<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE root>
<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">Current Gene Therapy</journal-id><journal-title-group><journal-title xml:lang="en">Current Gene Therapy</journal-title><trans-title-group xml:lang="ru"><trans-title>Current Gene Therapy</trans-title></trans-title-group></journal-title-group><issn publication-format="print">1566-5232</issn><issn publication-format="electronic">1875-5631</issn><publisher><publisher-name xml:lang="en">Bentham Science</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="publisher-id">643907</article-id><article-id pub-id-type="doi">10.2174/1566523223666230731093030</article-id><article-categories><subj-group subj-group-type="toc-heading"><subject>Life Sciences</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">Non-coding RNAs in Regulation of Protein Aggregation and Clearance Pathways: Current Perspectives Towards Alzheimer's Research and Therapy</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Sundram</surname><given-names>Sonali</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><name><surname>Dhiman</surname><given-names>Neerupma</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff2"/></contrib><contrib contrib-type="author"><name><surname>Malviya</surname><given-names>Rishabha</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><name><surname>Awasthi</surname><given-names>Rajendra</given-names></name><email>info@benthamscience.net</email><xref ref-type="aff" rid="aff3"/></contrib></contrib-group><aff id="aff1"><institution>Department of Pharmacy, School of Medical and Allied Sciences, Galgotias University</institution></aff><aff id="aff2"><institution>Amity Institute of Pharmacy, Amity University Uttar Pradesh</institution></aff><aff id="aff3"><institution>Department of Pharmaceutical Sciences, School of Health Sciences &amp; Technology, UPES University</institution></aff><pub-date date-type="pub" iso-8601-date="2024-01-01" publication-format="electronic"><day>01</day><month>01</month><year>2024</year></pub-date><volume>24</volume><issue>1</issue><fpage>8</fpage><lpage>16</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://journals.eco-vector.com/1566-5232/article/view/643907">https://journals.eco-vector.com/1566-5232/article/view/643907</self-uri><abstract xml:lang="en"><p id="idm46041443719344">Alzheimer's disease (AD) is the leading cause of dementia, affecting approximately 45.0 million people worldwide and ranking as the fifth leading cause of mortality. AD is identified by neurofibrillary tangles (NFTs), which include abnormally phosphorylated tau-protein and amyloid protein (amyloid plaques). Peptide dysregulation is caused by an imbalance between the production and clearance of the amyloid-beta (Aβ) and NFT. AD begins to develop when these peptides are not cleared from the body. As a result, understanding the processes that control both normal and pathological protein recycling in neuronal cells is critical. Insufficient Aβ and NFT clearance are important factors in the development of AD. Autophagy, lysosomal dysfunction, and ubiquitin-proteasome dysfunction have potential roles in the pathogenesis of many neurodegenerative disorders, particularly in AD. Modulation of these