyl free radicals by the nutritional antioxidant β-carotene. J Biol Chem, 271: 3988–3994, 1996.
46.
FergerB, RoseS, JennerA, HalliwellB, and JennerP. 6-Hydroxydopamine increases hydroxyl free radical production and DNA damage in rat striatum. Neuroreport, 12: 1155–1159, 2001.
47.
FergerB, ThemannC, RoseS, HalliwellB, and JennerP. 6-Hydroxydopamine increases the hydroxylation and nitration of phenylalanine in vivo: implication of peroxynitrite formation. J Neurochem, 78: 509–514, 2001.
48.
ForniLG and WillsonRL. Electron and hydrogen atom transfer reactions: determination of free radical redox potentials by pulse radiolysis. Methods Enzymol, 105: 179–188, 1984.
49.
FoyerCH and HalliwellB. The presence of glutathione and glutathione reductase in chloroplasts: a proposed role in ascorbic acid metabolism. Planta, 133: 21–25, 1976.
50.
FrostMT, HalliwellB, and MooreKP. Analysis of free and protein-bound nitrotyrosine in human plasma by a gas chromatography/mass spectrometry method that avoids nitration artifacts. Biochem J, 345: 453–458, 2000.
51.
Fuentes-LemusE, HägglundP, López-AlarcónC, and DaviesMJ. Oxidative crosslinking of peptides and proteins: mechanisms of formation, detection, characterization and quantification. Molecules, 27: 15, 2022.
52.
GarlickPB, DaviesMJ, HearseDJ, and SlaterTF. Direct detection of free radicals in the reperfused rat heart using electron spin resonance spectroscopy. Circ Res, 61: 757–760, 1987.
53.
GopaulNK, HalliwellB, and ÄnggårdEE. Measurement of plasma F2-isoprostanes as an index of lipid peroxidation does not appear to be confounded by diet. Free Radic Res, 33: 115–127, 2000.
54.
GowerJD and WillsED. The oxidation of benzo[a]pyrene mediated by lipid peroxidation in irradiated synthetic diets. Int J Radiat Biol, 49: 471–484, 1985.
55.
GrootveldM and HalliwellB. Measurement of allantoin and uric acid in human body fluids. A potential index of free-radical reactions in vivo?. Biochem J, 243: 803–808, 1987.
56.
GrootveldM and HalliwellB. Aromatic hydroxylation as a potential measure of hydroxyl-radical formation in vivo. Identification of hydroxylated derivatives of salicylate in human body fluids. Biochem J, 237: 499–504, 1986.
57.
GruberJ, NgLF, PoovathingalSK, and HalliwellB. Deceptively simple but simply deceptive - Caenorhabditis elegans lifespan studies: considerations for aging and antioxidant effects. FEBS Lett, 583: 3377–3387, 2009.
58.
GruberJ, TangSY, JennerAM, MudwayI, BlombergA, BehndigA, KasimanK, LeeCYJ, SeetRCS, ZhangW, ChenC, KellyFJ, and HalliwellB. Allantoin in human plasma, serum, and nasal-lining fluids as a biomarker of oxidative stress: avoiding artifacts and establishing real in vivo concentrations. Antioxid Redox Signal, 11: 1767–1776, 2009.
59.
GutteridgeJM and HalliwellB. The deoxyribose assay: an assay both for “free” hydroxyl radical and for site-specific hydroxyl radical production. Biochem J, 253: 932–933, 1988.
60.
GutteridgeJMC, PatersonSK, SegalAW, and HalliwellB. Inhibition of lipid peroxidation by the iron-binding protein lactoferrin. Biochem J, 199: 259–261, 1981.
61.
GutteridgeJMC, RichmondR, and HalliwellB. Inhibition of the iron-catalysed formation of hydroxyl radicals from superoxide and of lipid peroxidation by desferrioxamine. Biochem J, 184: 469–472, 1979.
62.
HalliwellB. Superoxide dismutase: a contaminant of bovine catalase. Biochem J, 135: 379–381, 1973.
63.
