<?xml version="1.0" encoding="utf-8" standalone="yes"?>
<TEI xmlns="http://www.tei-c.org/ns/1.0">
  <teiHeader>
    <fileDesc>
      <titleStmt>
        <title type="main">A multidisciplinary approach for the early diagnosis of Alzheimer’s disease and potential therapeutic applications</title>
        <author>
          <persName n="1" ref="https://orcid.org/0009-0004-3087-286X" type="ORCID">
            <forename>Liliana</forename>
            <surname>Napolitano</surname>
          </persName>
        </author>
      </titleStmt>
      <publicationStmt>
        <publisher>Firenze University Press</publisher>
        <pubPlace>Florence</pubPlace>
        <date when="2026">2026</date>
        <idno type="DOI">https://doi.org/10.36253/979-12-215-0993-9</idno>
        <availability>
          <p>Available for academic research purposes</p>
          <p>Open Access</p>
          <p>Copyright Author(s)</p>
          <licence source="text" target="https://creativecommons.org/licenses/by/4.0/legalcode">
            <p>Content licence CC BY 4.0</p>
          </licence>
          <licence source="metadata" target="https://creativecommons.org/publicdomain/zero/1.0/legalcode">
            <p>Metadata licence CC0 1.0</p>
          </licence>
        </availability>
      </publicationStmt>
      <seriesStmt>
        <title>Premio Tesi di Dottorato Città di Firenze</title>
        <idno type="ISSN" subtype="print">3103-3881</idno>
        <idno type="ISSN" subtype="electronic">3103-3989</idno>
      </seriesStmt>
      <sourceDesc>
        <bibl type="monograph">
          <edition n="1">Digital edition PDF</edition>
          <date>2026</date>
          <idno type="ISBN" subtype="electronic">979-12-215-0993-9</idno>
          <biblScope unit="page">184 pages</biblScope>
          <extent>0.00 MB</extent>
          <availability status="free">
            <p>This is original content, published in Open Access. It is also available to read for free online at <ref target="https://media.fupress.com/files/pdf/24/16502/50429">https://media.fupress.com/files/pdf/24/16502/50429</ref></p>
          </availability>
        </bibl>
        <bibl type="monograph">
          <edition n="2">Digital edition XML</edition>
          <date>2026</date>
          <idno type="ISBN" subtype="electronic">979-12-215-0994-6</idno>
          <availability status="free">
            <p>It is available to read for free online</p>
          </availability>
        </bibl>
        <bibl type="monograph">
          <edition n="3">Print edition</edition>
          <date>2026</date>
          <idno type="ISBN" subtype="print">979-12-215-0992-2</idno>
          <biblScope unit="page">184 pages</biblScope>
          <availability status="restricted">
            <p>It is available for online purchase at <ref target="https://books.fupress.com/isbn/9791221509939">https://books.fupress.com/isbn/9791221509939</ref></p>
          </availability>
        </bibl>
      </sourceDesc>
    </fileDesc>
    <encodingDesc>
      <appInfo>
        <application version="2.2" ident="Booksflow">
          <desc>Digital edition XML powered by Booksflow</desc>
        </application>
      </appInfo>
    </encodingDesc>
    <profileDesc>
      <creation>
        <tag>peer-reviewed</tag>
        <rs type="FUP_policy" source="https://doi.org/10.36253/fup_best_practice">Firenze University Press Best Practice in Scholarly Publishing</rs>
        <rs type="scientific_cloud" source="https://doi.org/10.36253/fup_best_practice.2">FUP Scientific Cloud for Books</rs>
        <rs type="peer_review" resp="scientific_board" source="https://books.fupress.com/scientific-board/c/167">Premio Tesi di Dottorato Città di Firenze 2025</rs>
      </creation>
      <abstract xml:lang="en">
        <p>This thesis presents a multidisciplinary approach to improve Alzheimer’s disease (AD) early diagnosis and therapy. The first part, based on the PRAMA cohort, identifies two novel CSF biomarkers using biophysical and cell viability assays to detect proteostasis failure. The second part focuses on the single-domain antibody DesAb-O, demonstrating its ability to selectively detect Aβ42 oligomers and neutralize their toxicity in patient-derived CSF. This tool was further engineered into Dimeric-DesAb-O. In the third part, ELISA, ThT, and TEM analyses confirm that dimerization enhances binding avidity, alters fibril morphology, and increases protective efficacy at low concentrations. This study suggests innovative immunodiagnostic and therapeutic strategies for future AD clinical applications.</p>
      </abstract>
      <abstract xml:lang="it">
        <p>This thesis presents a multidisciplinary approach to improve Alzheimer’s disease (AD) early diagnosis and therapy. The first part, based on the PRAMA cohort, identifies two novel CSF biomarkers using biophysical and cell viability assays to detect proteostasis failure. The second part focuses on the single-domain antibody DesAb-O, demonstrating its ability to selectively detect Aβ42 oligomers and neutralize their toxicity in patient-derived CSF. This tool was further engineered into Dimeric-DesAb-O. In the third part, ELISA, ThT, and TEM analyses confirm that dimerization enhances binding avidity, alters fibril morphology, and increases protective efficacy at low concentrations. This study suggests innovative immunodiagnostic and therapeutic strategies for future AD clinical applications.</p>
      </abstract>
      <textClass>
        <keywords>
          <list>
            <item>Alzheimer’disease</item>
            <item>Biomarkers</item>
            <item>Aβ42 oligomers</item>
            <item>Single-Domain antibody</item>
            <item>Antibody-engineering</item>
          </list>
        </keywords>
      </textClass>
    </profileDesc>
  </teiHeader>
  <text>
    <front>
      <div type="toc">
        <list>
          <item>Table of Contents</item>
          <item>Introduction</item>
          <item>Material and Methods</item>
          <item>First Section: Putative CSF biomarkers of Alzheimer’s disease based on the novel concept of generic protein misfolding and proteotoxicity: the PRAMA cohort</item>
          <item>Second Section: A single domain antibody detects and neutralises toxic Aβ42 oligomers in the Alzheimer’s disease CSF</item>
          <item>Third Section: Design of a dimeric-nanobody specific for Aβ42 oligomers: the Dimeric-DesAb-O</item>
          <item>Discussion</item>
          <item>Conclusion and Future Perspectives</item>
          <item>References</item>
          <item>Index of names</item>
        </list>
      </div>
    </front>
    <body>
      <p>It is available online at https://doi.org/10.36253/979-12-215-0993-9<ref target="https://doi.org/10.36253/979-12-215-0993-9" /></p>
      <div>
        <listBibl>
          <head>References</head>
          <bibl n="231154">
            <bibl>2021 Alzheimer’s disease facts and figures. (2021). Alzheimer’s &amp;amp; Dementia: The Journal of the Alzheimer’s Association, 17(3), 327–406.</bibl>
            <idno type="DOI">10.1002/alz.12328</idno>
          </bibl>
          <bibl n="231148">
            <bibl>2023 Alzheimer’s disease facts and figures. (2023). Alzheimer’s &amp;amp; Dementia: The Journal of the Alzheimer’s Association, 19(4), 1598–1695.</bibl>
            <idno type="DOI">10.1002/alz.13016</idno>
          </bibl>
          <bibl n="230855">
            <bibl>Abelein, A., Chen, G., Kitoka, K., Aleksis, R., Oleskovs, F., Sarr, M., Landreh, M., Pahnke, J., Nordling, K., Kronqvist, N., Jaudzems, K., Rising, A., Johansson, J., &amp;amp; Biverst&amp;#229;l, H. (2020). High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain. Scientific Reports, 10(1), 235.</bibl>
            <idno type="DOI">10.1038/s41598-019-57143-x</idno>
          </bibl>
          <bibl n="230894">
            <bibl>Ackaert, C., Smiejkowska, N., Xavier, C., Sterckx, Y. G. J., Denies, S., Stijlemans, B., Elkrim, Y., Devoogdt, N., Caveliers, V., Lahoutte, T., Muyldermans, S., Breckpot, K., &amp;amp; Keyaerts, M. (2021). Immunogenicity Risk Profile of Nanobodies. Frontiers in Immunology, 12, 632687.</bibl>
            <idno type="DOI">10.3389/fimmu.2021.632687</idno>
          </bibl>
          <bibl n="231113">
            <bibl>M. Ahmed, J. Davis, D. Aucoin, T. Sato, S. Ahuja, S. Aimoto, J. I. Elliott, W. E. Van Nostrand, S. O. Smith. Nature Structural &amp;amp; Molecular Biology, 17(5):561-7</bibl>
            <idno type="DOI">10.1038/nsmb.1799</idno>
          </bibl>
          <bibl n="231044">Alzheimer’s Disease and Dementia. Aducanumab Discontinued as an Alzheimer’s Treatment. (n.d.). Alzheimer’s Disease and Dementia. https://www.alz.org/alzheimers-dementia/treatments/aducanumab</bibl>
          <bibl n="230774">
            <bibl>Albert, M. S., DeKosky, S. T., Dickson, D., Dubois, B., Feldman, H. H., Fox, N. C., Gamst, A., Holtzman, D. M., Jagust, W. J., Petersen, R. C., Snyder, P. J., Carrillo, M. C., Thies, B., &amp;amp; Phelps, C. H. (2011). The diagnosis of mild cognitive impairment due to Alzheimer’s disease: Recommendations from the National Institute on Aging-Alzheimer’s Association workgroups on diagnostic guidelines for Alzheimer’s disease. Alzheimer’s &amp;amp; Dementia, 7(3), 270–279.</bibl>
            <idno type="DOI">10.1016/j.jalz.2011.03.008</idno>
          </bibl>
          <bibl n="230938">
            <bibl>Alonso, A. D., Cohen, L. S., Corbo, C., Morozova, V., ElIdrissi, A., Phillips, G., &amp;amp; Kleiman, F. E. (2018). Hyperphosphorylation of Tau Associates with Changes in Its Function Beyond Microtubule Stability. Frontiers in Cellular Neuroscience, 12, 338.</bibl>
            <idno type="DOI">10.3389/fncel.2018.00338</idno>
          </bibl>
          <bibl n="231205">Alzforum. (2023). Remternetug. alzforum.org/therapeutics/remternetug</bibl>
          <bibl n="231008">
            <bibl>Alzheimer, A., Stelzmann, R. A., Schnitzlein, H. N., &amp;amp; Murtagh, F. R. (1995). An English translation of Alzheimer’s 1907 paper, ‘Uber eine eigenartige Erkankung der Hirnrinde’. Clinical Anatomy, 8(6), 429–431.</bibl>
            <idno type="DOI">10.1002/ca.980080612</idno>
          </bibl>
          <bibl n="231165">Alzheimer Europe. (2020). Dementia in Europe Yearbook 2019: estimating the prevalence of dementia in Europe. ISBN: 978-99959-995-6-7</bibl>
          <bibl n="230936">
            <bibl>Amador-Ortiz, C., Lin, W.-L., Ahmed, Z., Personett, D., Davies, P., Duara, R., Graff-Radford, N. R., Hutton, M. L., &amp;amp; Dickson, D. W. (2007). TDP-43 immunoreactivity in hippocampal sclerosis and Alzheimer’s disease. Annals of Neurology, 61(5), 435–445.</bibl>
            <idno type="DOI">10.1002/ana.21154</idno>
          </bibl>
          <bibl n="231032">
            <bibl>Amm, I., Sommer, T., &amp;amp; Wolf, D. H. (2014). Protein quality control and elimination of protein waste: The role of the ubiquitin-proteasome system. Biochimica Et Biophysica Acta, 1843(1), 182–196.</bibl>
            <idno type="DOI">10.1016/j.bbamcr.2013.06.031</idno>
          </bibl>
          <bibl n="230836">
            <bibl>An, Y., Varma, V. R., Varma, S., Casanova, R., Dammer, E., Pletnikova, O., Chia, C. W., Egan, J. M., Ferrucci, L., Troncoso, J., Levey, A. I., Lah, J., Seyfried, N. T., Legido-Quigley, C., O’Brien, R., &amp;amp; Thambisetty, M. (2018). Evidence for brain glucose dysregulation in Alzheimer’s disease. Alzheimer’s &amp;amp; Dementia, 14(3), 318–329.</bibl>
            <idno type="DOI">10.1016/j.jalz.2017.09.011</idno>
          </bibl>
          <bibl n="230971">
            <bibl>Andrews, S. J., Renton, A. E., Fulton-Howard, B., Podlesny-Drabiniok, A., Marcora, E., &amp;amp; Goate, A. M. (2023). The complex genetic architecture of Alzheimer’s disease: Novel insights and future directions. EBioMedicine, 90, 104511.</bibl>
            <idno type="DOI">10.1016/j.ebiom.2023.104511</idno>
          </bibl>
          <bibl n="231127">
            <bibl>Angelova, P. R., &amp;amp; Abramov, A. Y. (2018). Role of mitochondrial ROS in the brain: From physiology to neurodegeneration. FEBS Letters, 592(5), 692–702.</bibl>
            <idno type="DOI">10.1002/1873-3468.12964</idno>
          </bibl>
          <bibl n="230895">
            <bibl>Antonell, A., Mansilla, A., Rami, L., Llad&amp;#243;, A., Iranzo, A., Olives, J., Balasa, M., S&amp;#225;nchez-Valle, R., &amp;amp; Molinuevo, J. L. (2014). Cerebrospinal fluid level of YKL-40 protein in preclinical and prodromal Alzheimer’s disease. Journal of Alzheimer’s Disease: JAD, 42(3), 901–908.</bibl>
            <idno type="DOI">10.3233/JAD-140624</idno>
          </bibl>
          <bibl n="230886">
            <bibl>Aprile, F. A., Sormanni, P., Perni, M., Arosio, P., Linse, S., Knowles, T. P. J., Dobson, C. M., &amp;amp; Vendruscolo, M. (2017). Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method. Science Advances, 3(6), e1700488.</bibl>
            <idno type="DOI">10.1126/sciadv.1700488</idno>
          </bibl>
          <bibl n="230772">
            <bibl>Aprile, F. A., Sormanni, P., Podpolny, M., Chhangur, S., Needham, L.-M., Ruggeri, F. S., Perni, M., Limbocker, R., Heller, G. T., Sneideris, T., Scheidt, T., Mannini, B., Habchi, J., Lee, S. F., Salinas, P. C., Knowles, T. P. J., Dobson, C. M., &amp;amp; Vendruscolo, M. (2020). Rational design of a conformation-specific antibody for the quantification of Aβ oligomers. Proceedings of the National Academy of Sciences of the United States of America, 117(24), 13509–13518.</bibl>
            <idno type="DOI">10.1073/pnas.1919464117</idno>
          </bibl>
          <bibl n="230801">
            <bibl>Arbel-Ornath, M., Hudry, E., Boivin, J. R., Hashimoto, T., Takeda, S., Kuchibhotla, K. V., Hou, S., Lattarulo, C. R., Belcher, A. M., Shakerdge, N., Trujillo, P. B., Muzikansky, A., Betensky, R. A., Hyman, B. T., &amp;amp; Bacskai, B. J. (2017). Soluble oligomeric amyloid-β induces calcium dyshomeostasis that precedes synapse loss in the living mouse brain. Molecular Neurodegeneration, 12(1), 27.</bibl>
            <idno type="DOI">10.1186/s13024-017-0169-9</idno>
          </bibl>
          <bibl n="231033">
            <bibl>Argos, P. (1990). An investigation of oligopeptides linking domains in protein tertiary structures and possible candidates for general gene fusion. Journal of Molecular Biology, 211(4), 943–958.</bibl>
            <idno type="DOI">10.1016/0022-2836(90)90085-Z</idno>
          </bibl>
          <bibl n="230968">
            <bibl>Ariga, T., Kobayashi, K., Hasegawa, A., Kiso, M., Ishida, H., &amp;amp; Miyatake, T. (2001). Characterization of high-affinity binding between gangliosides and amyloid beta-protein. Archives of Biochemistry and Biophysics, 388(2), 225–230.</bibl>
            <idno type="DOI">10.1006/abbi.2001.2304</idno>
          </bibl>
          <bibl n="231045">
            <bibl>Arispe, N., Diaz, J. C., &amp;amp; Simakova, O. (2007). Abeta ion channels. Prospects for treating Alzheimer’s disease with Abeta channel blockers. Biochimica Et Biophysica Acta, 1768(8), 1952–1965.</bibl>
            <idno type="DOI">10.1016/j.bbamem.2007.03.014</idno>
          </bibl>
          <bibl n="230861">
            <bibl>Arndt, J. W., Qian, F., Smith, B. A., Quan, C., Kilambi, K. P., Bush, M. W., Walz, T., Pepinsky, R. B., Bussi&amp;#232;re, T., Hamann, S., Cameron, T. O., &amp;amp; Weinreb, P. H. (2018). Structural and kinetic basis for the selectivity of aducanumab for aggregated forms of amyloid-β. Scientific Reports, 8(1), 6412.</bibl>
            <idno type="DOI">10.1038/s41598-018-24501-0</idno>
          </bibl>
          <bibl n="230823">
            <bibl>Ashton, N. J., Pascoal, T. A., Karikari, T. K., Benedet, A. L., Lantero-Rodriguez, J., Brinkmalm, G., Snellman, A., Sch&amp;#246;ll, M., Troakes, C., Hye, A., Gauthier, S., Vanmechelen, E., Zetterberg, H., Rosa-Neto, P., &amp;amp; Blennow, K. (2021). Plasma p-tau231: A new biomarker for incipient Alzheimer’s disease pathology. Acta Neuropathologica, 141(5), 709–724.</bibl>
            <idno type="DOI">10.1007/s00401-021-02275-6</idno>
          </bibl>
          <bibl n="231059">
            <bibl>B&amp;#228;ckman, L., Jones, S., Berger, A.-K., Laukka, E. J., &amp;amp; Small, B. J. (2005). Cognitive impairment in preclinical Alzheimer’s disease: A meta-analysis. Neuropsychology, 19(4), 520–531.</bibl>
            <idno type="DOI">10.1037/0894-4105.19.4.520</idno>
          </bibl>
          <bibl n="230958">
            <bibl>Baghallab, I., Reyes-Ruiz, J. M., Abulnaja, K., Huwait, E., &amp;amp; Glabe, C. (2018). Epitomic Characterization of the Specificity of the Anti-Amyloid Aβ Monoclonal Antibodies 6E10 and 4G8. Journal of Alzheimer’s Disease: JAD, 66(3), 1235–1244.</bibl>
            <idno type="DOI">10.3233/JAD-180582</idno>
          </bibl>
          <bibl n="231122">
            <bibl>Balchin, D., Hayer-Hartl, M., &amp;amp; Hartl, F. U. (2016). In vivo aspects of protein folding and quality control. Science (New York, N.Y.), 353(6294), aac4354.</bibl>
            <idno type="DOI">10.1126/science.aac4354</idno>
          </bibl>
          <bibl n="230844">
            <bibl>Banchelli, M., Cascella, R., D’Andrea, C., Cabaj, L., Osticioli, I., Ciofini, D., Li, M. S., Skupień, K., de Angelis, M., Siano, S., Cecchi, C., Pini, R., La Penna, G., Chiti, F., &amp;amp; Matteini, P. (2020). Nanoscopic insights into the surface conformation of neurotoxic amyloid β oligomers. RSC Advances, 10(37), 21907–21913.</bibl>
            <idno type="DOI">10.1039/d0ra03799k</idno>
          </bibl>
          <bibl n="231105">
            <bibl>Barenholz, Y. (2004). Sphingomyelin and cholesterol: From membrane biophysics and rafts to potential medical applications. Sub-Cellular Biochemistry, 37, 167–215.</bibl>
            <idno type="DOI">10.1007/978-1-4757-5806-1_5</idno>
          </bibl>
          <bibl n="231063">
            <bibl>Barrera, N. P., Zhou, M., &amp;amp; Robinson, C. V. (2013). The role of lipids in defining membrane protein interactions: Insights from mass spectrometry. Trends in Cell Biology, 23(1), 1–8.</bibl>