pathways may provide a novel treatment strategy for AD. Non-coding RNAs (ncRNAs) have recently emerged as important biological regulators, with particular relevance to the emergence and development of neurodegenerative disorders such as AD. ncRNAs can be used as potential therapeutic targets and diagnostic biomarkers due to their critical regulatory functions in several biological processes involved in disease development, such as the aggregation and accumulation of Aβ and NFT. It is evident that ncRNAs play a role in the pathophysiology of AD. In this communication, we explored the link between ncRNAs and AD and their regulatory mechanisms that may help in finding new therapeutic targets and AD medications.</p></abstract><kwd-group xml:lang="en"><kwd>Alzheimer's disease</kwd><kwd>dementia</kwd><kwd>neurodegenerative disorder</kwd><kwd>tau protein</kwd><kwd>Non-coding RNAs</kwd><kwd>motor skills impairment.</kwd></kwd-group></article-meta></front><body></body><back><ref-list><ref id="B1"><label>1.</label><mixed-citation>Hussain R, Zubair H, Pursell S, Shahab M. Neurodegenerative diseases: Regenerative mechanisms and novel therapeutic approaches. Brain Sci 2018; 8(9): 177. doi: 10.3390/brainsci8090177 PMID: 30223579</mixed-citation></ref><ref id="B2"><label>2.</label><mixed-citation>2023 Alzheimers disease facts and figures. Alzheimers Dement 2023; 19(4): 1598-695. doi: 10.1002/alz.13016 PMID: 36918389</mixed-citation></ref><ref id="B3"><label>3.</label><mixed-citation>Weglinski C, Jeans A. Amyloid-β in Alzheimers disease: Front and centre after all? Neuronal Signal 2023; 7(1): NS20220086. doi: 10.1042/NS20220086 PMID: 36687366</mixed-citation></ref><ref id="B4"><label>4.</label><mixed-citation>Rawat P, Sehar U, Bisht J, Selman A, Culberson J, Reddy PH. Phosphorylated tau in alzheimers disease and other tauopathies. Int J Mol Sci 2022; 23(21): 12841. doi: 10.3390/ijms232112841 PMID: 36361631</mixed-citation></ref><ref id="B5"><label>5.</label><mixed-citation>Ajmal MR. Protein misfolding and aggregation in proteinopathies: causes, mechanism and cellular response. Diseases 2023; 11(1): 30. doi: 10.3390/diseases11010030 PMID: 36810544</mixed-citation></ref><ref id="B6"><label>6.</label><mixed-citation>Tecalco-Cruz AC, Pedraza-Chaverri J, Briones-Herrera A, Cruz-Ramos E, López-Canovas L, Zepeda-Cervantes J. Protein degradation-associated mechanisms that are affected in Alzheimers disease. Mol Cell Biochem 2022; 477(3): 915-25. doi: 10.1007/s11010-021-04334-8 PMID: 35083609</mixed-citation></ref><ref id="B7"><label>7.</label><mixed-citation>Frankowska N, Lisowska K, Witkowski JM. Proteolysis dysfunction in the process of aging and age-related diseases. Frontiers in Aging 2022; 3: 927630. doi: 10.3389/fragi.2022.927630 PMID: 35958270</mixed-citation></ref><ref id="B8"><label>8.</label><mixed-citation>Vilchez D, Saez I, Dillin A. The role of protein clearance mechanisms in organismal ageing and age-related diseases. Nat Commun 2014; 5(1): 5659. doi: 10.1038/ncomms6659 PMID: 25482515</mixed-citation></ref><ref id="B9"><label>9.</label><mixed-citation>Boland B, Yu WH, Corti O, et al. Promoting the clearance of neurotoxic proteins in neurodegenerative disorders of ageing. Nat Rev Drug Discov 2018; 17(9): 660-88. doi: 10.1038/nrd.2018.109 PMID: 30116051</mixed-citation></ref><ref id="B10"><label>10.