{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T00:57:29Z","timestamp":1760057849811,"version":"build-2065373602"},"reference-count":70,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2025,2,26]],"date-time":"2025-02-26T00:00:00Z","timestamp":1740528000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001807","name":"State of S\u00e3o Paulo Research Foundation","doi-asserted-by":"publisher","award":["2023\/03608-1","2018\/13588-0","001","CEM-UFABC"],"award-info":[{"award-number":["2023\/03608-1","2018\/13588-0","001","CEM-UFABC"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Coordination for the Improvement of Higher Education Personnel (CAPES)","award":["2023\/03608-1","2018\/13588-0","001","CEM-UFABC"],"award-info":[{"award-number":["2023\/03608-1","2018\/13588-0","001","CEM-UFABC"]}]},{"name":"UFABC Multiuser Central Facilities","award":["2023\/03608-1","2018\/13588-0","001","CEM-UFABC"],"award-info":[{"award-number":["2023\/03608-1","2018\/13588-0","001","CEM-UFABC"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antioxidants"],"abstract":"<jats:p>Functional characterization of peptide fraction (PF) from snake venom has provided novel opportunities to investigate possible neuroprotective compounds relevant to pharmaceuticals. This study was performed to investigate the PF-mediated neuroprotection obtained from Naja mandalayensis snake venom, a member of the Elapidae family, using two neuronal cell lines, undifferentiated PC12 and differentiated mHippoE-18, in response to H2O2-induced oxidative stress. Cells were pre-treated for 4 h with PF (10, 1, 0.01, and 0.001 \u03bcg mL\u22121), and thereafter exposed to H2O2 (0.5 mmol L\u22121) for 20 h. Then, the oxidative stress markers and label-free differential proteome strategy were analyzed to understand the neuroprotective effects of PF. In PC12 cells, PF showed no neuroprotective effects against oxidative stress. In mHippoE-18 cells, PF at 0.01 and 0.001 \u03bcg mL\u22121 increased the viability and metabolism of cells against H2O2-induced neurotoxicity, reducing reactive oxygen species (ROS) generation. Interestingly, PF also exhibited a substantial reduction in baseline ROS levels compared to the control, indicating that PF could have compounds with antioxidant features. The comparative proteomic profiling identified 53 proteins with differential expression related to antioxidant action, catalysis, molecular function regulators, structural molecule activity, translation regulatory activity, ATP, and binding. The PF + H2O2 group indicated that protein expression is 6% upregulated, 4% downregulated, and 94% unchanged compared to the H2O2 group. Three significant proteins upregulated in the PF + H2O2 group, including elongation factor 2 (P58252), proteasome subunit alpha type (E9Q0X0), and E2 ubiquitin-conjugating enzyme (A0A338P786), suggested that PF-mediated neuroprotection happens through translational regulation and the degradation of defective proteins via the proteasome complex. Additionally, differential protein expression in PF changed the metabolism, protein synthesis, synaptic activity, and intracellular transport, suggesting that PF contains the rich mixture of bioactive peptides of interest pharmacologically. Overall, this study offers new opportunities for evaluating whether PF\u2019s neuroprotective features in specific neuronal cells are maintained and to investigate neurodegenerative disease drug development processes.<\/jats:p>","DOI":"10.3390\/antiox14030277","type":"journal-article","created":{"date-parts":[[2025,2,26]],"date-time":"2025-02-26T11:22:12Z","timestamp":1740568932000},"page":"277","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Peptide Fraction from Naja mandalayensis Snake Venom Showed Neuroprotection Against Oxidative Stress in Hippocampal mHippoE-18 Cells but Not in Neuronal PC12 Cells"],"prefix":"10.3390","volume":"14","author":[{"given":"Brenda R.","family":"Silva","sequence":"first","affiliation":[{"name":"Experimental Morphophysiology Laboratory, Natural and Humanities Sciences Center (CCNH), Universidade Federal do ABC (UFABC), S\u00e3o Bernardo do Campo 09606-070, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6313-7029","authenticated-orcid":false,"given":"Lais C.","family":"Mendes","sequence":"additional","affiliation":[{"name":"Biochemistry