References
- Luo H, Hanratty WP, Dearolf CR. An amino acid substitution in the Drosophila hopTum-l Jak kinase causes leukemia-like hematopoietic defects. Embo J. 1995;14(7):1412–20.
- Prasad KN. Micronutrients in protecting against lethal doses of ionizing radiation. Boca Raton (FL): CRC Press; 2019.
- Polyak E, Ostrovsky J, Peng M, Dingley SD, Tsukikawa M, Kwon YJ, McCormack SE, Bennett M, Xiao R, Seiler C, et al. N-acetylcysteine and vitamin E rescue animal longevity and cellular oxidative stress in pre-clinical models of mitochondrial complex I disease. Mol Genet Metab. 2018;123(4):449–62. doi:https://doi.org/10.1016/j.ymgme.2018.02.013.
- Selkoe DJ. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev. 2001;81(2):741–66. doi:https://doi.org/10.1152/physrev.2001.81.2.741.
- Bekris LM, Yu CE, Bird TD, Tsuang DW. Genetics of Alzheimer disease. J Geriatr Psychiatry Neurol. 2010;23(4):213–27. doi:https://doi.org/10.1177/0891988710383571.
- Bekris LM, Mata IF, Zabetian CP. The genetics of Parkinson disease. J Geriatr Psychiatry Neurol. 2010;23(4):228–42. doi:https://doi.org/10.1177/0891988710383572.
- Klein C, Westenberger A. Genetics of Parkinson's disease. Cold Spring Harb Perspect Med. 2012;2(1):a008888. doi:https://doi.org/10.1101/cshperspect.a008888.
- Cherian A, Divya KP. Genetics of Parkinson's disease. Acta Neurol Belg. 2020;120(6):1297–305. doi:https://doi.org/10.1007/s13760-020-01473-5.
- Crosiers D, Theuns J, Cras P, Van Broeckhoven C. Parkinson disease: insights in clinical, genetic and pathological features of monogenic disease subtypes. J Chem Neuroanat. 2011;42(2):131–41. doi:https://doi.org/10.1016/j.jchemneu.2011.07.003.
- Vrentas CE, Greenlee JJ, Foster GH, West J, Jahnke MM, Schmidt MT, Nicholson EM. Effects of a naturally occurring amino acid substitution in bovine PrP: a model for inherited prion disease in a natural host species. BMC Res Notes. 2017;10(1):759. doi:https://doi.org/10.1186/s13104-017-3085-8.
- Belay ED. Transmissible Spongiform encephalopathies. In: Quah SR, editor. International encyclopedia of public health. 2nd ed. New York: Academic Press; 2017. p. 206–11.
- Rawlins MD, Wexler NS, Wexler AR, Tabrizi SJ, Douglas I, Evans SJW, Smeeth L. The prevalence of Huntington's disease. Neuroepidemiology. 2016;46(2):144–53. doi:https://doi.org/10.1159/000443738.
- MacDonald ME, Ambrose CM, Duyao MP, Myers RH, Lin C, Srinidhi L, Barnes G, Taylor SA, James M, Groot N, MacFarlane, et al. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell. 1993;72(6):971–83. doi:https://doi.org/10.1016/0092-8674(93)90585-E.
- Snell RG, MacMillan JC, Cheadle JP, Fenton I, Lazarou LP, Davies P, MacDonald ME, Gusella JF, Harper PS, Shaw DJ, et al. Relationship between trinucleotide repeat expansion and phenotypic variation in Huntington's disease. Nat Genet. 1993;4(4):393–7. doi:https://doi.org/10.1038/ng0893-393.
- Furtado S, Suchowersky O, Rewcastle B, Graham L, Klimek ML, Garber A. Relationship between trinucleotide repeats and neuropathological changes in Huntington's disease. Ann Neurol. 1996;39(1):132–6. doi:https://doi.org/10.1002/ana.410390120.