            <idno type="DOI">10.1016/j.tcb.2012.08.007</idno>
          </bibl>
          <bibl n="230779">
            <bibl>Bateman, R. J., Xiong, C., Benzinger, T. L. S., Fagan, A. M., Goate, A., Fox, N. C., Marcus, D. S., Cairns, N. J., Xie, X., Blazey, T. M., Holtzman, D. M., Santacruz, A., Buckles, V., Oliver, A., Moulder, K., Aisen, P. S., Ghetti, B., Klunk, W. E., McDade, E., … Dominantly Inherited Alzheimer Network. (2012). Clinical and biomarker changes in dominantly inherited Alzheimer’s disease. The New England Journal of Medicine, 367(9), 795–804.</bibl>
            <idno type="DOI">10.1056/NEJMoa1202753</idno>
          </bibl>
          <bibl n="230981">
            <bibl>Batko, J., Antosz, K., Miśk&amp;#243;w, W., Pszczołowska, M., Walczak, K., &amp;amp; Leszek, J. (2024). Chaperones-A New Class of Potential Therapeutic Targets in Alzheimer’s Disease. International Journal of Molecular Sciences, 25(6), 3401.</bibl>
            <idno type="DOI">10.3390/ijms25063401</idno>
          </bibl>
          <bibl n="230977">
            <bibl>B&amp;#233;langer, K., Iqbal, U., Tanha, J., MacKenzie, R., Moreno, M., &amp;amp; Stanimirovic, D. (2019). Single-Domain Antibodies as Therapeutic and Imaging Agents for the Treatment of CNS Diseases. Antibodies (Basel, Switzerland), 8(2), 27.</bibl>
            <idno type="DOI">10.3390/antib8020027</idno>
          </bibl>
          <bibl n="230822">
            <bibl>Bellomo, G., Toja, A., Paolini Paoletti, F., Ma, Y., Farris, C. M., Gaetani, L., Salvadori, N., Chiasserini, D., Wojdaƚa, A. L., Concha-Marambio, L., &amp;amp; Parnetti, L. (2024). Investigating alpha-synuclein co-pathology in Alzheimer’s disease by means of cerebrospinal fluid alpha-synuclein seed amplification assay. Alzheimer’s &amp;amp; Dementia, 20(4), 2444–2452.</bibl>
            <idno type="DOI">10.1002/alz.13658</idno>
          </bibl>
          <bibl n="230864">
            <bibl>Benedet, A. L., Brum, W. S., Hansson, O., Alzheimer’s Disease Neuroimaging Initiative, Karikari, T. K., Zimmer, E. R., Zetterberg, H., Blennow, K., &amp;amp; Ashton, N. J. (2022). The accuracy and robustness of plasma biomarker models for amyloid PET positivity. Alzheimer’s Research &amp;amp; Therapy, 14(1), 26.</bibl>
            <idno type="DOI">10.1186/s13195-021-00942-0</idno>
          </bibl>
          <bibl n="231096">
            <bibl>Benilova, I., Karran, E., &amp;amp; De Strooper, B. (2012). The toxic Aβ oligomer and Alzheimer’s disease: An emperor in need of clothes. Nature Neuroscience, 15(3), 349–357.</bibl>
            <idno type="DOI">10.1038/nn.3028</idno>
          </bibl>
          <bibl n="231016">
            <bibl>Bento, C. F., Renna, M., Ghislat, G., Puri, C., Ashkenazi, A., Vicinanza, M., Menzies, F. M., &amp;amp; Rubinsztein, D. C. (2016). Mammalian Autophagy: How Does It Work? Annual Review of Biochemistry, 85, 685–713.</bibl>
            <idno type="DOI">10.1146/annurev-biochem-060815-014556</idno>
          </bibl>
          <bibl n="231204">
            <bibl>Berridge, M. J. (1998). Neuronal calcium signaling. Neuron, 21(1), 13–26.</bibl>
            <idno type="DOI">10.1016/s0896-6273(00)80510-3</idno>
          </bibl>
          <bibl n="231110">
            <bibl>Berridge, M. J., Lipp, P., &amp;amp; Bootman, M. D. (2000). The versatility and universality of calcium signalling. Nature Reviews. Molecular Cell Biology, 1(1), 11–21.</bibl>
            <idno type="DOI">10.1038/35036035</idno>
          </bibl>
          <bibl n="231017">
            <bibl>Bhatia, S., Rawal, R., Sharma, P., Singh, T., Singh, M., &amp;amp; Singh, V. (2022). Mitochondrial Dysfunction in Alzheimer’s Disease: Opportunities for Drug Development. Current Neuropharmacology, 20(4), 675–692.</bibl>
            <idno type="DOI">10.2174/1570159X19666210517114016</idno>
          </bibl>
          <bibl n="230866">
            <bibl>Bigi, A., Cascella, R., Fani, G., Bernacchioni, C., Cencetti, F., Bruni, P., Chiti, F., Donati, C., &amp;amp; Cecchi, C. (2023a). Sphingosine 1-phosphate attenuates neuronal dysfunction induced by amyloid-β oligomers through endocytic internalization of NMDA receptors. The FEBS Journal, 290(1), 112–133.</bibl>
            <idno type="DOI">10.1111/febs.16579</idno>
          </bibl>
          <bibl n="230818">
            <bibl>Bigi, A., Fani, G., Bessi, V., Napolitano, L., Bagnoli, S., Ingannato, A., Neri, L., Cascella, R., Matteini, P., Sorbi, S., Nacmias, B., Cecchi, C., &amp;amp; Chiti, F. (2024). Putative novel CSF biomarkers of Alzheimer’s disease based on the novel concept of generic protein misfolding and proteotoxicity: The PRAMA cohort. Translational Neurodegeneration, 13(1), 14.</bibl>
            <idno type="DOI">10.1186/s40035-024-00405-0</idno>
          </bibl>
          <bibl n="231056">
            <bibl>Bigi, A., Loffredo, G., Cascella, R., &amp;amp; Cecchi, C. (2020). Targeting Pathological Amyloid Aggregates with Conformation-Sensitive Antibodies. Current Alzheimer Research, 17(8), 722–734.</bibl>
            <idno type="DOI">10.2174/1567205017666201109093848</idno>
          </bibl>
          <bibl n="231050">
            <bibl>Bigi, A., Lombardo, E., Cascella, R., &amp;amp; Cecchi, C. (2023b). The Toxicity of Protein Aggregates: New Insights into the Mechanisms. International Journal of Molecular Sciences, 24(9), 7974.</bibl>
            <idno type="DOI">10.3390/ijms24097974</idno>
          </bibl>
          <bibl n="230943">
            <bibl>Bigi, A., Napolitano, L., Vadukul, D. M., Chiti, F., Cecchi, C., Aprile, F. A., &amp;amp; Cascella, R. (2024a). A single-domain antibody detects and neutralises toxic Aβ42 oligomers in the Alzheimer’s disease CSF. Alzheimer’s Research &amp;amp; Therapy, 16(1), 13.</bibl>
            <idno type="DOI">10.1186/s13195-023-01361-z</idno>
          </bibl>
          <bibl n="231060">
            <bibl>Biomarkers Definitions Working Group. (2001). Biomarkers and surrogate endpoints: Preferred definitions and conceptual framework. Clinical Pharmacology and Therapeutics, 69(3), 89–95.</bibl>
            <idno type="DOI">10.1067/mcp.2001.113989</idno>
          </bibl>
          <bibl n="230969">
            <bibl>Bird, R. E., Hardman, K. D., Jacobson, J. W., Johnson, S., Kaufman, B. M., Lee, S. M., Lee, T., Pope, S. H., Riordan, G. S., &amp;amp; Whitlow, M. (1988). Single-chain antigen-binding proteins. Science (New York, N.Y.), 242(4877), 423–426.</bibl>
            <idno type="DOI">10.1126/science.3140379</idno>
          </bibl>
          <bibl n="230865">
            <bibl>Bitan, G., Kirkitadze, M. D., Lomakin, A., Vollers, S. S., Benedek, G. B., &amp;amp; Teplow, D. B. (2003). Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways. Proceedings of the National Academy of Sciences of the United States of America, 100(1), 330–335.</bibl>
            <idno type="DOI">10.1073/pnas.222681699</idno>
          </bibl>
          <bibl n="230944">
            <bibl>Blennow, K., Wallin, A., Agren, H., Spenger, C., Siegfried, J., &amp;amp; Vanmechelen, E. (1995). Tau protein in cerebrospinal fluid: A biochemical marker for axonal degeneration in Alzheimer disease? Molecular and Chemical Neuropathology, 26(3), 231–245.</bibl>
            <idno type="DOI">10.1007/BF02815140</idno>
          </bibl>
          <bibl n="230915">
            <bibl>Blessed, G., Tomlinson, B. E., &amp;amp; Roth, M. (1968). The association between quantitative measures of dementia and of senile change in the cerebral grey matter of elderly subjects. The British Journal of Psychiatry: The Journal of Mental Science, 114(512), 797–811.</bibl>
            <idno type="DOI">10.1192/bjp.114.512.797</idno>
          </bibl>
          <bibl n="230927">
            <bibl>Bode, D. C., Freeley, M., Nield, J., Palma, M., &amp;amp; Viles, J. H. (2019). Amyloid-β oligomers have a profound detergent-like effect on lipid membrane bilayers, imaged by atomic force and electron microscopy. Journal of Biological Chemistry, 294(19), 7566–7572.</bibl>
            <idno type="DOI">10.1074/jbc.AC118.007195</idno>
          </bibl>
          <bibl n="230881">
            <bibl>Boess, F., Sakaoka, S., Abi-Saab, D., Scelsi, M., delmar, P., Hofmann, C., Klein, G., Baudler, M., Doody, R., &amp;amp; Kerchner, G. (2021). Graduation study design: Evaluation of once-weekly subcutaneous administration of gantenerumab on brain amyloid load. Alzheimer’s &amp;amp; Dementia, 17, e052060.</bibl>
            <idno type="DOI">10.1002/alz.052060</idno>
          </bibl>
          <bibl n="231061">
            <bibl>Bondi, M. W., Edmonds, E. C., &amp;amp; Salmon, D. P. (2017). Alzheimer’s Disease: Past, Present, and Future. Journal of the International Neuropsychological Society: JINS, 23(9–10), 818–831.</bibl>
            <idno type="DOI">10.1017/S135561771700100X</idno>
          </bibl>
          <bibl n="231047">
            <bibl>Bondi, M. W., Monsch, A. U., Galasko, D., Butters, N., Salmon, D. P., &amp;amp; Delis, D. C. (1994). Preclinical cognitive markers of dementia of the Alzheimer type. Neuropsychology, 8(3), 374–384.</bibl>
            <idno type="DOI">10.1037/0894-4105.8.3.374</idno>
          </bibl>
          <bibl n="231004">
            <bibl>Braak, H., &amp;amp; Braak, E. (1994). Morphological criteria for the recognition of Alzheimer’s disease and the distribution pattern of cortical changes related to this disorder. Neurobiology of Aging, 15(3), 355–356.</bibl>
            <idno type="DOI">10.1016/0197-4580(94)90032-9</idno>
          </bibl>
          <bibl n="231034">
            <bibl>Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248–254.</bibl>
            <idno type="DOI">10.1006/abio.1976.9999</idno>
          </bibl>
          <bibl n="230904">
            <bibl>Brehme, M., Voisine, C., Rolland, T., Wachi, S., Soper, J. H., Zhu, Y., Orton, K., Villella, A., Garza, D., Vidal, M., Ge, H., &amp;amp; Morimoto, R. I. (2014). A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease. Cell Reports, 9(3), 1135–1150.</bibl>
            <idno type="DOI">10.1016/j.celrep.2014.09.042</idno>
          </bibl>
          <bibl n="230869">
            <bibl>Brilhante-da-Silva, N., de Oliveira Sousa, R. M., Arruda, A., Dos Santos, E. L., Marinho, A. C. M., Stabeli, R. G., Fernandes, C. F. C., &amp;amp; Pereira, S. D. S. (2021). Camelid Single-Domain Antibodies for the Development of Potent Diagnosis Platforms. Molecular Diagnosis &amp;amp; Therapy, 25(4), 439–456.</bibl>
            <idno type="DOI">10.1007/s40291-021-00533-7</idno>
          </bibl>
          <bibl n="230933">
            <bibl>Brodaty, H., Heffernan, M., Kochan, N. A., Draper, B., Trollor, J. N., Reppermund, S., Slavin, M. J., &amp;amp; Sachdev, P. S. (2013). Mild cognitive impairment in a community sample: The Sydney Memory and Ageing Study. Alzheimer’s &amp;amp; Dementia, 9(3), 310-317.e1.</bibl>
            <idno type="DOI">10.1016/j.jalz.2011.11.010</idno>
          </bibl>
          <bibl n="231147">
            <bibl>Brooks, W. H. (2024). Polyamine Dysregulation and Nucleolar Disruption in Alzheimer’s Disease. Journal of Alzheimer’s Disease, 98(3), 837.</bibl>
            <idno type="DOI">10.3233/JAD-231184</idno>
          </bibl>
          <bibl n="230890">
            <bibl>Buchhave, P., Minthon, L., Zetterberg, H., Wallin, A. K., Blennow, K., &amp;amp; Hansson, O. (2012). Cerebrospinal fluid levels of β-amyloid 1-42, but not of tau, are fully changed already 5 to 10 years before the onset of Alzheimer dementia. Archives of General Psychiatry, 69(1), 98–106.</bibl>
            <idno type="DOI">10.1001/archgenpsychiatry.2011.155</idno>
          </bibl>
          <bibl n="230782">
            <bibl>Budd Haeberlein, S., Aisen, P. S., Barkhof, F., Chalkias, S., Chen, T., Cohen, S., Dent, G., Hansson, O., Harrison, K., von Hehn, C., Iwatsubo, T., Mallinckrodt, C., Mummery, C. J., Muralidharan, K. K., Nestorov, I., Nisenbaum, L., Rajagovindan, R., Skordos, L., Tian, Y., … Sandrock, A. (2022). Two Randomized Phase 3 Studies of Aducanumab in Early Alzheimer’s Disease. The Journal of Prevention of Alzheimer’s Disease, 9(2), 197–210.</bibl>
            <idno type="DOI">10.14283/jpad.2022.30</idno>
          </bibl>
          <bibl n="231111">
            <bibl>Butterfield, D. A., &amp;amp; Halliwell, B. (2019). Oxidative stress, dysfunctional glucose metabolism, and Alzheimer disease. Nature Reviews. Neuroscience, 20(3), 148.</bibl>
            <idno type="DOI">10.1038/s41583-019-0132-6</idno>
          </bibl>
          <bibl n="231114">
            <bibl>Cadonic, C., Sabbir, M. G., &amp;amp; Albensi, B. C. (2016). Mechanisms of Mitochondrial Dysfunction in Alzheimer’s Disease. Molecular Neurobiology, 53(9), 6078–6090.</bibl>
            <idno type="DOI">10.1007/s12035-015-9515-5</idno>
          </bibl>
          <bibl n="230941">
            <bibl>Caill&amp;#233;, I., Allinquant, B., Dupont, E., Bouillot, C., Langer, A., M&amp;#252;ller, U., &amp;amp; Prochiantz, A. (2004). Soluble form of amyloid precursor protein regulates proliferation of progenitors in the adult subventricular zone. Development, 131(9), 2173–2181.</bibl>
            <idno type="DOI">10.1242/dev.01103</idno>
          </bibl>
          <bibl n="231155">
            <bibl>Camberg, J., Doyle, S., Johnston, D., &amp;amp; Wickner, S. (2013). Molecular Chaperones. In Brenner’s Encyclopedia of Genetics (pp. 456–460).</bibl>
            <idno type="DOI">10.1016/B978-0-12-374984-0.00221-7</idno>
          </bibl>
          <bibl n="231070">
            <bibl>Canevari, L., Clark, J. B., &amp;amp; Bates, T. E. (1999). Beta-Amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria. FEBS Letters, 457(1), 131–134.</bibl>
            <idno type="DOI">10.1016/s0014-5793(99)01028-5</idno>
          </bibl>
          <bibl n="230891">
            <bibl>Capitini, C., Conti, S., Perni, M., Guidi, F., Cascella, R., De Poli, A., Penco, A., Relini, A., Cecchi, C., &amp;amp; Chiti, F. (2014). TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells. PloS One, 9(1), e86720.</bibl>
            <idno type="DOI">10.1371/journal.pone.0086720</idno>
          </bibl>
          <bibl n="230845">
            <bibl>Cardoso, F. M., Iba&amp;#241;ez, L. I., Van den Hoecke, S., De Baets, S., Smet, A., Roose, K., Schepens, B., Descamps, F. J., Fiers, W., Muyldermans, S., Depicker, A., &amp;amp; Saelens, X. (2014). Single-domain antibodies targeting neuraminidase protect against an H5N1 influenza virus challenge. Journal of Virology, 88(15), 8278–8296.</bibl>
            <idno type="DOI">10.1128/JVI.03178-13</idno>
          </bibl>
          <bibl n="231149">
            <bibl>Carmona, S., Hardy, J., &amp;amp; Guerreiro, R. (2018). The genetic landscape of Alzheimer disease. Handbook of Clinical Neurology, 148, 395–408.</bibl>
            <idno type="DOI">10.1016/B978-0-444-64076-5.00026-0</idno>
          </bibl>
          <bibl n="231062">
            <bibl>Caroli, A., &amp;amp; Frisoni, G. B. (2010). The dynamics of Alzheimer&amp;#39;s disease biomarkers in the Alzheimer&amp;#39;s Disease Neuroimaging Initiative cohort. Neurobiology of Aging, 31(8), 1263–1274.</bibl>
            <idno type="DOI">10.1016/j.neurobiolaging.2010.04.024</idno>
          </bibl>
          <bibl n="230919">
            <bibl>Cascella, R., Bigi, A., Riffert, D. G., Gagliani, M. C., Ermini, E., Moretti, M., Cortese, K., Cecchi, C., &amp;amp; Chiti, F. (2022). A quantitative biology approach correlates neuronal toxicity with the largest inclusions of TDP-43. Science Advances, 8(30), eabm6376.</bibl>
            <idno type="DOI">10.1126/sciadv.abm6376</idno>
          </bibl>
          <bibl n="231125">
            <bibl>Cascella, R., &amp;amp; Cecchi, C. (2021). Calcium Dyshomeostasis in Alzheimer’s Disease Pathogenesis. International Journal of Molecular Sciences, 22(9), 4914.</bibl>
            <idno type="DOI">10.3390/ijms22094914</idno>
          </bibl>
          <bibl n="230931">
            <bibl>Cascella, R., Chen, S. W., Bigi, A., Camino, J. D., Xu, C. K., Dobson, C. M., Chiti, F., Cremades, N., &amp;amp; Cecchi, C. (2021). The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells. Nature Communications, 12(1), 1814.</bibl>
            <idno type="DOI">10.1038/s41467-021-21937-3</idno>
          </bibl>
          <bibl n="230939">
            <bibl>Cascella, R., Conti, S., Mannini, B., Li, X., Buxbaum, J. N., Tiribilli, B., Chiti, F., &amp;amp; Cecchi, C. (2013). Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro. Biochimica Et Biophysica Acta, 1832(12), 2302–2314.</bibl>
            <idno type="DOI">10.1016/j.bbadis.2013.09.011</idno>
          </bibl>
          <bibl n="230934">
            <bibl>Cascella, R., Conti, S., Tatini, F., Evangelisti, E., Scartabelli, T., Casamenti, F., Wilson, M. R., Chiti, F., &amp;amp; Cecchi, C. (2013). Extracellular chaperones prevent Aβ42-induced toxicity in rat brains. Biochimica Et Biophysica Acta, 1832(8), 1217–1226.</bibl>
            <idno type="DOI">10.1016/j.bbadis.2013.04.012</idno>
          </bibl>
          <bibl n="230953">
            <bibl>Cascella, R., Evangelisti, E., Bigi, A., Becatti, M., Fiorillo, C., Stefani, M., Chiti, F., &amp;amp; Cecchi, C. (2017). Soluble Oligomers Require a Ganglioside to Trigger Neuronal Calcium Overload. Journal of Alzheimer’s Disease: JAD, 60(3), 923–938.</bibl>
            <idno type="DOI">10.3233/JAD-170340</idno>
          </bibl>
          <bibl n="230852">
            <bibl>Cecchi, C., Nichino, D., Zampagni, M., Bernacchioni, C., Evangelisti, E., Pensalfini, A., Liguri, G., Gliozzi, A., Stefani, M., &amp;amp; Relini, A. (2009). A protective role for lipid raft cholesterol against amyloid-induced membrane damage in human neuroblastoma cells. Biochimica Et Biophysica Acta, 1788(10), 2204–2216.</bibl>
            <idno type="DOI">10.1016/j.bbamem.2009.07.019</idno>
          </bibl>
          <bibl n="231118">
            <bibl>Chasseigneaux, S., &amp;amp; Allinquant, B. (2012). Functions of Aβ, sAPPα and sAPPβ: Similarities and differences. Journal of Neurochemistry, 120 Suppl 1, 99–108.</bibl>
            <idno type="DOI">10.1111/j.1471-4159.2011.07584.x</idno>
          </bibl>