</label><mixed-citation>Hipp MS, Kasturi P, Hartl FU. The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 2019; 20(7): 421-35. doi: 10.1038/s41580-019-0101-y PMID: 30733602</mixed-citation></ref><ref id="B11"><label>11.</label><mixed-citation>Sengupta S. Noncoding RNAs in protein clearance pathways: implications in neurodegenerative diseases. J Genet 2017; 96(1): 203-10. doi: 10.1007/s12041-017-0747-1 PMID: 28360406</mixed-citation></ref><ref id="B12"><label>12.</label><mixed-citation>Wang M, Qin L, Tang B. MicroRNAs in Alzheimers disease. Front Genet 2019; 10: 153. doi: 10.3389/fgene.2019.00153 PMID: 30881384</mixed-citation></ref><ref id="B13"><label>13.</label><mixed-citation>Peplow PV, Martinez B. MicroRNAs as diagnostic and therapeutic tools for Alzheimers disease: Advances and limitations. Neural Regen Res 2019; 14(2): 242-55. doi: 10.4103/1673-5374.244784 PMID: 30531004</mixed-citation></ref><ref id="B14"><label>14.</label><mixed-citation>Idda ML, Munk R, Abdelmohsen K, Gorospe M. Noncoding RNAs in Alzheimers disease. Wiley Interdiscip Rev RNA 2018; 9(2): e1463. doi: 10.1002/wrna.1463 PMID: 29327503</mixed-citation></ref><ref id="B15"><label>15.</label><mixed-citation>Statello L, Guo CJ, Chen LL, Huarte M. Gene regulation by long non-coding RNAs and its biological functions. Nat Rev Mol Cell Biol 2021; 22(2): 96-118. doi: 10.1038/s41580-020-00315-9 PMID: 33353982</mixed-citation></ref><ref id="B16"><label>16.</label><mixed-citation>Hombach S, Kretz M. Non-coding RNAs: Classification, biology and functioning. Adv Exp Med Biol 2016; 937: 3-17. doi: 10.1007/978-3-319-42059-2_1 PMID: 27573892</mixed-citation></ref><ref id="B17"><label>17.</label><mixed-citation>Losko M, Kotlinowski J, Jura J. Long Noncoding RNAs in metabolic syndrome related disorders. Mediators Inflamm 2016; 2016: 1-12. doi: 10.1155/2016/5365209 PMID: 27881904</mixed-citation></ref><ref id="B18"><label>18.</label><mixed-citation>Morey C, Avner P. Employment opportunities for non-coding RNAs. FEBS Lett 2004; 567(1): 27-34. doi: 10.1016/j.febslet.2004.03.117 PMID: 15165889</mixed-citation></ref><ref id="B19"><label>19.</label><mixed-citation>Guennewig B, Cooper AA. The central role of noncoding RNA in the brain. Int Rev Neurobiol 2014; 116: 153-94. doi: 10.1016/B978-0-12-801105-8.00007-2 PMID: 25172475</mixed-citation></ref><ref id="B20"><label>20.</label><mixed-citation>Wu YY, Kuo HC. Functional roles and networks of non-coding RNAs in the pathogenesis of neurodegenerative diseases. J Biomed Sci 2020; 27(1): 49. doi: 10.1186/s12929-020-00636-z PMID: 32264890</mixed-citation></ref><ref id="B21"><label>21.</label><mixed-citation>Taylor JP, Hardy J, Fischbeck KH. Toxic proteins in neurodegenerative disease. Science 2002; 296(5575): 1991-5. doi: 10.1126/science.1067122 PMID: 12065827</mixed-citation></ref><ref id="B22"><label>22.</label><mixed-citation>Lim J, Yue Z. Neuronal aggregates: Formation, clearance, and spreading. Dev Cell 2015; 32(4): 491-501. doi: 10.1016/j.devcel.2015.02.002 PMID: 25710535</mixed-citation></ref><ref id="B23"><label>23.