- Ravina B, Romer M, Constantinescu R, Biglan K, Brocht A, Kieburtz K, Shoulson I, McDermott MP. The relationship between CAG repeat length and clinical progression in Huntington's disease. Mov Disord. 2008;23(9):1223–7. doi:https://doi.org/10.1002/mds.21988.
- Inusa BPD, Hsu LL, Kohli N, Patel A, Ominu-Evbota K, Anie KA, Atoyebi W. Sickle cell disease-genetics, pathophysiology, clinical presentation and treatment. Int J Neonatal Screen. 2019;5(2):20. doi:https://doi.org/10.3390/ijns5020020.
- CDC. Hemophilia facts. Atlanta (GA): CDC; 2020.
- Meraz-Rios MA, Franco-Bocanegra D, Toral Rios D, Campos-Pena V. Early onset Alzheimer's disease and oxidative stress. Oxid Med Cell Longev. 2014;2014:375968. doi:https://doi.org/10.1155/2014/375968.
- Muche A, Arendt T, Schliebs R. Oxidative stress affects processing of amyloid precursor protein in vascular endothelial cells. PLoS One. 2017;12(6):e0178127. doi:https://doi.org/10.1371/journal.pone.0178127.
- Cheignon C, Tomas M, Bonnefont-Rousselot D, Faller P, Hureau C, Collin F. Oxidative stress and the amyloid beta peptide in Alzheimer's disease. Redox Biol. 2018;14:450–64. doi:https://doi.org/10.1016/j.redox.2017.10.014.
- Yankner BA, Mesulam MM. Seminars in medicine of the Beth Israel Hospital, Boston. Beta-amyloid and the pathogenesis of Alzheimer's disease. N Engl J Med. 1991;325(26):1849–57. doi:https://doi.org/10.1056/NEJM199112263252605.
- Selkoe DJ. Cell biology of the amyloid beta-protein precursor and the mechanism of Alzheimer's disease. Annu Rev Cell Biol. 1994;10:373–403. doi:https://doi.org/10.1146/annurev.cb.10.110194.002105.
- Schubert D, Behl C, Lesley R, Brack A, Dargusch R, Sagara Y, Kimura H. Amyloid peptides are toxic via a common oxidative mechanism. Proc Natl Acad Sci USA. 1995;92(6):1989–93. doi:https://doi.org/10.1073/pnas.92.6.1989.
- Butterfield DA, Bush AI. Alzheimer's amyloid beta-peptide (1-42): involvement of methionine residue 35 in the oxidative stress and neurotoxicity properties of this peptide. Neurobiol Aging. 2004;25(5):563–8. doi:https://doi.org/10.1016/j.neurobiolaging.2003.12.027.
- Behl C, Davis J, Cole GM, Schubert D. Vitamin E protects nerve cells from amyloid beta protein toxicity. Biochem Biophys Res Commun. 1992;186(2):944–50. doi:https://doi.org/10.1016/0006-291x(92)90837-b.
- Yang X, Yang Y, Li G, Wang J, Yang ES. Coenzyme Q10 attenuates beta-amyloid pathology in the aged transgenic mice with Alzheimer presenilin 1 mutation. J Mol Neurosci. 2008;34(2):165–71. doi:https://doi.org/10.1007/s12031-007-9033-7.
- Moreira PI, Santos MS, Sena C, Nunes E, Seica R, Oliveira CR. CoQ10 therapy attenuates amyloid beta-peptide toxicity in brain mitochondria isolated from aged diabetic rats. Exp Neurol. 2005;196(1):112–9. doi:https://doi.org/10.1016/j.expneurol.2005.07.012.
- Ringman JM, Fithian AT, Gylys K, Cummings JL, Coppola G, Elashoff D, Pratico D, Moskovitz J, Bitan G. Plasma methionine sulfoxide in persons with familial Alzheimer's disease mutations. Dement Geriatr Cogn Disord. 2012;33(4):219–25. doi:https://doi.org/10.1159/000338546.