HalliwellB. Superoxide-dependent formation of hydroxyl radicals in the presence of iron chelates. Is it a mechanism for hydroxyl radical production in biochemical systems?. FEBS Lett, 92: 321–326, 1978.
64.
HalliwellB. How I became a biochemist. IUBMB Life, 56: 569–570, 2004.
65.
HalliwellB. The wanderings of a free radical. Free Radic Biol Med, 46: 531–542, 2008.
66.
HalliwellB. An interview with Barry Halliwell. Trends Pharmacol Sci, 34: 301–302, 2013.
HalliwellB. Artefacts with ascorbate and other redox-active compounds in cell culture: epigenetic modifications, and cell killing due to hydrogen peroxide generation in cell culture media. Free Radic Res, 52: 907–909, 2018.
69.
HalliwellB. Reflections of an aging free radical. Free Radic Biol Med, 161: 234–245, 2020.
70.
HalliwellB.Commentary for “Oxygen free radicals and iron in relation to biology and medicine: some problems and concepts. Arch Biochem Biophys, 718: 109151, 2022.
71.
HalliwellB, ChiricoS, CrawfordMA, BjerveKS, and GeyKF. Lipid peroxidation: its mechanism, measurement, and significance. Am J Clin Nutr, 57: 715S–725S, 1993.
72.
HalliwellB and GutteridgeJM. Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem J, 219: 1–14, 1984.
73.
HalliwellB, AdhikaryA, DingfelderM, and DizdarogluM. Hydroxyl radical is a significant player in oxidative DNA damage in vivo. Chem Soc Rev, 50: 8355–8360, 2021.
74.
HalliwellB, GrootveldM, and GutteridgeJMC. Methods for the measurement of hydroxyl radicals in biochemical systems: deoxyribose degradation and aromatic hydroxylation. Methods Biochem Anal, 33: 59–90, 2006.
75.
HalliwellB and GutteridgeJMC. The antioxidants of human extracellular fluids. Arch Biochem Biophys, 280: 1–8, 1990.
76.
HalliwellB and GutteridgeJMC. Oxygen free radicals and iron in relation to biology and medicine: some problems and concepts. Arch Biochem Biophys, 246: 501–514, 1986.
77.
HalliwellB and GutteridgeJMC. The importance of free radicals and catalytic metal ions in human diseases. Mol Aspects Med, 8: 89–193, 1985.
78.
HalliwellB and GutteridgeJMC. Biologically relevant metal ion-dependent hydroxyl radical generation: an update. FEBS Lett, 307: 108–112, 1992.
79.
HalliwellB, GutteridgeJMC, and AruomaOI. The deoxyribose method: a simple “test-tube” assay for determination of rate constants for reactions of hydroxyl radicals. Anal Biochem, 165: 215–219, 1987.
80.
HalliwellB, HoultJR, and BlakeDR. Oxidants, inflammation, and anti-inflammatory drugs. FASEB J, 2: 2867–2873, 1988.
81.
HalliwellB, HuML, LouieS, DuvallTR, TarkingtonBK, MotchnikP, and CrossCE. Interaction of nitrogen dioxide with human plasma Antioxidant depletion and oxidative damage. FEBS Lett, 313: 62–66, 1992.
82.
HalliwellB and KaurH. Hydroxylation of salicylate and phenylalanine as assays for hydroxyl radicals: a cautionary note visited for the third time. Free Radic Res, 27: 239–244, 1997.
83.
HalliwellB and LeeCYJ. Using isoprostanes as biomarkers of oxidative stress: some rarely considered issues. Antioxid Redox Signal, 13: 145–156, 2010.
84.
HalliwellB and WhitemanM. Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean?. Br J Pharmacol, 142: 231–255, 2004.
85.
HawkinsCL and DaviesMJ. Detection, identification, and quantification of oxidative protein modifications. J Biol Chem, 294: 19683–19708, 2019.
86.
HiderRC and HoffbrandAV. The role of deferiprone in iron chelation. N Engl J Med, 379: 2140–2150, 2018.
87.
