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<article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:ali="http://www.niso.org/schemas/ali/1.0/" article-type="research-article" dtd-version="1.2" xml:lang="en"><front><journal-meta><journal-id journal-id-type="publisher-id">Combinatorial Chemistry &amp; High Throughput Screening</journal-id><journal-title-group><journal-title xml:lang="en">Combinatorial Chemistry &amp; High Throughput Screening</journal-title><trans-title-group xml:lang="ru"><trans-title>Combinatorial Chemistry &amp; High Throughput Screening</trans-title></trans-title-group></journal-title-group><issn publication-format="print">1386-2073</issn><issn publication-format="electronic">1875-5402</issn><publisher><publisher-name xml:lang="en">Bentham Science</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="publisher-id">644119</article-id><article-id pub-id-type="doi">10.2174/0113862073280680240101065732</article-id><article-categories><subj-group subj-group-type="toc-heading"><subject>Chemistry</subject></subj-group><subj-group subj-group-type="article-type"><subject>Research Article</subject></subj-group></article-categories><title-group><article-title xml:lang="en">Potential Role of Oxidative Stress in the Pathophysiology of Neurodegenerative Disorders</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Singh</surname><given-names>Sonia</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><name><surname>Ahuja</surname><given-names>Ashima</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff2"/></contrib><contrib contrib-type="author"><name><surname>Pathak</surname><given-names>Shilpi</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff3"/></contrib></contrib-group><aff id="aff1"><institution>Institute of Pharmaceutical Research,, GLA University Mathura</institution></aff><aff id="aff2"><institution>Institute of Pharmaceutical Research, GLA University Mathura</institution></aff><aff id="aff3"><institution>Institute of Pharmaceutical ResearchPharmacy, GLA University Mathura,</institution></aff><pub-date date-type="pub" iso-8601-date="2024-07-15" publication-format="electronic"><day>15</day><month>07</month><year>2024</year></pub-date><volume>27</volume><issue>14</issue><issue-title xml:lang="ru"/><fpage>2043</fpage><lpage>2061</lpage><history><date date-type="received" iso-8601-date="2025-01-07"><day>07</day><month>01</month><year>2025</year></date></history><permissions><copyright-statement xml:lang="en">Copyright ©; 2024, Bentham Science Publishers</copyright-statement><copyright-year>2024</copyright-year><copyright-holder xml:lang="en">Bentham Science Publishers</copyright-holder><ali:free_to_read xmlns:ali="http://www.niso.org/schemas/ali/1.0/"/></permissions><self-uri xlink:href="https://rjpbr.com/1386-2073/article/view/644119">https://rjpbr.com/1386-2073/article/view/644119</self-uri><abstract xml:lang="en"><p id="idm46041443549568">Neurodegeneration causes premature death in the peripheral and central nervous system. Neurodegeneration leads to the accumulation of oxidative stress, inflammatory responses, and the generation of free radicals responsible for nervous disorders like amyotrophic lateral sclerosis, Alzheimer's disease, Parkinson's disease, and Huntington's disorders. Therefore, focus must be diverted towards treating and managing these disorders, as it is very challenging. Furthermore, effective therapies are also lacking, so the growing interest of the global market must be inclined towards developing newer therapeutic approaches that can intercept the progression of neurodegeneration. Emerging evidences of research findings suggest that antioxidant therapy has significant potential in modulating disease phenotypes. This makes them promising candidates for further investigation. This review focuses on the role of oxidative stress and reactive oxygen species in the pathological mechanisms of various neurodegenerative diseases, amyotrophic lateral sclerosis, Alzheimer's disease, Parkinson's disease, and Huntington's disorders and their neuroprotection. Additionally, it highlights the potential of antioxidant-based therapeutics in mitigating disease severity in humans and improving patient compliance. Ongoing extensive global research further sheds light on exploring new therapeutic targets for a deeper understanding of disease mechanisms in the field of medicine and biology targeting neurogenerative disorders.</p></abstract><kwd-group xml:lang="en"><kwd>Neurodegeneration</kwd><kwd>alzheimer's disease</kwd><kwd>antioxidant therapy</kwd><kwd>reactive oxygen species</kwd><kwd>inflammatory responses</kwd><kwd>patient compliance</kwd><kwd>oxidative stress</kwd><kwd>free radicals</kwd><kwd>Parkinson's disease.</kwd></kwd-group></article-meta></front><body></body><back><ref-list><ref id="B1"><label>1.</label><mixed-citation>Chiurchiù, V.; Orlacchio, A.; Maccarrone, M. Is modulation of oxidative stress an answer? The state of the art of redox therapeutic actions in neurodegenerative diseases. Oxidat. Med. Cell. Long., 2016, 2016, 7909380. doi: 10.1155/2016/7909380</mixed-citation></ref><ref id="B2"><label>2.</label><mixed-citation>Zheng, M.; Storz, G. Redox sensing by prokaryotic transcription factors. Biochem. Pharmacol., 2000, 59(1), 1-6. doi: 10.1016/S0006-2952(99)00289-0 PMID: 10605928</mixed-citation></ref><ref id="B3"><label>3.</label><mixed-citation>Aikens, J.; Dix, T.A. Perhydroxyl radical (HOO.) initiated lipid peroxidation. The role of fatty acid hydroperoxides. J. Biol. Chem., 1991, 266(23), 15091-15098. doi: 10.1016/S0021-9258(18)98591-1 PMID: 1869544</mixed-citation></ref><ref id="B4"><label>4.</label><mixed-citation>Dröge, W. Free radicals in the physiological control of cell function. Physiol. Rev., 2002, 82(1), 47-95. doi: 10.1152/physrev.00018.2001 PMID: 11773609</mixed-citation></ref><ref id="B5"><label>5.</label><mixed-citation>Chiurchiù, V.; Maccarrone, M. Chronic inflammatory disorders and their redox control: From molecular mechanisms to therapeutic opportunities. Antioxid. Redox Signal., 2011, 15(9), 2605-2641. doi: 10.1089/ars.2010.3547 PMID: 21391902</mixed-citation></ref><ref id="B6"><label>6.</label><mixed-citation>Halliwell, B. Reactive species and antioxidants. Redox biology is a fundamental theme of aerobic life. Plant Physiol., 2006, 141(2), 312-322. doi: 10.1104/pp.106.077073 PMID: 16760481</mixed-citation></ref><ref id="B7"><label>7.</label><mixed-citation>Poulsen, H.E.; Prieme, H.; Loft, S. Role of oxidative DNA damage in cancer initiation and promotion. Eur. J. Cancer Prev., 1998, 7(1), 9-16. PMID: 9511847</mixed-citation></ref><ref id="B8"><label>8.