          <bibl n="231018">
            <bibl>Chatani, E., Yuzu, K., Ohhashi, Y., &amp;amp; Goto, Y. (2021). Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils. International Journal of Molecular Sciences, 22(9), 4349.</bibl>
            <idno type="DOI">10.3390/ijms22094349</idno>
          </bibl>
          <bibl n="230876">
            <bibl>Chatziefstathiou, A., Canaslan, S., Kanata, E., Vekrellis, K., Constantinides, V. C., Paraskevas, G. P., Kapaki, E., Schmitz, M., Zerr, I., Xanthopoulos, K., Sklaviadis, T., &amp;amp; Dafou, D. (2024). SIMOA Diagnostics on Alzheimer’s Disease and Frontotemporal Dementia. Biomedicines, 12(6), 1253.</bibl>
            <idno type="DOI">10.3390/biomedicines12061253</idno>
          </bibl>
          <bibl n="231038">
            <bibl>Cheignon, C., Tomas, M., Bonnefont-Rousselot, D., Faller, P., Hureau, C., &amp;amp; Collin, F. (2018). Oxidative stress and the amyloid beta peptide in Alzheimer’s disease. Redox Biology, 14, 450–464.</bibl>
            <idno type="DOI">10.1016/j.redox.2017.10.014</idno>
          </bibl>
          <bibl n="230817">
            <bibl>Chen, T., O’Gorman, J., Castrillo-Viguera, C., Rajagovindan, R., Curiale, G. G., Tian, Y., Patel, D., von Rosenstiel, P., von Hehn, C., Salloway, S., Hock, C., Nitsch, R. M., Haeberlein, S. B., Sandrock, A., &amp;amp; Singhal, P. (2024). Results from the long-term extension of PRIME: A randomized Phase 1b trial of aducanumab. Alzheimer’s &amp;amp; Dementia, 20(5), 3406–3415.</bibl>
            <idno type="DOI">10.1002/alz.13755</idno>
          </bibl>
          <bibl n="231119">
            <bibl>Chen, X., Zaro, J. L., &amp;amp; Shen, W.-C. (2013). Fusion protein linkers: Property, design and functionality. Advanced Drug Delivery Reviews, 65(10), 1357–1369.</bibl>
            <idno type="DOI">10.1016/j.addr.2012.09.039</idno>
          </bibl>
          <bibl n="230951">
            <bibl>Chen, Y. R., &amp;amp; Glabe, C. G. (2006). Distinct early folding and aggregation properties of Alzheimer amyloid-beta peptides Abeta40 and Abeta42: Stable trimer or tetramer formation by Abeta42. Journal of Biological Chemistry, 281(34), 24414–24422.</bibl>
            <idno type="DOI">10.1074/jbc.M602363200</idno>
          </bibl>
          <bibl n="230955">
            <bibl>Cheng, B., Gong, H., Xiao, H., Petersen, R. B., Zheng, L., &amp;amp; Huang, K. (2013). Inhibiting Toxic Aggregation of Amyloidogenic Proteins: A Therapeutic Strategy for Protein Misfolding Diseases. Biochimica Et Biophysica Acta, 1830(10), 4860–4871.</bibl>
            <idno type="DOI">10.1016/j.bbagen.2013.05.035</idno>
          </bibl>
          <bibl n="230783">
            <bibl>Ch&amp;#233;telat, G., Arbizu, J., Barthel, H., Garibotto, V., Law, I., Morbelli, S., van de Giessen, E., Agosta, F., Barkhof, F., Brooks, D. J., Carrillo, M. C., Dubois, B., Fjell, A. M., Frisoni, G. B., Hansson, O., Herholz, K., Hutton, B. F., Jack, C. R., Lammertsma, A. A., … Drzezga, A. (2020). Amyloid-PET and 18F-FDG-PET in the diagnostic investigation of Alzheimer’s disease and other dementias. The Lancet Neurology, 19(11), 951–962.</bibl>
            <idno type="DOI">10.1016/S1474-4422(20)30314-8</idno>
          </bibl>
          <bibl n="231150">
            <bibl>Chiti, F., &amp;amp; Dobson, C. M. (2006). Protein misfolding, functional amyloid, and human disease. Annual Review of Biochemistry, 75, 333–366.</bibl>
            <idno type="DOI">10.1146/annurev.biochem.75.101304.123901</idno>
          </bibl>
          <bibl n="231068">
            <bibl>Chiti, F., &amp;amp; Dobson, C. M. (2017). Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. Annual Review of Biochemistry, 86, 27–68.</bibl>
            <idno type="DOI">10.1146/annurev-biochem-061516-045115</idno>
          </bibl>
          <bibl n="231092">
            <bibl>Ciechanover, A., &amp;amp; Brundin, P. (2003). The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg. Neuron, 40(2), 427–446.</bibl>
            <idno type="DOI">10.1016/s0896-6273(03)00606-8</idno>
          </bibl>
          <bibl n="231074">
            <bibl>Cinquanta, L., Fontana, D. E., &amp;amp; Bizzaro, N. (2017). Chemiluminescent immunoassay technology: What does it change in autoantibody detection? Auto-Immunity Highlights, 8(1), 9.</bibl>
            <idno type="DOI">10.1007/s13317-017-0097-2</idno>
          </bibl>
          <bibl n="231207">
            <bibl>Clapham, D. E. (2007). Calcium signaling. Cell, 131(6), 1047–1058.</bibl>
            <idno type="DOI">10.1016/j.cell.2007.11.028</idno>
          </bibl>
          <bibl n="231053">
            <bibl>Cline, E. N., Bicca, M. A., Viola, K. L., &amp;amp; Klein, W. L. (2018). The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade. Journal of Alzheimer’s Disease: JAD, 64(s1), S567–S610.</bibl>
            <idno type="DOI">10.3233/JAD-179941</idno>
          </bibl>
          <bibl n="230826">
            <bibl>Cohen, S. I. A., Linse, S., Luheshi, L. M., Hellstrand, E., White, D. A., Rajah, L., Otzen, D. E., Vendruscolo, M., Dobson, C. M., &amp;amp; Knowles, T. P. J. (2013). Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism. Proceedings of the National Academy of Sciences of the United States of America, 110(24), 9758–9763.</bibl>
            <idno type="DOI">10.1073/pnas.1218402110</idno>
          </bibl>
          <bibl n="230903">
            <bibl>Colom-Cadena, M., Gelpi, E., Charif, S., Belbin, O., Blesa, R., Mart&amp;#237;, M. J., Clarim&amp;#243;n, J., &amp;amp; Lle&amp;#243;, A. (2013). Confluence of α-synuclein, tau, and β-amyloid pathologies in dementia with Lewy bodies. Journal of Neuropathology and Experimental Neurology, 72(12), 1203–1212.</bibl>
            <idno type="DOI">10.1097/NEN.0000000000000018</idno>
          </bibl>
          <bibl n="231160">
            <bibl>Congdon, E. E., &amp;amp; Sigurdsson, E. M. (2018). Tau-targeting therapies for Alzheimer disease. Nature Reviews. Neurology, 14(7), 399–415.</bibl>
            <idno type="DOI">10.1038/s41582-018-0013-z</idno>
          </bibl>
          <bibl n="231042">
            <bibl>Corey-Bloom, J. (2002). The ABC of Alzheimer’s disease: Cognitive changes and their management in Alzheimer’s disease and related dementias. International Psychogeriatrics, 14 Suppl 1, 51–75.</bibl>
            <idno type="DOI">10.1017/s1041610203008664</idno>
          </bibl>
          <bibl n="230896">
            <bibl>Colvin, M. T., Silvers, R., Ni, Q. Z., Can, T. V., Sergeyev, I., Rosay, M., Donovan, K. J., Michael, B., Wall, J., Linse, S., &amp;amp; Griffin, R. G. (2016). Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils. Journal of the American Chemical Society, 138(30), 9663–9674.</bibl>
            <idno type="DOI">10.1021/jacs.6b05129</idno>
          </bibl>
          <bibl n="231077">
            <bibl>Cummings, J., Osse, A. M. L., Cammann, D., Powell, J., &amp;amp; Chen, J. (2024). Anti-Amyloid Monoclonal Antibodies for the Treatment of Alzheimer’s Disease. BioDrugs, 38(1), 5–22.</bibl>
            <idno type="DOI">10.1007/s40259-023-00633-2</idno>
          </bibl>
          <bibl n="230935">
            <bibl>Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., &amp;amp; LaDu, M. J. (2002). Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. Journal of Biological Chemistry, 277(35), 32046–32053.</bibl>
            <idno type="DOI">10.1074/jbc.M201750200</idno>
          </bibl>
          <bibl n="230819">
            <bibl>Danis, C., Dupr&amp;#233;, E., Zejneli, O., Caillierez, R., Arrial, A., B&amp;#233;gard, S., Mortelecque, J., Eddarkaoui, S., Loyens, A., Cantrelle, F.-X., Hanoulle, X., Rain, J.-C., Colin, M., Bu&amp;#233;e, L., &amp;amp; Landrieu, I. (2022). Inhibition of Tau seeding by targeting Tau nucleation core within neurons with a single domain antibody fragment. Molecular Therapy, 30(4), 1484–1499.</bibl>
            <idno type="DOI">10.1016/j.ymthe.2022.01.009</idno>
          </bibl>
          <bibl n="231064">
            <bibl>David, M. A., Jones, D. R., &amp;amp; Tayebi, M. (2014). Potential candidate camelid antibodies for the treatment of protein-misfolding diseases. Journal of Neuroimmunology, 272(1-2), 76-85.</bibl>
            <idno type="DOI">10.1016/j.jneuroim.2014.05.001</idno>
          </bibl>
          <bibl n="231134">
            <bibl>de la Monte, S. M., &amp;amp; Tong, M. (2014). Brain metabolic dysfunction at the core of Alzheimer&amp;#39;s disease. Biochemical Pharmacology, 88(4), 548-559.</bibl>
            <idno type="DOI">10.1016/j.bcp.2013.12.012</idno>
          </bibl>
          <bibl n="230785">
            <bibl>De, S., Whiten, D. R., Ruggeri, F. S., Hughes, C., Rodrigues, M., Sideris, D. I., Taylor, C. G., Aprile, F. A., Muyldermans, S., Knowles, T. P. J., Vendruscolo, M., Bryant, C., Blennow, K., Skoog, I., Kern, S., Zetterberg, H., &amp;amp; Klenerman, D. (2019). Soluble aggregates present in cerebrospinal fluid change in size and mechanism of toxicity during Alzheimer’s disease progression. Acta Neuropathologica Communications, 7(1), 120.</bibl>
            <idno type="DOI">10.1186/s40478-019-0777-4</idno>
          </bibl>
          <bibl n="231166">
            <bibl>De Strooper, B. (2003). Aph-1, Pen-2, and Nicastrin with Presenilin generate an active gamma-Secretase complex. Neuron, 38(1), 9–12.</bibl>
            <idno type="DOI">10.1016/s0896-6273(03)00205-8</idno>
          </bibl>
          <bibl n="231195">
            <bibl>De Strooper, B., &amp;amp; Karran, E. (2016). The Cellular Phase of Alzheimer’s Disease. Cell, 164(4), 603–615.</bibl>
            <idno type="DOI">10.1016/j.cell.2015.12.056</idno>
          </bibl>
          <bibl n="230856">
            <bibl>Demattos, R. B., Lu, J., Tang, Y., Racke, M. M., Delong, C. A., Tzaferis, J. A., Hole, J. T., Forster, B. M., McDonnell, P. C., Liu, F., Kinley, R. D., Jordan, W. H., &amp;amp; Hutton, M. L. (2012). A plaque-specific antibody clears existing β-amyloid plaques in Alzheimer’s disease mice. Neuron, 76(5), 908–920.</bibl>
            <idno type="DOI">10.1016/j.neuron.2012.10.029</idno>
          </bibl>
          <bibl n="230940">
            <bibl>Demuro, A., Mina, E., Kayed, R., Milton, S. C., Parker, I., &amp;amp; Glabe, C. G. (2005). Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. Journal of Biological Chemistry, 280(17), 17294–17300.</bibl>
            <idno type="DOI">10.1074/jbc.M500997200</idno>
          </bibl>
          <bibl n="230892">
            <bibl>Deng, J., Habib, A., Obregon, D. F., Barger, S. W., Giunta, B., Wang, Y.-J., Hou, H., Sawmiller, D., &amp;amp; Tan, J. (2015). Soluble amyloid precursor protein alpha inhibits tau phosphorylation through modulation of GSK3β signaling pathway. Journal of Neurochemistry, 135(3), 630–637.</bibl>
            <idno type="DOI">10.1111/jnc.13351</idno>
          </bibl>
          <bibl n="231208">
            <bibl>B. C. Dickerson, &amp;amp; D. A. Wolk. Neurology, 78(2):84-90</bibl>
            <idno type="DOI">10.1212/WNL.0b013e31823efc6c</idno>
          </bibl>
          <bibl n="230800">
            <bibl>Dickey, C. A., Koren, J., Zhang, Y.-J., Xu, Y.-F., Jinwal, U. K., Birnbaum, M. J., Monks, B., Sun, M., Cheng, J. Q., Patterson, C., Bailey, R. M., Dunmore, J., Soresh, S., Leon, C., Morgan, D., &amp;amp; Petrucelli, L. (2008). Akt and CHIP coregulate tau degradation through coordinated interactions. Proceedings of the National Academy of Sciences of the United States of America, 105(9), 3622–3627.</bibl>
            <idno type="DOI">10.1073/pnas.0709180105</idno>
          </bibl>
          <bibl n="231071">
            <bibl>Ding, Q., Markesbery, W. R., Chen, Q., Li, F., &amp;amp; Keller, J. N. (2005). Ribosome dysfunction is an early event in Alzheimer’s disease. Journal of Neuroscience, 25(40), 9171–9175.</bibl>
            <idno type="DOI">10.1523/JNEUROSCI.3040-05.2005</idno>
          </bibl>
          <bibl n="230834">
            <bibl>Drews, A., De, S., Flagmeier, P., Wirthensohn, D. C., Chen, W.-H., Whiten, D. R., Rodrigues, M., Vincke, C., Muyldermans, S., Paterson, R. W., Slattery, C. F., Fox, N. C., Schott, J. M., Zetterberg, H., Dobson, C. M., Gandhi, S., &amp;amp; Klenerman, D. (2017). Inhibiting the Ca2+ Influx Induced by Human CSF. Cell Reports, 21(11), 3310–3316.</bibl>
            <idno type="DOI">10.1016/j.celrep.2017.11.057</idno>
          </bibl>
          <bibl n="230879">
            <bibl>Dufour-Rainfray, D., Beaufils, E., Vourc’h, P., Vierron, E., Mereghetti, L., Gendrot, C., Hommet, C., Andres, C. R., Guilloteau, D., &amp;amp; Mondon, K. (2013). Total protein level in cerebrospinal fluid is stable in elderly adults. Journal of the American Geriatrics Society, 61(10), 1819–1821.</bibl>
            <idno type="DOI">10.1111/jgs.12489</idno>
          </bibl>
          <bibl n="231199">
            <bibl>Edelman, G. M. (1970). The structure and function of antibodies. Scientific American, 223(2), 34–42.</bibl>
            <idno type="DOI">10.1038/scientificamerican0870-34</idno>
          </bibl>
          <bibl n="231188">
            <bibl>Eisenberg, D., &amp;amp; Jucker, M. (2012). The amyloid state of proteins in human diseases. Cell, 148(6), 1188–1203.</bibl>
            <idno type="DOI">10.1016/j.cell.2012.02.022</idno>
          </bibl>
          <bibl n="231088">Eli Lilly and Company. (2023). Lilly’s Donanemab Significantly Slowed Cognitive and Functional Decline in Phase 3 Study of Early Alzheimer’s Disease. investor.lilly.com</bibl>
          <bibl n="231201">
            <bibl>Engelman, D. M. (2005). Membranes are more mosaic than fluid. Nature, 438(7068), 578–580.</bibl>
            <idno type="DOI">10.1038/nature04394</idno>
          </bibl>
          <bibl n="230942">
            <bibl>Englund, H., Sehlin, D., Johansson, A. S., Nilsson, L. N., Gellerfors, P., Paulie, S., Lannfelt, L., &amp;amp; Pettersson, F. E. (2007). Sensitive ELISA detection of amyloid-beta protofibrils in biological samples. Journal of Neurochemistry, 103(1), 334-45.</bibl>
            <idno type="DOI">10.1111/j.1471-4159.2007.04759.x</idno>
          </bibl>
          <bibl n="231019">
            <bibl>Esteves, A., Ardu&amp;#237;no, D., Silva, D. F., Martins-Branco, D., Oliveira, C., &amp;amp; Cardoso, S. (2009). Mitochondrial Metabolism in Age-Related Neurodegenerative Disorders: Alzheimer&amp;#39;s and Parkinson&amp;#39;s Revisited.</bibl>
            <idno type="DOI">10.1007/978-0-387-84835-8_7</idno>
          </bibl>
          <bibl n="230883">
            <bibl>Evangelisti, E., Cascella, R., Becatti, M., Marrazza, G., Dobson, C. M., Chiti, F., Stefani, M., &amp;amp; Cecchi, C. (2016). Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases. Scientific Reports, 6, 32721.</bibl>
            <idno type="DOI">10.1038/srep32721</idno>
          </bibl>
          <bibl n="230848">
            <bibl>Evangelisti, E., Wright, D., Zampagni, M., Cascella, R., Fiorillo, C., Bagnoli, S., Relini, A., Nichino, D., Scartabelli, T., Nacmias, B., Sorbi, S., &amp;amp; Cecchi, C. (2013). Lipid rafts mediate amyloid-induced calcium dyshomeostasis and oxidative stress in Alzheimer&amp;#39;s disease. Current Alzheimer Research, 10(2), 143-53.</bibl>
            <idno type="DOI">10.2174/1567205011310020004</idno>
          </bibl>
          <bibl n="230914">
            <bibl>Evangelisti, E., Zampagni, M., Cascella, R., Becatti, M., Fiorillo, C., Caselli, A., Bagnoli, S., Nacmias, B., &amp;amp; Cecchi, C. (2014). Plasma membrane injury depends on bilayer lipid composition in Alzheimer&amp;#39;s disease. Journal of Alzheimer&amp;#39;s Disease, 41(1), 289-300.</bibl>
            <idno type="DOI">10.3233/JAD-131406</idno>
          </bibl>
          <bibl n="230798">
            <bibl>Ewers, M., Mattsson, N., Minthon, L., Molinuevo, J. L., Antonell, A., Popp, J., Jessen, F., Herukka, S.-K., Soininen, H., Maetzler, W., Leyhe, T., B&amp;#252;rger, K., Taniguchi, M., Urakami, K., Lista, S., Dubois, B., Blennow, K., &amp;amp; Hampel, H. (2015). CSF biomarkers for the differential diagnosis of Alzheimer’s disease: A large-scale international multicenter study. Alzheimer’s &amp;amp; Dementia, 11(11), 1306–1315.</bibl>
            <idno type="DOI">10.1016/j.jalz.2014.12.006</idno>
          </bibl>
          <bibl n="230975">
            <bibl>Fabiani, C., &amp;amp; Antollini, S. S. (2019). Alzheimer’s Disease as a Membrane Disorder: Spatial Cross-Talk Among Beta-Amyloid Peptides, Nicotinic Acetylcholine Receptors and Lipid Rafts. Frontiers in Cellular Neuroscience, 13, 309.</bibl>
            <idno type="DOI">10.3389/fncel.2019.00309</idno>
          </bibl>
          <bibl n="230824">
            <bibl>Fagan, A. M., Mintun, M. A., Shah, A. R., Aldea, P., Roe, C. M., Mach, R. H., Marcus, D., Morris, J. C., &amp;amp; Holtzman, D. M. (2009). Cerebrospinal fluid tau and ptau(181) increase with cortical amyloid deposition in cognitively normal individuals: Implications for future clinical trials of Alzheimer’s disease. EMBO Molecular Medicine, 1(8–9), 371–380.</bibl>
            <idno type="DOI">10.1002/emmm.200900048</idno>
          </bibl>
          <bibl n="230920">
            <bibl>Fani, G., La Torre, C. E., Cascella, R., Cecchi, C., Vendruscolo, M., &amp;amp; Chiti, F. (2022). Misfolded protein oligomers induce an increase of intracellular Ca2+ causing an escalation of reactive oxidative species. Cellular and Molecular Life Sciences, 79(9), 500.</bibl>
            <idno type="DOI">10.1007/s00018-022-04513-w</idno>
          </bibl>
          <bibl n="230923">
            <bibl>Fani, G., Mannini, B., Vecchi, G., Cascella, R., Cecchi, C., Dobson, C. M., Vendruscolo, M., &amp;amp; Chiti, F. (2021). Aβ Oligomers Dysregulate Calcium Homeostasis by Mechanosensitive Activation of AMPA and NMDA Receptors. ACS Chemical Neuroscience, 12(4), 766–781.</bibl>
            <idno type="DOI">10.1021/acschemneuro.0c00811</idno>
          </bibl>
          <bibl n="231185">FDA Office of the Commissioner. (2023). FDA Grants Accelerated Approval for Alzheimer’s Disease Treatment. fda.gov</bibl>
          <bibl n="231002">