Laboratory, Butantan Institute, S\u00e3o Paulo 05503-900, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marcela B.","family":"Echeverry","sequence":"additional","affiliation":[{"name":"Center for Mathematics, Computation and Cognition (CMCC), Universidade Federal do ABC UFABC, S\u00e3o Bernardo do Campo 09606-070, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maria Aparecida","family":"Juliano","sequence":"additional","affiliation":[{"name":"Departament of Biophysical, Escola Paulista de Medicina, Instituto de Ci\u00eancias Ambientais, Qu\u00edmicas e Farmac\u00eauticas, Universidade Federal de S\u00e3o Paulo, S\u00e3o Paulo 04023-062, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Emidio","family":"Beraldo-Neto","sequence":"additional","affiliation":[{"name":"Biochemistry Laboratory, Butantan Institute, S\u00e3o Paulo 05503-900, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4519-8930","authenticated-orcid":false,"given":"Carlos","family":"Alberto-Silva","sequence":"additional","affiliation":[{"name":"Experimental Morphophysiology Laboratory, Natural and Humanities Sciences Center (CCNH), Universidade Federal do ABC (UFABC), S\u00e3o Bernardo do Campo 09606-070, SP, Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2025,2,26]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"897","DOI":"10.32604\/biocell.2024.050443","article-title":"Molecular and Cellular Mechanisms of Neuroprotection by Oligopeptides from Snake Venoms","volume":"48","year":"2024","journal-title":"Biocell"},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Alberto-Silva, C., and Portaro, F.C.V. (2024). Neuroprotection Mediated by Snake Venom. Natural Molecules in Neuroprotection and Neurotoxicity, Academic Press.","DOI":"10.1016\/B978-0-443-23763-8.00019-1"},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Frangieh, J., Rima, M., Fajloun, Z., Henrion, D., Sabatier, J.M., Legros, C., and Mattei, C. (2021). Snake Venom Components: Tools and Cures to Target Cardiovascular Diseases. Molecules, 26.","DOI":"10.3390\/molecules26082223"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"20230039","DOI":"10.1590\/1678-9199-jvatitd-2023-0039","article-title":"Snake Venom Disintegrins Update: Insights about New Findings","volume":"29","author":"Arantes","year":"2023","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.cbi.2015.04.004","article-title":"A Tripeptide Isolated from Bothrops atrox Venom Has Neuroprotective and Neurotrophic Effects on a Cellular Model of Parkinson\u2019s Disease","volume":"235","author":"Martins","year":"2015","journal-title":"Chem. Biol. Interact."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.toxicon.2010.03.014","article-title":"Low-Molecular-Mass Peptides from the Venom of the Amazonian Viper Bothrops atrox Protect against Brain Mitochondrial Swelling in Rat: Potential for Neuroprotection","volume":"56","author":"Martins","year":"2010","journal-title":"Toxicon"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.peptides.2018.03.017","article-title":"Bradykinin-Potentiating PEPTIDE-10C, an Argininosuccinate Synthetase Activator, Protects against H2O2-Induced Oxidative Stress in SH-SY5Y Neuroblastoma Cells","volume":"103","author":"Querobino","year":"2018","journal-title":"Peptides"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.toxicon.2017.02.015","article-title":"Neuroprotective Property of Low Molecular Weight Fraction from B. jararaca Snake Venom in H2O2-Induced Cytotoxicity in Cultured Hippocampal Cells","volume":"129","author":"Querobino","year":"2017","journal-title":"Toxicon"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.toxicon.2019.06.012","article-title":"Protective Effects of Distinct Proline-Rich Oligopeptides from B. jararaca Snake Venom against Oxidative Stress-Induced Neurotoxicity","volume":"167","author":"Querobino","year":"2019","journal-title":"Toxicon"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"e20230043","DOI":"10.1590\/1678-9199-jvatitd-2023-0043","article-title":"Activation of M1 Muscarinic Acetylcholine Receptors by Proline-Rich Oligopeptide 7a (<EDGPIPP) from Bothrops jararaca Snake Venom Rescues Oxidative Stress-Induced Neurotoxicity in PC12 Cells","volume":"30","author":"Echeverry","year":"2024","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"107178","DOI":"10.1016\/j.toxicon.2023.107178","article-title":"Peptide