</label><mixed-citation>Fang, Y.Z.; Yang, S.; Wu, G. Free radicals, antioxidants, and nutrition. Nutrition, 2002, 18(10), 872-879. doi: 10.1016/S0899-9007(02)00916-4 PMID: 12361782</mixed-citation></ref><ref id="B9"><label>9.</label><mixed-citation>Singh, A.; Kukreti, R.; Saso, L.; Kukreti, S. Oxidative stress: A key modulator in neurodegenerative diseases. Molecules, 2019, 24(8), 1583. doi: 10.3390/molecules24081583 PMID: 31013638</mixed-citation></ref><ref id="B10"><label>10.</label><mixed-citation>Lin, M.T.; Beal, M.F. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature, 2006, 443(7113), 787-795. doi: 10.1038/nature05292 PMID: 17051205</mixed-citation></ref><ref id="B11"><label>11.</label><mixed-citation>Gandhi, S.; Abramov, A.Y. Mechanism of oxidative stress in neurodegeneration. Oxidat. Med. Cell. Longev., 2012, 2012, 428010. doi: 10.1155/2012/428010</mixed-citation></ref><ref id="B12"><label>12.</label><mixed-citation>de Rijk, M.C.; Launer, L.J.; Berger, K.; Breteler, M.M.; Dartigues, J.F.; Baldereschi, M.; Fratiglioni, L.; Lobo, A.; Martinez-Lage, J.; Trenkwalder, C.; Hofman, A. Prevalence of Parkinsons disease in Europe: A collaborative study of population-based cohorts. Neurology, 2000, 54(11), S21-S23. PMID: 10854357</mixed-citation></ref><ref id="B13"><label>13.</label><mixed-citation>Bekris, L.M.; Mata, I.F.; Zabetian, C.P. The genetics of Parkinson disease. J. Geriatr. Psychiatry Neurol., 2010, 23(4), 228-242. doi: 10.1177/0891988710383572 PMID: 20938043</mixed-citation></ref><ref id="B14"><label>14.</label><mixed-citation>Farrer, M.J. Genetics of Parkinson disease: Paradigm shifts and future prospects. Nat. Rev. Genet., 2006, 7(4), 306-318. doi: 10.1038/nrg1831 PMID: 16543934</mixed-citation></ref><ref id="B15"><label>15.</label><mixed-citation>Alzheimers Association. 2011 Alzheimers disease facts and figures. Alzheimers Dement., 2011, 7(2), 208-244. doi: 10.1016/j.jalz.2011.02.004 PMID: 21414557</mixed-citation></ref><ref id="B16"><label>16.</label><mixed-citation>Song, P.; Zou, M.H. Roles of reactive oxygen species in physiology and pathology. In: Atherosclerosis: Risks, Mechanisms, and Therapies; Wiley, 2015. doi: 10.1002/9781118828533.ch30</mixed-citation></ref><ref id="B17"><label>17.</label><mixed-citation>Federico, A.; Cardaioli, E.; Da Pozzo, P.; Formichi, P.; Gallus, G.N.; Radi, E. Mitochondria, oxidative stress and neurodegeneration. J. Neurol. Sci., 2012, 322(1-2), 254-262. doi: 10.1016/j.jns.2012.05.030 PMID: 22669122</mixed-citation></ref><ref id="B18"><label>18.</label><mixed-citation>Patten, D.A.; Germain, M.; Kelly, M.A.; Slack, R.S. Reactive oxygen species: Stuck in the middle of neurodegeneration. J. Alzheimers Dis., 2010, 20(s2), S357-S367. doi: 10.3233/JAD-2010-100498 PMID: 20421690</mixed-citation></ref><ref id="B19"><label>19.</label><mixed-citation>Perneczky, R. Dementia prevention and reserve against neurodegenerative disease. Dialogues Clin. Neurosci., 2019, 21(1), 53-60. PMID: 31607780</mixed-citation></ref><ref id="B20"><label>20.</label><mixed-citation>Banerjee, S.; McCracken, S.; Hossain, M.F.; Slaughter, G. Electrochemical detection of neurotransmitters. Biosensors, 2020, 10(8), 101. doi: 10.3390/bios10080101 PMID: 32824869</mixed-citation></ref><ref id="B21"><label>21.</label><mixed-citation>Arumugasamy, S.K.; Chellasamy, G.; Gopi, S.; Govindaraju, S.; Yun, K. Current advances in the detection of neurotransmitters by nanomaterials: An update. Trends Analyt. Chem., 2020, 123, 115766. doi: 10.1016/j.trac.2019.115766</mixed-citation></ref><ref id="B22"><label>22.</label><mixed-citation>Niyonambaza, S.D.; Kumar, P.; Xing, P.; Mathault, J.; De Koninck, P.; Boisselier, E.; Boukadoum, M.; Miled, A. A review of neurotransmitters sensing methods for neuro-engineering research. Appl. Sci. , 2019, 9(21), 4719. doi: 10.3390/app9214719</mixed-citation></ref><ref id="B23"><label>23.</label><mixed-citation>Xia, X.; Wang, Y.; Qin, Y.; Zhao, S.; Zheng, J.C. Exosome: A novel neurotransmission modulator or non-canonical neurotransmitter? Ageing Res. Rev., 2022, 74, 101558. doi: 10.1016/j.arr.2021.101558 PMID: 34990846</mixed-citation></ref><ref id="B24"><label>24.</label><mixed-citation>Tiedje, K.E. Stevens, K.; Barnes, S.; Weaver, D.F. β-Alanine as a small molecule neurotransmitter. Neurochem. Int., 2010, 57(3), 177-188. doi: 10.1016/j.neuint.2010.06.001 PMID: 20540981</mixed-citation></ref><ref id="B25"><label>25.</label><mixed-citation>Onose, G.; Anghelescu, A.; Blendea, D.; Ciobanu, V.; Daia, C.; Firan, F.; Oprea, M.; Spinu, A.; Popescu, C.; Ionescu, A.; Busnatu, Ș.; Munteanu, C. Cellular and molecular targets for non-invasive, non-pharmacological therapeutic/rehabilitative interventions in acute ischemic stroke. Int. J. Mol. Sci., 2022, 23(2), 907. doi: 10.3390/ijms23020907 PMID: 35055089</mixed-citation></ref><ref id="B26"><label>26.</label><mixed-citation>Tam, K.Y.; Ju, Y. Pathological mechanisms and therapeutic strategies for Alzheimers disease. Neural Regen. Res., 2022, 17(3), 543-549. doi: 10.4103/1673-5374.320970 PMID: 34380884</mixed-citation></ref><ref id="B27"><label>27.</label><mixed-citation>Satarker, S.; Bojja, S.L.; Gurram, P.C.; Mudgal, J.; Arora, D.; Nampoothiri, M. Astrocytic glutamatergic transmission and its implications in neurodegenerative disorders. Cells, 2022, 11(7), 1139. doi: 10.3390/cells11071139 PMID: 35406702</mixed-citation></ref><ref id="B28"><label>28.</label><mixed-citation>Murley, A.G.; Rowe, J.B. Neurotransmitter deficits from frontotemporal lobar degeneration. Brain, 2018, 141(5), 1263-1285. doi: 10.1093/brain/awx327 PMID: 29373632</mixed-citation></ref><ref id="B29"><label>29.</label><mixed-citation>Le Gall, L.; Anakor, E.; Connolly, O.; Vijayakumar, U.; Duddy, W.; Duguez, S. Molecular and cellular mechanisms affected in ALS. J. Pers. Med., 2020, 10(3), 101. doi: 10.3390/jpm10030101 PMID: 32854276</mixed-citation></ref><ref id="B30"><label>30.</label><mixed-citation>Iovino, L.; Tremblay, M.E.; Civiero, L. Glutamate-induced excitotoxicity in Parkinsons disease: The role of glial cells. J. Pharmacol. Sci., 2020, 144(3), 151-164. doi: 10.1016/j.jphs.2020.07.011 PMID: 32807662</mixed-citation></ref><ref id="B31"><label>31.</label><mixed-citation>Moraes, B.J.; Coelho, P.; Fão, L.; Ferreira, I.L.; Rego, A.C. Modified glutamatergic postsynapse in neurodegenerative disorders. Neuroscience, 2021, 454, 116-139. doi: 10.1016/j.neuroscience.2019.12.002 PMID: 31887357</mixed-citation></ref><ref id="B32"><label>32.