            <bibl>Ferrer, I. (2002). Differential expression of phosphorylated translation initiation factor 2 alpha in Alzheimer’s disease and Creutzfeldt-Jakob’s disease. Neuropathology and Applied Neurobiology, 28(6), 441–451.</bibl>
            <idno type="DOI">10.1046/j.1365-2990.2002.t01-1-00410.x</idno>
          </bibl>
          <bibl n="230807">
            <bibl>Ferrer, I., Blanco, R., Carmona, M., Puig, B., Barrachina, M., G&amp;#243;mez, C., &amp;amp; Ambrosio, S. (2001). Active, phosphorylation-dependent mitogen-activated protein kinase (MAPK/ERK), stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK), and p38 kinase expression in Parkinson’s disease and Dementia with Lewy bodies. Journal of Neural Transmission, 108(12), 1383–1396.</bibl>
            <idno type="DOI">10.1007/s007020100015</idno>
          </bibl>
          <bibl n="230974">
            <bibl>Finder, V. H., Vodopivec, I., Nitsch, R. M., &amp;amp; Glockshuber, R. (2010). The recombinant amyloid-beta peptide Abeta1-42 aggregates faster and is more neurotoxic than synthetic Abeta1-42. Journal of Molecular Biology, 396(1), 9–18.</bibl>
            <idno type="DOI">10.1016/j.jmb.2009.12.016</idno>
          </bibl>
          <bibl n="230771">
            <bibl>Fitzpatrick, A. W. P., Debelouchina, G. T., Bayro, M. J., Clare, D. K., Caporini, M. A., Bajaj, V. S., Jaroniec, C. P., Wang, L., Ladizhansky, V., M&amp;#252;ller, S. A., MacPhee, C. E., Waudby, C. A., Mott, H. R., De Simone, A., Knowles, T. P. J., Saibil, H. R., Vendruscolo, M., Orlova, E. V., Griffin, R. G., &amp;amp; Dobson, C. M. (2013). Atomic structure and hierarchical assembly of a cross-β amyloid fibril. Proceedings of the National Academy of Sciences, 110(14), 5468–5473.</bibl>
            <idno type="DOI">10.1073/pnas.1219476110</idno>
          </bibl>
          <bibl n="230766">
            <bibl>Fleisher, A. S., Chen, K., Quiroz, Y. T., Jakimovich, L. J., Gomez, M. G., Langois, C. M., Langbaum, J. B., Ayutyanont, N., Roontiva, A., Thiyyagura, P., Lee, W., Mo, H., Lopez, L., Moreno, S., Acosta-Baena, N., Giraldo, M., Garcia, G., Reiman, R. A., Huentelman, M. J., Kosik, K. S., Tariot, P. N., Lopera, F., &amp;amp; Reiman, E. M. (2012). Florbetapir PET analysis of amyloid-β deposition in the presenilin 1 E280A autosomal dominant Alzheimer&amp;#39;s disease kindred: a cross-sectional study. Lancet Neurology, 11(12), 1057-65.</bibl>
            <idno type="DOI">10.1016/S1474-4422(12)70227-2</idno>
          </bibl>
          <bibl n="231143">Fletcher, J. (2023). Lilly’s Donanemab Significantly Slowed Cognitive and Functional Decline in Phase 3 Study of Early Alzheimer’s Disease.</bibl>
          <bibl n="230842">
            <bibl>F&amp;#246;rster, S., Grimmer, T., Miederer, I., Henriksen, G., Yousefi, B. H., Graner, P., Wester, H.-J., F&amp;#246;rstl, H., Kurz, A., Dickerson, B. C., Bartenstein, P., &amp;amp; Drzezga, A. (2012). Regional expansion of hypometabolism in Alzheimer’s disease follows amyloid deposition with temporal delay. Biological Psychiatry, 71(9), 792–797.</bibl>
            <idno type="DOI">10.1016/j.biopsych.2011.04.023</idno>
          </bibl>
          <bibl n="231072">
            <bibl>Friede, R. L., &amp;amp; Samorajski, T. (1970). Axon caliber related to neurofilaments and microtubules in sciatic nerve fibers of rats and mice. The Anatomical Record, 167(4), 379–387.</bibl>
            <idno type="DOI">10.1002/ar.1091670402</idno>
          </bibl>
          <bibl n="231069">
            <bibl>Frisoni, G. B., Fox, N. C., Jack, C. R., Scheltens, P., &amp;amp; Thompson, P. M. (2010). The clinical use of structural MRI in Alzheimer disease. Nature Reviews. Neurology, 6(2), 67–77.</bibl>
            <idno type="DOI">10.1038/nrneurol.2009.215</idno>
          </bibl>
          <bibl n="231023">
            <bibl>Frost, D., Gorman, P. M., Yip, C. M., &amp;amp; Chakrabartty, A. (2003). Co-incorporation of A beta 40 and A beta 42 to form mixed pre-fibrillar aggregates. European Journal of Biochemistry, 270(4), 654–663.</bibl>
            <idno type="DOI">10.1046/j.1432-1033.2003.03415.x</idno>
          </bibl>
          <bibl n="230877">
            <bibl>Fukuchi, K., Accavitti-Loper, M. A., Kim, H.-D., Tahara, K., Cao, Y., Lewis, T. L., Caughey, R. C., Kim, H., &amp;amp; Lalonde, R. (2006a). Amelioration of amyloid load by anti-Abeta single-chain antibody in Alzheimer mouse model. Biochemical and Biophysical Research Communications, 344(1), 79–86.</bibl>
            <idno type="DOI">10.1016/j.bbrc.2006.03.145</idno>
          </bibl>
          <bibl n="230882">
            <bibl>Fukuchi, K., Tahara, K., Kim, H.-D., Maxwell, J. A., Lewis, T. L., Accavitti-Loper, M. A., Kim, H., Ponnazhagan, S., &amp;amp; Lalonde, R. (2006b). Anti-Abeta single-chain antibody delivery via adeno-associated virus for treatment of Alzheimer’s disease. Neurobiology of Disease, 23(3), 502–511.</bibl>
            <idno type="DOI">10.1016/j.nbd.2006.04.012</idno>
          </bibl>
          <bibl n="230950">
            <bibl>Fukumoto, H., Tokuda, T., Kasai, T., Ishigami, N., Hidaka, H., Kondo, M., Allsop, D., &amp;amp; Nakagawa, M. (2010). High-molecular-weight beta-amyloid oligomers are elevated in cerebrospinal fluid of Alzheimer patients. FASEB Journal, 24(8), 2716–2726.</bibl>
            <idno type="DOI">10.1096/fj.09-150359</idno>
          </bibl>
          <bibl n="231011">
            <bibl>Fukunaga, S., Ueno, H., Yamaguchi, T., Yano, Y., Hoshino, M., &amp;amp; Matsuzaki, K. (2012). GM1 cluster mediates formation of toxic Aβ fibrils by providing hydrophobic environments. Biochemistry, 51(41), 8125–8131.</bibl>
            <idno type="DOI">10.1021/bi300839u</idno>
          </bibl>
          <bibl n="230870">
            <bibl>Georganopoulou, D. G., Chang, L., Nam, J.-M., Thaxton, C. S., Mufson, E. J., Klein, W. L., &amp;amp; Mirkin, C. A. (2005). Nanoparticle-based detection in cerebral spinal fluid of a soluble pathogenic biomarker for Alzheimer’s disease. Proceedings of the National Academy of Sciences, 102(7), 2273–2276.</bibl>
            <idno type="DOI">10.1073/pnas.0409336102</idno>
          </bibl>
          <bibl n="230830">
            <bibl>Giacomucci, G., Mazzeo, S., Bagnoli, S., Ingannato, A., Leccese, D., Berti, V., Padiglioni, S., Galdo, G., Ferrari, C., Sorbi, S., Bessi, V., &amp;amp; Nacmias, B. (2022). Plasma neurofilament light chain as a biomarker of Alzheimer’s disease in Subjective Cognitive Decline and Mild Cognitive Impairment. Journal of Neurology, 269(8), 4270–4280.</bibl>
            <idno type="DOI">10.1007/s00415-022-11055-5</idno>
          </bibl>
          <bibl n="230885">
            <bibl>Gibbs, E., Silverman, J. M., Zhao, B., Peng, X., Wang, J., Wellington, C. L., Mackenzie, I. R., Plotkin, S. S., Kaplan, J. M., &amp;amp; Cashman, N. R. (2019). A Rationally Designed Humanized Antibody Selective for Amyloid Beta Oligomers in Alzheimer’s Disease. Scientific Reports, 9(1), 9870.</bibl>
            <idno type="DOI">10.1038/s41598-019-46306-5</idno>
          </bibl>
          <bibl n="231112">
            <bibl>Gill, S. C., &amp;amp; von Hippel, P. H. (1989). Calculation of protein extinction coefficients from amino acid sequence data. Analytical Biochemistry, 182(2), 319–326.</bibl>
            <idno type="DOI">10.1016/0003-2697(89)90602-7</idno>
          </bibl>
          <bibl n="231009">
            <bibl>Ginsberg, S. D., Galvin, J. E., Chiu, T. S., Lee, V. M., Masliah, E., &amp;amp; Trojanowski, J. Q. (1998). RNA sequestration to pathological lesions of neurodegenerative diseases. Acta Neuropathologica, 96(5), 487-94.</bibl>
            <idno type="DOI">10.1007/s004010050923</idno>
          </bibl>
          <bibl n="230858">
            <bibl>Gissl&amp;#233;n, M., Price, R. W., Andreasson, U., Norgren, N., Nilsson, S., Hagberg, L., Fuchs, D., Spudich, S., Blennow, K., &amp;amp; Zetterberg, H. (2016). Plasma Concentration of the Neurofilament Light Protein (NFL) is a Biomarker of CNS Injury in HIV Infection: A Cross-Sectional Study. EBioMedicine, 3, 135–140.</bibl>
            <idno type="DOI">10.1016/j.ebiom.2015.11.036</idno>
          </bibl>
          <bibl n="231005">
            <bibl>Glenner, G. G., &amp;amp; Wong, C. W. (1984). Alzheimer’s disease and Down’s syndrome: Sharing of a unique cerebrovascular amyloid fibril protein. Biochemical and Biophysical Research Communications, 122(3), 1131–1135.</bibl>
            <idno type="DOI">10.1016/0006-291x(84)91209-9</idno>
          </bibl>
          <bibl n="231104">
            <bibl>Goedert, M., Masuda-Suzukake, M., &amp;amp; Falcon, B. (2017). Like prions: the propagation of aggregated tau and α-synuclein in neurodegeneration. Brain, 140(2), 266-278.</bibl>
            <idno type="DOI">10.1093/brain/aww230</idno>
          </bibl>
          <bibl n="230985">
            <bibl>Golde, T. E., Eckman, C. B., &amp;amp; Younkin, S. G. (2000). Biochemical detection of Abeta isoforms: Implications for pathogenesis, diagnosis, and treatment of Alzheimer’s disease. Biochimica Et Biophysica Acta, 1502(1), 172–187.</bibl>
            <idno type="DOI">10.1016/s0925-4439(00)00043-0</idno>
          </bibl>
          <bibl n="230840">
            <bibl>Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., Krafft, G. A., &amp;amp; Klein, W. L. (2003). Alzheimer’s disease-affected brain: Presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proceedings of the National Academy of Sciences, 100(18), 10417–10422.</bibl>
            <idno type="DOI">10.1073/pnas.1834302100</idno>
          </bibl>
          <bibl n="231097">
            <bibl>Gorantla, N. V., &amp;amp; Chinnathambi, S. (2018). Tau Protein Squired by Molecular Chaperones During Alzheimer’s Disease. Journal of Molecular Neuroscience, 66(3), 356–368.</bibl>
            <idno type="DOI">10.1007/s12031-018-1174-3</idno>
          </bibl>
          <bibl n="231209">
            <bibl>N. J. Greenfield. Nature Protocols, 1, 2733–2741</bibl>
            <idno type="DOI">10.1038/nprot.2006.202</idno>
          </bibl>
          <bibl n="231098">
            <bibl>Greenough, M. A., Camakaris, J., &amp;amp; Bush, A. I. (2013). Metal dyshomeostasis and oxidative stress in Alzheimer’s disease. Neurochemistry International, 62(5), 540–555.</bibl>
            <idno type="DOI">10.1016/j.neuint.2012.08.014</idno>
          </bibl>
          <bibl n="231082">
            <bibl>Guerreiro, R. J., Gustafson, D. R., &amp;amp; Hardy, J. (2012). The genetic architecture of Alzheimer’s disease: Beyond APP, PSENs and APOE. Neurobiology of Aging, 33(3), 437–456.</bibl>
            <idno type="DOI">10.1016/j.neurobiolaging.2010.03.025</idno>
          </bibl>
          <bibl n="231029">
            <bibl>Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., &amp;amp; Zhao, Y. (2020). Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease. Molecular Neurodegeneration, 15(1), 40.</bibl>
            <idno type="DOI">10.1186/s13024-020-00391-7</idno>
          </bibl>
          <bibl n="230916">
            <bibl>Habiba, U., Descallar, J., Kreilaus, F., Adhikari, U. K., Kumar, S., Morley, J. W., Bui, B. V., Koronyo-Hamaoui, M., &amp;amp; Tayebi, M. (2021). Detection of retinal and blood Aβ oligomers with nanobodies. Alzheimer’s &amp;amp; Dementia (Amsterdam, Netherlands), 13(1), e12193.</bibl>
            <idno type="DOI">10.1002/dad2.12193</idno>
          </bibl>
          <bibl n="231189">
            <bibl>Halliwell, B., &amp;amp; Gutteridge, J. M. C. (2015). Free Radicals in Biology and Medicine. Oxford University Press.</bibl>
            <idno type="DOI">10.1093/acprof:oso/9780198717478.001.0001</idno>
          </bibl>
          <bibl n="231000">
            <bibl>Hamers-Casterman, C., Atarhouch, T., Muyldermans, S., Robinson, G., Hamers, C., Songa, E. B., Bendahman, N., &amp;amp; Hamers, R. (1993). Naturally occurring antibodies devoid of light chains. Nature, 363(6428), 446–448.</bibl>
            <idno type="DOI">10.1038/363446a0</idno>
          </bibl>
          <bibl n="231001">
            <bibl>Hampel, H., Cummings, J., Blennow, K., Gao, P., Jack, C. R., &amp;amp; Vergallo, A. (2021a). Developing the ATX(N) classification for use across the Alzheimer disease continuum. Nature Reviews. Neurology, 17(9), 580–589.</bibl>
            <idno type="DOI">10.1038/s41582-021-00520-w</idno>
          </bibl>
          <bibl n="230867">
            <bibl>Hampel, H., Hardy, J., Blennow, K., Chen, C., Perry, G., Kim, S. H., Villemagne, V. L., Aisen, P., Vendruscolo, M., Iwatsubo, T., Masters, C. L., Cho, M., Lannfelt, L., Cummings, J. L., &amp;amp; Vergallo, A. (2021b). The Amyloid-β Pathway in Alzheimer’s Disease. Molecular Psychiatry, 26(10), 5481–5503.</bibl>
            <idno type="DOI">10.1038/s41380-021-01249-0</idno>
          </bibl>
          <bibl n="231178">
            <bibl>Hansen, D. V., Hanson, J. E., &amp;amp; Sheng, M. (2018). Microglia in Alzheimer’s disease. Journal of Cell Biology, 217(2), 459–472.</bibl>
            <idno type="DOI">10.1083/jcb.201709069</idno>
          </bibl>
          <bibl n="230878">
            <bibl>Hansson, O., Janelidze, S., Hall, S., Magdalinou, N., Lees, A. J., Andreasson, U., Norgren, N., Linder, J., Forsgren, L., Constantinescu, R., Zetterberg, H., &amp;amp; Blennow, K. (2017). Blood-based NfL: A biomarker for differential diagnosis of parkinsonian disorder. Neurology, 88(10), 930–937.</bibl>
            <idno type="DOI">10.1212/WNL.0000000000003680</idno>
          </bibl>
          <bibl n="230964">
            <bibl>Hansson, O., Lehmann, S., Otto, M., Zetterberg, H., &amp;amp; Lewczuk, P. (2019). Advantages and disadvantages of the use of the CSF Amyloid β (Aβ) 42/40 ratio in the diagnosis of Alzheimer’s Disease. Alzheimer’s Research &amp;amp; Therapy, 11(1), 34.</bibl>
            <idno type="DOI">10.1186/s13195-019-0485-0</idno>
          </bibl>
          <bibl n="231101">
            <bibl>Hardy, J., &amp;amp; Allsop, D. (1991). Amyloid deposition as the central event in the aetiology of Alzheimer’s disease. Trends in Pharmacological Sciences, 12(10), 383–388.</bibl>
            <idno type="DOI">10.1016/0165-6147(91)90609-v</idno>
          </bibl>
          <bibl n="231106">
            <bibl>Hardy, J., &amp;amp; Selkoe, D. J. (2002). The amyloid hypothesis of Alzheimer’s disease: Progress and problems on the road to therapeutics. Science, 297(5580), 353–356.</bibl>
            <idno type="DOI">10.1126/science.1072994</idno>
          </bibl>
          <bibl n="230982">
            <bibl>Hashimoto, M., Rockenstein, E., Crews, L., &amp;amp; Masliah, E. (2003). Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer’s and Parkinson’s diseases. Neuromolecular Medicine, 4(1–2), 21–36.</bibl>
            <idno type="DOI">10.1385/NMM:4:1-2:21</idno>
          </bibl>
          <bibl n="231027">
            <bibl>Hebda, J. A., &amp;amp; Miranker, A. D. (2009). The Interplay of Catalysis and Toxicity by Amyloid Intermediates on Lipid Bilayers: Insights from Type II Diabetes. Annual Review of Biophysics, 38, 125–152.</bibl>
            <idno type="DOI">10.1146/annurev.biophys.050708.133641</idno>
          </bibl>
          <bibl n="230991">
            <bibl>Hefti, F., Goure, W. F., Jerecic, J., Iverson, K. S., Walicke, P. A., &amp;amp; Krafft, G. A. (2013). The case for soluble Aβ oligomers as a drug target in Alzheimer’s disease. Trends in Pharmacological Sciences, 34(5), 261–266.</bibl>
            <idno type="DOI">10.1016/j.tips.2013.03.002</idno>
          </bibl>
          <bibl n="230802">
            <bibl>Heneka, M. T., Carson, M. J., El Khoury, J., Landreth, G. E., Brosseron, F., Feinstein, D. L., Jacobs, A. H., Wyss-Coray, T., Vitorica, J., Ransohoff, R. M., Herrup, K., Frautschy, S. A., Finsen, B., Brown, G. C., Verkhratsky, A., Yamanaka, K., Koistinaho, J., Latz, E., Halle, A., … Kummer, M. P. (2015). Neuroinflammation in Alzheimer’s disease. The Lancet Neurology, 14(4), 388–405.</bibl>
            <idno type="DOI">10.1016/S1474-4422(15)70016-5</idno>
          </bibl>
          <bibl n="230849">
            <bibl>Hepp, D. H., Vergoossen, D. L. E., Huisman, E., Lemstra, A. W., Berendse, H. W., Rozemuller, A. J., Foncke, E. M. J., &amp;amp; van de Berg, W. D. J. (2016). Distribution and Load of Amyloid-β Pathology in Parkinson Disease and Dementia with Lewy Bodies. Journal of Neuropathology and Experimental Neurology, 75(10), 936–945.</bibl>
            <idno type="DOI">10.1093/jnen/nlw070</idno>
          </bibl>
          <bibl n="231006">
            <bibl>Hern&amp;#225;ndez-Ortega, K., Garcia-Esparcia, P., Gil, L., Lucas, J. J., &amp;amp; Ferrer, I. (2016). Altered Machinery of Protein Synthesis in Alzheimer’s: From the Nucleolus to the Ribosome. Brain Pathology, 26(5), 593–605.</bibl>
            <idno type="DOI">10.1111/bpa.12335</idno>
          </bibl>
          <bibl n="230948">
            <bibl>Herring, W. L., Gould, I. G., Fillit, H., Lindgren, P., Forrestal, F., Thompson, R., &amp;amp; Pemberton-Ross, P. (2021). Predicted Lifetime Health Outcomes for Aducanumab in Patients with Early Alzheimer’s Disease. Neurology and Therapy, 10(2), 919–940.</bibl>
            <idno type="DOI">10.1007/s40120-021-00273-0</idno>
          </bibl>
          <bibl n="231193">
            <bibl>Hershko, A., &amp;amp; Ciechanover, A. (1998). The ubiquitin system. Annual Review of Biochemistry, 67, 425–479.</bibl>
            <idno type="DOI">10.1146/annurev.biochem.67.1.425</idno>
          </bibl>
          <bibl n="231035">
            <bibl>Herskovits, A. Z., Locascio, J. J., Peskind, E. R., Li, G., &amp;amp; Hyman, B. T. (2013). A Luminex assay detects amyloid β oligomers in Alzheimer’s disease cerebrospinal fluid. PloS One, 8(7), e67898.</bibl>
            <idno type="DOI">10.1371/journal.pone.0067898</idno>
          </bibl>
          <bibl n="230928">
            <bibl>Heyman, A., Peterson, B., Fillenbaum, G., &amp;amp; Pieper, C. (1996). The consortium to establish a registry for Alzheimer’s disease (CERAD). Part XIV: Demographic and clinical predictors of survival in patients with Alzheimer’s disease. Neurology, 46(3), 656–660.</bibl>
            <idno type="DOI">10.1212/wnl.46.3.656</idno>