Fraction from B. jararaca Snake Venom Protects against Oxidative Stress-Induced Changes in Neuronal PC12 Cell but Not in Astrocyte-like C6 Cell","volume":"231","author":"Echeverry","year":"2023","journal-title":"Toxicon"},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Munawar, A., Ali, S.A., Akrem, A., and Betzel, C. (2018). Snake Venom Peptides: Tools of Biodiscovery. Toxins, 10.","DOI":"10.3390\/toxins10110474"},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Dugger, B.N., and Dickson, D.W. (2017). Pathology of Neurodegenerative Diseases. Cold Spring Harb. Perspect. Biol., 9.","DOI":"10.1101\/cshperspect.a028035"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"102357","DOI":"10.1016\/j.arr.2024.102357","article-title":"Neurodegenerative Disorders: Mechanisms of Degeneration and Therapeutic Approaches with Their Clinical Relevance","volume":"99","author":"Gadhave","year":"2024","journal-title":"Ageing Res. Rev."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"170528","DOI":"10.1016\/j.peptides.2021.170528","article-title":"Whether Short Peptides Are Good Candidates for Future Neuroprotective Therapeutics?","volume":"140","author":"Perlikowska","year":"2021","journal-title":"Peptides"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1038\/s41392-024-01839-8","article-title":"Mitochondrial Dysfunction: Mechanisms and Advances in Therapy","volume":"9","author":"Zong","year":"2024","journal-title":"Signal Transduct. Target. Ther."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Dur\u00e3es, F., Pinto, M., and Sousa, E. (2018). Old Drugs as New Treatments for Neurodegenerative Diseases. Pharmaceuticals, 11.","DOI":"10.3390\/ph11020044"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1038\/s41582-020-00435-y","article-title":"Neuroinflammation and Microglial Activation in Alzheimer Disease: Where Do We Go from Here?","volume":"17","author":"Leng","year":"2021","journal-title":"Nat. Rev. Neurol."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Kumar, H., Dhalaria, R., Guleria, S., Cimler, R., Sharma, R., Siddiqui, S.A., Valko, M., Nepovimova, E., Dhanjal, D.S., and Singh, R. (2023). Anti-Oxidant Potential of Plants and Probiotic Spp. in Alleviating Oxidative Stress Induced by H2O2. Biomed. Pharmacother., 165.","DOI":"10.1016\/j.biopha.2023.115022"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1007\/s10522-023-10050-1","article-title":"Aging, Oxidative Stress and Degenerative Diseases: Mechanisms, Complications and Emerging Therapeutic Strategies","volume":"24","author":"Chaudhary","year":"2023","journal-title":"Biogerontology"},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Demirci-\u00c7eki\u00e7, S., \u00d6zkan, G., Avan, A.N., Uzunboy, S., \u00c7apano\u011flu, E., and Apak, R. (2022). Biomarkers of Oxidative Stress and Antioxidant Defense. J. Pharm. Biomed. Anal., 209.","DOI":"10.1016\/j.jpba.2021.114477"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"310504","DOI":"10.1155\/2014\/310504","article-title":"N-Acetyl-Serotonin Protects HepG2 Cells from Oxidative Stress Injury Induced by Hydrogen Peroxide","volume":"2014","author":"Jiang","year":"2014","journal-title":"Oxid. Med. Cell Longev."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Alberto-Silva, C., da Silva, B.R., da Silva, J.C.A., Cunha e Silva, F.A.D., Kodama, R.T., da Silva, W.D., Costa, M.S., and Portaro, F.C.V. (2024). Small Structural Differences in Proline-Rich Decapeptides Have Specific Effects on Oxidative Stress-Induced Neurotoxicity and L-Arginine Generation by Arginosuccinate Synthase. Pharmaceuticals, 17.","DOI":"10.3390\/ph17070931"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.biochi.2020.11.022","article-title":"Reactive Oxygen and Nitrogen Species and Innate Immune Response","volume":"181","year":"2021","journal-title":"Biochimie"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"428010","DOI":"10.1155\/2012\/428010","article-title":"Mechanism of Oxidative Stress in Neurodegeneration","volume":"2012","author":"Gandhi","year":"2012","journal-title":"Oxid. Med. Cell Longev."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"17","DOI":"10.33549\/physiolres.933895","article-title":"In Vivo, in Vitro and Pharmacologic Models of Parkinson\u2019s Disease","volume":"68","author":"Salari","year":"2019","journal-title":"Physiol. Res."