</label><mixed-citation>Kazama, M.; Kato, Y.; Kakita, A.; Noguchi, N.; Urano, Y.; Masui, K.; Niida-Kawaguchi, M.; Yamamoto, T.; Watabe, K.; Kitagawa, K.; Shibata, N. Astrocytes release glutamate via cystine/glutamate antiporter upregulated in response to increased oxidative stress related to sporadic amyotrophic lateral sclerosis. Neuropathology, 2020, 40(6), 587-598. doi: 10.1111/neup.12716 PMID: 33305472</mixed-citation></ref><ref id="B33"><label>33.</label><mixed-citation>Qu, Y.; Shi, J.; Tang, Y.; Zhao, F.; Li, S.; Meng, J.; Tang, J.; Lin, X.; Peng, X.; Mu, D. MLKL inhibition attenuates hypoxia-ischemia induced neuronal damage in developing brain. Exp. Neurol., 2016, 279, 223-231. doi: 10.1016/j.expneurol.2016.03.011 PMID: 26980487</mixed-citation></ref><ref id="B34"><label>34.</label><mixed-citation>Gao, F.; Yin, X.; Edden, R.A.E.; Evans, A.C.; Xu, J.; Cao, G.; Li, H.; Li, M.; Zhao, B.; Wang, J.; Wang, G. Altered hippocampal GABA and glutamate levels and uncoupling from functional connectivity in multiple sclerosis. Hippocampus, 2018, 28(11), 813-823. doi: 10.1002/hipo.23001 PMID: 30069963</mixed-citation></ref><ref id="B35"><label>35.</label><mixed-citation>Bukke, V.N.; Archana, M.; Villani, R.; Romano, A.D.; Wawrzyniak, A.; Balawender, K.; Orkisz, S.; Beggiato, S.; Serviddio, G.; Cassano, T. The dual role of glutamatergic neurotransmission in Alzheimers disease: From pathophysiology to pharmacotherapy. Int. J. Mol. Sci., 2020, 21(20), 7452. doi: 10.3390/ijms21207452 PMID: 33050345</mixed-citation></ref><ref id="B36"><label>36.</label><mixed-citation>Madeira, C.; Vargas-Lopes, C.; Brandão, C.O.; Reis, T.; Laks, J.; Panizzutti, R.; Ferreira, S.T. Elevated glutamate and glutamine levels in the cerebrospinal fluid of patients with probable Alzheimers disease and depression. Front. Psychiatry, 2018, 9, 561. doi: 10.3389/fpsyt.2018.00561 PMID: 30459657</mixed-citation></ref><ref id="B37"><label>37.</label><mixed-citation>Zhang, Z.; Zhang, S.; Fu, P.; Zhang, Z.; Lin, K.; Ko, J.K.S.; Yung, K.K.L. Roles of glutamate receptors in Parkinsons disease. Int. J. Mol. Sci., 2019, 20(18), 4391. doi: 10.3390/ijms20184391 PMID: 31500132</mixed-citation></ref><ref id="B38"><label>38.</label><mixed-citation>Tsuang, D.W.; Greenwood, T.A.; Jayadev, S.; Davis, M.; Shutes-David, A.; Bird, T.D. A genetic study of psychosis in Huntingtons disease: Evidence for the involvement of glutamate signaling pathways. J. Huntingtons Dis., 2018, 7(1), 51-59. doi: 10.3233/JHD-170277 PMID: 29480208</mixed-citation></ref><ref id="B39"><label>39.</label><mixed-citation>Alcoreza, O.B.; Patel, D.C.; Tewari, B.P.; Sontheimer, H. Dysregulation of ambient glutamate and glutamate receptors in epilepsy: An astrocytic perspective. Front. Neurol., 2021, 12, 652159. doi: 10.3389/fneur.2021.652159 PMID: 33828523</mixed-citation></ref><ref id="B40"><label>40.</label><mixed-citation>Koshal, P.; Jamwal, S.; Kumar, P. Glucagon-like Peptide-1 (GLP- 1) and neurotransmitters signaling in epilepsy: An insight review. Neuropharmacology, 2018, 136(Pt B), 271-279. doi: 10.1016/j.neuropharm.2017.11.015 PMID: 29129776</mixed-citation></ref><ref id="B41"><label>41.</label><mixed-citation>Ochoa-de la Paz, L.; Zenteno, E.; Gulias-Cañizo, R.; Quiroz-Mercado, H. Taurine and GABA neurotransmitter receptors, a relationship with therapeutic potential? Expert Rev. Neurother., 2019, 19(4), 289-291. doi: 10.1080/14737175.2019.1593827 PMID: 30892104</mixed-citation></ref><ref id="B42"><label>42.</label><mixed-citation>Duman, R.S.; Sanacora, G.; Krystal, J.H. Altered connectivity in depression: GABA and glutamate neurotransmitter deficits and reversal by novel treatments. Neuron, 2019, 102(1), 75-90. doi: 10.1016/j.neuron.2019.03.013 PMID: 30946828</mixed-citation></ref><ref id="B43"><label>43.</label><mixed-citation>Strandwitz, P. Neurotransmitter modulation by the gut microbiota. Brain Res. 2018, 1693(Pt B), 128-133. doi: 10.1016/j.brainres.2018.03.015 PMID: 29903615</mixed-citation></ref><ref id="B44"><label>44.</label><mixed-citation>Teleanu, R.I.; Niculescu, A.G.; Roza, E.; Vladâcenco, O.; Grumezescu, A.M.; Teleanu, D.M. Neurotransmitters-key factors in neurological and neurodegenerative disorders of the central nervous system. Int. J. Mol. Sci., 2022, 23(11), 5954. doi: 10.3390/ijms23115954 PMID: 35682631</mixed-citation></ref><ref id="B45"><label>45.</label><mixed-citation>Kölker, S. Metabolism of amino acid neurotransmitters: The synaptic disorder underlying inherited metabolic diseases. J. Inherit. Metab. Dis., 2018, 41(6), 1055-1063. doi: 10.1007/s10545-018-0201-4 PMID: 29869166</mixed-citation></ref><ref id="B46"><label>46.</label><mixed-citation>Juliá-Palacios, N.; Molina-Anguita, C.; Sigatulina Bondarenko, M.; Cortès-Saladelafont, E.; Aparicio, J.; Cuadras, D.; Horvath, G.; Fons, C.; Artuch, R.; García-Cazorla, À. Monoamine neurotransmitters in early epileptic encephalopathies: New insights into pathophysiology and therapy. Dev. Med. Child Neurol., 2022, 64(7), 915-923. doi: 10.1111/dmcn.15140 PMID: 35833444</mixed-citation></ref><ref id="B47"><label>47.</label><mixed-citation>Franco, R.; Reyes-Resina, I.; Navarro, G. Dopamine in health and disease: Much more than a neurotransmitter. Biomedicines, 2021, 9(2), 109. doi: 10.3390/biomedicines9020109 PMID: 33499192</mixed-citation></ref><ref id="B48"><label>48.</label><mixed-citation>Swamy, B.K.; Shiprath, K.; Rakesh, G.; Ratnam, K.V.; Manjunatha, H.; Janardan, S.; Naidu, K.C.; Ramesh, S.; Suresh, K.; Ratnamala, A. Simultaneous detection of dopamine, tyrosine and ascorbic acid using NiO/graphene modified graphite electrode. Biointerface Res. Appl. Chem., 2020, 10(3), 5599-5609. doi: 10.33263/BRIAC103.599609</mixed-citation></ref><ref id="B49"><label>49.</label><mixed-citation>Swamy, B.K.; Shiprath, K.; Ratnam, K.V.; Manjunatha, H.; Janardan, S.; Ratnamala, A.; Naidu, K.C.; Ramesh, S.; Babu, K.S. Electrochemical detection of dopamine and tyrosine using metal oxide (MO, M= Cu and Ni) modified graphite electrode: A comparative study. Biointerface Res. Appl. Chem., 2020, 10(5), 6460-6473. doi: 10.33263/BRIAC105.64606473</mixed-citation></ref><ref id="B50"><label>50.</label><mixed-citation>Burnstock, G. Chemical names. Trends Pharmacol. Sci., 2006, 3(27), 166-176. doi: 10.1016/j.tips.2006.01.005 PMID: 16487603</mixed-citation></ref><ref id="B51"><label>51.</label><mixed-citation>Nowaczyk, A.; Kowalska, M.; Nowaczyk, J. Grześk, G. Carbon monoxide and nitric oxide as examples of the youngest class of transmitters. Int. J. Mol. Sci., 2021, 22(11), 6029. doi: 10.3390/ijms22116029 PMID: 34199647</mixed-citation></ref><ref id="B52"><label>52.</label><mixed-citation>Folasire, O.; Mills, K.A.; Sellers, D.J.; Chess-Williams, R. Three gaseous neurotransmitters, nitric oxide, carbon monoxide, and hydrogen sulfide, are involved in the neurogenic relaxation responses of the porcine internal anal sphincter. J. Neurogastroenterol. Motil., 2015, 22(1), 141-148. doi: 10.5056/jnm15036 PMID: 26486177</mixed-citation></ref><ref id="B53"><label>53.