          </bibl>
          <bibl n="230810">
            <bibl>Hillen, H., Barghorn, S., Striebinger, A., Labkovsky, B., M&amp;#252;ller, R., Nimmrich, V., Nolte, M. W., Perez-Cruz, C., van der Auwera, I., van Leuven, F., van Gaalen, M., Bespalov, A. Y., Schoemaker, H., Sullivan, J. P., &amp;amp; Ebert, U. (2010). Generation and therapeutic efficacy of highly oligomer-specific beta-amyloid antibodies. Journal of Neuroscience, 30(31), 10369–10379.</bibl>
            <idno type="DOI">10.1523/JNEUROSCI.5721-09.2010</idno>
          </bibl>
          <bibl n="231107">
            <bibl>Hipp, M. S., Park, S.-H., &amp;amp; Hartl, F. U. (2014). Proteostasis impairment in protein-misfolding and -aggregation diseases. Trends in Cell Biology, 24(9), 506–514.</bibl>
            <idno type="DOI">10.1016/j.tcb.2014.05.003</idno>
          </bibl>
          <bibl n="231073">
            <bibl>Hodges, J. R., Graham, N., &amp;amp; Patterson, K. (1995). Charting the progression in semantic dementia: Implications for the organisation of semantic memory. Memory, 3(3–4), 463–495.</bibl>
            <idno type="DOI">10.1080/09658219508253161</idno>
          </bibl>
          <bibl n="230909">
            <bibl>Hof, P. R., Vogt, B. A., Bouras, C., &amp;amp; Morrison, J. H. (1997). Atypical form of Alzheimer’s disease with prominent posterior cortical atrophy: A review of lesion distribution and circuit disconnection in cortical visual pathways. Vision Research, 37(24), 3609–3625.</bibl>
            <idno type="DOI">10.1016/S0042-6989(96)00240-4</idno>
          </bibl>
          <bibl n="230945">
            <bibl>H&amp;#246;ltt&amp;#228;, M., Hansson, O., Andreasson, U., Hertze, J., Minthon, L., N&amp;#228;gga, K., Andreasen, N., Zetterberg, H., &amp;amp; Blennow, K. (2013). Evaluating amyloid-β oligomers in cerebrospinal fluid as a biomarker for Alzheimer’s disease. PloS One, 8(6), e66381.</bibl>
            <idno type="DOI">10.1371/journal.pone.0066381</idno>
          </bibl>
          <bibl n="230908">
            <bibl>Hong, S., Ostaszewski, B. L., Yang, T., O’Malley, T. T., Jin, M., Yanagisawa, K., Li, S., Bartels, T., &amp;amp; Selkoe, D. J. (2014). Soluble Aβ oligomers are rapidly sequestered from brain ISF in vivo and bind GM1 ganglioside on cellular membranes. Neuron, 82(2), 308–319.</bibl>
            <idno type="DOI">10.1016/j.neuron.2014.02.027</idno>
          </bibl>
          <bibl n="231012">
            <bibl>Hong, S., Beja-Glasser, V. F., Nfonoyim, B. M., Frouin, A., Li, S., Ramakrishnan, S., et al. (2016). Complement and microglia mediate early synapse loss in Alzheimer mouse models. Science, 352(6286), 712–716.</bibl>
            <idno type="DOI">10.1126/science.aad8373</idno>
          </bibl>
          <bibl n="231170">
            <bibl>Huang, W.-J., Zhang, X., &amp;amp; Chen, W.-W. (2016). Role of oxidative stress in Alzheimer’s disease. Biomedical Reports, 4(5), 519–522.</bibl>
            <idno type="DOI">10.3892/br.2016.630</idno>
          </bibl>
          <bibl n="231129">
            <bibl>Huang, Y. R., &amp;amp; Liu, R.-T. (2020). The Toxicity and Polymorphism of β-Amyloid Oligomers. International Journal of Molecular Sciences, 21(12), 4477.</bibl>
            <idno type="DOI">10.3390/ijms21124477</idno>
          </bibl>
          <bibl n="231028">
            <bibl>Hubin, E., van Nuland, N. a. J., Broersen, K., &amp;amp; Pauwels, K. (2014). Transient dynamics of Aβ contribute to toxicity in Alzheimer’s disease. Cellular and Molecular Life Sciences, 71(18), 3507–3521.</bibl>
            <idno type="DOI">10.1007/s00018-014-1634-z</idno>
          </bibl>
          <bibl n="230795">
            <bibl>Hultberg, A., Temperton, N. J., Rosseels, V., Koenders, M., Gonzalez-Pajuelo, M., Schepens, B., Iba&amp;#241;ez, L. I., Vanlandschoot, P., Schillemans, J., Saunders, M., Weiss, R. A., Saelens, X., Melero, J. A., Verrips, C. T., Van Gucht, S., &amp;amp; de Haard, H. J. (2011). Llama-derived single domain antibodies to build multivalent, superpotent and broadened neutralizing anti-viral molecules. PloS One, 6(4), e17665.</bibl>
            <idno type="DOI">10.1371/journal.pone.0017665</idno>
          </bibl>
          <bibl n="230809">
            <bibl>Huston, J. S., Levinson, D., Mudgett-Hunter, M., Tai, M. S., Novotn&amp;#253;, J., Margolies, M. N., Ridge, R. J., Bruccoleri, R. E., Haber, E., &amp;amp; Crea, R. (1988). Protein engineering of antibody binding sites: Recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli. Proceedings of the National Academy of Sciences, 85(16), 5879–5883.</bibl>
            <idno type="DOI">10.1073/pnas.85.16.5879</idno>
          </bibl>
          <bibl n="231057">
            <bibl>Hyman, B. T., Van Hoesen, G. W., Damasio, A. R., &amp;amp; Barnes, C. L. (1984). Alzheimer’s disease: Cell-specific pathology isolates the hippocampal formation. Science, 225(4667), 1168–1170.</bibl>
            <idno type="DOI">10.1126/science.6474172</idno>
          </bibl>
          <bibl n="231135">
            <bibl>Iadecola, C. (2017). The Neurovascular Unit Coming of Age: A Journey through Neurovascular Coupling in Health and Disease. Neuron, 96(1), 17-42.</bibl>
            <idno type="DOI">10.1016/j.neuron.2017.07.030</idno>
          </bibl>
          <bibl n="230791">
            <bibl>Jack, C. R., Bennett, D. A., Blennow, K., Carrillo, M. C., Dunn, B., Haeberlein, S. B., Holtzman, D. M., Jagust, W., Jessen, F., Karlawish, J., Liu, E., Molinuevo, J. L., Montine, T., Phelps, C., Rankin, K. P., Rowe, C. C., Scheltens, P., Siemers, E., Snyder, H. M., … Contributors. (2018). NIA-AA Research Framework: Toward a biological definition of Alzheimer’s disease. Alzheimer’s &amp;amp; Dementia, 14(4), 535–562.</bibl>
            <idno type="DOI">10.1016/j.jalz.2018.02.018</idno>
          </bibl>
          <bibl n="230857">
            <bibl>Jack, C. R., Dickson, D. W., Parisi, J. E., Xu, Y. C., Cha, R. H., O’Brien, P. C., Edland, S. D., Smith, G. E., Boeve, B. F., Tangalos, E. G., Kokmen, E., &amp;amp; Petersen, R. C. (2002). Antemortem MRI findings correlate with hippocampal neuropathology in typical aging and dementia. Neurology, 58(5), 750–757.</bibl>
            <idno type="DOI">10.1212/wnl.58.5.750</idno>
          </bibl>
          <bibl n="231191">
            <bibl>Jack, C. R., &amp;amp; Holtzman, D. M. (2013). Biomarker modeling of Alzheimer’s disease. Neuron, 80(6), 1347–1358.</bibl>
            <idno type="DOI">10.1016/j.neuron.2013.12.003</idno>
          </bibl>
          <bibl n="230808">
            <bibl>Jack, C. R., Knopman, D. S., Jagust, W. J., Petersen, R. C., Weiner, M. W., Aisen, P. S., Shaw, L. M., Vemuri, P., Wiste, H. J., Weigand, S. D., Lesnick, T. G., Pankratz, V. S., Donohue, M. C., &amp;amp; Trojanowski, J. Q. (2013). Tracking pathophysiological processes in Alzheimer’s disease: An updated hypothetical model of dynamic biomarkers. The Lancet Neurology, 12(2), 207–216.</bibl>
            <idno type="DOI">10.1016/S1474-4422(12)70291-0</idno>
          </bibl>
          <bibl n="230937">
            <bibl>Jack, C. R., Knopman, D. S., Jagust, W. J., Shaw, L. M., Aisen, P. S., Weiner, M. W., Petersen, R. C., &amp;amp; Trojanowski, J. Q. (2010a). Hypothetical model of dynamic biomarkers of the Alzheimer’s pathological cascade. The Lancet Neurology, 9(1), 119–128.</bibl>
            <idno type="DOI">10.1016/S1474-4422(09)70299-6</idno>
          </bibl>
          <bibl n="230837">
            <bibl>Jack, C. R., Lowe, V. J., Senjem, M. L., Weigand, S. D., Kemp, B. J., Shiung, M. M., Knopman, D. S., Boeve, B. F., Klunk, W. E., Mathis, C. A., &amp;amp; Petersen, R. C. (2008). 11C PiB and structural MRI provide complementary information in imaging of Alzheimer’s disease and amnestic mild cognitive impairment. Brain, 131(Pt 3), 665–680.</bibl>
            <idno type="DOI">10.1093/brain/awm336</idno>
          </bibl>
          <bibl n="230816">
            <bibl>Jack, C. R., Lowe, V. J., Weigand, S. D., Wiste, H. J., Senjem, M. L., Knopman, D. S., Shiung, M. M., Gunter, J. L., Boeve, B. F., Kemp, B. J., Weiner, M., &amp;amp; Petersen, R. C. (2009). Serial PIB and MRI in normal, mild cognitive impairment and Alzheimer’s disease: Implications for sequence of pathological events in Alzheimer’s disease. Brain, 132(Pt 5), 1355–1365.</bibl>
            <idno type="DOI">10.1093/brain/awp062</idno>
          </bibl>
          <bibl n="230811">
            <bibl>Jack, C. R., Vemuri, P., Wiste, H. J., Weigand, S. D., Lesnick, T. G., Lowe, V., Kantarci, K., Bernstein, M. A., Senjem, M. L., Gunter, J. L., Boeve, B. F., Trojanowski, J. Q., Shaw, L. M., Aisen, P. S., Weiner, M. W., Petersen, R. C., &amp;amp; Knopman, D. S. (2012). Shapes of the trajectories of 5 major biomarkers of Alzheimer disease. Archives of Neurology, 69(7), 856–867.</bibl>
            <idno type="DOI">10.1001/archneurol.2011.3405</idno>
          </bibl>
          <bibl n="230789">
            <bibl>Jack, C. R., Wiste, H. J., Vemuri, P., Weigand, S. D., Senjem, M. L., Zeng, G., Bernstein, M. A., Gunter, J. L., Pankratz, V. S., Aisen, P. S., Weiner, M. W., Petersen, R. C., Shaw, L. M., Trojanowski, J. Q., &amp;amp; Knopman, D. S. (2010b). Brain beta-amyloid measures and magnetic resonance imaging atrophy both predict time-to-progression from mild cognitive impairment to Alzheimer’s disease. Brain, 133(11), 3336–3348.</bibl>
            <idno type="DOI">10.1093/brain/awq277</idno>
          </bibl>
          <bibl n="231024">
            <bibl>Jackson, R. J., Hellen, C. U. T., &amp;amp; Pestova, T. V. (2010). The mechanism of eukaryotic translation initiation and principles of its regulation. Nature Reviews. Molecular Cell Biology, 11(2), 113–127.</bibl>
            <idno type="DOI">10.1038/nrm2838</idno>
          </bibl>
          <bibl n="231190">
            <bibl>Jagust, W. J. (2010). Amyloid imaging: Coming to a PET scanner near you. Annals of Neurology, 68(3), 277–278.</bibl>
            <idno type="DOI">10.1002/ana.22144</idno>
          </bibl>
          <bibl n="231080">
            <bibl>Jakob-Roetne, R., &amp;amp; Jacobsen, H. (2009). Alzheimer’s disease: From pathology to therapeutic approaches. Angewandte Chemie (International Ed. in English), 48(17), 3030–3059.</bibl>
            <idno type="DOI">10.1002/anie.200802808</idno>
          </bibl>
          <bibl n="230787">
            <bibl>Janelidze, S., Mattsson, N., Palmqvist, S., Smith, R., Beach, T. G., Serrano, G. E., Chai, X., Proctor, N. K., Eichenlaub, U., Zetterberg, H., Blennow, K., Reiman, E. M., Stomrud, E., Dage, J. L., &amp;amp; Hansson, O. (2020). Plasma P-tau181 in Alzheimer’s disease: Relationship to other biomarkers, differential diagnosis, neuropathology and longitudinal progression to Alzheimer’s dementia. Nature Medicine, 26(3), 379–386.</bibl>
            <idno type="DOI">10.1038/s41591-020-0755-1</idno>
          </bibl>
          <bibl n="230910">
            <bibl>Janelidze, S., Stomrud, E., Palmqvist, S., Zetterberg, H., van Westen, D., Jeromin, A., Song, L., Hanlon, D., Tan Hehir, C. A., Baker, D., Blennow, K., &amp;amp; Hansson, O. (2016). Plasma β-amyloid in Alzheimer’s disease and vascular disease. Scientific Reports, 6, 26801.</bibl>
            <idno type="DOI">10.1038/srep26801</idno>
          </bibl>
          <bibl n="230780">
            <bibl>Jansen, W. J., Ossenkoppele, R., Knol, D. L., Tijms, B. M., Scheltens, P., Verhey, F. R. J., Visser, P. J., Amyloid Biomarker Study Group, Aalten, P., Aarsland, D., Alcolea, D., Alexander, M., Almdahl, I. S., Arnold, S. E., Baldeiras, I., Barthel, H., van Berckel, B. N. M., Bibeau, K., Blennow, K., … Zetterberg, H. (2015). Prevalence of cerebral amyloid pathology in persons without dementia: A meta-analysis. JAMA, 313(19), 1924–1938.</bibl>
            <idno type="DOI">10.1001/jama.2015.4668</idno>
          </bibl>
          <bibl n="230949">
            <bibl>Jarrett, J. T., Berger, E. P., &amp;amp; Lansbury, P. T. (1993). The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer’s disease. Biochemistry, 32(18), 4693–4697.</bibl>
            <idno type="DOI">10.1021/bi00069a001</idno>
          </bibl>
          <bibl n="230784">
            <bibl>Jekel, K., Damian, M., Wattmo, C., Hausner, L., Bullock, R., Connelly, P. J., Dubois, B., Eriksdotter, M., Ewers, M., Graessel, E., Kramberger, M. G., Law, E., Mecocci, P., Molinuevo, J. L., Nyg&amp;#229;rd, L., Olde-Rikkert, M. G., Orgogozo, J.-M., Pasquier, F., Peres, K., … Fr&amp;#246;lich, L. (2015). Mild cognitive impairment and deficits in instrumental activities of daily living: A systematic review. Alzheimer’s Research &amp;amp; Therapy, 7(1), 17.</bibl>
            <idno type="DOI">10.1186/s13195-015-0099-0</idno>
          </bibl>
          <bibl n="230946">
            <bibl>Ji, S. R., Wu, Y., &amp;amp; Sui, S. (2002). Cholesterol is an important factor affecting the membrane insertion of beta-amyloid peptide (A beta 1-40), which may potentially inhibit the fibril formation. Journal of Biological Chemistry, 277(8), 6273–6279.</bibl>
            <idno type="DOI">10.1074/jbc.M104146200</idno>
          </bibl>
          <bibl n="230833">
            <bibl>Jinwal, U. K., Trotter, J. H., Abisambra, J. F., Koren, J., Lawson, L. Y., Vestal, G. D., O’Leary, J. C., Johnson, A. G., Jin, Y., Jones, J. R., Li, Q., Weeber, E. J., &amp;amp; Dickey, C. A. (2011). The Hsp90 kinase co-chaperone Cdc37 regulates tau stability and phosphorylation dynamics. Journal of Biological Chemistry, 286(19), 16976–16983.</bibl>
            <idno type="DOI">10.1074/jbc.M110.182493</idno>
          </bibl>
          <bibl n="231046">
            <bibl>Johnson, J. K., Head, E., Kim, R., Starr, A., &amp;amp; Cotman, C. W. (1999). Clinical and pathological evidence for a frontal variant of Alzheimer disease. Archives of Neurology, 56(10), 1233–1239.</bibl>
            <idno type="DOI">10.1001/archneur.56.10.1233</idno>
          </bibl>
          <bibl n="231184">
            <bibl>Kagan, B. L., Azimov, R., &amp;amp; Azimova, R. (2004). Amyloid peptide channels. Journal of Membrane Biology, 202(1), 1–10.</bibl>
            <idno type="DOI">10.1007/s00232-004-0709-4</idno>
          </bibl>
          <bibl n="230924">
            <bibl>Kakio, A., Nishimoto, S. I., Yanagisawa, K., Kozutsumi, Y., &amp;amp; Matsuzaki, K. (2001). Cholesterol-dependent formation of GM1 ganglioside-bound amyloid beta-protein, an endogenous seed for Alzheimer amyloid. Journal of Biological Chemistry, 276(27), 24985–24990.</bibl>
            <idno type="DOI">10.1074/jbc.M100252200</idno>
          </bibl>
          <bibl n="230884">
            <bibl>Kakio, A., Nishimoto, S., Yanagisawa, K., Kozutsumi, Y., &amp;amp; Matsuzaki, K. (2002). Interactions of amyloid beta-protein with various gangliosides in raft-like membranes: Importance of GM1 ganglioside-bound form as an endogenous seed for Alzheimer amyloid. Biochemistry, 41(23), 7385–7390.</bibl>
            <idno type="DOI">10.1021/bi0255874</idno>
          </bibl>
          <bibl n="230905">
            <bibl>Kamat, P. K., Kalani, A., Rai, S., Swarnkar, S., Tota, S., Nath, C., &amp;amp; Tyagi, N. (2016). Mechanism of Oxidative Stress and Synapse Dysfunction in the Pathogenesis of Alzheimer’s Disease: Understanding the Therapeutics Strategies. Molecular Neurobiology, 53(1), 648–661.</bibl>
            <idno type="DOI">10.1007/s12035-014-9053-6</idno>
          </bibl>
          <bibl n="230956">
            <bibl>Kaneko, M., Koike, H., Saito, R., Kitamura, Y., Okuma, Y., &amp;amp; Nomura, Y. (2010). Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-beta generation. Journal of Neuroscience, 30(11), 3924–3932.</bibl>
            <idno type="DOI">10.1523/JNEUROSCI.2422-09.2010</idno>
          </bibl>
          <bibl n="231030">
            <bibl>Kaneko, M., Saito, R., Okuma, Y., &amp;amp; Nomura, Y. (2012). Possible involvement of ubiquitin ligase HRD1 insolubilization in amyloid β generation. Biological &amp;amp; Pharmaceutical Bulletin, 35(2), 269–272.</bibl>
            <idno type="DOI">10.1248/bpb.35.269</idno>
          </bibl>
          <bibl n="231093">
            <bibl>Kapasi, A., DeCarli, C., &amp;amp; Schneider, J. A. (2017). Impact of multiple pathologies on the threshold for clinically overt dementia. Acta Neuropathologica, 134, 171–186.</bibl>
            <idno type="DOI">10.1007/s00401-017-1717-7</idno>
          </bibl>
          <bibl n="231167">
            <bibl>Karch, C. M., Cruchaga, C., &amp;amp; Goate, A. M. (2014). Alzheimer’s disease genetics: From the bench to the clinic. Neuron, 83(1), 11–26.</bibl>
            <idno type="DOI">10.1016/j.neuron.2014.05.041</idno>
          </bibl>
          <bibl n="230767">
            <bibl>Karikari, T. K., Pascoal, T. A., Ashton, N. J., Janelidze, S., Benedet, A. L., Rodriguez, J. L., Chamoun, M., Savard, M., Kang, M. S., Therriault, J., Sch&amp;#246;ll, M., Massarweh, G., Soucy, J.-P., H&amp;#246;glund, K., Brinkmalm, G., Mattsson, N., Palmqvist, S., Gauthier, S., Stomrud, E., … Blennow, K. (2020). Blood phosphorylated tau 181 as a biomarker for Alzheimer’s disease: A diagnostic performance and prediction modelling study using data from four prospective cohorts. The Lancet Neurology, 19(5), 422–433.</bibl>
            <idno type="DOI">10.1016/S1474-4422(20)30071-5</idno>
          </bibl>
          <bibl n="231099">
            <bibl>Karran, E., &amp;amp; De Strooper, B. (2022). The amyloid hypothesis in Alzheimer disease: New insights from new therapeutics. Nature Reviews. Drug Discovery, 21(4), 306–318.</bibl>
            <idno type="DOI">10.1038/s41573-022-00391-w</idno>
          </bibl>
          <bibl n="231025">
            <bibl>Kasturirangan, S., Li, L., Emadi, S., Boddapati, S., Schulz, P., &amp;amp; Sierks, M. R. (2012). Nanobody specific for oligomeric β-amyloid stabilizes nontoxic form. Neurobiology of Aging, 33(7), 1320–1328.</bibl>
            <idno type="DOI">10.1016/j.neurobiolaging.2010.09.020</idno>
          </bibl>
          <bibl n="230803">