</label><mixed-citation>Petrella C, Di Certo MG, Barbato C, et al. Neuropeptides in Alzheimers disease: An update. Curr Alzheimer Res 2019; 16(6): 544-58. doi: 10.2174/1567205016666190503152555 PMID: 31456515</mixed-citation></ref><ref id="B24"><label>24.</label><mixed-citation>OBrien RJ, Wong PC. Amyloid precursor protein processing and Alzheimers disease. Annu Rev Neurosci 2011; 34(1): 185-204. doi: 10.1146/annurev-neuro-061010-113613 PMID: 21456963</mixed-citation></ref><ref id="B25"><label>25.</label><mixed-citation>Vu Nguyen K. β-Amyloid precursor protein (APP) and the human diseases. AIMS Neurosci 2019; 6(4): 273-81. doi: 10.3934/Neuroscience.2019.4.273 PMID: 32341983</mixed-citation></ref><ref id="B26"><label>26.</label><mixed-citation>Kolarova M, García-Sierra F, Bartos A, Ricny J, Ripova D. Structure and pathology of tau protein in Alzheimer disease. Int J Alzheimers Dis 2012; 2012: 1-13. doi: 10.1155/2012/731526 PMID: 22690349</mixed-citation></ref><ref id="B27"><label>27.</label><mixed-citation>Martin L, Latypova X, Terro F. Post-translational modifications of tau protein: Implications for Alzheimers disease. Neurochem Int 2011; 58(4): 458-71. doi: 10.1016/j.neuint.2010.12.023 PMID: 21215781</mixed-citation></ref><ref id="B28"><label>28.</label><mixed-citation>Buée L, Bussière T, Buée-Scherrer V, Delacourte A, Hof PR. Tau protein isoforms, phosphorylation and role in neurodegenerative disorders. Brain Res Brain Res Rev 2000; 33(1): 95-130. doi: 10.1016/S0165-0173(00)00019-9 PMID: 10967355</mixed-citation></ref><ref id="B29"><label>29.</label><mixed-citation>Kadavath H, Hofele RV, Biernat J, et al. Tau stabilizes microtubules by binding at the interface between tubulin heterodimers. Proc Natl Acad Sci 2015; 112(24): 7501-6. doi: 10.1073/pnas.1504081112 PMID: 26034266</mixed-citation></ref><ref id="B30"><label>30.</label><mixed-citation>Matsui T, Ingelsson M, Fukumoto H, et al. Expression of APP pathway mRNAs and proteins in Alzheimers disease. Brain Res 2007; 1161: 116-23. doi: 10.1016/j.brainres.2007.05.050 PMID: 17586478</mixed-citation></ref><ref id="B31"><label>31.</label><mixed-citation>Estrada L, Soto C. Disrupting β-amyloid aggregation for Alzheimer disease treatment. Curr Top Med Chem 2007; 7(1): 115-26. doi: 10.2174/156802607779318262 PMID: 17266599</mixed-citation></ref><ref id="B32"><label>32.</label><mixed-citation>Hommen F, Bilican S, Vilchez D. Protein clearance strategies for disease intervention. J Neural Transm 2022; 129(2): 141-72. doi: 10.1007/s00702-021-02431-y PMID: 34689261</mixed-citation></ref><ref id="B33"><label>33.</label><mixed-citation>Jayaraj GG, Hipp MS, Hartl FU. Functional modules of the proteostasis network. Cold Spring Harb Perspect Biol 2020; 12(1): a033951. doi: 10.1101/cshperspect.a033951 PMID: 30833457</mixed-citation></ref><ref id="B34"><label>34.</label><mixed-citation>Fecto F, Esengul Y, Siddique T. Protein recycling pathways in neurodegenerative diseases. Alzheimers Res Ther 2014; 6(2): 13. doi: 10.1186/alzrt243 PMID: 25031631</mixed-citation></ref><ref id="B35"><label>35.</label><mixed-citation>Bukau B, Weissman J, Horwich A. Molecular chaperones and protein quality control. Cell 2006; 125(3): 443-51. doi: 10.1016/j.cell.2006.04.014 PMID: 16678092</mixed-citation></ref><ref id="B36"><label>36.