</label><mixed-citation>You, Y.; Ikezu, T. Emerging roles of extracellular vesicles in neurodegenerative disorders. Neurobiol. Dis., 2019, 130, 104512. doi: 10.1016/j.nbd.2019.104512 PMID: 31229685</mixed-citation></ref><ref id="B54"><label>54.</label><mixed-citation>Verweij, F.J.; Bebelman, M.P.; Jimenez, C.R.; Garcia-Vallejo, J.J.; Janssen, H.; Neefjes, J.; Knol, J.C.; de Goeij-de Haas, R.; Piersma, S.R.; Baglio, S.R.; Verhage, M.; Middeldorp, J.M.; Zomer, A.; van Rheenen, J.; Coppolino, M.G.; Hurbain, I.; Raposo, G.; Smit, M.J.; Toonen, R.F.G.; van Niel, G.; Pegtel, D.M. Quantifying exosome secretion from single cells reveals a modulatory role for GPCR signaling. J. Cell Biol., 2018, 217(3), 1129-1142. doi: 10.1083/jcb.201703206 PMID: 29339438</mixed-citation></ref><ref id="B55"><label>55.</label><mixed-citation>Saeedi, S.; Israel, S.; Nagy, C.; Turecki, G. The emerging role of exosomes in mental disorders. Transl. Psychiatry, 2019, 9(1), 122. doi: 10.1038/s41398-019-0459-9 PMID: 30923321</mixed-citation></ref><ref id="B56"><label>56.</label><mixed-citation>Shi, M.; Liu, C.; Cook, T.J.; Bullock, K.M.; Zhao, Y.; Ginghina, C.; Li, Y.; Aro, P.; Dator, R.; He, C.; Hipp, M.J.; Zabetian, C.P.; Peskind, E.R.; Hu, S.C.; Quinn, J.F.; Galasko, D.R.; Banks, W.A.; Zhang, J. Plasma exosomal α-synuclein is likely CNS-derived and increased in Parkinsons disease. Acta Neuropathol., 2014, 128(5), 639-650. doi: 10.1007/s00401-014-1314-y PMID: 24997849</mixed-citation></ref><ref id="B57"><label>57.</label><mixed-citation>Rudolph, L.M.; Cornil, C.A.; Mittelman-Smith, M.A.; Rainville, J.R.; Remage-Healey, L.; Sinchak, K.; Micevych, P.E. Actions of steroids: New neurotransmitters. J. Neurosci., 2016, 36(45), 11449-11458. doi: 10.1523/JNEUROSCI.2473-16.2016 PMID: 27911748</mixed-citation></ref><ref id="B58"><label>58.</label><mixed-citation>DAniello, S.; Somorjai, I.; Garcia-Fernàndez, J.; Topo, E.; DAniello, A. D-Aspartic acid is a novel endogenous neurotransmitter. FASEB J., 2011, 25(3), 1014-1027. doi: 10.1096/fj.10-168492 PMID: 21163862</mixed-citation></ref><ref id="B59"><label>59.</label><mixed-citation>Relja, M. Pathophysiology and classification of neurodegenerative diseases. EJIFCC, 2004, 15(3), 97-99. PMID: 29988912</mixed-citation></ref><ref id="B60"><label>60.</label><mixed-citation>Bennett, D.A.; Beckett, L.A.; Murray, A.M.; Shannon, K.M.; Goetz, C.G.; Pilgrim, D.M.; Evans, D.A. Prevalence of parkinsonian signs and associated mortality in a community population of older people. N. Engl. J. Med., 1996, 334(2), 71-76. doi: 10.1056/NEJM199601113340202 PMID: 8531961</mixed-citation></ref><ref id="B61"><label>61.</label><mixed-citation>Norris, F.; Shepherd, R.; Denys, E.; U, K.; Mukai, E.; Elias, L.; Holden, D.; Norris, H. Onset, natural history and outcome in idiopathic adult motor neuron disease. J. Neurol. Sci., 1993, 118(1), 48-55. doi: 10.1016/0022-510X(93)90245-T PMID: 8229050</mixed-citation></ref><ref id="B62"><label>62.</label><mixed-citation>Margolis, R.L.; McInnis, M.G.; Rosenblatt, A.; Ross, C.A. Trinucleotide repeat expansion and neuropsychiatric disease. Arch. Gen. Psychiatry, 1999, 56(11), 1019-1031. doi: 10.1001/archpsyc.56.11.1019 PMID: 10565502</mixed-citation></ref><ref id="B63"><label>63.</label><mixed-citation>Niedzielska, E.; Smaga, I.; Gawlik, M.; Moniczewski, A.; Stankowicz, P.; Pera, J.; Filip, M. Oxidative stress in neurodegenerative diseases. Mol. Neurobiol., 2016, 53(6), 4094-4125. doi: 10.1007/s12035-015-9337-5 PMID: 26198567</mixed-citation></ref><ref id="B64"><label>64.</label><mixed-citation>Chen, X.; Guo, C.; Kong, J. Oxidative stress in neurodegenerative diseases. Neural Regen. Res., 2012, 7(5), 376-385. PMID: 25774178</mixed-citation></ref><ref id="B65"><label>65.</label><mixed-citation>Wang, X.; Michaelis, E.K. Selective neuronal vulnerability to oxidative stress in the brain. Front. Aging Neurosci., 2010, 2, 12. doi: 10.3389/fnagi.2010.00012 PMID: 20552050</mixed-citation></ref><ref id="B66"><label>66.</label><mixed-citation>Dauer, W.; Przedborski, S. Parkinsons disease. Neuron, 2003, 39(6), 889-909. doi: 10.1016/S0896-6273(03)00568-3 PMID: 12971891</mixed-citation></ref><ref id="B67"><label>67.</label><mixed-citation>Rowland, L.P.; Shneider, N.A. Amyotrophic lateral sclerosis. N. Engl. J. Med., 2001, 344(22), 1688-1700. doi: 10.1056/NEJM200105313442207 PMID: 11386269</mixed-citation></ref><ref id="B68"><label>68.</label><mixed-citation>Dinkova-Kostova, A.T.; Talalay, P.; Sharkey, J.; Zhang, Y.; Holtzclaw, W.D.; Wang, X.J.; David, E.; Schiavoni, K.H.; Finlayson, S.; Mierke, D.F.; Honda, T. An exceptionally potent inducer of cytoprotective enzymes: Elucidation of the structural features that determine inducer potency and reactivity with Keap1. J. Biol. Chem., 2010, 285(44), 33747-33755. doi: 10.1074/jbc.M110.163485 PMID: 20801881</mixed-citation></ref><ref id="B69"><label>69.</label><mixed-citation>Finkel, T.; Holbrook, N.J. Oxidants, oxidative stress and the biology of ageing. Nature, 2000, 408(6809), 239-247.</mixed-citation></ref><ref id="B70"><label>70.</label><mixed-citation>Bertram, L.; Tanzi, R.E. Thirty years of Alzheimers disease genetics: The implications of systematic meta-analyses. Nat. Rev. Neurosci., 2008, 9(10), 768-778. doi: 10.1038/nrn2494 PMID: 18802446</mixed-citation></ref><ref id="B71"><label>71.</label><mixed-citation>Christen, Y. Oxidative stress and Alzheimer disease. Am. J. Clin. Nutr., 2000, 71(2), 621S-629S. doi: 10.1093/ajcn/71.2.621s PMID: 10681270</mixed-citation></ref><ref id="B72"><label>72.</label><mixed-citation>Querfurth, H.W.; LaFerla, F.M. Alzheimers disease. N. Engl. J. Med., 2010, 362(4), 329-344. doi: 10.1056/NEJMra0909142 PMID: 20107219</mixed-citation></ref><ref id="B73"><label>73.</label><mixed-citation>Praticò, D. Oxidative stress hypothesis in Alzheimers disease: A reappraisal. Trends Pharmacol. Sci., 2008, 29(12), 609-615. doi: 10.1016/j.tips.2008.09.001 PMID: 18838179</mixed-citation></ref><ref id="B74"><label>74.</label><mixed-citation>Montine, K.S.; Reich, E.; Neely, M.D.; Sidell, K.R.; Olson, S.J.; Markesbery, W.R.; Montine, T.J. Distribution of reducible 4-hydroxynonenal adduct immunoreactivity in Alzheimer disease is associated with APOE genotype. J. Neuropathol. Exp. Neurol., 1998, 57(5), 415-425. doi: 10.1097/00005072-199805000-00005 PMID: 9596412</mixed-citation></ref><ref id="B75"><label>75.