            <bibl>Kayed, R., Head, E., Sarsoza, F., Saing, T., Cotman, C. W., Necula, M., Margol, L., Wu, J., Breydo, L., Thompson, J. L., Rasool, S., Gurlo, T., Butler, P., &amp;amp; Glabe, C. G. (2007). Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Molecular Neurodegeneration, 2, 18.</bibl>
            <idno type="DOI">10.1186/1750-1326-2-18</idno>
          </bibl>
          <bibl n="230983">
            <bibl>Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., &amp;amp; Glabe, C. G. (2003). Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science, 300(5618), 486–489.</bibl>
            <idno type="DOI">10.1126/science.1079469</idno>
          </bibl>
          <bibl n="230863">
            <bibl>Kayed, R., Sokolov, Y., Edmonds, B., McIntire, T. M., Milton, S. C., Hall, J. E., &amp;amp; Glabe, C. G. (2004). Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. Journal of Biological Chemistry, 279(45), 46363–46366.</bibl>
            <idno type="DOI">10.1074/jbc.C400260200</idno>
          </bibl>
          <bibl n="231200">
            <bibl>Kaushik, S., &amp;amp; Cuervo, A. M. (2015). Proteostasis and aging. Nature Medicine, 21(12), 1406-15.</bibl>
            <idno type="DOI">10.1038/nm.4001</idno>
          </bibl>
          <bibl n="231026">
            <bibl>Keck, S., Nitsch, R., Grune, T., &amp;amp; Ullrich, O. (2003). Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer’s disease. Journal of Neurochemistry, 85(1), 115–122.</bibl>
            <idno type="DOI">10.1046/j.1471-4159.2003.01642.x</idno>
          </bibl>
          <bibl n="231161">
            <bibl>Khachaturian, Z. S. (1989). The role of calcium regulation in brain aging: Reexamination of a hypothesis. Aging (Milan), 1(1), 17–34.</bibl>
            <idno type="DOI">10.1007/BF03323872</idno>
          </bibl>
          <bibl n="231054">
            <bibl>Kim, S., Sharma, C., Jung, U. J., &amp;amp; Kim, S. R. (2023). Pathophysiological Role of Microglial Activation Induced by Blood-Borne Proteins in Alzheimer’s Disease. Biomedicines, 11(5), 1383.</bibl>
            <idno type="DOI">10.3390/biomedicines11051383</idno>
          </bibl>
          <bibl n="231123">
            <bibl>Kim, S. I., Yi, J. S., &amp;amp; Ko, Y. G. (2006). Amyloid beta oligomerization is induced by brain lipid rafts. Journal of Cellular Biochemistry, 99(3), 878–889.</bibl>
            <idno type="DOI">10.1002/jcb.20978</idno>
          </bibl>
          <bibl n="231048">
            <bibl>Kim, Y. E., Hipp, M. S., Bracher, A., Hayer-Hartl, M., &amp;amp; Hartl, F. U. (2013). Molecular chaperone functions in protein folding and proteostasis. Annual Review of Biochemistry, 82, 323–355.</bibl>
            <idno type="DOI">10.1146/annurev-biochem-060208-092442</idno>
          </bibl>
          <bibl n="230962">Kim, K. S., Wen, G. Y., Bancher, C., Chen, C. M. J., Sapienza, V., Hong, H., &amp;amp; Wisniewski, H. M. (1990). Detection and quantification of amyloid β-peptide with two monoclonal antibodies. Neuroscience Research Communications, 7, 113–122.</bibl>
          <bibl n="230997">
            <bibl>Kinger, S., Jagtap, Y. A., Kumar, P., Choudhary, A., Prasad, A., Prajapati, V. K., Kumar, A., Mehta, G., &amp;amp; Mishra, A. (2024). Proteostasis in neurodegenerative diseases. Advances in Clinical Chemistry, 121, 270–333.</bibl>
            <idno type="DOI">10.1016/bs.acc.2024.04.002</idno>
          </bibl>
          <bibl n="231021">
            <bibl>Kish, S. J. (1997). Brain energy metabolizing enzymes in Alzheimer’s disease: Alpha-ketoglutarate dehydrogenase complex and cytochrome oxidase. Annals of the New York Academy of Sciences, 826, 218–228.</bibl>
            <idno type="DOI">10.1111/j.1749-6632.1997.tb48473.x</idno>
          </bibl>
          <bibl n="231162">
            <bibl>Kleiger, G., &amp;amp; Mayor, T. (2014). Perilous journey: A tour of the ubiquitin-proteasome system. Trends in Cell Biology, 24(6), 352–359.</bibl>
            <idno type="DOI">10.1016/j.tcb.2013.12.003</idno>
          </bibl>
          <bibl n="230970">
            <bibl>Klement, M., Liu, C., Loo, B. L. W., Choo, A. B.-H., Ow, D. S.-W., &amp;amp; Lee, D.-Y. (2015). Effect of linker flexibility and length on the functionality of a cytotoxic engineered antibody fragment. Journal of Biotechnology, 199, 90–97.</bibl>
            <idno type="DOI">10.1016/j.jbiotec.2015.02.008</idno>
          </bibl>
          <bibl n="230815">
            <bibl>Klyubin, I., Betts, V., Welzel, A. T., Blennow, K., Zetterberg, H., Wallin, A., Lemere, C. A., Cullen, W. K., Peng, Y., Wisniewski, T., Selkoe, D. J., Anwyl, R., Walsh, D. M., &amp;amp; Rowan, M. J. (2008). Amyloid beta protein dimer-containing human CSF disrupts synaptic plasticity: Prevention by systemic passive immunization. Journal of Neuroscience, 28(16), 4231–4237.</bibl>
            <idno type="DOI">10.1523/JNEUROSCI.5161-07.2008</idno>
          </bibl>
          <bibl n="231049">
            <bibl>Knopman, D. S., Amieva, H., Petersen, R. C., Ch&amp;#233;telat, G., Holtzman, D. M., Hyman, B. T., Nixon, R. A., &amp;amp; Jones, D. T. (2021). Alzheimer disease. Nature Reviews. Disease Primers, 7(1), 33.</bibl>
            <idno type="DOI">10.1038/s41572-021-00269-y</idno>
          </bibl>
          <bibl n="230897">
            <bibl>Kollmer, M., Close, W., Funk, L., Rasmussen, J., Bsoul, A., Schierhorn, A., Schmidt, M., Sigurdson, C. J., Jucker, M., &amp;amp; F&amp;#228;ndrich, M. (2019). Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue. Nature Communications, 10(1), 4760.</bibl>
            <idno type="DOI">10.1038/s41467-019-12683-8</idno>
          </bibl>
          <bibl n="230954">
            <bibl>Kosik, K. S., Joachim, C. L., &amp;amp; Selkoe, D. J. (1986). Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proceedings of the National Academy of Sciences, 83(11), 4044–4048.</bibl>
            <idno type="DOI">10.1073/pnas.83.11.4044</idno>
          </bibl>
          <bibl n="231187">
            <bibl>Kravats, A. N., Wickner, S., &amp;amp; Camberg, J. L. (2022). Molecular Chaperones. Reference Module in Life Sciences.</bibl>
            <idno type="DOI">10.1016/B978-0-12-809633-8.21045-8</idno>
          </bibl>
          <bibl n="230990">
            <bibl>Kremer, J. J., Pallitto, M. M., Sklansky, D. J., &amp;amp; Murphy, R. M. (2000). Correlation of beta-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity of model membranes. Biochemistry, 39(33), 10309–10318.</bibl>
            <idno type="DOI">10.1021/bi0001980</idno>
          </bibl>
          <bibl n="230860">
            <bibl>Kulichikhin, K. Y., Fedotov, S. A., Rubel, M. S., Zalutskaya, N. M., Zobnina, A. E., Malikova, O. A., Neznanov, N. G., Chernoff, Y. O., &amp;amp; Rubel, A. A. (2021). Development of molecular tools for diagnosis of Alzheimer’s disease that are based on detection of amyloidogenic proteins. Prion, 15(1), 56–69.</bibl>
            <idno type="DOI">10.1080/19336896.2021.1917289</idno>
          </bibl>
          <bibl n="231163">
            <bibl>Labbadia, J., &amp;amp; Morimoto, R. I. (2015). The biology of proteostasis in aging and disease. Annual Review of Biochemistry, 84, 435–464.</bibl>
            <idno type="DOI">10.1146/annurev-biochem-060614-033955</idno>
          </bibl>
          <bibl n="230871">
            <bibl>Ladiwala, A. R. A., Litt, J., Kane, R. S., Aucoin, D. S., Smith, S. O., Ranjan, S., Davis, J., Van Nostrand, W. E., &amp;amp; Tessier, P. M. (2012). Conformational differences between two amyloid β oligomers of similar size and dissimilar toxicity. Journal of Biological Chemistry, 287(29), 24765–24773.</bibl>
            <idno type="DOI">10.1074/jbc.M111.329763</idno>
          </bibl>
          <bibl n="230911">
            <bibl>Lafaye, P., Achour, I., England, P., Duyckaerts, C., &amp;amp; Rougeon, F. (2009). Single-domain antibodies recognize selectively small oligomeric forms of amyloid beta, prevent Abeta-induced neurotoxicity and inhibit fibril formation. Molecular Immunology, 46(4), 695–704.</bibl>
            <idno type="DOI">10.1016/j.molimm.2008.09.008</idno>
          </bibl>
          <bibl n="231136">
            <bibl>LaFerla, F. M., Green, K. N., &amp;amp; Oddo, S. (2007). Intracellular amyloid-beta in Alzheimer’s disease. Nature Reviews. Neuroscience, 8(7), 499–509.</bibl>
            <idno type="DOI">10.1038/nrn2168</idno>
          </bibl>
          <bibl n="231177">
            <bibl>Lafleche, G., &amp;amp; Albert, M. S. (1995). Executive function deficits in mild Alzheimer’s disease. Neuropsychology, 9(3), 313–320.</bibl>
            <idno type="DOI">10.1037/0894-4105.9.3.313</idno>
          </bibl>
          <bibl n="230805">
            <bibl>Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., Wals, P., Zhang, C., Finch, C. E., Krafft, G. A., &amp;amp; Klein, W. L. (1998). Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proceedings of the National Academy of Sciences, 95(11), 6448–6453.</bibl>
            <idno type="DOI">10.1073/pnas.95.11.6448</idno>
          </bibl>
          <bibl n="230898">
            <bibl>Lambert, M. P., Viola, K. L., Chromy, B. A., Chang, L., Morgan, T. E., Yu, J., Venton, D. L., Krafft, G. A., Finch, C. E., &amp;amp; Klein, W. L. (2001). Vaccination with soluble Abeta oligomers generates toxicity-neutralizing antibodies. Journal of Neurochemistry, 79(3), 595–605.</bibl>
            <idno type="DOI">10.1046/j.1471-4159.2001.00592.x</idno>
          </bibl>
          <bibl n="230960">
            <bibl>Landau, S. M., Mintun, M. A., Joshi, A. D., Koeppe, R. A., Petersen, R. C., Aisen, P. S., Weiner, M. W., &amp;amp; Jagust, W. J. (2012). Amyloid deposition, hypometabolism, and longitudinal cognitive decline. Annals of Neurology, 72(4), 578–586.</bibl>
            <idno type="DOI">10.1002/ana.23650</idno>
          </bibl>
          <bibl n="230888">
            <bibl>Lardinois, O., Kirby, P. J., Morgan, D. L., Sills, R. C., Tomer, K. B., &amp;amp; Deterding, L. J. (2014). Mass spectrometric analysis of rat cerebrospinal fluid proteins following exposure to the neurotoxicant carbonyl sulfide. Rapid Communications in Mass Spectrometry, 28(23), 2531–2538.</bibl>
            <idno type="DOI">10.1002/rcm.7046</idno>
          </bibl>
          <bibl n="230873">
            <bibl>Le Bastard, N., Coart, E., Vanderstichele, H., Vanmechelen, E., Martin, J. J., &amp;amp; Engelborghs, S. (2013). Comparison of two analytical platforms for the clinical qualification of Alzheimer&amp;#39;s disease biomarkers in pathologically-confirmed dementia. Journal of Alzheimer&amp;#39;s Disease, 33(1), 117-31.</bibl>
            <idno type="DOI">10.3233/JAD-2012-121246</idno>
          </bibl>
          <bibl n="231140">
            <bibl>Lee, A. G. (2003). Lipid-protein interactions in biological membranes: A structural perspective. Biochimica Et Biophysica Acta, 1612(1), 1–40.</bibl>
            <idno type="DOI">10.1016/s0005-2736(03)00056-7</idno>
          </bibl>
          <bibl n="230831">
            <bibl>Lee, J.-H., Yu, W. H., Kumar, A., Lee, S., Mohan, P. S., Peterhoff, C. M., Wolfe, D. M., Martinez-Vicente, M., Massey, A. C., Sovak, G., Uchiyama, Y., Westaway, D., Cuervo, A. M., &amp;amp; Nixon, R. A. (2010). Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations. Cell, 141(7), 1146–1158.</bibl>
            <idno type="DOI">10.1016/j.cell.2010.05.008</idno>
          </bibl>
          <bibl n="231089">
            <bibl>Lesne, J., Chang, H.-J., De Visch, A., et al. (2019). Structural basis for chemically-induced homodimerization of a single domain antibody. Scientific Reports, 9, 1840.</bibl>
            <idno type="DOI">10.1038/s41598-019-38752-y</idno>
          </bibl>
          <bibl n="231055">
            <bibl>Leuzy, A., Mattsson-Carlgren, N., Palmqvist, S., Janelidze, S., Dage, J. L., &amp;amp; Hansson, O. (2022). Blood-based biomarkers for Alzheimer’s disease. EMBO Molecular Medicine, 14(1), e14408.</bibl>
            <idno type="DOI">10.15252/emmm.202114408</idno>
          </bibl>
          <bibl n="230893">
            <bibl>Lewczuk, P., Matzen, A., Blennow, K., Parnetti, L., Molinuevo, J. L., Eusebi, P., Kornhuber, J., Morris, J. C., &amp;amp; Fagan, A. M. (2017). Cerebrospinal Fluid Aβ42/40 Corresponds Better than Aβ42 to Amyloid PET in Alzheimer&amp;#39;s Disease. Journal of Alzheimer&amp;#39;s Disease, 55(2), 813-822.</bibl>
            <idno type="DOI">10.3233/JAD-160722</idno>
          </bibl>
          <bibl n="230899">
            <bibl>Li, G., Bien-Ly, N., Andrews-Zwilling, Y., Xu, Q., Bernardo, A., Ring, K., Halabisky, B., Deng, C., Mahley, R. W., &amp;amp; Huang, Y. (2009). GABAergic interneuron dysfunction impairs hippocampal neurogenesis in adult apolipoprotein E4 knockin mice. Cell Stem Cell, 5(6), 634–645.</bibl>
            <idno type="DOI">10.1016/j.stem.2009.10.015</idno>
          </bibl>
          <bibl n="230959">
            <bibl>Li, S., Hong, S., Shepardson, N. E., Walsh, D. M., Shankar, G. M., &amp;amp; Selkoe, D. (2009). Soluble oligomers of amyloid Beta protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake. Neuron, 62(6), 788–801.</bibl>
            <idno type="DOI">10.1016/j.neuron.2009.05.012</idno>
          </bibl>
          <bibl n="230812">
            <bibl>Li, T., Vandesquille, M., Koukouli, F., Dudeffant, C., Youssef, I., Lenormand, P., Ganneau, C., Maskos, U., Czech, C., Grueninger, F., Duyckaerts, C., Dhenain, M., Bay, S., Delatour, B., &amp;amp; Lafaye, P. (2016). Camelid single-domain antibodies: A versatile tool for in vivo imaging of extracellular and intracellular brain targets. Journal of Controlled Release, 243, 1–10.</bibl>
            <idno type="DOI">10.1016/j.jconrel.2016.09.019</idno>
          </bibl>
          <bibl n="231037">
            <bibl>Li, X., An, W.-L., Alafuzoff, I., Soininen, H., Winblad, B., &amp;amp; Pei, J.-J. (2004). Phosphorylated eukaryotic translation factor 4E is elevated in Alzheimer brain. Neuroreport, 15(14), 2237–2240.</bibl>
            <idno type="DOI">10.1097/00001756-200410050-00019</idno>
          </bibl>
          <bibl n="231094">
            <bibl>Lin, H., Bhatia, R., &amp;amp; Lal, R. (2001). Amyloid beta protein forms ion channels: Implications for Alzheimer’s disease pathophysiology. FASEB Journal, 15(13), 2433–2444.</bibl>
            <idno type="DOI">10.1096/fj.01-0377com</idno>
          </bibl>
          <bibl n="230929">
            <bibl>Lin, M. S., Chen, L. Y., Wang, S. S. S., Chang, Y., &amp;amp; Chen, W. Y. (2008). Examining the levels of ganglioside and cholesterol in cell membrane on attenuation the cytotoxicity of beta-amyloid peptide. Colloids and Surfaces. B, Biointerfaces, 65(2), 172–177.</bibl>
            <idno type="DOI">10.1016/j.colsurfb.2008.03.012</idno>
          </bibl>
          <bibl n="231076">
            <bibl>Liu, C. C., Liu, C. C., Kanekiyo, T., Xu, H., &amp;amp; Bu, G. (2013). Apolipoprotein E and Alzheimer disease: Risk, mechanisms and therapy. Nature Reviews. Neurology, 9(2), 106–118.</bibl>
            <idno type="DOI">10.1038/nrneurol.2012.263</idno>
          </bibl>
          <bibl n="230912">
            <bibl>Liu, P., Li, L., He, F., Meng, F., Liu, X., Su, Y., Su, X., Luo, B., &amp;amp; Peng, G. (2023). Identification of Candidate Biomarkers of Alzheimer’s Disease via Multiplex Cerebrospinal Fluid and Serum Proteomics. International Journal of Molecular Sciences, 24(18), 14225.</bibl>
            <idno type="DOI">10.3390/ijms241814225</idno>
          </bibl>
          <bibl n="230976">
            <bibl>Lo, R. Y., Hubbard, A. E., Shaw, L. M., Trojanowski, J. Q., Petersen, R. C., Aisen, P. S., Weiner, M. W., &amp;amp; Jagust, W. J. (2011). Longitudinal change of biomarkers in cognitive decline. Archives of Neurology, 68(10), 1257–1266.</bibl>
            <idno type="DOI">10.1001/archneurol.2011.123</idno>
          </bibl>
          <bibl n="231003">
            <bibl>Lopez Salon, M., Pasquini, L., Besio Moreno, M., Pasquini, J. M., &amp;amp; Soto, E. (2003). Relationship between beta-amyloid degradation and the 26S proteasome in neural cells. Experimental Neurology, 180(2), 131–143.</bibl>
            <idno type="DOI">10.1016/s0014-4886(02)00060-2</idno>
          </bibl>
          <bibl n="231013">
            <bibl>L&amp;#246;pp&amp;#246;nen, M., R&amp;#228;ih&amp;#228;, I., Isoaho, R., Vahlberg, T., &amp;amp; Kivel&amp;#228;, S.-L. (2003). Diagnosing cognitive impairment and dementia in primary healthcare—A more active approach is needed. Age and Ageing, 32(6), 606–612.</bibl>
            <idno type="DOI">10.1093/ageing/afg097</idno>
          </bibl>
          <bibl n="231172">
            <bibl>Love, S., &amp;amp; Miners, J. S. (2016). Cerebrovascular disease in ageing and Alzheimer’s disease. Acta Neuropathologica, 131, 645–658.</bibl>
            <idno type="DOI">10.1007/s00401-015-1522-0</idno>
          </bibl>
          <bibl n="231102">
            <bibl>Lu, R. C., Tan, M. S., Wang, H., Xie, A. M., Yu, J. T., &amp;amp; Tan, L. (2014). Heat shock protein 70 in Alzheimer’s disease. BioMed Research International, 2014, 435203.</bibl>
            <idno type="DOI">10.1155/2014/435203</idno>
          </bibl>
          <bibl n="230907">
            <bibl>Lusardi, T. A., Phillips, J. I., Wiedrick, J. T., Harrington, C. A., Lind, B., Lapidus, J. A., Quinn, J. F., &amp;amp; Saugstad, J. A. (2017). MicroRNAs in Human Cerebrospinal Fluid as Biomarkers for Alzheimer’s Disease. Journal of Alzheimer’s Disease: JAD, 55(3), 1223–1233.</bibl>
            <idno type="DOI">10.3233/JAD-160835</idno>
          </bibl>
          <bibl n="230850">
            <bibl>Manoutcharian, K., Acero, G., Munguia, M. E., Becerril, B., Massieu, L., Govezensky, T., Ortiz, E., Marks, J. D., Cao, C., Ugen, K., &amp;amp; Gevorkian, G. (2004). Human single chain Fv antibodies and a complementarity determining region-derived peptide binding to amyloid-beta 1-42. Neurobiology of Disease, 17(1), 114–121.</bibl>
            <idno type="DOI">10.1016/j.nbd.2004.06.005</idno>
          </bibl>
          <bibl n="230902">
            <bibl>Mar&amp;#237;n-Argany, M., Rivera-Hern&amp;#225;ndez, G., Mart&amp;#237;, J., &amp;amp; Villegas, S. (2011). An anti-Aβ (amyloid β) single-chain variable fragment prevents amyloid fibril formation and cytotoxicity by withdrawing Aβ oligomers from the amyloid pathway. The Biochemical Journal, 437(1), 25–34.</bibl>