HoeyBM, ButlerJ, and HalliwellB. On the specificity of allopurinol and oxypurinol as inhibitors of xanthine oxidase. A pulse radiolysis determination of rate constants for reaction of allopurinol and oxypurinol with hydroxyl radicals. Free Radic Res, 4: 259–263, 1988.
88.
HolleyAE and SlaterTF. Measurement of lipid hydroperoxides in normal human blood plasma using HPLC-chemiluminescence linked to a diode array detector for measuring conjugated dienes. Free Radic Res, 15: 51–63, 1991.
89.
HyunDH, GrayDA, HalliwellB, and JennerP. Interference with ubiquitination causes oxidative damage and increased protein nitration: implications for neurodegenerative diseases. J Neurochem, 90: 422–430, 2004.
90.
HyunDH, LeeMH, HalliwellB, and JennerP. Proteasomal inhibition causes the formation of protein aggregates containing a wide range of proteins, including nitrated proteins. J Neurochem, 86: 363–373, 2003.
91.
HyunDH, LeeMH, HalliwellB, and JennerP. Effect of overexpression of wild-type or mutant parkin on the cellular response induced by toxic insults. J Neurosci Res, 82: 232–244, 2005.
92.
HyunDH, LeeMH, HattoriN, KuboSI, MizunoY, HalliwellB, and JennerP. Effect of wild-type or mutant parkin on oxidative damage, nitric oxide, antioxidant defenses, and the proteasome. J Biol Chem, 277: 28572–28577, 2002.
93.
JacksonMJ, StrettonC, and McArdleA. Hydrogen peroxide as a signal for skeletal muscle adaptations to exercise: what do concentrations tell us about potential mechanisms?. Redox Biol, 35: 101484, 2020.
94.
JeffreyS, Isaac SamrajP, and Sundara RajB. Therapeutic benefits of alpha-lipoic acid supplementation in diabetes mellitus: a narrative review. J Diet Suppl, 19: 566–586, 2022.
95.
JennerP. Altered mitochondrial function, iron metabolism and glutathione levels inParkinson's. disease. Acta Neurol Scand Suppl, 87: 6–13, 1993.
96.
KaurH, EdmondsSE, BlakeDR, and HalliwellB. Hydroxyl radical generation by rheumatoid blood and knee joint synovial fluid. Ann Rheum Dis, 55: 915–920, 1996.
97.
KaurH, FagerheimI, GrootveldM, PuppoA, and HalliwellB. Aromatic hydroxylation of phenylalanine as an assay for hydroxyl radicals: application to activated human neutrophils and to the heme protein leghemoglobin. Anal Biochem, 172: 360–367, 1988.
98.
KaurH and HalliwellB. Aromatic hydroxylation of phenylalanine as an assay for hydroxyl radicals. Measurement of hydroxyl radical formation from ozone and in blood from premature babies using improvedHPLC. methodology. Anal Biochem, 220: 11–15, 1994.
99.
KaurH and HalliwellB. Action of biologically-relevant oxidizing species upon uric acid. Identification of uric acid oxidation products. Chem Biol Interact, 73: 235–247, 1990.
100.
KaurH, LyrasL, JennerP, and HalliwellB. Artefacts in HPLC detection of 3-nitrotyrosine in human brain tissue. J Neurochem, 70: 2220–2223, 1998.
101.
KellyR, Poo YeoK, IsaacH, LeeCY, HuangSH, TengL, HalliwellB, and WiseS. Lack of effect of acute oral ingestion of vitaminC on oxidative stress, arterial stiffness or blood pressure in healthy subjects. Free Radic Res, 42: 514–522, 2008.
102.
LeeCYJ, HuangSH, JennerAM, and HalliwellB. Measurement of F2-isoprostanes, hydroxyeicosatetraenoic products, and oxysterols from a single plasma sample. Free Radic Biol Med, 44: 1314–1322, 2008.
103.
LeeCYJ, IsaacHB, WangH, HuangSH, LongLH, JennerAM, KellyRP, and HalliwellB. Cautions in the use of biomarkers of oxidative damage; the vascular and antioxidant effects of dark soy sauce in humans. Biochem Biophys Res Commun, 344: 906–911, 2006.