</label><mixed-citation>Ahmed, N.; Ahmed, U.; Thornalley, P.J.; Hager, K.; Fleischer, G.; Münch, G. Protein glycation, oxidation and nitration adduct residues and free adducts of cerebrospinal fluid in Alzheimers disease and link to cognitive impairment. J. Neurochem., 2005, 92(2), 255-263. doi: 10.1111/j.1471-4159.2004.02864.x PMID: 15663474</mixed-citation></ref><ref id="B76"><label>76.</label><mixed-citation>Choi, J.; Rees, H.D.; Weintraub, S.T.; Levey, A.I.; Chin, L.S.; Li, L. Oxidative modifications and aggregation of Cu,Zn-superoxide dismutase associated with Alzheimer and Parkinson diseases. J. Biol. Chem., 2005, 280(12), 11648-11655. doi: 10.1074/jbc.M414327200 PMID: 15659387</mixed-citation></ref><ref id="B77"><label>77.</label><mixed-citation>Wong, A.; Lüth, H.J.; Deuther-Conrad, W.; Dukic-Stefanovic, S.; Gasic-Milenkovic, J.; Arendt, T.; Münch, G. Advanced glycation endproducts co-localize with inducible nitric oxide synthase in Alzheimers disease. Brain Res., 2001, 920(1-2), 32-40. doi: 10.1016/S0006-8993(01)02872-4 PMID: 11716809</mixed-citation></ref><ref id="B78"><label>78.</label><mixed-citation>Poppek, D.; Keck, S.; Ermak, G.; Jung, T.; Stolzing, A.; Ullrich, O.; Davies, K.J.A.; Grune, T. Phosphorylation inhibits turnover of the tau protein by the proteasome: influence of RCAN1 and oxidative stress. Biochem. J., 2006, 400(3), 511-520. doi: 10.1042/BJ20060463 PMID: 16939415</mixed-citation></ref><ref id="B79"><label>79.</label><mixed-citation>Keck, S.; Nitsch, R.; Grune, T.; Ullrich, O. Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimers disease. J. Neurochem., 2003, 85(1), 115-122. doi: 10.1046/j.1471-4159.2003.01642.x PMID: 12641733</mixed-citation></ref><ref id="B80"><label>80.</label><mixed-citation>Bonda, D.J.; Lee, H.; Blair, J.A.; Zhu, X.; Perry, G.; Smith, M.A. Role of metal dyshomeostasis in Alzheimers disease. Metallomics, 2011, 3(3), 267-270. doi: 10.1039/c0mt00074d PMID: 21298161</mixed-citation></ref><ref id="B81"><label>81.</label><mixed-citation>Zhang, L.; Zhao, B.; Yew, D.T.; Kusiak, J.W.; Roth, G.S. Processing of Alzheimers amyloid precursor protein during H2O2-induced apoptosis in human neuronal cells. Biochem. Biophys. Res. Commun., 1997, 235(3), 845-848. doi: 10.1006/bbrc.1997.6698 PMID: 9207249</mixed-citation></ref><ref id="B82"><label>82.</label><mixed-citation>Atwood, C.S.; Moir, R.D.; Huang, X.; Scarpa, R.C.; Bacarra, N.M.E.; Romano, D.M.; Hartshorn, M.A.; Tanzi, R.E.; Bush, A.I. Dramatic aggregation of Alzheimer abeta by Cu(II) is induced by conditions representing physiological acidosis. J. Biol. Chem., 1998, 273(21), 12817-12826. doi: 10.1074/jbc.273.21.12817 PMID: 9582309</mixed-citation></ref><ref id="B83"><label>83.</label><mixed-citation>Atwood, C.S.; Scarpa, R.C.; Huang, X.; Moir, R.D.; Jones, W.D.; Fairlie, D.P.; Tanzi, R.E.; Bush, A.I. Characterization of copper interactions with alzheimer amyloid β peptides: identification of an attomolar-affinity copper binding site on amyloid β1-42. J. Neurochem., 2000, 75(3), 1219-1233. doi: 10.1046/j.1471-4159.2000.0751219.x PMID: 10936205</mixed-citation></ref><ref id="B84"><label>84.</label><mixed-citation>Atwood, C.S.; Obrenovich, M.E.; Liu, T.; Chan, H.; Perry, G.; Smith, M.A.; Martins, R.N. Amyloid-β a chameleon walking in two worlds: A review of the trophic and toxic properties of amyloid-β. Brain Res. Brain Res. Rev., 2003, 43(1), 1-16. doi: 10.1016/S0165-0173(03)00174-7 PMID: 14499458</mixed-citation></ref><ref id="B85"><label>85.</label><mixed-citation>Cherny, R.A.; Barnham, K.J.; Lynch, T.; Volitakis, I.; Li, Q.X.; McLean, C.A.; Multhaup, G.; Beyreuther, K.; Tanzi, R.E.; Masters, C.L.; Bush, A.I. Chelation and intercalation: Complementary properties in a compound for the treatment of Alzheimers disease. J. Struct. Biol., 2000, 130(2-3), 209-216. doi: 10.1006/jsbi.2000.4285 PMID: 10940226</mixed-citation></ref><ref id="B86"><label>86.</label><mixed-citation>González, H.; Pacheco, R. T-cell-mediated regulation of neuroinflammation involved in neurodegenerative diseases. J. Neuroinflammation, 2014, 11(1), 201. doi: 10.1186/s12974-014-0201-8 PMID: 25441979</mixed-citation></ref><ref id="B87"><label>87.</label><mixed-citation>Dias, V.; Junn, E.; Mouradian, M.M. The role of oxidative stress in Parkinsons disease. J. Parkinsons Dis., 2013, 3(4), 461-491. doi: 10.3233/JPD-130230 PMID: 24252804</mixed-citation></ref><ref id="B88"><label>88.</label><mixed-citation>Puspita, L.; Chung, S.Y.; Shim, J. Oxidative stress and cellular pathologies in Parkinsons disease. Mol. Brain, 2017, 10(1), 53. doi: 10.1186/s13041-017-0340-9 PMID: 29183391</mixed-citation></ref><ref id="B89"><label>89.</label><mixed-citation>Zeevalk, G.D.; Razmpour, R.; Bernard, L.P. Glutathione and Parkinsons disease: Is this the elephant in the room? Biomed. Pharmacother., 2008, 62(4), 236-249. doi: 10.1016/j.biopha.2008.01.017 PMID: 18400456</mixed-citation></ref><ref id="B90"><label>90.</label><mixed-citation>Torres-Vega, A.; Pliego-Rivero, B.F.; Otero-Ojeda, G.A.; Gómez-Oliván, L.M.; Vieyra-Reyes, P. Limbic system pathologies associated with deficiencies and excesses of the trace elements iron, zinc, copper, and selenium. Nutr. Rev., 2012, 70(12), 679-692. doi: 10.1111/j.1753-4887.2012.00521.x PMID: 23206282</mixed-citation></ref><ref id="B91"><label>91.</label><mixed-citation>Tieu, K.; Ischiropoulos, H.; Przedborski, S. Nitric oxide and reactive oxygen species in Parkinsons disease. IUBMB Life, 2003, 55(6), 329-335. doi: 10.1080/1521654032000114320 PMID: 12938735</mixed-citation></ref><ref id="B92"><label>92.</label><mixed-citation>Hunot, S.; Boissière, F.; Faucheux, B.; Brugg, B.; Mouatt-Prigent, A.; Agid, Y.; Hirsch, E.C. Nitric oxide synthase and neuronal vulnerability in parkinsons disease. Neuroscience, 1996, 72(2), 355-363. doi: 10.1016/0306-4522(95)00578-1 PMID: 8737406</mixed-citation></ref><ref id="B93"><label>93.</label><mixed-citation>Eve, D.J.; Nisbet, A.P.; Kingsbury, A.E.; Hewson, E.L.; Daniel, S.E.; Lees, A.J.; Marsden, C.D.; Foster, O.J.F. Basal ganglia neuronal nitric oxide synthase mRNA expression in Parkinsons disease. Brain Res. Mol. Brain Res., 1998, 63(1), 62-71. doi: 10.1016/S0169-328X(98)00259-9 PMID: 9838046</mixed-citation></ref><ref id="B94"><label>94.</label><mixed-citation>Kikuchi, S.; Shinpo, K.; Ogata, A.; Tsuji, S.; Takeuchi, M.; Makita, Z.; Tashiro, K. Detection of N epsilon-(carboxymethyl) lysine (CML) and non-CML advanced glycation end-products in the anterior horn of amyotrophic lateral sclerosis spinal cord. Amyotrophic lateral sclerosis and other motor neuron disorders: Official publication of the World Federation of Neurology. Res. Group Motor Neuron Dis., 2002, 3(2), 63-68.</mixed-citation></ref><ref id="B95"><label>95.