            <idno type="DOI">10.1042/BJ20101712</idno>
          </bibl>
          <bibl n="231144">
            <bibl>Martinez-Lopez, N., Athonvarangkul, D., &amp;amp; Singh, R. (2015). Autophagy and aging. Advances in Experimental Medicine and Biology, 847, 73–87.</bibl>
            <idno type="DOI">10.1007/978-1-4939-2404-2_3</idno>
          </bibl>
          <bibl n="230966">
            <bibl>Mason, R. P., Shoemaker, W. J., Shajenko, L., Chambers, T. E., &amp;amp; Herbette, L. G. (1992). Evidence for changes in the Alzheimer’s disease brain cortical membrane structure mediated by cholesterol. Neurobiology of Aging, 13(3), 413–419.</bibl>
            <idno type="DOI">10.1016/0197-4580(92)90116-f</idno>
          </bibl>
          <bibl n="230999">
            <bibl>Mastrogiacoma, F., Lindsay, J. G., Bettendorff, L., Rice, J., &amp;amp; Kish, S. J. (1996). Brain protein and alpha-ketoglutarate dehydrogenase complex activity in Alzheimer’s disease. Annals of Neurology, 39(5), 592–598.</bibl>
            <idno type="DOI">10.1002/ana.410390508</idno>
          </bibl>
          <bibl n="231131">
            <bibl>Matsuzaki, K. (2007). Physicochemical interactions of amyloid beta-peptide with lipid bilayers. Biochimica Et Biophysica Acta, 1768(8), 1935–1942.</bibl>
            <idno type="DOI">10.1016/j.bbamem.2007.02.009</idno>
          </bibl>
          <bibl n="231095">
            <bibl>Matsuzaki, K., Kato, K., &amp;amp; Yanagisawa, K. (2010). Abeta polymerization through interaction with membrane gangliosides. Biochimica Et Biophysica Acta, 1801(8), 868–877.</bibl>
            <idno type="DOI">10.1016/j.bbalip.2010.01.008</idno>
          </bibl>
          <bibl n="231196">
            <bibl>Mattson, M. P. (2004). Pathways towards and away from Alzheimer’s disease. Nature, 430(7000), 631–639.</bibl>
            <idno type="DOI">10.1038/nature02621</idno>
          </bibl>
          <bibl n="230947">
            <bibl>Mattson, M. P., Cheng, B., Davis, D., Bryant, K., Lieberburg, I., &amp;amp; Rydel, R. E. (1992). Beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. Journal of Neuroscience, 12(2), 376–389.</bibl>
            <idno type="DOI">10.1523/JNEUROSCI.12-02-00376.1992</idno>
          </bibl>
          <bibl n="230794">
            <bibl>Mattsson, N., Zetterberg, H., Hansson, O., Andreasen, N., Parnetti, L., Jonsson, M., Herukka, S.-K., van der Flier, W. M., Blankenstein, M. A., Ewers, M., Rich, K., Kaiser, E., Verbeek, M., Tsolaki, M., Mulugeta, E., Ros&amp;#233;n, E., Aarsland, D., Visser, P. J., Schr&amp;#246;der, J., … Blennow, K. (2009). CSF biomarkers and incipient Alzheimer disease in patients with mild cognitive impairment. JAMA, 302(4), 385–393.</bibl>
            <idno type="DOI">10.1001/jama.2009.1064</idno>
          </bibl>
          <bibl n="230806">
            <bibl>McKeith, I. G., Boeve, B. F., Dickson, D. W., Halliday, G., Taylor, J. P., Weintraub, D., Aarsland, D., Galvin, J., Attems, J., Ballard, C. G., Bayston, A., Beach, T. G., Blanc, F., Bohnen, N., Bonanni, L., Bras, J., Brundin, P., Burn, D., et al. (2017). Diagnosis and management of dementia with Lewy bodies: Fourth consensus report of the DLB Consortium. Neurology, 89(1), 88-100.</bibl>
            <idno type="DOI">10.1212/WNL.0000000000004058</idno>
          </bibl>
          <bibl n="230889">
            <bibl>G. M. McKhann, D. S. Knopman, H. Chertkow, B. T. Hyman, C. R. Jack Jr, C. H. Kawas, W. E. Klunk, W. J. Koroshetz, J. J. Manly, R. Mayeux, R. C. Mohs, J. C. Morris, M. N. Rossor, P. Scheltens, M. C. Carrillo, B. Thies, S. Weintraub, &amp;amp; C. H. Phelps. Alzheimer’s &amp;amp; Dementia, 7(3):263-9</bibl>
            <idno type="DOI">10.1016/j.jalz.2011.03.005</idno>
          </bibl>
          <bibl n="231138">
            <bibl>McKinnon, C., &amp;amp; Tabrizi, S. J. (2014). The ubiquitin-proteasome system in neurodegeneration. Antioxidants &amp;amp; Redox Signaling, 21(17), 2302–2321.</bibl>
            <idno type="DOI">10.1089/ars.2013.5802</idno>
          </bibl>
          <bibl n="230972">
            <bibl>McLaurin, J., Franklin, T., Fraser, P. E., &amp;amp; Chakrabartty, A. (1998). Structural transitions associated with the interaction of Alzheimer beta-amyloid peptides with gangliosides. Journal of Biological Chemistry, 273(8), 4506–4515.</bibl>
            <idno type="DOI">10.1074/jbc.273.8.4506</idno>
          </bibl>
          <bibl n="231202">
            <bibl>Mendez, M. F. (2017). Early-Onset Alzheimer Disease. Neurologic Clinics, 35(2), 263–281.</bibl>
            <idno type="DOI">10.1016/j.ncl.2017.01.005</idno>
          </bibl>
          <bibl n="230995">
            <bibl>Miao, J., Ma, H., Yang, Y., Liao, Y., Lin, C., Zheng, J., Yu, M., &amp;amp; Lan, J. (2023). Microglia in Alzheimer’s disease: Pathogenesis, mechanisms, and therapeutic potentials. Frontiers in Aging Neuroscience, 15, 1201982.</bibl>
            <idno type="DOI">10.3389/fnagi.2023.1201982</idno>
          </bibl>
          <bibl n="231182">
            <bibl>Miao, W. (2008). Electrogenerated chemiluminescence and its biorelated applications. Chemical Reviews, 108(7), 2506–2553.</bibl>
            <idno type="DOI">10.1021/cr068083a</idno>
          </bibl>
          <bibl n="230874">
            <bibl>Micsonai, A., Wien, F., Buly&amp;#225;ki, &amp;#201;., Kun, J., Moussong, &amp;#201;., Lee, Y.-H., Goto, Y., R&amp;#233;fr&amp;#233;giers, M., &amp;amp; Kardos, J. (2018). BeStSel: A web server for accurate protein secondary structure prediction and fold recognition from the circular dichroism spectra. Nucleic Acids Research, 46(W1), W315–W322.</bibl>
            <idno type="DOI">10.1093/nar/gky497</idno>
          </bibl>
          <bibl n="231115">
            <bibl>Mielke, M. M., &amp;amp; Fowler, N. R. (2024). Alzheimer disease blood biomarkers: Considerations for population-level use. Nature Reviews. Neurology, 20(8), 495–504.</bibl>
            <idno type="DOI">10.1038/s41582-024-00989-1</idno>
          </bibl>
          <bibl n="231203">
            <bibl>Milstein, C. (1980). Monoclonal antibodies. Scientific American, 243(4), 66–74.</bibl>
            <idno type="DOI">10.1038/scientificamerican1080-66</idno>
          </bibl>
          <bibl n="230875">
            <bibl>Mormino, E. C., Kluth, J. T., Madison, C. M., Rabinovici, G. D., Baker, S. L., Miller, B. L., Koeppe, R. A., Mathis, C. A., Weiner, M. W., &amp;amp; Jagust, W. J. (2009). Episodic memory loss is related to hippocampal-mediated beta-amyloid deposition in elderly subjects. Brain, 132(Pt 5), 1310–1323.</bibl>
            <idno type="DOI">10.1093/brain/awn320</idno>
          </bibl>
          <bibl n="231065">
            <bibl>Mosmann, T. (1983). Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays. Journal of Immunological Methods, 65(1–2), 55–63.</bibl>
            <idno type="DOI">10.1016/0022-1759(83)90303-4</idno>
          </bibl>
          <bibl n="231007">
            <bibl>Murakami, K. (2014). Conformation-specific antibodies to target amyloid β oligomers and their application to immunotherapy for Alzheimer’s disease. Bioscience, Biotechnology, and Biochemistry, 78(8), 1293–1305.</bibl>
            <idno type="DOI">10.1080/09168451.2014.940275</idno>
          </bibl>
          <bibl n="231186">
            <bibl>Muyldermans, S. (2013). Nanobodies: Natural single-domain antibodies. Annual Review of Biochemistry, 82, 775–797.</bibl>
            <idno type="DOI">10.1146/annurev-biochem-063011-092449</idno>
          </bibl>
          <bibl n="230799">
            <bibl>Nakashima-Yasuda, H., Uryu, K., Robinson, J., Xie, S. X., Hurtig, H., Duda, J. E., Arnold, S. E., Siderowf, A., Grossman, M., Leverenz, J. B., Woltjer, R., Lopez, O. L., Hamilton, R., Tsuang, D. W., Galasko, D., Masliah, E., Kaye, J., Clark, C. M., Montine, T. J., … Trojanowski, J. Q. (2007). Co-morbidity of TDP-43 proteinopathy in Lewy body related diseases. Acta Neuropathologica, 114(3), 221–229.</bibl>
            <idno type="DOI">10.1007/s00401-007-0261-2</idno>
          </bibl>
          <bibl n="231083">
            <bibl>Nalivaeva, N. N., &amp;amp; Turner, A. J. (2013). The amyloid precursor protein: A biochemical enigma in brain development, function and disease. FEBS Letters, 587(13), 2046–2054.</bibl>
            <idno type="DOI">10.1016/j.febslet.2013.05.010</idno>
          </bibl>
          <bibl n="230859">
            <bibl>Neary, D., Snowden, J. S., Gustafson, L., Passant, U., Stuss, D., Black, S., Freedman, M., Kertesz, A., Robert, P. H., Albert, M., Boone, K., Miller, B. L., Cummings, J., &amp;amp; Benson, D. F. (1998). Frontotemporal lobar degeneration: A consensus on clinical diagnostic criteria. Neurology, 51(6), 1546–1554.</bibl>
            <idno type="DOI">10.1212/wnl.51.6.1546</idno>
          </bibl>
          <bibl n="231197">
            <bibl>Nebes, R. D. (1989). Semantic memory in Alzheimer’s disease. Psychological Bulletin, 106(3), 377–394.</bibl>
            <idno type="DOI">10.1037/0033-2909.106.3.377</idno>
          </bibl>
          <bibl n="230957">
            <bibl>Nicolson, G. L. (2014). The Fluid-Mosaic Model of Membrane Structure: Still relevant to understanding the structure, function and dynamics of biological membranes after more than 40 years. Biochimica Et Biophysica Acta, 1838(6), 1451–1466.</bibl>
            <idno type="DOI">10.1016/j.bbamem.2013.10.019</idno>
          </bibl>
          <bibl n="231058">
            <bibl>Nikolaev, A., McLaughlin, T., O’Leary, D. D. M., &amp;amp; Tessier-Lavigne, M. (2009). APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature, 457(7232), 981–989.</bibl>
            <idno type="DOI">10.1038/nature07767</idno>
          </bibl>
          <bibl n="230932">
            <bibl>Nisbet, R. M., Nigro, J., Breheney, K., Caine, J., Hattarki, M. K., &amp;amp; Nuttall, S. D. (2013). Central amyloid-β-specific single chain variable fragment ameliorates Aβ aggregation and neurotoxicity. Protein Engineering, Design &amp;amp; Selection, 26(10), 571–580.</bibl>
            <idno type="DOI">10.1093/protein/gzt025</idno>
          </bibl>
          <bibl n="231039">
            <bibl>Nonaka, T., Masuda-Suzukake, M., &amp;amp; Hasegawa, M. (2018). Molecular mechanisms of the co-deposition of multiple pathological proteins in neurodegenerative diseases. Neuropathology, 38(1), 64–71.</bibl>
            <idno type="DOI">10.1111/neup.12427</idno>
          </bibl>
          <bibl n="230839">
            <bibl>Nunomura, A., Perry, G., Aliev, G., Hirai, K., Takeda, A., Balraj, E. K., Jones, P. K., Ghanbari, H., Wataya, T., Shimohama, S., Chiba, S., Atwood, C. S., Petersen, R. B., &amp;amp; Smith, M. A. (2001). Oxidative damage is the earliest event in Alzheimer disease. Journal of Neuropathology and Experimental Neurology, 60(8), 759–767.</bibl>
            <idno type="DOI">10.1093/jnen/60.8.759</idno>
          </bibl>
          <bibl n="231116">
            <bibl>Nyhus, C., Pihl, M., Hyttel, P., &amp;amp; Hall, V. (2019). Evidence for nucleolar dysfunction in Alzheimer’s disease. Reviews in the Neurosciences, 30(7), 685–700.</bibl>
            <idno type="DOI">10.1515/revneuro-2018-0104</idno>
          </bibl>
          <bibl n="230913">
            <bibl>Obregon, D., Hou, H., Deng, J., Giunta, B., Tian, J., Darlington, D., Shahaduzzaman, M., Zhu, Y., Mori, T., Mattson, M. P., &amp;amp; Tan, J. (2012). Soluble amyloid precursor protein-α modulates β-secretase activity and amyloid-β generation. Nature Communications, 3, 777.</bibl>
            <idno type="DOI">10.1038/ncomms1781</idno>
          </bibl>
          <bibl n="230778">
            <bibl>O’Connor, A., Karikari, T. K., Poole, T., Ashton, N. J., Lantero Rodriguez, J., Khatun, A., Swift, I., Heslegrave, A. J., Abel, E., Chung, E., Weston, P. S. J., Pavisic, I. M., Ryan, N. S., Barker, S., Rossor, M. N., Polke, J. M., Frost, C., Mead, S., Blennow, K., … Fox, N. C. (2021). Plasma phospho-tau181 in presymptomatic and symptomatic familial Alzheimer’s disease: A longitudinal cohort study. Molecular Psychiatry, 26(10), 5967–5976.</bibl>
            <idno type="DOI">10.1038/s41380-020-0838-x</idno>
          </bibl>
          <bibl n="230900">
            <bibl>Olsson, B., Alberg, L., Cullen, N. C., Michael, E., Wahlgren, L., Kroksmark, A.-K., Rostasy, K., Blennow, K., Zetterberg, H., &amp;amp; Tulinius, M. (2019). NFL is a marker of treatment response in children with SMA treated with nusinersen. Journal of Neurology, 266(9), 2129–2136.</bibl>
            <idno type="DOI">10.1007/s00415-019-09389-8</idno>
          </bibl>
          <bibl n="230829">
            <bibl>Olsson, B., Lautner, R., Andreasson, U., &amp;#214;hrfelt, A., Portelius, E., Bjerke, M., H&amp;#246;ltt&amp;#228;, M., Ros&amp;#233;n, C., Olsson, C., Strobel, G., Wu, E., Dakin, K., Petzold, M., Blennow, K., &amp;amp; Zetterberg, H. (2016). CSF and blood biomarkers for the diagnosis of Alzheimer’s disease: A systematic review and meta-analysis. The Lancet Neurology, 15(7), 673–684.</bibl>
            <idno type="DOI">10.1016/S1474-4422(16)00070-3</idno>
          </bibl>
          <bibl n="230777">
            <bibl>Ossenkoppele, R., Rabinovici, G. D., Smith, R., Cho, H., Sch&amp;#246;ll, M., Strandberg, O., Palmqvist, S., Mattsson, N., Janelidze, S., Santillo, A., Ohlsson, T., J&amp;#246;gi, J., Tsai, R., La Joie, R., Kramer, J., Boxer, A. L., Gorno-Tempini, M. L., Miller, B. L., Choi, J. Y., … Hansson, O. (2018). Discriminative Accuracy of [18F]flortaucipir Positron Emission Tomography for Alzheimer Disease vs Other Neurodegenerative Disorders. JAMA, 320(11), 1151–1162.</bibl>
            <idno type="DOI">10.1001/jama.2018.12917</idno>
          </bibl>
          <bibl n="230775">
            <bibl>Ostrowitzki, S., Bittner, T., Sink, K. M., Mackey, H., Rabe, C., Honig, L. S., Cassetta, E., Woodward, M., Boada, M., van Dyck, C. H., Grimmer, T., Selkoe, D. J., Schneider, A., Blondeau, K., Hu, N., Quartino, A., Clayton, D., Dolton, M., Dang, Y., … Doody, R. S. (2022). Evaluating the Safety and Efficacy of Crenezumab vs Placebo in Adults With Early Alzheimer Disease: Two Phase 3 Randomized Placebo-Controlled Trials. JAMA Neurology, 79(11), 1113–1121.</bibl>
            <idno type="DOI">10.1001/jamaneurol.2022.2909</idno>
          </bibl>
          <bibl n="231043">
            <bibl>S. Ostrowitzki, D. Deptula, L. Thurfjell, F. Barkhof, B. Bohrmann, D. J. Brooks, W. E. Klunk, E. Ashford, K. Yoo, Z. X. Xu, H. Loetscher, &amp;amp; L. Santarelli. Archives of Neurology, 69(2):198-207</bibl>
            <idno type="DOI">10.1001/archneurol.2011.1538</idno>
          </bibl>
          <bibl n="230804">
            <bibl>Ovod, V., Ramsey, K. N., Mawuenyega, K. G., Bollinger, J. G., Hicks, T., Schneider, T., Sullivan, M., Paumier, K., Holtzman, D. M., Morris, J. C., Benzinger, T., Fagan, A. M., Patterson, B. W., &amp;amp; Bateman, R. J. (2017). Amyloid β concentrations and stable isotope labeling kinetics of human plasma specific to central nervous system amyloidosis. Alzheimer’s &amp;amp; Dementia, 13(8), 841–849.</bibl>
            <idno type="DOI">10.1016/j.jalz.2017.06.2266</idno>
          </bibl>
          <bibl n="230965">
            <bibl>Pain, C., Dumont, J., &amp;amp; Dumoulin, M. (2015). Camelid single-domain antibody fragments: Uses and prospects to investigate protein misfolding and aggregation, and to treat diseases associated with these phenomena. Biochimie, 111, 82–106.</bibl>
            <idno type="DOI">10.1016/j.biochi.2015.01.012</idno>
          </bibl>
          <bibl n="230786">
            <bibl>Palmqvist, S., Janelidze, S., Quiroz, Y. T., Zetterberg, H., Lopera, F., Stomrud, E., Su, Y., Chen, Y., Serrano, G. E., Leuzy, A., Mattsson-Carlgren, N., Strandberg, O., Smith, R., Villegas, A., Sepulveda-Falla, D., Chai, X., Proctor, N. K., Beach, T. G., Blennow, K., … Hansson, O. (2020). Discriminative Accuracy of Plasma Phospho-tau217 for Alzheimer Disease vs Other Neurodegenerative Disorders. JAMA, 324(8), 772–781.</bibl>
            <idno type="DOI">10.1001/jama.2020.12134</idno>
          </bibl>
          <bibl n="230776">
            <bibl>Pannee, J., Shaw, L. M., Korecka, M., Waligorska, T., Teunissen, C. E., Stoops, E., Vanderstichele, H. M. J., Mauroo, K., Verberk, I. M. W., Keshavan, A., Pesini, P., Sarasa, L., Pascual-Lucas, M., Fandos, N., Allu&amp;#233;, J.-A., Portelius, E., Andreasson, U., Yoda, R., Nakamura, A., … Zetterberg, H. (2021). The global Alzheimer’s Association round robin study on plasma amyloid β methods. Alzheimer’s &amp;amp; Dementia (Amsterdam, Netherlands), 13(1), e12242.</bibl>
            <idno type="DOI">10.1002/dad2.12242</idno>
          </bibl>
          <bibl n="231090">
            <bibl>Panza, F., Lozupone, M., Seripa, D., &amp;amp; Imbimbo, B. P. (2019). Amyloid-β immunotherapy for alzheimer disease: Is it now a long shot? Annals of Neurology, 85(3), 303–315.</bibl>
            <idno type="DOI">10.1002/ana.25410</idno>
          </bibl>
          <bibl n="230996">
            <bibl>Paravastu, A. K., Leapman, R. D., Yau, W.-M., &amp;amp; Tycko, R. (2008). Molecular structural basis for polymorphism in Alzheimer’s beta-amyloid fibrils. Proceedings of the National Academy of Sciences, 105(47), 18349–18354.</bibl>
            <idno type="DOI">10.1073/pnas.0806270105</idno>
          </bibl>
          <bibl n="231156">
            <bibl>Parker, W. D., Filley, C. M., &amp;amp; Parks, J. K. (1990). Cytochrome oxidase deficiency in Alzheimer’s disease. Neurology, 40(8), 1302–1303.</bibl>
            <idno type="DOI">10.1212/wnl.40.8.1302</idno>
          </bibl>
          <bibl n="230961">
            <bibl>Perchiacca, J. M., Ladiwala, A. R. A., Bhattacharya, M., &amp;amp; Tessier, P. M. (2012). Structure-based design of conformation- and sequence-specific antibodies against amyloid β. Proceedings of the National Academy of Sciences, 109(1), 84–89.</bibl>
            <idno type="DOI">10.1073/pnas.1111232108</idno>
          </bibl>
          <bibl n="231108">