</label><mixed-citation>Miller DJ, Fort PE. Heat shock proteins regulatory role in neurodevelopment. Front Neurosci 2018; 12: 821. doi: 10.3389/fnins.2018.00821 PMID: 30483047</mixed-citation></ref><ref id="B37"><label>37.</label><mixed-citation>Chen JJ, Lin F, Qin ZH. The roles of the proteasome pathway in signal transduction and neurodegenerative diseases. Neurosci Bull 2008; 24(3): 183-94. doi: 10.1007/s12264-008-0183-6 PMID: 18500392</mixed-citation></ref><ref id="B38"><label>38.</label><mixed-citation>Melino G. Discovery of the ubiquitin proteasome system and its involvement in apoptosis. Cell Death Differ 2005; 12(9): 1155-7. doi: 10.1038/sj.cdd.4401740 PMID: 16094390</mixed-citation></ref><ref id="B39"><label>39.</label><mixed-citation>Goldberg AL. Protein degradation and protection against misfolded or damaged proteins. Nature 2003; 426(6968): 895-9. doi: 10.1038/nature02263 PMID: 14685250</mixed-citation></ref><ref id="B40"><label>40.</label><mixed-citation>Lambert-Smith IA, Saunders DN, Yerbury JJ. The pivotal role of ubiquitin-activating enzyme E1 (UBA1) in neuronal health and neurodegeneration. Int J Biochem Cell Biol 2020; 123: 105746. doi: 10.1016/j.biocel.2020.105746 PMID: 32315770</mixed-citation></ref><ref id="B41"><label>41.</label><mixed-citation>Ross CA, Poirier MA. Protein aggregation and neurodegenerative disease. Nat Med 2004; 10(S7) (Suppl.): S10-7. doi: 10.1038/nm1066 PMID: 15272267</mixed-citation></ref><ref id="B42"><label>42.</label><mixed-citation>Zhang T, Pang P, Fang Z, et al. Expression of BC1 impairs spatial learning and memory in Alzheimers disease via APP translation. Mol Neurobiol 2018; 55(7): 6007-20. doi: 10.1007/s12035-017-0820-z PMID: 29134514</mixed-citation></ref><ref id="B43"><label>43.</label><mixed-citation>Ciarlo E, Massone S, Penna I, et al. An intronic ncRNA-dependent regulation of SORL1 expression affecting Aβ formation is upregulated in post-mortem Alzheimers disease brain samples. Dis Model Mech 2012; 6(2): dmm.009761. doi: 10.1242/dmm.009761 PMID: 22996644</mixed-citation></ref><ref id="B44"><label>44.</label><mixed-citation>Taylor HA, Przemylska L, Clavane EM, Meakin PJ. BACE1: More than just a β-secretase. Obes Rev 2022; 23(7): e13430. doi: 10.1111/obr.13430 PMID: 35119166</mixed-citation></ref><ref id="B45"><label>45.</label><mixed-citation>Andersen OM, Reiche J, Schmidt V, et al. Neuronal sorting protein-related receptor sorLA/LR11 regulates processing of the amyloid precursor protein. Proc Natl Acad Sci 2005; 102(38): 13461-6. doi: 10.1073/pnas.0503689102 PMID: 16174740</mixed-citation></ref><ref id="B46"><label>46.</label><mixed-citation>Deng Y, Xiao L, Li W, et al. Plasma long noncoding RNA 51A as a stable biomarker of Alzheimers disease. Int J Clin Exp Pathol 2017; 10(4): 4694-9.</mixed-citation></ref><ref id="B47"><label>47.</label><mixed-citation>Long JM, Ray B, Lahiri DK. MicroRNA-153 physiologically inhibits expression of amyloid-β precursor protein in cultured human fetal brain cells and is dysregulated in a subset of Alzheimer disease patients. J Biol Chem 2012; 287(37): 31298-310. doi: 10.1074/jbc.M112.366336 PMID: 22733824</mixed-citation></ref><ref id="B48"><label>48.</label><mixed-citation>Bartel DP. MicroRNAs: Target recognition and regulatory functions. Cell 2009; 136(2): 215-33. doi: 10.1016/j.cell.2009.01.002 PMID: 19167326</mixed-citation></ref><ref id="B49"><label>49.