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1016\/j.tips.2020.05.006","article-title":"Causes and Consequences of Snake Venom Variation","volume":"41","author":"Casewell","year":"2020","journal-title":"Trends Pharmacol. Sci."},{"key":"ref_28","first-page":"257","article-title":"A New Cobra (Elapidae: Naja) from Myanmar (Burma) on JSTOR","volume":"56","author":"Slowinski","year":"2000","journal-title":"Herpetologica"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"e20200125","DOI":"10.1590\/1678-9199-jvatitd-2020-0125","article-title":"Proteomic Characterization of Naja mandalayensis Venom","volume":"27","author":"Neto","year":"2021","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Abdullah, N.A.H., Sainik, N.Q.A.V., Esa, E., Muhamad Hendri, N.A., Ahmad Rusmili, M.R., Hodgson, W.C., Shaikh, M.F., and Othman, I. (2022). Neuroprotective Effect of Phospholipase A2 from Malaysian Naja sumatrana Venom against H2O2-Induced Cell Damage and Apoptosis. Front. Pharmacol., 13.","DOI":"10.3389\/fphar.2022.935418"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"61","DOI":"10.6000\/1927-3037.2015.04.02.3","article-title":"Current Situation of PC12 Cell Use in Neuronal Injury Study","volume":"4","author":"Duan","year":"2015","journal-title":"Int. J. Biotechnol. Wellness Ind."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1007\/s00424-017-2044-5","article-title":"Chromaffin Cells as a Model to Evaluate Mechanisms of Cell Death and Neuroprotective Compounds","volume":"470","author":"Villarroya","year":"2018","journal-title":"Pflug. Arch."},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Wiatrak, B., Kubis-Kubiak, A., Piwowar, A., and Barg, E. (2020). PC12 Cell Line: Cell Types, Coating of Culture Vessels, Differentiation and Other Culture Conditions. Cells, 9.","DOI":"10.3390\/cells9040958"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"2424","DOI":"10.1073\/pnas.73.7.2424","article-title":"Establishment of a Noradrenergic Clonal Line of Rat Adrenal Pheochromocytoma Cells Which Respond to Nerve Growth Factor","volume":"73","author":"Greene","year":"1976","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.neuroscience.2010.06.076","article-title":"Estrogen Receptor \u03b1 and G-Protein Coupled Receptor 30 Mediate the Neuroprotective Effects of 17\u03b2-Estradiol in Novel Murine Hippocampal Cell Models","volume":"170","author":"Gingerich","year":"2010","journal-title":"Neuroscience"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1101\/pdb.prot087379","article-title":"Crystal Violet Assay for Determining Viability of Cultured Cells","volume":"2016","author":"Feoktistova","year":"2016","journal-title":"Cold Spring Harb. Protoc."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/j.freeradbiomed.2018.10.446","article-title":"Mitochondrial Superoxide Generation Induces a Parkinsonian Phenotype in Zebrafish and Huntingtin Aggregation in Human Cells","volume":"130","author":"Pinho","year":"2019","journal-title":"Free Radic. Biol. Med."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/j.jtemb.2014.08.001","article-title":"Diphenyl Diselenide (PhSe)2 Inhibits Biofilm Formation by Candida Albicans, Increasing Both ROS Production and Membrane Permeability","volume":"29","author":"Rosseti","year":"2015","journal-title":"J. Trace Elem. Med. Biol."},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Beraldo-Neto, E., Ferreira, V.F., Vigerelli, H., Fernandes, K.R., Juliano, M.A., Nencioni, A.L.A., and Pimenta, D.C. (2024). Unraveling Neuroprotection with Kv1.3 Potassium Channel Blockade by a Scorpion Venom Peptide. Sci. Rep., 14.","DOI":"10.1038\/s41598-024-79152-1"},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"de Souza, J.M., Goncalves, B.D.C., Gomez, M.V., Vieira, L.B., and Ribeiro, F.M. (2018). Animal Toxins as Therapeutic Tools to Treat Neurodegenerative Diseases. Front. Pharmacol., 9.","DOI":"10.3389\/fphar.2018.00145"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"850","DOI":"10.3390\/toxins6030850","article-title":"Elapid Snake Venom Analyses Show the Specificity of the Peptide Composition at the Level of Genera Naja and Notechis","volume":"6","author":"Munawar","year":"2014","journal-title":"Toxins"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1007\/s00204-022-03420-0","article-title":"A Current Perspective on Snake Venom Composition and Constituent Protein Families","volume":"97","author":"Tasoulis","year":"2022","journal-title":"Arch. Toxicol."