- Lee M, Hyun D, Halliwell B, Jenner P. Effect of the overexpression of wild-type or mutant alpha-synuclein on cell susceptibility to insult. J Neurochem. 2001;76(4):998–1009. doi:https://doi.org/10.1046/j.1471-4159.2001.00149.x.
- Hyun DH, Lee M, Halliwell B, Jenner P. Effect of overexpression of wild-type or mutant parkin on the cellular response induced by toxic insults. J Neurosci Res. 2005;82(2):232–44. doi:https://doi.org/10.1002/jnr.20638.
- Loeffler DA, Klaver AC, Coffey MP, Aasly JO, LeWitt PA. Increased oxidative stress markers in cerebrospinal fluid from healthy subjects with Parkinson's disease-associated LRRK2 gene mutations. Front Aging Neurosci. 2017;9:89.
- Barodia SK, Creed RB, Goldberg MS. Parkin and PINK1 functions in oxidative stress and neurodegeneration. Brain Res Bull. 2017;133:51–9. doi:https://doi.org/10.1016/j.brainresbull.2016.12.004.
- Dodson MW, Guo M. Pink1, Parkin, DJ-1 and mitochondrial dysfunction in Parkinson's disease. Curr Opin Neurobiol. 2007;17(3):331–7. doi:https://doi.org/10.1016/j.conb.2007.04.010.
- Varcin M, Bentea E, Michotte Y, Sarre S. Oxidative stress in genetic mouse models of Parkinson's disease. Oxid Med Cell Longev. 2012;2012:624925. doi:https://doi.org/10.1155/2012/624925.
- Brown DR, Wong BS, Hafiz F, Clive C, Haswell SJ, Jones IM. Normal prion protein has an activity like that of superoxide dismutase. Biochem J. 1999;344 Pt 1:1–5.
- Minghetti L, Cardone F, Greco A, Puopolo M, Levi G, Green AJE, Knight R, Pocchiari M. Increased CSF levels of prostaglandin E(2) in variant Creutzfeldt-Jakob disease. Neurology. 2002;58(1):127–9. doi:https://doi.org/10.1212/wnl.58.1.127.
- Miller E, Morel A, Saso L, Saluk J. Isoprostanes and neuroprostanes as biomarkers of oxidative stress in neurodegenerative diseases. Oxid Med Cell Longev. 2014;2014:572491. doi:https://doi.org/10.1155/2014/572491.
- Bleich S, Kropp S, Degner D, Zerr I, Pilz J, Gleiter CH, Otto M, Rüther E, Kretzschmar HA, Wiltfang J, et al. Creutzfeldt-Jakob disease and oxidative stress. Acta Neurol Scand. 2000;101(5):332–4. doi:https://doi.org/10.1034/j.1600-0404.2000.9s290a.x.
- Prasad KN, Bondy SC. Oxidative and inflammatory events in prion diseases: can they be therapeutic targets? Curr Aging Sci. 2019;11(4):216–25. doi:https://doi.org/10.2174/1874609812666190111100205.
- Brazier MW, Lewis V, Ciccotosto GD, Klug GM, Lawson VA, Cappai R, Ironside JW, Masters CL, Hill AF, White AR, et al. Correlative studies support lipid peroxidation is linked to PrP(res) propagation as an early primary pathogenic event in prion disease. Brain Res Bull. 2006;68(5):346–54. doi:https://doi.org/10.1016/j.brainresbull.2005.09.010.
- Arlt S, Kontush A, Zerr I, Buhmann C, Jacobi C, Schroter A, Poser S, Beisiegel U. Increased lipid peroxidation in cerebrospinal fluid and plasma from patients with Creutzfeldt-Jakob disease. Neurobiol Dis. 2002;10(2):150–6. doi:https://doi.org/10.1006/nbdi.2002.0496.
- Zheng J, Winderickx J, Franssens V, Liu B. A mitochondria-associated oxidative stress perspective on Huntington's disease. Front Mol Neurosci. 2018;11:329. doi:https://doi.org/10.3389/fnmol.2018.00329.