</label><mixed-citation>Kleinberger G, Yamanishi Y, Suárez-Calvet M, et al. TREM2 mutations implicated in neurodegeneration impair cell surface transport and phagocytosis. Sci Transl Med 2014; 6(243): 243ra86. doi: 10.1126/scitranslmed.3009093 PMID: 24990881</mixed-citation></ref><ref id="B50"><label>50.</label><mixed-citation>Tiribuzi R, Crispoltoni L, Porcellati S, et al. miR128 up-regulation correlates with impaired amyloid β(1-42) degradation in monocytes from patients with sporadic Alzheimers disease. Neurobiol Aging 2014; 35(2): 345-56. doi: 10.1016/j.neurobiolaging.2013.08.003 PMID: 24064186</mixed-citation></ref><ref id="B51"><label>51.</label><mixed-citation>Patel N, Hoang D, Miller N, et al. MicroRNAs can regulate human APP levels. Mol Neurodegener 2008; 3(1): 10. doi: 10.1186/1750-1326-3-10 PMID: 18684319</mixed-citation></ref><ref id="B52"><label>52.</label><mixed-citation>Zhang H, Liang J, Chen N. The potential role of miRNA-regulated autophagy in Alzheimers disease. Int J Mol Sci 2022; 23(14): 7789. doi: 10.3390/ijms23147789 PMID: 35887134</mixed-citation></ref><ref id="B53"><label>53.</label><mixed-citation>Kim J, Fiesel FC, Belmonte KC, et al. miR-27a and miR-27b regulate autophagic clearance of damaged mitochondria by targeting PTEN-induced putative kinase 1 (PINK1). Mol Neurodegener 2016; 11(1): 55. doi: 10.1186/s13024-016-0121-4 PMID: 27456084</mixed-citation></ref><ref id="B54"><label>54.</label><mixed-citation>Yang L, Wang H, Shen Q, Feng L, Jin H. Long non-coding RNAs involved in autophagy regulation. Cell Death Dis 2017; 8(10): e3073. doi: 10.1038/cddis.2017.464 PMID: 28981093</mixed-citation></ref><ref id="B55"><label>55.</label><mixed-citation>Xu X, Cui L, Zhong W, Cai Y. Autophagy-associated lncRNAs: Promising targets for neurological disease diagnosis and therapy. Neural Plast 2020; 2020: 1-13. doi: 10.1155/2020/8881687 PMID: 33029125</mixed-citation></ref><ref id="B56"><label>56.</label><mixed-citation>Cortini F, Roma F, Villa C. Emerging roles of long non-coding RNAs in the pathogenesis of Alzheimers disease. Ageing Res Rev 2019; 50: 19-26. doi: 10.1016/j.arr.2019.01.001 PMID: 30610928</mixed-citation></ref><ref id="B57"><label>57.</label><mixed-citation>Ballantyne MD, McDonald RA, Baker AH. lncRNA/MicroRNA interactions in the vasculature. Clin Pharmacol Ther 2016; 99(5): 494-501. doi: 10.1002/cpt.355 PMID: 26910520</mixed-citation></ref><ref id="B58"><label>58.</label><mixed-citation>Massone S, Vassallo I, Fiorino G, et al. 17A, a novel non-coding RNA, regulates GABA B alternative splicing and signaling in response to inflammatory stimuli and in Alzheimer disease. Neurobiol Dis 2011; 41(2): 308-17. doi: 10.1016/j.nbd.2010.09.019 PMID: 20888417</mixed-citation></ref><ref id="B59"><label>59.</label><mixed-citation>Asadi MR, Hassani M, Kiani S, et al. The perspective of dysregulated LncRNAs in Alzheimers Disease: A systematic scoping review. Front Aging Neurosci 2021; 13: 709568. doi: 10.3389/fnagi.2021.709568 PMID: 34621163</mixed-citation></ref><ref id="B60"><label>60.</label><mixed-citation>Zhang M, He P, Bian Z. Long noncoding rnas in neurodegenerative diseases: Pathogenesis and potential implications as clinical biomarkers. Front Mol Neurosci 2021; 14: 685143. doi: 10.3389/fnmol.2021.685143 PMID: 34421536</mixed-citation></ref><ref id="B61"><label>61.