},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Peng, Y., Chu, S., Yang, Y., Zhang, Z., Pang, Z., and Chen, N. (2021). Neuroinflammatory In Vitro Cell Culture Models and the Potential Applications for Neurological Disorders. Front. Pharmacol., 12.","DOI":"10.3389\/fphar.2021.671734"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"giac024","DOI":"10.1093\/gigascience\/giac024","article-title":"The Rise of Genomics in Snake Venom Research: Recent Advances and Future Perspectives","volume":"11","author":"Rao","year":"2022","journal-title":"GigaScience"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"4205","DOI":"10.3892\/mmr.2016.5056","article-title":"Lycopene Protects Human SH-SY5Y Neuroblastoma Cells against Hydrogen Peroxide-Induced Death via Inhibition of Oxidative Stress and Mitochondria-Associated Apoptotic Pathways","volume":"13","author":"Feng","year":"2016","journal-title":"Mol. Med. Rep."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"338","DOI":"10.4062\/biomolther.2015.135","article-title":"The Neuro-Protective Effect of the Methanolic Extract of Perilla frutescens Var. Japonicaand Rosmarinic Acid against H2O2-Induced Oxidative Stress in C6 Glial Cells","volume":"24","author":"Lee","year":"2016","journal-title":"Biomol. Ther."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1007\/s10695-015-0179-x","article-title":"Effects of L-Carnitine against H2O2-Induced Oxidative Stress in Grass Carp Ovary Cells (Ctenopharyngodon idellus)","volume":"42","author":"Wang","year":"2016","journal-title":"Fish. Physiol. Biochem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"S21","DOI":"10.3233\/JAD-221233","article-title":"Centella asiatica (L.) Urban. Attenuates Cell Damage in Hydrogen Peroxide-Induced Oxidative Stress in Transgenic Murine Embryonic Stem Cell Line-Derived Neural-Like Cells: A Preliminary Study for Potential Treatment of Alzheimer\u2019s Disease","volume":"94","author":"Mansor","year":"2023","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Collin, F. (2019). Chemical Basis of Reactive Oxygen Species Reactivity and Involvement in Neurodegenerative Diseases. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20102407"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"867","DOI":"10.4014\/jmb.2101.01002","article-title":"Neuroprotective Effect of Epalrestat on Hydrogen Peroxide-Induced Neurodegeneration in SH-SY5Y Cellular Model","volume":"31","author":"Lingappa","year":"2021","journal-title":"J. Microbiol. Biotechnol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1007\/s12031-009-9285-5","article-title":"Neuroprotective Effect of Baicalein on Hydrogen Peroxide-Mediated Oxidative Stress and Mitochondrial Dysfunction in PC12 Cells","volume":"40","author":"Zhang","year":"2010","journal-title":"J. Mol. Neurosci."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"118","DOI":"10.17221\/401\/2015-CJFS","article-title":"Determination of Trans-Resveratrol Action on Two Different Types of Neuronal Cells, Neuroblastoma and Hippocampal Cells","volume":"34","author":"Gerszon","year":"2016","journal-title":"Czech J. Food Sci."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"391","DOI":"10.3390\/neuroglia5040026","article-title":"Harnessing Mitophagy for Therapeutic Advances in Aging and Chronic Neurodegenerative Diseases","volume":"5","author":"Ghosh","year":"2024","journal-title":"Neuroglia"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"fcad356","DOI":"10.1093\/braincomms\/fcad356","article-title":"Role of Oxidative Stress in Neurodegenerative Disorders: A Review of Reactive Oxygen Species and Prevention by Antioxidants","volume":"6","author":"Houldsworth","year":"2024","journal-title":"Brain Commun."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1016\/j.redox.2014.02.006","article-title":"Hydrogen Peroxide Sensing, Signaling and Regulation of Transcription Factors","volume":"2","author":"Marinho","year":"2014","journal-title":"Redox Biol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.mam.2016.05.001","article-title":"Degradation of Oxidized Proteins by the Proteasome: Distinguishing between the 20S, 26S, and Immunoproteasome Proteolytic Pathways","volume":"50","author":"Raynes","year":"2016","journal-title":"Mol. Asp. Med."