- Klepac N, Relja M, Klepac R, Hecimovic S, Babic T, Trkulja V. Oxidative stress parameters in plasma of Huntington's disease patients, asymptomatic Huntington's disease gene carriers and healthy subjects: a cross-sectional study. J Neurol. 2007;254(12):1676–83. doi:https://doi.org/10.1007/s00415-007-0611-y.
- Duran R, Barrero FJ, Morales B, Luna JD, Ramirez M, Vives F. Oxidative stress and plasma aminopeptidase activity in Huntington's disease. J Neural Transm (Vienna). 2010;117(3):325–32. doi:https://doi.org/10.1007/s00702-009-0364-0.
- Chen CM, Wu YR, Cheng ML, Liu JL, Lee YM, Lee PW, Soong BW, Chiu DT. Increased oxidative damage and mitochondrial abnormalities in the peripheral blood of Huntington's disease patients. Biochem Biophys Res Commun. 2007;359(2):335–40. doi:https://doi.org/10.1016/j.bbrc.2007.05.093.
- Queiroz RF, Lima ES. Oxidative stress in sickle cell disease. Rev Bras Hematol Hemoter. 2013;35(1):16–7. doi:https://doi.org/10.5581/1516-8484.20130008.
- Belcher JD, Beckman JD, Balla G, Balla J, Vercellotti G. Heme degradation and vascular injury. Antioxid Redox Signal. 2010;12(2):233–48. doi:https://doi.org/10.1089/ars.2009.2822.
- Chirico EN, Pialoux V. Role of oxidative stress in the pathogenesis of sickle cell disease. IUBMB Life. 2012;64(1):72–80. doi:https://doi.org/10.1002/iub.584.
- Aslan M, Thornley-Brown D, Freeman BA. Reactive species in sickle cell disease. Ann N Y Acad Sci. 2000;899:375–91. doi:https://doi.org/10.1111/j.1749-6632.2000.tb06201.x.
- Osarogiagbon UR, Choong S, Belcher JD, Vercellotti GM, Paller MS, Hebbel RP. Reperfusion injury pathophysiology in sickle transgenic mice. Blood. 2000;96(1):314–20.
- Malhotra JD, Miao H, Zhang K, Wolfson A, Pennathur S, Pipe SW, Kaufman RJ. Antioxidants reduce endoplasmic reticulum stress and improve protein secretion. Proc Natl Acad Sci USA. 2008;105(47):18525–30. doi:https://doi.org/10.1073/pnas.0809677105.
- Ringman JM, Elashoff D, Geschwind DH, Welsh BT, Gylys KH, Lee C, Cummings JL, Cole GM. Plasma signaling proteins in persons at genetic risk for Alzheimer disease: influence of APOE genotype. Arch Neurol. 2012;69(6):757–64. doi:https://doi.org/10.1001/archneurol.2012.277.
- Ringman JM, Schulman H, Becker C, Jones T, Bai Y, Immermann F, Cole G, Sokolow S, Gylys K, Geschwind DH, et al. Proteomic changes in cerebrospinal fluid of presymptomatic and affected persons carrying familial Alzheimer disease mutations. Arch Neurol. 2012;69(1):96–104. doi:https://doi.org/10.1001/archneurol.2011.642.
- Jeong JK, Moon MH, Bae BC, Lee YJ, Seol JW, Kang HS, Kim JS, Kang SJ, Park SY. Autophagy induced by resveratrol prevents human prion protein-mediated neurotoxicity. Neurosci Res. 2012;73(2):99–105. doi:https://doi.org/10.1016/j.neures.2012.03.005.
- Brazier MW, Doctrow SR, Masters CL, Collins SJ. A manganese-superoxide dismutase/catalase mimetic extends survival in a mouse model of human prion disease. Free Radic Biol Med. 2008;45(2):184–92. doi:https://doi.org/10.1016/j.freeradbiomed.2008.04.006.