</label><mixed-citation>Mendez, E.F.; Sattler, R. Biomarker development for C9orf72 repeat expansion in ALS. Brain Res., 2015, 1607, 26-35. doi: 10.1016/j.brainres.2014.09.041 PMID: 25261695</mixed-citation></ref><ref id="B96"><label>96.</label><mixed-citation>Lacomblez, L.; Bensimon, G.; Meininger, V.; Leigh, P.N.; Guillet, P. Dose-ranging study of riluzole in amyotrophic lateral sclerosis. Lancet, 1996, 347(9013), 1425-1431. doi: 10.1016/S0140-6736(96)91680-3 PMID: 8676624</mixed-citation></ref><ref id="B97"><label>97.</label><mixed-citation>Yoshino, H.; Kimura, A. Investigation of the therapeutic effects of edaravone, a free radical scavenger, on amyotrophic lateral sclerosis (Phase II study). Amyotroph. Lateral Scler., 2006, 7(4), 247-251. doi: 10.1080/17482960600881870 PMID: 17127563</mixed-citation></ref><ref id="B98"><label>98.</label><mixed-citation>Louwerse, E.S.; Weverling, G.J.; Bossuyt, P.M.M.; Meyjes, F.E.P.; de Jong, J.M.B.V. Randomized, double-blind, controlled trial of acetylcysteine in amyotrophic lateral sclerosis. Arch. Neurol., 1995, 52(6), 559-564. doi: 10.1001/archneur.1995.00540300031009 PMID: 7763202</mixed-citation></ref><ref id="B99"><label>99.</label><mixed-citation>Vonsattel, J.P.; DiFiglia, M. Huntington disease. J. Neuropathol. Exp. Neurol., 1998, 57(5), 369-384. doi: 10.1097/00005072-199805000-00001 PMID: 9596408</mixed-citation></ref><ref id="B100"><label>100.</label><mixed-citation>Li, S.H.; Li, X.J. Huntingtin and its role in neuronal degeneration. Neuroscientist, 2004, 10(5), 467-475. doi: 10.1177/1073858404266777 PMID: 15359012</mixed-citation></ref><ref id="B101"><label>101.</label><mixed-citation>Stack, E.C.; Matson, W.R.; Ferrante, R.J. Evidence of oxidant damage in Huntingtons disease: Translational strategies using antioxidants. Ann. N. Y. Acad. Sci., 2008, 1147(1), 79-92. doi: 10.1196/annals.1427.008 PMID: 19076433</mixed-citation></ref><ref id="B102"><label>102.</label><mixed-citation>Túnez, I.; Sánchez-López, F.; Agüera, E.; Fernández-Bolaños, R.; Sánchez, F.M.; Tasset-Cuevas, I. Important role of oxidative stress biomarkers in Huntingtons disease. J. Med. Chem., 2011, 54(15), 5602-5606. doi: 10.1021/jm200605a PMID: 21678912</mixed-citation></ref><ref id="B103"><label>103.</label><mixed-citation>Johri, A.; Beal, M.F. Antioxidants in huntingtons disease. Biochim. Biophys. Acta Mol. Basis Dis., 2012, 1822(5), 664-674. doi: 10.1016/j.bbadis.2011.11.014</mixed-citation></ref><ref id="B104"><label>104.</label><mixed-citation>Kumar, A.; Ratan, R.R. Oxidative stress and Huntingtons disease: The good, the bad, and the ugly. J. Huntingtons Dis., 2016, 5(3), 217-237. doi: 10.3233/JHD-160205 PMID: 27662334</mixed-citation></ref><ref id="B105"><label>105.</label><mixed-citation>Khan, F.; Kumar Garg, V.; Kumar Singh, A.; Tinku, T. Role of free radicals and certain antioxidants in the management of huntingtons disease: A review. J. Anal. Pharm. Res., 2018, 7(4), 386-392. doi: 10.15406/japlr.2018.07.00256</mixed-citation></ref><ref id="B106"><label>106.</label><mixed-citation>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: 10.3389/fnmol.2018.00329 PMID: 30283298</mixed-citation></ref><ref id="B107"><label>107.</label><mixed-citation>Forman, H.J.; Maiorino, M.; Ursini, F. Signaling functions of reactive oxygen species. Biochemistry, 2010, 49(5), 835-842. doi: 10.1021/bi9020378 PMID: 20050630</mixed-citation></ref><ref id="B108"><label>108.</label><mixed-citation>Evans, J.L.; Goldfine, I.D.; Maddux, B.A.; Grodsky, G.M. Oxidative stress and stress-activated signaling pathways: A unifying hypothesis of type 2 diabetes. Endocr. Rev., 2002, 23(5), 599-622. doi: 10.1210/er.2001-0039 PMID: 12372842</mixed-citation></ref><ref id="B109"><label>109.</label><mixed-citation>Liochev, S.I.; Fridovich, I. The role of O2.- in the production of HO.: In vitro and in vivo . Free Radic. Biol. Med., 1994, 16(1), 29-33. doi: 10.1016/0891-5849(94)90239-9 PMID: 8299992</mixed-citation></ref><ref id="B110"><label>110.</label><mixed-citation>Castro, L.; Tórtora, V.; Mansilla, S.; Radi, R. Aconitases: Non-redox iron-sulfur proteins sensitive to reactive species. Acc. Chem. Res., 2019, 52(9), 2609-2619. doi: 10.1021/acs.accounts.9b00150 PMID: 31287291</mixed-citation></ref><ref id="B111"><label>111.</label><mixed-citation>Zhang, H.; Forman, H.J. 4-hydroxynonenal-mediated signaling and aging. Free Radic. Biol. Med., 2017, 111, 219-225. doi: 10.1016/j.freeradbiomed.2016.11.032 PMID: 27876535</mixed-citation></ref><ref id="B112"><label>112.</label><mixed-citation>Haque, R.; Uddin, S.N.; Hossain, A. Amyloid Beta (Aβ) and oxidative stress: Progression of alzheimers disease. Adv. Biotechnol. Microbiol., 2018, 11(1), 555802. doi: 10.19080/AIBM.2018.11.555802</mixed-citation></ref><ref id="B113"><label>113.</label><mixed-citation>Galluzzi, S.; Zanardini, R.; Ferrari, C.; Gipponi, S.; Passeggia, I.; Rampini, M.; Sgrò, G.; Genovese, S.; Fiorito, S.; Palumbo, L.; Pievani, M.; Frisoni, G.B.; Epifano, F. Cognitive and biological effects of citrus phytochemicals in subjective cognitive decline: A 36-week, randomized, placebo-controlled trial. Nutr. J., 2022, 21(1), 64. doi: 10.1186/s12937-022-00817-6 PMID: 36253765</mixed-citation></ref><ref id="B114"><label>114.</label><mixed-citation>Mendoza, BM.; Ortiz, GG.; Romero, LS.; Lara, DL.; Martínez, MT.; Ramírez, MA.; Serrano, JA.; Pacheco-Moisés, FP. Dietary fish oil increases catalase activity in patients with probable Alzheimers disease. Nutr. Hosp., 2022, 39(6), 1364-1368.</mixed-citation></ref><ref id="B115"><label>115.</label><mixed-citation>Clark, D.O.; Xu, H.; Moser, L.; Adeoye, P.; Lin, A.W.; Tangney, C.C.; Risacher, S.L.; Saykin, A.J.; Considine, R.V.; Unverzagt, F.W. MIND food and speed of processing training in older adults with low education, the MINDSpeed Alzheimers disease prevention pilot trial. Contemp. Clin. Trials, 2019, 84, 105814. doi: 10.1016/j.cct.2019.105814 PMID: 31326523</mixed-citation></ref><ref id="B116"><label>116.</label><mixed-citation>Sala-Vila, A.; Valls-Pedret, C.; Rajaram, S.; Coll-Padrós, N.; Cofán, M.; Serra-Mir, M.; Pérez-Heras, A.M.; Roth, I.; Freitas-Simoes, T.M.; Doménech, M.; Calvo, C.; López-Illamola, A.; Bitok, E.; Buxton, N.K.; Huey, L.; Arechiga, A.; Oda, K.; Lee, G.J.; Corella, D.; Vaqué-Alcázar, L.; Sala-Llonch, R.; Bartrés-Faz, D.; Sabaté, J.; Ros, E. Effect of a 2-year diet intervention with walnuts on cognitive decline. The Walnuts And Healthy Aging (WAHA) study: A randomized controlled trial. Am. J. Clin. Nutr., 2020, 111(3), 590-600. doi: 10.1093/ajcn/nqz328 PMID: 31912155</mixed-citation></ref><ref id="B117"><label>117.