</label><mixed-citation>Huang Z, Zhao J, Wang W, Zhou J, Zhang J. Depletion of LncRNA NEAT1 rescues mitochondrial dysfunction through NEDD4L-dependent PINK1 degradation in animal models of Alzheimers disease. Front Cell Neurosci 2020; 14: 28. doi: 10.3389/fncel.2020.00028 PMID: 32140098</mixed-citation></ref><ref id="B62"><label>62.</label><mixed-citation>Pathak GA, Silzer TK, Sun J, et al. Genome-wide methylation of mild cognitive impairment in mexican americans highlights genes involved in synaptic transport, alzheimers disease-precursor phenotypes, and metabolic morbidities. J Alzheimers Dis 2019; 72(3): 733-49. doi: 10.3233/JAD-190634 PMID: 31640099</mixed-citation></ref><ref id="B63"><label>63.</label><mixed-citation>Zhao MY, Wang GQ, Wang NN, Yu QY, Liu RL, Shi WQ. The long-non-coding RNA NEAT1 is a novel target for Alzheimers disease progression via miR-124/BACE1 axis. Neurol Res 2019; 41(6): 489-97. doi: 10.1080/01616412.2018.1548747 PMID: 31014193</mixed-citation></ref><ref id="B64"><label>64.</label><mixed-citation>Matsuda S, Kitagishi Y, Kobayashi M. Function and characteristics of PINK1 in mitochondria. Oxid Med Cell Longev 2013; 2013: 1-6. doi: 10.1155/2013/601587 PMID: 23533695</mixed-citation></ref><ref id="B65"><label>65.</label><mixed-citation>Zhou Y, Ge Y, Liu Q, et al. LncRNA BACE1-AS promotes autophagy-mediated neuronal damage through the miR-214-3p/ATG5 signaling axis in Alzheimers disease. Neuroscience 2021; 455: 52-64. doi: 10.1016/j.neuroscience.2020.10.028 PMID: 33197504</mixed-citation></ref><ref id="B66"><label>66.</label><mixed-citation>Faghihi MA, Zhang M, Huang J, et al. Evidence for natural antisense transcript-mediated inhibition of microRNA function. Genome Biol 2010; 11(5): R56. doi: 10.1186/gb-2010-11-5-r56 PMID: 20507594</mixed-citation></ref><ref id="B67"><label>67.</label><mixed-citation>Memczak S, Jens M, Elefsinioti A, et al. Circular RNAs are a large class of animal RNAs with regulatory potency. Nature 2013; 495(7441): 333-8. doi: 10.1038/nature11928 PMID: 23446348</mixed-citation></ref><ref id="B68"><label>68.</label><mixed-citation>Shao Y, Chen Y. Roles of circular RNAs in neurologic disease. Front Mol Neurosci 2016; 9: 25. doi: 10.3389/fnmol.2016.00025 PMID: 27147959</mixed-citation></ref><ref id="B69"><label>69.</label><mixed-citation>Sierksma A, Lu A, Salta E, et al. Deregulation of neuronal miRNAs induced by amyloid-β or TAU pathology. Mol Neurodegener 2018; 13(1): 54. doi: 10.1186/s13024-018-0285-1 PMID: 30314521</mixed-citation></ref><ref id="B70"><label>70.</label><mixed-citation>Banzhaf-Strathmann J, Benito E, May S, et al. Micro RNA ‐125b induces tau hyperphosphorylation and cognitive deficits in Alzheimers disease. EMBO J 2014; 33(15): 1667-80. doi: 10.15252/embj.201387576 PMID: 25001178</mixed-citation></ref><ref id="B71"><label>71.</label><mixed-citation>Smith PY, Hernandez-Rapp J, Jolivette F, et al. miR-132/212 deficiency impairs tau metabolism and promotes pathological aggregation in vivo. Hum Mol Genet 2015; 24(23): 6721-35. doi: 10.1093/hmg/ddv377 PMID: 26362250</mixed-citation></ref></ref-list></back></article>