- Mizrahi M, Friedman-Levi Y, Larush L, Frid K, Binyamin O, Dori D, Fainstein N, Ovadia H, Ben-Hur T, Magdassi S, et al. Pomegranate seed oil nanoemulsions for the prevention and treatment of neurodegenerative diseases: the case of genetic CJD. Nanomedicine. 2014;10(6):1353–63. doi:https://doi.org/10.1016/j.nano.2014.03.015.
- Rambold AS, Miesbauer M, Olschewski D, Seidel R, Riemer C, Smale L, Brumm L, Levy M, Gazit E, Oesterhelt D, et al. Green tea extracts interfere with the stress-protective activity of PrP and the formation of PrP. J Neurochem. 2008;107(1):218–29. doi:https://doi.org/10.1111/j.1471-4159.2008.05611.x.
- Hyacinth HI, Gee BE, Hibbert JM. The role of nutrition in sickle cell disease. Nutr Metab Insights. 2010;3:57–67. doi:https://doi.org/10.4137/NMI.S5048.
- Khan SA, Damanhouri G, Ali A, Khan SA, Khan A, Bakillah A, Marouf S, Al Harbi G, Halawani SH, Makki A. Precipitating factors and targeted therapies in combating the perils of sickle cell disease – a special nutritional consideration. Nutr Metab (Lond). 2016;13:50. doi:https://doi.org/10.1186/s12986-016-0109-7.
- Jaja SI, Aigbe PE, Gbenebitse S, Temiye EO. Changes in erythrocytes following supplementation with alpha-tocopherol in children suffering from sickle cell anaemia. Niger Postgrad Med J. 2005;12(2):110–4.
- Gbenebitse S, Jaja SI, Kehinde MO. Effect of changes in plasma vitamin E level of vascular responses and lipid peroxidation in sickle cell anaemia subjects. Niger Postgrad Med J. 2005;12(2):81–4.
- Jaja SI, Ikotun AR, Gbenebitse S, Temiye EO. Blood pressure, hematologic and erythrocyte fragility changes in children suffering from sickle cell anemia following ascorbic acid supplementation. J Trop Pediatr. 2002;48(6):366–70. doi:https://doi.org/10.1093/tropej/48.6.366.
- Arruda MM, Mecabo G, Rodrigues CA, Matsuda SS, Rabelo IB, Figueiredo MS. Antioxidant vitamins C and E supplementation increases markers of haemolysis in sickle cell anaemia patients: a randomized, double-blind, placebo-controlled trial. Br J Haematol. 2013;160(5):688–700. doi:https://doi.org/10.1111/bjh.12185.
- Prasad KN. Simultaneous activation of Nrf2 and elevation of antioxidant compounds for reducing oxidative stress and chronic inflammation in human Alzheimer's disease. Mech Ageing Dev. 2016;153:41–7. doi:https://doi.org/10.1016/j.mad.2016.01.002.
- Isaac MG, Quinn R, Tabet N. Vitamin E for Alzheimer's disease and mild cognitive impairment. Cochrane Database Syst Rev. 2008;(3):CD002854. doi:https://doi.org/10.1002/146551858CD002854.pub2.
- Fillenbaum GG, Kuchibhatla MN, Hanlon JT, Artz MB, Pieper CF, Schmader KE, Dysken MW, Gray SL. Dementia and Alzheimer's disease in community-dwelling elders taking vitamin C and/or vitamin E. Ann Pharmacother. 2005;39(12):2009–14. doi:https://doi.org/10.1345/aph.1G280.
- Shoulson I. DATATOP: a decade of neuroprotective inquiry. Parkinson Study Group. Deprenyl and tocopherol antioxidative therapy of Parkinsonism. Ann Neurol. 1998;44(S1):S160–S6. doi:https://doi.org/10.1002/ana.410440724.
- Group TPS. Effect of tocopherol and deprenylon the progression ofdisability in early Parkinson’s disease. N Engl J Med. 1993;328:176–83.
- Peyser CE, Folstein M, Chase GA, Starkstein S, Brandt J, Cockrell JR, Bylsma F, Coyle JT, McHugh PR, Folstein SE. Trial of d-alpha-tocopherol in Huntington's disease. Am J Psychiatry. 1995;152(12):1771–5.