</label><mixed-citation>Ton, A.M.M.; Campagnaro, B.P.; Alves, G.A.; Aires, R.; Côco, L.Z.; Arpini, C.M.; Guerra e Oliveira, T.; Campos-Toimil, M.; Meyrelles, S.S.; Pereira, T.M.C.; Vasquez, E.C. Oxidative stress and dementia in Alzheimers patients: Effects of synbiotic supplementation. Oxid. Med. Cell. Longev., 2020, 2020, 1-14. doi: 10.1155/2020/2638703 PMID: 32411323</mixed-citation></ref><ref id="B118"><label>118.</label><mixed-citation>Tamtaji, O.R.; Heidari-soureshjani, R.; Asemi, Z.; Kouchaki, E. The effects of spirulina intake on clinical and metabolic parameters in Alzheimers disease: A randomized, double-blind, controlled trial. Phytother. Res., 2023, 37(7), 2957-2964. doi: 10.1002/ptr.7791 PMID: 36861852</mixed-citation></ref><ref id="B119"><label>119.</label><mixed-citation>Foroumandi, E.; Javan, R.; Moayed, L.; Fahimi, H.; Kheirabadi, F.; Neamatshahi, M.; Shogofteh, F.; Zarghi, A. The effects of fenugreek seed extract supplementation in patients with Alzheimers disease: A randomized, double-blind, placebo-controlled trial. Phytother. Res., 2023, 37(1), 285-294. doi: 10.1002/ptr.7612 PMID: 36199177</mixed-citation></ref><ref id="B120"><label>120.</label><mixed-citation>Tamtaji, O.R.; Heidari-soureshjani, R.; Mirhosseini, N.; Kouchaki, E.; Bahmani, F.; Aghadavod, E.; Tajabadi-Ebrahimi, M.; Asemi, Z. Probiotic and selenium co-supplementation, and the effects on clinical, metabolic and genetic status in Alzheimers disease: A randomized, double-blind, controlled trial. Clin. Nutr., 2019, 38(6), 2569-2575. doi: 10.1016/j.clnu.2018.11.034 PMID: 30642737</mixed-citation></ref><ref id="B121"><label>121.</label><mixed-citation>Yang, T.; Wang, H.; Xiong, Y.; Chen, C.; Duan, K.; Jia, J.; Ma, F. Vitamin D supplementation improves cognitive function through reducing oxidative stress regulated by telomere length in older adults with mild cognitive impairment: A 12-month randomized controlled trial. J. Alzheimers Dis., 2020, 78(4), 1509-1518. doi: 10.3233/JAD-200926 PMID: 33164936</mixed-citation></ref><ref id="B122"><label>122.</label><mixed-citation>Lee, W.J.; Shin, Y.W.; Kim, D.E.; Kweon, M.H.; Kim, M. Effect of desalted Salicornia europaea L. ethanol extract (PM-EE) on the subjects complaining memory dysfunction without dementia: A 12 week, randomized, double-blind, placebo-controlled clinical trial. Sci. Rep., 2020, 10(1), 19914. doi: 10.1038/s41598-020-76938-x PMID: 33199752</mixed-citation></ref><ref id="B123"><label>123.</label><mixed-citation>Kamalashiran, C.; Sriyakul, K.; Pattaraarchachai, J.; Muengtaweepongsa, S. Outcomes of perilla seed oil as an additional neuroprotective therapy in patients with mild to moderate dementia: A randomized control trial. Curr. Alzheimer Res., 2019, 16(2), 146-155. doi: 10.2174/1567205016666181212153720 PMID: 30543172</mixed-citation></ref><ref id="B124"><label>124.</label><mixed-citation>Rosli, H.; Shahar, S.; Rajab, N.F.; Che Din, N.; Haron, H. The effects of polyphenols-rich tropical fruit juice on cognitive function and metabolomics profile - A randomized controlled trial in middle-aged women. Nutr. Neurosci., 2022, 25(8), 1577-1593. doi: 10.1080/1028415X.2021.1880312 PMID: 33666540</mixed-citation></ref><ref id="B125"><label>125.</label><mixed-citation>Awasthi, A.; Matsunaga, Y.; Yamada, T. Amyloid-beta causes apoptosis of neuronal cells via caspase cascade, which can be prevented by amyloid-beta-derived short peptides. Exp. Neurol., 2005, 196(2), 282-289. doi: 10.1016/j.expneurol.2005.08.001 PMID: 16137679</mixed-citation></ref><ref id="B126"><label>126.</label><mixed-citation>Giraldo, E.; Lloret, A.; Fuchsberger, T.; Viña, J. Aβ and tau toxicities in Alzheimers are linked via oxidative stress-induced p38 activation: Protective role of vitamin E. Redox Biol., 2014, 2, 873-877. doi: 10.1016/j.redox.2014.03.002 PMID: 25061569</mixed-citation></ref><ref id="B127"><label>127.</label><mixed-citation>Liu, Z.; Zhou, T.; Ziegler, AC.; Dimitrion, P.; Zuo, L. Oxidative stress in neurodegenerative diseases: From molecular mechanisms to clinical applications. Oxid. Med. Cell. Longev., 2017, 2017, 2525967. doi: 10.1155/2017/2525967</mixed-citation></ref><ref id="B128"><label>128.</label><mixed-citation>Lees, A.J. Unresolved issues relating to the shaking palsy on the celebration of james parkinsons 250th birthday. Mov. Disord., 2007, 22(S17), S327-S334. doi: 10.1002/mds.21684 PMID: 18175393</mixed-citation></ref><ref id="B129"><label>129.</label><mixed-citation>Miller, D.B.; OCallaghan, J.P. Biomarkers of Parkinsons disease: Present and future. Metabolism, 2015, 64(3), S40-S46. doi: 10.1016/j.metabol.2014.10.030 PMID: 25510818</mixed-citation></ref><ref id="B130"><label>130.</label><mixed-citation>Solleiro-Villavicencio, H.; Rivas-Arancibia, S. Effect of chronic oxidative stress on neuroinflammatory response mediated by CD4+ T cells in neurodegenerative diseases. Front. Cell. Neurosci., 2018, 12, 114. doi: 10.3389/fncel.2018.00114 PMID: 29755324</mixed-citation></ref><ref id="B131"><label>131.</label><mixed-citation>Peplow, P.V.; Martinez, B. Neuroprotection by immunomodulatory agents in animal models of Parkinsons disease. Neural Regen. Res., 2018, 13(9), 1493-1506. doi: 10.4103/1673-5374.237108 PMID: 30127102</mixed-citation></ref><ref id="B132"><label>132.</label><mixed-citation>Kobelt, G.; Thompson, A.; Berg, J.; Gannedahl, M.; Eriksson, J. New insights into the burden and costs of multiple sclerosis in Europe. Mult. Scler., 2017, 23(8), 1123-1136. doi: 10.1177/1352458517694432 PMID: 28273775</mixed-citation></ref><ref id="B133"><label>133.</label><mixed-citation>Haider, L.; Fischer, M.T.; Frischer, J.M.; Bauer, J.; Höftberger, R.; Botond, G.; Esterbauer, H.; Binder, C.J.; Witztum, J.L.; Lassmann, H. Oxidative damage in multiple sclerosis lesions. Brain, 2011, 134(7), 1914-1924. doi: 10.1093/brain/awr128 PMID: 21653539</mixed-citation></ref><ref id="B134"><label>134.</label><mixed-citation>Hooten, K.G.; Beers, D.R.; Zhao, W.; Appel, S.H. Protective and toxic neuroinflammation in amyotrophic lateral sclerosis. Neurotherapeutics, 2015, 12(2), 364-375. doi: 10.1007/s13311-014-0329-3 PMID: 25567201</mixed-citation></ref><ref id="B135"><label>135.</label><mixed-citation>Petrillo, S.; Pelosi, L.; Piemonte, F.; Travaglini, L.; Forcina, L.; Catteruccia, M.; Petrini, S.; Verardo, M.; DAmico, A.; Musarò, A.; Bertini, E. Oxidative stress in Duchenne muscular dystrophy: Focus on the NRF2 redox pathway. Hum. Mol. Genet., 2017, 26(14), 2781-2790. doi: 10.1093/hmg/ddx173 PMID: 28472288</mixed-citation></ref><ref id="B136"><label>136.</label><mixed-citation>Fusco, M.; Skaper, S.D.; Coaccioli, S.; Varrassi, G.; Paladini, A. Degenerative joint diseases and neuroinflammation. Pain Pract., 2017, 17(4), 522-532. doi: 10.1111/papr.12551 PMID: 28039964</mixed-citation></ref><ref id="B137"><label>137.