104.
LeeMH, HyunDH, HalliwellB, and JennerP. Effect of overexpression of wild-type and mutant Cu/Zn-superoxide dismutases on oxidative stress and cell death induced by hydrogen peroxide, 4-hydroxynonenal or serum deprivation: potentiation of injury byALS-related mutant superoxide dismutases and protection by. Bcl-2. J Neurochem, 78: 209–220, 2001.
105.
LeeM, HyunDH, HalliwellB, and JennerP. Effect of the overexpression of wild-type or mutant α-synuclein on cell susceptibility to insult. J Neurochem, 76: 998–1009, 2001.
106.
LeeM, HyunDH, JennerP, and HalliwellB. Effect of proteasome inhibition on cellular oxidative damage, antioxidant defences and nitric oxide production. J Neurochem, 78: 32–41, 2001.
107.
LeeM, HyunDH, JennerP, and HalliwellB. Effect of overexpression of wild-type and mutant Cu/Zn-superoxide dismutases on oxidative damage and antioxidant defences: relevance toDown's syndrome and familial amyotrophic lateral. sclerosis. J Neurochem, 76: 957–965, 2001.
108.
LevineAP and SegalAW. The NADPH oxidase and microbial killing by neutrophils, with a particular emphasis on the proposed antimicrobial role of myeloperoxidase within the phagocytic vacuole. Microbiol Spectr, 4: 4, 2016.
109.
LimKHC, LeeCYJ, EarnestA, SeetRCS, and HalliwellB. Does radiotherapy increase oxidative stress?A study with nasopharyngeal cancer patients revealing anomalies in isoprostanes. measurements. Free Radic Res, 44: 1064–1071, 2010.
110.
LimKS, HuangSH, JennerA, WangH, TangSY, and HalliwellB. Potential artifacts in the measurement of DNA deamination. Free Radic Biol Med, 40: 1939–1948, 2006.
111.
LouieS, HalliwellB, and CrossCE. Adult respiratory distress syndrome: a radical perspective. Adv Pharmacol, 38: 457–490, 1996.
112.
LyrasL, CairnsNJ, JennerA, JennerP, and HalliwellB. An assessment of oxidative damage to proteins, lipids, and DNA in brain from patients withAlzheimer's. disease. J Neurochem, 68: 2061–2069, 1997.
113.
LyrasL, PerryRH, PerryEK, IncePG, JennerA, JennerP, and HalliwellB. Oxidative damage to proteins, lipids, and DNA in cortical brain regions from patients with dementia withLewy. bodies. J Neurochem, 71: 302–312, 1998.
114.
MatayatsukC, LeeCYJ, KalpravidhRW, SirankaprachaP, WilairatP, FucharoenS, and HalliwellB. Elevated F2-isoprostanes in thalassemic patients. Free Radic Biol Med, 43: 1649–1655, 2007.
115.
McCordJM and FridovichI. The reduction of cytochrome c by milk xanthine oxidase. J Biol Chem, 243: 5753–5760, 1968.
116.
McCordJM and FridovichI. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem, 244: 6049–6055, 1969.
117.
McNaughtKSP, OlanowCW, HalliwellB, IsacsonO, and JennerP. Failure of the ubiquitin proteasome system in Parkinson's disease. Nat Rev Neurosci, 2: 589–594, 2001.
118.
McNeillJM, GowerJD, and WillsED. The formation of the ultimate carcinogen of benzo(a)pyrene during non-enzymic lipid peroxidation. Biochem Pharmacol, 34: 4066–4068, 1985.
119.
McNultyMJ, SilbersteinDZ, KuhnBT, PadgettHS, NandiS, McDonaldKA, and CrossCE. Alpha-1 antitrypsin deficiency and recombinant protein sources with focus on plant sources: updates, challenges and perspectives. Free Radic Biol Med, 163: 10–30, 2021.
120.
MilneGL and MorrowJD. Isoprostanes and related compounds: update 2006. Antioxid Redox Signal, 8: 1379–1384, 2006.
121.