- Sano M, Ernesto C, Thomas RG, Klauber MR, Schafer K, Grundman M, Woodbury P, Growdon J, Cotman CW, Pfeiffer E, et al. A controlled trial of selegiline, alpha-tocopherol, or both as treatment for Alzheimer's disease. The Alzheimer's Disease Cooperative Study. N Engl J Med. 1997;336(17):1216–22. doi:https://doi.org/10.1056/NEJM199704243361704.
- Fariss MW, Fortuna MB, Everett CK, Smith JD, Trent DF, Djuric Z. The selective antiproliferative effects of alpha-tocopheryl hemisuccinate and cholesteryl hemisuccinate on murine leukemia cells result from the action of the intact compounds. Cancer Res. 1994;54(13):3346–51.
- Vile GF, Winterbourn CC. Inhibition of adriamycin-promoted microsomal lipid peroxidation by beta-carotene, alpha-tocopherol and retinol at high and low oxygen partial pressures. FEBS Lett. 1988;238(2):353–6. doi:https://doi.org/10.1016/0014-5793(88)80511-8.
- Prasad KN, Bondy SC. MicroRNAs in hearing disorders: their regulation by oxidative stress, inflammation and antioxidants. Front Cell Neurosci. 2017;11:276. doi:https://doi.org/10.3389/fncel.2017.00276.
- Wu H, Kong L, Tan Y, Epstein PN, Zeng J, Gu J, Liang G, Kong M, Chen X, Miao L, et al. C66 ameliorates diabetic nephropathy in mice by both upregulating NRF2 function via increase in miR-200a and inhibiting miR-21. Diabetologia. 2016;59(7):1558–68. doi:https://doi.org/10.1007/s00125-016-3958-8.
- Prasad KN, Bondy SC. Inhibition of early upstream events in prodromal Alzheimer's disease by use of targeted antioxidants. Curr Aging Sci. 2014;7(2):77–90. doi:https://doi.org/10.2174/1874609807666140804115633.
- Itoh K, Chiba T, Takahashi S, Ishii T, Igarashi K, Katoh Y, Oyake T, Hayashi N, Satoh K, Hatayama I, et al. An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements. Biochem Biophys Res Commun. 1997;236(2):313–22. doi:https://doi.org/10.1006/bbrc.1997.6943.
- Chan K, Han XD, Kan YW. An important function of Nrf2 in combating oxidative stress: detoxification of acetaminophen. Proc Natl Acad Sci USA. 2001;98(8):4611–6. doi:https://doi.org/10.1073/pnas.081082098.
- Hayes JD, Chanas SA, Henderson CJ, McMahon M, Sun C, Moffat GJ, Wolf CR, Yamamoto M. The Nrf2 transcription factor contributes both to the basal expression of glutathione S-transferases in mouse liver and to their induction by the chemopreventive synthetic antioxidants, butylated hydroxyanisole and ethoxyquin. Biochem Soc Trans. 2000;28(2):33–41. doi:https://doi.org/10.1042/bst0280033.
- Williamson TP, Johnson DA, Johnson JA. Activation of the Nrf2-ARE pathway by siRNA knockdown of Keap1 reduces oxidative stress and provides partial protection from MPTP-mediated neurotoxicity. Neurotoxicology. 2012;33(3):272–9. doi:https://doi.org/10.1016/j.neuro.2012.01.015.
- Jaramillo MC, Zhang DD. The emerging role of the Nrf2-Keap1 signaling pathway in cancer. Genes Dev. 2013;27(20):2179–91. doi:https://doi.org/10.1101/gad.225680.113.
- Ramsey CP, Glass CA, Montgomery MB, Lindl KA, Ritson GP, Chia LA, Hamilton RL, Chu CT, Jordan-Sciutto KL. Expression of Nrf2 in neurodegenerative diseases. J Neuropathol Exp Neurol. 2007;66(1):75–85.