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"23105","DOI":"10.1074\/jbc.271.38.23105","article-title":"Effect of Oxidative Stress, Produced by Cumene Hydroperoxide, on the Various Steps of Protein Synthesis. Modifications of Elongation Factor-2","volume":"271","author":"Ayala","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1096\/fj.09-136259","article-title":"The Family of Ubiquitin-Conjugating Enzymes (E2s): Deciding between Life and Death of Proteins","volume":"24","author":"Wijk","year":"2010","journal-title":"FASEB J."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/BST0340001","article-title":"The Life and Death of Translation Elongation Factor 2","volume":"34","author":"Merrill","year":"2006","journal-title":"Biochem. Soc. Trans."},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Ngo, V., and Duennwald, M.L. (2022). Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease. Antioxidants, 11.","DOI":"10.3390\/antiox11122345"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1038\/s12276-021-00560-8","article-title":"The Aftermath of the Interplay between the Endoplasmic Reticulum Stress Response and Redox Signaling","volume":"53","author":"Bhattarai","year":"2021","journal-title":"Exp. Mol. Med."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1016\/j.freeradbiomed.2012.09.016","article-title":"Oxidative Stress, Neurodegeneration, and the Balance of Protein Degradation and Protein Synthesis","volume":"62","author":"Dasuri","year":"2013","journal-title":"Free Radic. Biol. Med."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1002\/bip.21292","article-title":"Hsp90 and Co-Chaperones Twist the Functions of Diverse Client Proteins","volume":"93","author":"Zuehlke","year":"2010","journal-title":"Biopolymers"},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Seixas, C., Cruto, T., Tavares, A., Gaertig, J., and Soares, H. (2010). CCT\u03b1 and CCT\u03b4 Chaperonin Subunits Are Essential and Required for Cilia Assembly and Maintenance in Tetrahymena. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0010704"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"29398","DOI":"10.1074\/jbc.M110.141440","article-title":"Regulation of Integrin \u03b2 1 Recycling to Lipid Rafts by Rab1a to Promote Cell Migration","volume":"285","author":"Wang","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"2523","DOI":"10.1172\/JCI65401","article-title":"Endocytosis of Synaptic ADAM10 in Neuronal Plasticity and Alzheimer\u2019s Disease","volume":"123","author":"Marcello","year":"2013","journal-title":"J. Clin. Invest."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"525","DOI":"10.3892\/ijo.2016.3814","article-title":"Fructose-Bisphosphate Aldolase A Is a Key Regulator of Hypoxic Adaptation in Colorectal Cancer Cells and Involved in Treatment Resistance and Poor Prognosis","volume":"50","author":"Kawai","year":"2017","journal-title":"Int. J. Oncol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1016\/j.semcdb.2011.08.009","article-title":"14-3-3 Proteins: Diverse Functions in Cell Proliferation and Cancer Progression","volume":"22","author":"Freeman","year":"2011","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1016\/S0092-8674(00)80361-X","article-title":"Nuclear Export Receptors: From Importin to Exportin","volume":"90","author":"Ullman","year":"1997","journal-title":"Cell"},{"key":"ref_70","unstructured":"Farhana, A., and Lappin, S.L. (2023). Biochemistry, Lactate Dehydrogenase. StatPearls, StatPearls Publishing."}],"container-title":["Antioxidants"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-3921\/14\/3\/277\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T16:43:30Z","timestamp":1760028210000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-3921\/14\/3\/277"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,2,26]]},"references-count":70,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2025,3]]}},"alternative-id":["antiox14030277"],"URL":"https:\/\/doi.org\/10.3390\/antiox14030277","relation":{},"ISSN":["2076-3921"],"issn-type":[{"type":"electronic","value":"2076-3921"}],"subject":[],"published":{"date-parts":[[2025,2,26]]}}}