MilneGL, YinH, and MorrowJD. Human biochemistry of the isoprostane pathway. J Biol Chem, 283: 15533–15537, 2008.
122.
MoiniH, PackerL, and SarisNEL. Antioxidant and prooxidant activities of α-lipoic acid and dihydrolipoic acid. Toxicol Appl Pharmacol, 182: 84–90, 2002.
123.
MurphyMP, BayirH, BelousovV, ChangCJ, DaviesKJ, DaviesMJ, DickTP, FinkelT, FormanHJ, GemsD, Janssen-HeiningerY, KaganVE, KalyanaramanB, LarssonNG, MileGL, NyströmT, PoulsenHE, RadiR, RemmenHV, SchumackerPT, ThornalleyPJ, ToyokuniS, WinterbournCC, YinH, and HalliwellB. Guidelines for measuring reactive oxygen species and oxidative damage in cells and in vivo. Nat Metab, 4: 651–662, 2022.
124.
Nourooz-ZadehJ, HalliwellB, and ÄnggårdEE. Evidence for the formation of F3−isoprostanes during peroxidation of eicosapentaenoic acid. Biochem Biophys Res Commun, 236: 467–472, 1997.
125.
Nourooz-ZadehJ, LiuEHC, YhlenB, ÄnggårdEE, and HalliwellB. F4-isoprostanes as specific marker of docosahexaenoic acid peroxidation in Alzheimer's disease. J Neurochem, 72: 734–740, 1999.
126.
OldreiveC, ZhaoK, PagangaG, HalliwellB, and Rice-EvansC. Inhibition of nitrous acid-dependent tyrosine nitration and DNA base deamination by flavonoids and other phenolic compounds. Chem Res Toxicol, 11: 1574–1579, 1998.
127.
O'NeillCA, HalliwellB, van der VlietA, DavisPA, PackerL, TritschlerH, StrohmanWJ, RielandT, CrossCE, and ReznickAZ. Aldehyde-induced protein modifications in human plasma: protection by glutathione and dihydrolipoic acid. J Lab Clin Med, 124: 359–370, 1994.
128.
O'NeillCA, FuLW, HalliwellB, and LonghurstJC. Hydroxyl radical production during myocardial ischemia and reperfusion in cats. Am J Physiol Hear Circ Physiol, 271: H660–H667, 1996.
129.
O'NeillCA, StebbinsCL, BonigutS, HalliwellB, and LonghurstJC. Production of hydroxyl radicals in contracting skeletal muscle of cats. J Appl Physiol, 81: 1197–1206, 1996.
130.
O'ReillyJD, MalletAI, McAnlisGT, YoungIS, HalliwellB, SandersTAB, and WisemanH. Consumption of flavonoids in onions and black tea: lack of effect on F2-isoprostanes and autoantibodies to oxidized LDL in healthy humans. Am J Clin Nutr, 73: 1040–1044, 2001.
131.
PackerJE, SlaterTF, and WillsonRL. Direct observation of a free radical interaction between vitamin E and vitamin C. Nature, 278: 737–738, 1979.
132.
PackerL, OngCN, and HalliwellB. Herbal and Traditional Medicine: Biomolecular and Clinical Aspects. Marcel Dekker, New York, 2004.
133.
PackerL and CadenasE. Lipoic acid: energy metabolism and redox regulation of transcription and cell signaling. J Clin Biochem Nutr, 48: 26–32, 2011.
134.
PackerL, CadenasE, and DaviesKJA. Free radicals and exercise: an introduction. Free Radic Biol Med, 44: 123–125, 2008.
135.
PackerL, KraemerK, and RimbachG. Molecular aspects of lipoic acid in the prevention of diabetes complications. Nutrition, 17: 888–895, 2001.
136.
PagangaG, Al-HashimH, KhodrH, ScottBC, AruomaOI, HiderRC, HalliwellB, and Rice-EvansCA. Mechanisms of antioxidant activities of quercetin and catechin. Redox Rep, 2: 359–364, 1996.
137.