- Chen PC, Vargas MR, Pani AK, Smeyne RJ, Johnson DA, Kan YW, Johnson JA. Nrf2-mediated neuroprotection in the MPTP mouse model of Parkinson's disease: critical role for the astrocyte. Proc Natl Acad Sci USA. 2009;106(8):2933–8. doi:https://doi.org/10.1073/pnas.0813361106.
- Lastres-Becker I, Ulusoy A, Innamorato NG, Sahin G, Rabano A, Kirik D, Cuadrado A. α-Synuclein expression and Nrf2 deficiency cooperate to aggravate protein aggregation, neuronal death and inflammation in early-stage Parkinson's disease. Hum Mol Genet. 2012;21(14):3173–92. doi:https://doi.org/10.1093/hmg/dds143.
- Xi YD, Yu HL, Ding J, Ma WW, Yuan LH, Feng JF, Xiao YX, Xiao R. Flavonoids protect cerebrovascular endothelial cells through Nrf2 and PI3K from β-amyloid peptide-induced oxidative damage. Curr Neurovasc Res. 2012;9(1):32–41. doi:https://doi.org/10.2174/156720212799297092.
- Suh JH, Shenvi SV, Dixon BM, Liu H, Jaiswal AK, Liu R-M, Hagen TM. Decline in transcriptional activity of Nrf2 causes age-related loss of glutathione synthesis, which is reversible with lipoic acid. Proc Natl Acad Sci USA. 2004;101(10):3381–6. doi:https://doi.org/10.1073/pnas.0400282101.
- Trujillo J, Chirino YI, Molina-Jijon E, Anderica-Romero AC, Tapia E, Pedraza-Chaverri J. Renoprotective effect of the antioxidant curcumin: recent findings. Redox Biol. 2013;1(1):448–56. doi:https://doi.org/10.1016/j.redox.2013.09.003.
- Steele ML, Fuller S, Patel M, Kersaitis C, Ooi L, Munch G. Effect of Nrf2 activators on release of glutathione, cysteinylglycine and homocysteine by human U373 astroglial cells. Redox Biol. 2013;1(1):441–5. doi:https://doi.org/10.1016/j.redox.2013.08.006.
- Kode A, Rajendrasozhan S, Caito S, Yang SR, Megson IL, Rahman I. Resveratrol induces glutathione synthesis by activation of Nrf2 and protects against cigarette smoke-mediated oxidative stress in human lung epithelial cells. Am J Physiol Lung Cell Mol Physiol. 2008;294(3):L478–88. doi:https://doi.org/10.1152/ajplung.00361.2007.
- Gao L, Wang J, Sekhar KR, Yin H, Yared NF, Schneider SN, Sasi S, Dalton TP, Anderson ME, Chan JY. Novel n-3 fatty acid oxidation products activate Nrf2 by destabilizing the association between Keap1 and Cullin3. J Biol Chem. 2007;282(4):2529–37. doi:https://doi.org/10.1074/jbc.M607622200.
- Saw CL, Yang AY, Guo Y, Kong AN. Astaxanthin and omega-3 fatty acids individually and in combination protect against oxidative stress via the Nrf2-ARE pathway. Food Chem Toxicol. 2013;62:869–75. doi:https://doi.org/10.1016/j.fct.2013.10.023.
- Song J, Kang SM, Lee WT, Park KA, Lee KM, Lee JE. Glutathione protects brain endothelial cells from hydrogen peroxide-induced oxidative stress by increasing nrf2 expression. Exp Neurobiol. 2014;23(1):93–103. doi:https://doi.org/10.5607/en.2014.23.1.93.
- Ji L, Liu R, Zhang XD, Chen HL, Bai H, Wang X, Zhao HL, Liang X, Hai CX. N-acetylcysteine attenuates phosgene-induced acute lung injury via up-regulation of Nrf2 expression. Inhal Toxicol. 2010;22(7):535–42. doi:https://doi.org/10.3109/08958370903525183.