</label><mixed-citation>Nathan, C.; Ding, A. Nonresolving inflammation. Cell, 2010, 140(6), 871-882. doi: 10.1016/j.cell.2010.02.029 PMID: 20303877</mixed-citation></ref><ref id="B138"><label>138.</label><mixed-citation>Varrassi, G.; Fusco, M.; Skaper, S.D.; Battelli, D.; Zis, P.; Coaccioli, S.; Pace, M.C.; Paladini, A. A pharmacological rationale to reduce the incidence of opioid induced tolerance and hyperalgesia: A review. Pain Ther., 2018, 7(1), 59-75. doi: 10.1007/s40122-018-0094-9 PMID: 29594972</mixed-citation></ref><ref id="B139"><label>139.</label><mixed-citation>Emerit, J.; Edeas, M.; Bricaire, F. Neurodegenerative diseases and oxidative stress. Biomed. Pharmacother., 2004, 58(1), 39-46. doi: 10.1016/j.biopha.2003.11.004 PMID: 14739060</mixed-citation></ref><ref id="B140"><label>140.</label><mixed-citation>Schieber, M.; Chandel, N.S. ROS function in redox signaling and oxidative stress. Curr. Biol., 2014, 24(10), R453-R462. doi: 10.1016/j.cub.2014.03.034 PMID: 24845678</mixed-citation></ref><ref id="B141"><label>141.</label><mixed-citation>Fischer, R.; Maier, O. Interrelation of oxidative stress and inflammation in neurodegenerative disease: role of TNF. Oxid. Med. Cell. Longev., 2015, 2015, 610813. doi: 10.1155/2015/610813</mixed-citation></ref><ref id="B142"><label>142.</label><mixed-citation>Dröse, S.; Brandt, U. The mechanism of mitochondrial superoxide production by the cytochrome bc1 complex. J. Biol. Chem., 2008, 283(31), 21649-21654. doi: 10.1074/jbc.M803236200 PMID: 18522938</mixed-citation></ref><ref id="B143"><label>143.</label><mixed-citation>Mueller, A.M.; Yoon, B.H.; Sadiq, S.A. Inhibition of hyaluronan synthesis protects against central nervous system (CNS) autoimmunity and increases CXCL12 expression in the inflamed CNS. J. Biol. Chem., 2014, 289(33), 22888-22899. doi: 10.1074/jbc.M114.559583 PMID: 24973214</mixed-citation></ref><ref id="B144"><label>144.</label><mixed-citation>Tao, L.; Zhang, F.; Hao, L.; Wu, J.; Jia, J.; Liu, J.; Zheng, L.T.; Zhen, X. 1-O-tigloyl-1-O-deacetyl-nimbolinin B inhibits LPS-stimulated inflammatory responses by suppressing NF-κB and JNK activation in microglia cells. J. Pharmacol. Sci., 2014, 125(4), 364-374. doi: 10.1254/jphs.14025FP PMID: 25018136</mixed-citation></ref><ref id="B145"><label>145.</label><mixed-citation>Chakrabarti, S.; Munshi, S.; Banerjee, K.; Thakurta, I.G.; Sinha, M.; Bagh, M.B. Mitochondrial dysfunction during brain aging: Role of oxidative stress and modulation by antioxidant supplementation. Aging Dis., 2011, 2(3), 242-256. PMID: 22396876</mixed-citation></ref><ref id="B146"><label>146.</label><mixed-citation>Halliwell, B. Reactive oxygen species and the central nervous system. J. Neurochem., 1992, 59(5), 1609-1623. doi: 10.1111/j.1471-4159.1992.tb10990.x PMID: 1402908</mixed-citation></ref><ref id="B147"><label>147.</label><mixed-citation>Navarro, A.; Boveris, A. Brain mitochondrial dysfunction in aging, neurodegeneration and Parkinsons disease. Front. Aging Neurosci., 2010, 2, 34. doi: 10.3389/fnagi.2010.00034 PMID: 20890446</mixed-citation></ref><ref id="B148"><label>148.</label><mixed-citation>Mecocci, P.; Beal, M.F.; Cecchetti, R.; Polidori, M.C.; Cherubini, A.; Chionne, F.; Avellini, L.; Romano, G.; Senin, U. Mitochondrial membrane fluidity and oxidative damage to mitochondrial DNA in aged and AD human brain. Mol. Chem. Neuropathol., 1997, 31(1), 53-64. doi: 10.1007/BF02815160 PMID: 9271005</mixed-citation></ref><ref id="B149"><label>149.</label><mixed-citation>Corral-Debrinski, M.; Horton, T.; Lott, M.T.; Shoffner, J.M.; Flint Beal, M.; Wallace, D.C. Mitochondrial DNA deletions in human brain: Regional variability and increase with advanced age. Nat. Genet., 1992, 2(4), 324-329. doi: 10.1038/ng1292-324 PMID: 1303288</mixed-citation></ref><ref id="B150"><label>150.</label><mixed-citation>Imam, S.Z.; Karahalil, B.; Hogue, B.A.; Souza-Pinto, N.C.; Bohr, V.A. Mitochondrial and nuclear DNA-repair capacity of various brain regions in mouse is altered in an age-dependent manner. Neurobiol. Aging, 2006, 27(8), 1129-1136. doi: 10.1016/j.neurobiolaging.2005.06.002 PMID: 16005114</mixed-citation></ref><ref id="B151"><label>151.</label><mixed-citation>Uttara, B.; Singh, A.; Zamboni, P.; Mahajan, R. Oxidative stress and neurodegenerative diseases: A review of upstream and downstream antioxidant therapeutic options. Curr. Neuropharmacol., 2009, 7(1), 65-74. doi: 10.2174/157015909787602823 PMID: 19721819</mixed-citation></ref><ref id="B152"><label>152.</label><mixed-citation>Rekatsina, M.; Paladini, A.; Piroli, A.; Zis, P.; Pergolizzi, J.V.; Varrassi, G. Pathophysiology and therapeutic perspectives of oxidative stress and neurodegenerative diseases: A narrative review. Adv. Ther., 2020, 37(1), 113-139. doi: 10.1007/s12325-019-01148-5 PMID: 31782132</mixed-citation></ref><ref id="B153"><label>153.</label><mixed-citation>Buccellato, F.R.; DAnca, M.; Fenoglio, C.; Scarpini, E.; Galimberti, D. Role of oxidative damage in alzheimers disease and neurodegeneration: From pathogenic mechanisms to biomarker discovery. Antioxidants, 2021, 10(9), 1353. doi: 10.3390/antiox10091353 PMID: 34572985</mixed-citation></ref><ref id="B154"><label>154.</label><mixed-citation>Forman, H.J.; Zhang, H. Targeting oxidative stress in disease: Promise and limitations of antioxidant therapy. Nat. Rev. Drug Discov., 2021, 20(9), 689-709. doi: 10.1038/s41573-021-00233-1 PMID: 34194012</mixed-citation></ref><ref id="B155"><label>155.</label><mixed-citation>Goyal, A.; Verma, A.; Dubey, N.; Raghav, J.; Agrawal, A. Naringenin: A prospective therapeutic agent for Alzheimers and Parkinsons disease. J. Food Biochem., 2022, 46(12), e14415. doi: 10.1111/jfbc.14415 PMID: 36106706</mixed-citation></ref><ref id="B156"><label>156.</label><mixed-citation>Goyal, A.; Agrawal, A.; Verma, A.; Dubey, N. The PI3K-AKT pathway: A plausible therapeutic target in Parkinsons disease. Exp. Mol. Pathol., 2023, 129, 104846. doi: 10.1016/j.yexmp.2022.104846 PMID: 36436571</mixed-citation></ref><ref id="B157"><label>157.</label><mixed-citation>Goyal, A.; Verma, A.; Agrawal, A.; Dubey, N.; Kumar, A.; Behl, T. Therapeutic implications of crocin in Parkinsons disease: A review of preclinical research. Chem. Biol. Drug Des., 2023, 101(6), 1229-1240. doi: 10.1111/cbdd.14210 PMID: 36752710</mixed-citation></ref><ref id="B158"><label>158.</label><mixed-citation>Goyal, A.; Verma, A.; Agrawal, N. Dietary phytoestrogens: Neuroprotective role in Parkinsons disease. Curr. Neurovasc. Res., 2021, 18(2), 254-267. doi: 10.2174/1567202618666210604121233 PMID: 34086550</mixed-citation></ref></ref-list></back></article>