PannalaA, RazaqR, HalliwellB, SinghS, and Rice-EvansCA. Inhibition of peroxynitrite dependent tyrosine nitration by hydroxycinnamates: nitration or electron donation?. Free Radic Biol Med, 24: 594–606, 1998.
138.
PasternackRF and HalliwellB. Superoxide dismutase activities of an iron porphyrin and other iron complexes. J Am Chem Soc, 101: 1026–1031, 1979.
139.
PedreB, BarayeuU, EzeriņaD, and DickTP. The mechanism of action of N-acetylcysteine (NAC): the emerging role of H2S and sulfane sulfur species. Pharmacol Ther, 228: 107916, 2021.
140.
PoliG, CheesemanKH, BiasiF, ChiarpottoE, DianzaniMU, EsterbauerH, and SlaterTF. Promethazine inhibits the formation of aldehydic products of lipid peroxidation but not covalent binding resulting from the exposure of rat liver fractions to CCl4. Biochem J, 264: 527–532, 1989.
141.
PrützWA, ButlerJ, LandEJ, and SwallowAJ. The role of sulphur peptide functions in free radical transfer: a pulse radiolysis study. Int J Radiat Biol, 55: 539–556, 1989.
142.
PughJN, StrettonC, McDonaghB, BrownridgeP, McArdleA, JacksonMJ, and CloseGL. Exercise stress leads to an acute loss of mitochondrial proteins and disruption of redox control in skeletal muscle of older subjects: an underlying decrease in resilience with aging?. Free Radic Biol Med, 177: 88–99, 2021.
ReddyS, HalliwellB, JonesAD, and LonghurstJC. The use of phenylalanine to detect hydroxyl radical production in vivo: a cautionary note. Free Radic Biol Med, 27: 1465, 1999.
145.
RehmanA, CollisCS, YangM, KellyM, DiplockAT, HalliwellB, and Rice-EvansC. The effects of iron and vitamin C co-supplementation on oxidative damage to DNA in healthy volunteers. Biochem Biophys Res Commun, 246: 293–298, 1998.
146.
ReznickAZ, CrossCE, HuML, SuzukiYJ, KhwajaS, SafadiA, MotchnikPA, PackerL, and HalliwellB. Modification of plasma proteins by cigarette smoke as measured by protein carbonyl formation. Biochem J, 286: 607–611, 1992.
147.
RichmondR, HalliwellB, ChauhanJ, and DarbreA. Superoxide-dependent formation of hydroxyl radicals: detection of hydroxyl radicals by the hydroxylation of aromatic compounds. Anal Biochem, 118: 328–335, 1981.
148.
ScottBC, AruomaOI, EvansPJ, O'NeillC, Van Der VlietA, CrossCE, TritschlerH, and HalliwellB. Lipoic and dihydrolipoic acids as antioxidants. A critical evaluation. Free Radic Res, 20: 119–133, 1994.
149.
SeetRCS, LeeCYJ, ChanBPL, SharmaVK, TeohHL, VenketasubramanianN, LimECH, ChongWL, LooiWF, HuangSH, OngBKC, and HalliwellB. Oxidative damage in ischemic stroke revealed using multiple biomarkers. Stroke, 42: 2326–2329, 2011.
150.
SeetRCS, LeeCYJ, LimECH, TanJJH, QuekAML, ChongWL, LooiWF, HuangSH, WangH, ChanYH, and HalliwellB. Oxidative damage in Parkinson disease: measurement using accurate biomarkers. Free Radic Biol Med, 48: 560–566, 2010.
151.
SeetRCS, LeeCYJ, LokeWM, HuangSH, HuangH, LooiWF, ChewES, QuekAML, LimECH, and HalliwellB. Biomarkers of oxidative damage in cigarette smokers: which biomarkers might reflect acute versus chronic oxidative stress?. Free Radic Biol Med, 50: 1787–1793, 2011.
152.
SharmanMJ, GyengesiE, LiangH, ChatterjeeP, KarlT, LiQX, WenkMR, HalliwellB, MartinsRN, and MünchG. Assessment of diets containing curcumin, epigallocatechin-3-gallate, docosahexaenoic acid and α-lipoic acid on amyloid load and inflammation in a male transgenic mouse model of Alzheimer's disease: are combinations more effective?. Neurobiol Dis, 124: 505–519, 2019.