- Choi HK, Pokharel YR, Lim SC, Han HK, Ryu CS, Kim SK, Kwak MK, Kang KW. Inhibition of liver fibrosis by solubilized coenzyme Q10: role of Nrf2 activation in inhibiting transforming growth factor-beta1 expression. Toxicol Appl Pharmacol. 2009;240(3):377–84. doi:https://doi.org/10.1016/j.taap.2009.07.030.
- Kim J, Cha YN, Surh YJ. A protective role of nuclear factor-erythroid 2-related factor-2 (Nrf2) in inflammatory disorders. Mutat Res. 2010;690(1-2):12–23. doi:https://doi.org/10.1016/j.mrfmmm.2009.09.007.
- Li W, Khor TO, Xu C, Shen G, Jeong WS, Yu S, Kong AN. Activation of Nrf2-antioxidant signaling attenuates NFkappaB-inflammatory response and elicits apoptosis. Biochem Pharmacol. 2008;76(11):1485–9. doi:https://doi.org/10.1016/j.bcp.2008.07.017.
- Abate A, Yang G, Dennery PA, Oberle S, Schroder H. Synergistic inhibition of cyclooxygenase-2 expression by vitamin E and aspirin. Free Radic Biol Med. 2000;29(11):1135–42. doi:https://doi.org/10.1016/S0891-5849(00)00425-1.
- Fu Y, Zheng S, Lin J, Ryerse J, Chen A. Curcumin protects the rat liver from CCl4-caused injury and fibrogenesis by attenuating oxidative stress and suppressing inflammation. Mol Pharmacol. 2008;73(2):399–409. doi:https://doi.org/10.1124/mol.107.039818.
- Lee HS, Jung KK, Cho JY, Rhee MH, Hong S, Kwon M, Kim SH, Kang SY. Neuroprotective effect of curcumin is mainly mediated by blockade of microglial cell activation. Pharmazie. 2007;62(12):937–42.
- Rahman S, Bhatia K, Khan AQ, Kaur M, Ahmad F, Rashid H, Athar M, Islam F, Raisuddin S. Topically applied vitamin E prevents massive cutaneous inflammatory and oxidative stress responses induced by double application of 12-O-tetradecanoylphorbol-13-acetate (TPA) in mice. Chem Biol Interact. 2008;172(3):195–205. doi:https://doi.org/10.1016/j.cbi.2007.11.017.
- Suzuki YJ, Aggarwal BB, Packer L. Alpha-lipoic acid is a potent inhibitor of NF-kappa B activation in human T cells. Biochem Biophys Res Commun. 1992;189(3):1709–15. doi:https://doi.org/10.1016/0006-291X(92)90275-P.
- Zhu J, Yong W, Wu X, Yu Y, Lv J, Liu C, Mao X, Zhu Y, Xu K, Han X, et al. Anti-inflammatory effect of resveratrol on TNF-alpha-induced MCP-1 expression in adipocytes. Biochem Biophys Res Commun. 2008;369(2):471–7. doi:https://doi.org/10.1016/j.bbrc.2008.02.034.
- Gaziano JM, Sesso HD, Christen WG, Bubes V, Smith JP, MacFadyen J, Schvartz M, Manson JE, Glynn RJ, Buring JE. Multivitamins in the prevention of cancer in men: the Physicians' Health Study II randomized controlled trial. JAMA. 2012;308(18):1871–80. doi:https://doi.org/10.1001/jama.2012.14641.
- Baum MK, Campa A, Lai S, Sales Martinez S, Tsalaile L, Burns P, Farahani M, Li Y, van Widenfelt E, Page JB, et al. Effect of micronutrient supplementation on disease progression in asymptomatic, antiretroviral-naive, HIV-infected adults in Botswana: a randomized clinical trial. JAMA. 2013;310(20):2154–63. doi:https://doi.org/10.1001/jama.2013.280923.
- Yahfoufi N, Alsadi N, Jambi M, Matar, C. The immunomodulatory and anti-inflammation role of polyphenols. Nutrients. 2018;10:1618. doi:https://doi.org/10.3390/nu1011618.