153.
ShuterSL, DaviesMJ, GarlickPB, HearseDJ, and SlaterTF. Studies on the effects of antioxidants and inhibitors of radical generation on free radical production in the reperfused rat heart using electron spin resonance spectroscopy. Free Radic Res, 9: 223–232, 1990.
SpencerJPE, Abd El MohsenMM, and Rice-EvansC. Cellular uptake and metabolism of flavonoids and their metabolites: implications for their bioactivity. Arch Biochem Biophys, 423: 148–161, 2004.
156.
SpencerJPE, JennerA, ChimelK, AruomaOI, CrossCE, WuR, and HalliwellB. DNA damage in human respiratory tract epithelial cells: damage by gas phase cigarette smoke apparently involves attack by reactive nitrogen species in addition to oxygen radicals. FEBS Lett, 375: 179–182, 1995.
157.
StahlGL, HalliwellB, and LonghurstJC. Hydrogen peroxide-induced cardiovascular reflexes: role of hydroxyl radicals. Circ Res, 71: 295–302, 1992.
158.
SunJZ, KaurH, HalliwellB, LiXY, and BolliR. Use of aromatic hydroxylation of phenylalanine to measure production of hydroxyl radicals after myocardial ischemia in vivo: direct evidence for a pathogenetic role of the hydroxyl radical in myocardial stunning. Circ Res, 73: 534–549, 1993.
159.
TangXL, KaurH, SunJZ, QiuY, ParkSW, SchlemanM, HalliwellB, and BolliR. Effect of the hydrophilic α-tocopherol analog MDL 74,405 on detection of hydroxyl radicals in stunned myocardium in dogs. Am Heart J, 130: 940–948, 1995.
ToyokuniS, KongY, and MiD. Commentary for an article on photooxidation in isolated chloroplasts. Arch Biochem Biophys, 726: 109133, 2022.
162.
van der VlietA, EiserichJP, HalliwellB, and CrossCE. Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite: a potential additional mechanism of nitric oxide- dependent toxicity. J Biol Chem, 272: 7617–7625, 1997.
163.
van der VlietA, EiserichJP, MarelichGP, HalliwellB, and CrossCE. Oxidative stress in cystic fibrosis: does it occur and does it matter?. Adv Pharmacol, 38: 491–513, 1996.
164.
van der VlietA, EiserichJP, O'NeillCA, HalliwellB, and CrossCE. Tyrosine modification by reactive nitrogen species: a closer look. Arch Biochem Biophys, 319: 341–349, 1995.
165.
van Der VlietA, O'NeillCA, CrossCE, KoostraJM, VolzWG, HalliwellB, and LouieS. Determination of low-molecular-mass antioxidant concentrations in human respiratory tract lining fluids. Am J Physiol Lung Cell Mol Physiol, 276: L289–L296, 1999.
166.
WhitemanM, TritschlerH, and HalliwellB. Protection against peroxynitrite-dependent tyrosine nitration and α1-antiproteinase inactivation by oxidized and reduced lipoic acid. FEBS Lett, 379: 74–76, 1996.
167.
WickensDG, DaviesMJ, FairbankJ, TaySK, SlaterTF, and DormandyTL. Studies on cervical intraepithelial neoplasia: the level of octadeca-9,11-dienoic acid and measurement of free radical content by electron spin resonance spectroscopy. Am J Obstet Gynecol, 162: 854–858, 1990.
168.
WilliamsRJ, SpencerJPE, and Rice-EvansC. Flavonoids: antioxidants or signalling molecules?. Free Radic Biol Med, 36: 838–849, 2004.
169.
WillsED. Lipid peroxide formation in microsomes. The role of non-haem iron. Biochem J, 113: 325–332, 1969.
170.
WillsonRL, GilbertBC, MarshallPDR, and NormanROC. Metronidazole (“flagyl”): a pulse radiolysis and E.S.R. Study. Int J Radiat Biol, 26: 427–434, 1974.