            <bibl>Pereira, C., Santos, M. S., &amp;amp; Oliveira, C. (1998). Mitochondrial function impairment induced by amyloid beta-peptide on PC12 cells. Neuroreport, 9(8), 1749–1755.</bibl>
            <idno type="DOI">10.1097/00001756-199806010-00015</idno>
          </bibl>
          <bibl n="231117">
            <bibl>Perrin, R. J., Fagan, A. M., &amp;amp; Holtzman, D. M. (2009). Multimodal techniques for diagnosis and prognosis of Alzheimer’s disease. Nature, 461(7266), 916–922.</bibl>
            <idno type="DOI">10.1038/nature08538</idno>
          </bibl>
          <bibl n="231141">
            <bibl>Perry, R. J., &amp;amp; Hodges, J. R. (1999). Attention and executive deficits in Alzheimer’s disease. A critical review. Brain, 122 ( Pt 3), 383–404.</bibl>
            <idno type="DOI">10.1093/brain/122.3.383</idno>
          </bibl>
          <bibl n="230978">
            <bibl>Peters, C., Espinoza, M. P., Gallegos, S., Opazo, C., &amp;amp; Aguayo, L. G. (2015). Alzheimer’s Aβ interacts with cellular prion protein inducing neuronal membrane damage and synaptotoxicity. Neurobiology of Aging, 36(3), 1369–1377.</bibl>
            <idno type="DOI">10.1016/j.neurobiolaging.2014.11.019</idno>
          </bibl>
          <bibl n="230821">
            <bibl>Pickford, F., Masliah, E., Britschgi, M., Lucin, K., Narasimhan, R., Jaeger, P. A., Small, S., Spencer, B., Rockenstein, E., Levine, B., &amp;amp; Wyss-Coray, T. (2008). The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid-beta accumulation in mice. Journal of Clinical Investigation, 118(6), 2190–2199.</bibl>
            <idno type="DOI">10.1172/JCI33585</idno>
          </bibl>
          <bibl n="231086">
            <bibl>Pietrzak, M., Rempala, G., Nelson, P. T., Zheng, J.-J., &amp;amp; Hetman, M. (2011). Epigenetic silencing of nucleolar rRNA genes in Alzheimer’s disease. PloS One, 6(7), e22585.</bibl>
            <idno type="DOI">10.1371/journal.pone.0022585</idno>
          </bibl>
          <bibl n="230925">
            <bibl>Pollard, H. B., Rojas, E., &amp;amp; Arispe, N. (1993). A New Hypothesis for the Mechanism of Amyloid Toxicity, Based on the Calcium Channel Activity of Amyloid Protein (A P) in Phospholipid Bilayer Membranes. Annals of the New York Academy of Sciences, 695, 165–168.</bibl>
            <idno type="DOI">10.1111/j.1749-6632.1993.tb23044.x</idno>
          </bibl>
          <bibl n="231066">
            <bibl>Popugaeva, E., Pchitskaya, E., &amp;amp; Bezprozvanny, I. (2018). Dysregulation of Intracellular Calcium Signaling in Alzheimer’s Disease. Antioxidants &amp;amp; Redox Signaling, 29(12), 1176–1188.</bibl>
            <idno type="DOI">10.1089/ars.2018.7506</idno>
          </bibl>
          <bibl n="231145">
            <bibl>Pratic&amp;#242;, D. (2008). Oxidative stress hypothesis in Alzheimer’s disease: A reappraisal. Trends in Pharmacological Sciences, 29(12), 609–615.</bibl>
            <idno type="DOI">10.1016/j.tips.2008.09.001</idno>
          </bibl>
          <bibl n="231198">
            <bibl>Rabinovici, G. D. (2019). Late-onset Alzheimer Disease. Continuum (Minneapolis, Minn.), 25(1), 14–33.</bibl>
            <idno type="DOI">10.1212/CON.0000000000000700</idno>
          </bibl>
          <bibl n="231022">
            <bibl>Rai, S. N., Singh, C., Singh, A., Singh, M. P., &amp;amp; Singh, B. K. (2020). Mitochondrial Dysfunction: A Potential Therapeutic Target to Treat Alzheimer’s Disease. Molecular Neurobiology, 57(7), 3075–3088.</bibl>
            <idno type="DOI">10.1007/s12035-020-01945-y</idno>
          </bibl>
          <bibl n="231132">
            <bibl>Rasmussen, M. K., Mestre, H., &amp;amp; Nedergaard, M. (2018). The glymphatic pathway in neurological disorders. The Lancet Neurology, 17(11), 1016–1024.</bibl>
            <idno type="DOI">10.1016/S1474-4422(18)30318-1</idno>
          </bibl>
          <bibl n="230984">
            <bibl>Reed, B. R., Mungas, D., Farias, S. T., Harvey, D., Beckett, L., Widaman, K., Hinton, L., &amp;amp; DeCarli, C. (2010). Measuring cognitive reserve based on the decomposition of episodic memory variance. Brain, 133(Pt 8), 2196–2209.</bibl>
            <idno type="DOI">10.1093/brain/awq154</idno>
          </bibl>
          <bibl n="231171">
            <bibl>Reese, L. C., &amp;amp; Taglialatela, G. A. (2011). Role for calcineurin in Alzheimer’s disease. Current Neuropharmacology, 9(4), 685–692.</bibl>
            <idno type="DOI">10.2174/156802611798192661</idno>
          </bibl>
          <bibl n="230765">
            <bibl>Reiman, E. M., Quiroz, Y. T., Fleisher, A. S., Chen, K., Velez-Pardo, C., Jimenez-Del-Rio, M., Fagan, A. M., Shah, A. R., Alvarez, S., Arbelaez, A., Giraldo, M., Acosta-Baena, N., Sperling, R. A., Dickerson, B., Stern, C. E., Tirado, V., Munoz, C., Reiman, R. A., Huentelman, M. J., … Lopera, F. (2012). Brain imaging and fluid biomarker analysis in young adults at genetic risk for autosomal dominant Alzheimer’s disease in the presenilin 1 E280A kindred: A case-control study. The Lancet Neurology, 11(12), 1048–1056.</bibl>
            <idno type="DOI">10.1016/S1474-4422(12)70228-4</idno>
          </bibl>
          <bibl n="231078">
            <bibl>Reiss, A. B., Arain, H. A., Stecker, M. M., Siegart, N. M., &amp;amp; Kasselman, L. J. (2018). Amyloid toxicity in Alzheimer’s disease. Reviews in the Neurosciences, 29(6), 613–627.</bibl>
            <idno type="DOI">10.1515/revneuro-2017-0063</idno>
          </bibl>
          <bibl n="231103">
            <bibl>Relkin, N., Marmarou, A., Klinge, P., Bergsneider, M., &amp;amp; Black, P. M. (2005). Diagnosing idiopathic normal-pressure hydrocephalus. Neurosurgery, 57(3 Suppl), S4-16.</bibl>
            <idno type="DOI">10.1227/01.neu.0000168185.29659.c5</idno>
          </bibl>
          <bibl n="231036">
            <bibl>Renner, J. A., Burns, J. M., Hou, C. E., McKeel, D. W., Storandt, M., &amp;amp; Morris, J. C. (2004). Progressive posterior cortical dysfunction: A clinicopathologic series. Neurology, 63(7), 1175–1180.</bibl>
            <idno type="DOI">10.1212/01.wnl.0000140290.80962.bf</idno>
          </bibl>
          <bibl n="231179">
            <bibl>Revi, M. (2020). Alzheimer’s Disease Therapeutic Approaches. Advances in Experimental Medicine and Biology, 1195, 105–116.</bibl>
            <idno type="DOI">10.1007/978-3-030-32633-3_15</idno>
          </bibl>
          <bibl n="230814">
            <bibl>Rissin, D. M., Kan, C. W., Campbell, T. G., Howes, S. C., Fournier, D. R., Song, L., Piech, T., Patel, P. P., Chang, L., Rivnak, A. J., Ferrell, E. P., Randall, J. D., Provuncher, G. K., Walt, D. R., &amp;amp; Duffy, D. C. (2010). Single-molecule enzyme-linked immunosorbent assay detects serum proteins at subfemtomolar concentrations. Nature Biotechnology, 28(6), 595–599.</bibl>
            <idno type="DOI">10.1038/nbt.1641</idno>
          </bibl>
          <bibl n="231153">
            <bibl>Robertson, D. S. (2010). The physical chemistry of brain and neural cell membranes: An overview. Neurochemical Research, 35(5), 681–687.</bibl>
            <idno type="DOI">10.1007/s11064-010-0121-7</idno>
          </bibl>
          <bibl n="231085">
            <bibl>Roychaudhuri, R., Yang, M., Hoshi, M. M., &amp;amp; Teplow, D. B. (2009). Amyloid beta-protein assembly and Alzheimer disease. Journal of Biological Chemistry, 284(8), 4749–4753.</bibl>
            <idno type="DOI">10.1074/jbc.R800036200</idno>
          </bibl>
          <bibl n="231151">
            <bibl>Rudajev, V., &amp;amp; Novotny, J. (2020). The Role of Lipid Environment in Ganglioside GM1-Induced Amyloid β Aggregation. Membranes, 10(9), 226.</bibl>
            <idno type="DOI">10.3390/membranes10090226</idno>
          </bibl>
          <bibl n="230773">
            <bibl>Sachdev, P., Kalaria, R., O’Brien, J., Skoog, I., Alladi, S., Black, S. E., Blacker, D., Blazer, D. G., Chen, C., Chui, H., Ganguli, M., Jellinger, K., Jeste, D. V., Pasquier, F., Paulsen, J., Prins, N., Rockwood, K., Roman, G., Scheltens, P., &amp;amp; Internationlal Society for Vascular Behavioral and Cognitive Disorders. (2014). Diagnostic criteria for vascular cognitive disorders: A VASCOG statement. Alzheimer Disease and Associated Disorders, 28(3), 206–218.</bibl>
            <idno type="DOI">10.1097/WAD.0000000000000034</idno>
          </bibl>
          <bibl n="231139">
            <bibl>Saido, T., &amp;amp; Leissring, M. A. (2012). Proteolytic degradation of amyloid β-protein. Cold Spring Harbor Perspectives in Medicine, 2(6), a006379.</bibl>
            <idno type="DOI">10.1101/cshperspect.a006379</idno>
          </bibl>
          <bibl n="230979">
            <bibl>Saito, R., Kaneko, M., Kitamura, Y., Takata, K., Kawada, K., Okuma, Y., &amp;amp; Nomura, Y. (2014). Effects of oxidative stress on the solubility of HRD1, a ubiquitin ligase implicated in Alzheimer’s disease. PloS One, 9(5), e94576.</bibl>
            <idno type="DOI">10.1371/journal.pone.0094576</idno>
          </bibl>
          <bibl n="231010">
            <bibl>Saito, R., Kaneko, M., Okuma, Y., &amp;amp; Nomura, Y. (2010). Correlation between decrease in protein levels of ubiquitin ligase HRD1 and amyloid-beta production. Journal of Pharmacological Sciences, 113(3), 285–288.</bibl>
            <idno type="DOI">10.1254/jphs.10118sc</idno>
          </bibl>
          <bibl n="231081">
            <bibl>Sajdel-Sulkowska, E. M., &amp;amp; Marotta, C. A. (1984). Alzheimer’s disease brain: Alterations in RNA levels and in a ribonuclease-inhibitor complex. Science, 225(4665), 947–949.</bibl>
            <idno type="DOI">10.1126/science.6206567</idno>
          </bibl>
          <bibl n="231173">
            <bibl>Sakono, M., &amp;amp; Zako, T. (2010). Amyloid oligomers: Formation and toxicity of Abeta oligomers. The FEBS Journal, 277(6), 1348–1358.</bibl>
            <idno type="DOI">10.1111/j.1742-4658.2010.07568.x</idno>
          </bibl>
          <bibl n="231014">Samad, N., Ishaq, S., Bano, S., &amp;amp; Manzoor, N. (2017). Calcium Regulation in Alzheimer’s Disease: Mechanistic Understanding. Journal of the College of Physicians and Surgeons--Pakistan: JCPSP, 27(9), 566–571.</bibl>
          <bibl n="230973">
            <bibl>Santoro, M. M. &amp;amp; Bolen, D. W. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl .alpha.-chymotrypsin using different denaturants. Biochemistry 27, 8063–8068 (1988).</bibl>
            <idno type="DOI">10.1021/bi00421a014</idno>
          </bibl>
          <bibl n="230838">
            <bibl>Santos, A. N., Torkler, S., Nowak, D., Schlittig, C., Goerdes, M., Lauber, T., Trischmann, L., Schaupp, M., Penz, M., Tiller, F.-W., &amp;amp; B&amp;#246;hm, G. (2007). Detection of amyloid-beta oligomers in human cerebrospinal fluid by flow cytometry and fluorescence resonance energy transfer. Journal of Alzheimer’s Disease, 11(1), 117–125.</bibl>
            <idno type="DOI">10.3233/jad-2007-11114</idno>
          </bibl>
          <bibl n="230926">
            <bibl>Santos, R. X., Correia, S. C., Wang, X., Perry, G., Smith, M. A., Moreira, P. I., &amp;amp; Zhu, X. (2010). A synergistic dysfunction of mitochondrial fission/fusion dynamics and mitophagy in Alzheimer’s disease. Journal of Alzheimer’s Disease, 20 Suppl 2, S401-412.</bibl>
            <idno type="DOI">10.3233/JAD-2010-100666</idno>
          </bibl>
          <bibl n="230827">
            <bibl>Savage, M. J., Kalinina, J., Wolfe, A., Tugusheva, K., Korn, R., Cash-Mason, T., Maxwell, J. W., Hatcher, N. G., Haugabook, S. J., Wu, G., Howell, B. J., Renger, J. J., Shughrue, P. J., &amp;amp; McCampbell, A. (2014). A sensitive aβ oligomer assay discriminates Alzheimer’s and aged control cerebrospinal fluid. Journal of Neuroscience, 34(8), 2884–2897.</bibl>
            <idno type="DOI">10.1523/JNEUROSCI.1675-13.2014</idno>
          </bibl>
          <bibl n="230901">
            <bibl>Scalia, F., Vitale, A. M., Santonocito, R., Conway de Macario, E., Macario, A. J. L., &amp;amp; Cappello, F. (2021). The Neurochaperonopathies: Anomalies of the Chaperone System with Pathogenic Effects in Neurodegenerative and Neuromuscular Disorders. Applied Sciences, 11(3), 898.</bibl>
            <idno type="DOI">10.3390/app11030898</idno>
          </bibl>
          <bibl n="231192">
            <bibl>Schengrund, C. L. (2010). Lipid rafts: Keys to neurodegeneration. Brain Research Bulletin, 82(1–2), 7–17.</bibl>
            <idno type="DOI">10.1016/j.brainresbull.2010.02.013</idno>
          </bibl>
          <bibl n="230769">
            <bibl>Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., Larson, E., Levy-Lahad, E., Viitanen, M., Peskind, E., Poorkaj, P., Schellenberg, G., Tanzi, R., Wasco, W., Lannfelt, L., … Younkin, S. (1996). Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer’s disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer’s disease. Nature Medicine, 2(8), 864–870.</bibl>
            <idno type="DOI">10.1038/nm0896-864</idno>
          </bibl>
          <bibl n="231040">
            <bibl>Schneider, J. A., Arvanitakis, Z., Bang, W., &amp;amp; Bennett, D. A. (2007). Mixed brain pathologies account for most dementia cases in community-dwelling older persons. Neurology, 69(24), 2197–2204.</bibl>
            <idno type="DOI">10.1212/01.wnl.0000271090.28148.24</idno>
          </bibl>
          <bibl n="230922">
            <bibl>Schwab, C., Arai, T., Hasegawa, M., Yu, S., &amp;amp; McGeer, P. L. (2008). Colocalization of transactivation-responsive DNA-binding protein 43 and huntingtin in inclusions of Huntington disease. Journal of Neuropathology and Experimental Neurology, 67(12), 1159–1165.</bibl>
            <idno type="DOI">10.1097/NEN.0b013e31818e8951</idno>
          </bibl>
          <bibl n="231168">
            <bibl>Sciacca, M. F. M., La Rosa, C., &amp;amp; Milardi, D. (2021). Amyloid-Mediated Mechanisms of Membrane Disruption. Biophysica, 1(2), 137-156.</bibl>
            <idno type="DOI">10.3390/biophysica1020011</idno>
          </bibl>
          <bibl n="231174">
            <bibl>Selkoe, D. J. (1999). Translating cell biology into therapeutic advances in Alzheimer’s disease. Nature, 399(6738 Suppl), A23-31.</bibl>
            <idno type="DOI">10.1038/399a023</idno>
          </bibl>
          <bibl n="231180">
            <bibl>Selkoe, D. J. (2019). Alzheimer disease and aducanumab: Adjusting our approach. Nature Reviews. Neurology, 15(7), 365–366.</bibl>
            <idno type="DOI">10.1038/s41582-019-0205-1</idno>
          </bibl>
          <bibl n="230768">
            <bibl>Selles, M. C., Fortuna, J. T. S., Cercato, M. C., Santos, L. E., Domett, L., Bitencourt, A. L. B., Carraro, M. F., Souza, A. S., Janickova, H., Azevedo, C. V., Campos, H. C., de Souza, J. M., Alves-Leon, S., Prado, V. F., Prado, M. A. M., Epstein, A. L., Salvetti, A., Longo, B. M., Arancio, O., … Ferreira, S. T. (2023). AAV-mediated neuronal expression of an scFv antibody selective for Aβ oligomers protects synapses and rescues memory in Alzheimer models. Molecular Therapy, 31(2), 409–419.</bibl>
            <idno type="DOI">10.1016/j.ymthe.2022.11.002</idno>
          </bibl>
          <bibl n="230843">
            <bibl>Sengupta, U., Guerrero-Mu&amp;#241;oz, M. J., Castillo-Carranza, D. L., Lasagna-Reeves, C. A., Gerson, J. E., Paulucci-Holthauzen, A. A., Krishnamurthy, S., Farhed, M., Jackson, G. R., &amp;amp; Kayed, R. (2015). Pathological interface between oligomeric alpha-synuclein and tau in synucleinopathies. Biological Psychiatry, 78(10), 672–683.</bibl>
            <idno type="DOI">10.1016/j.biopsych.2014.12.019</idno>
          </bibl>
          <bibl n="230986">
            <bibl>Senjem, M. L., Gunter, J. L., Shiung, M. M., Petersen, R. C., &amp;amp; Jack, C. R. (2005). Comparison of different methodological implementations of voxel-based morphometry in neurodegenerative disease. NeuroImage, 26(2), 600–608.</bibl>
            <idno type="DOI">10.1016/j.neuroimage.2005.02.005</idno>
          </bibl>
          <bibl n="230813">
            <bibl>Sevigny, J., Chiao, P., Bussi&amp;#232;re, T., Weinreb, P. H., Williams, L., Maier, M., Dunstan, R., Salloway, S., Chen, T., Ling, Y., O’Gorman, J., Qian, F., Arastu, M., Li, M., Chollate, S., Brennan, M. S., Quintero-Monzon, O., Scannevin, R. H., Arnold, H. M., … Sandrock, A. (2016). The antibody aducanumab reduces Aβ plaques in Alzheimer’s disease. Nature, 537(7618), 50–56.</bibl>
            <idno type="DOI">10.1038/nature19323</idno>
          </bibl>
          <bibl n="230797">
            <bibl>Shaw, L. M., Vanderstichele, H., Knapik-Czajka, M., Clark, C. M., Aisen, P. S., Petersen, R. C., Blennow, K., Soares, H., Simon, A., Lewczuk, P., Dean, R., Siemers, E., Potter, W., Lee, V. M.-Y., Trojanowski, J. Q., &amp;amp; Alzheimer’s Disease Neuroimaging Initiative. (2009). Cerebrospinal fluid biomarker signature in Alzheimer’s disease neuroimaging initiative subjects. Annals of Neurology, 65(4), 403–413.</bibl>
            <idno type="DOI">10.1002/ana.21610</idno>
          </bibl>
          <bibl n="230963">
            <bibl>Sheu, K. F., Cooper, A. J., Koike, K., Koike, M., Lindsay, J. G., &amp;amp; Blass, J. P. (1994). Abnormality of the alpha-ketoglutarate dehydrogenase complex in fibroblasts from familial Alzheimer’s disease. Annals of Neurology, 35(3), 312–318.</bibl>
            <idno type="DOI">10.1002/ana.410350311</idno>
          </bibl>
          <bibl n="231041">
            <bibl>Sheu, K. F., Kim, Y. T., Blass, J. P., &amp;amp; Weksler, M. E. (1985). An immunochemical study of the pyruvate dehydrogenase deficit in Alzheimer’s disease brain. Annals of Neurology, 17(5), 444–449.</bibl>
            <idno type="DOI">10.1002/ana.410170505</idno>
          </bibl>
          <bibl n="230853">
            <bibl>Shughrue, P. J., Acton, P. J., Breese, R. S., Zhao, W.-Q., Chen-Dodson, E., Hepler, R. W., Wolfe, A. L., Matthews, M., Heidecker, G. J., Joyce, J. G., Villarreal, S. A., &amp;amp; Kinney, G. G. (2010). Anti-ADDL antibodies differentially block oligomer binding to hippocampal neurons. Neurobiology of Aging, 31(2), 189–202.</bibl>
            <idno type="DOI">10.1016/j.neurobiolaging.2008.04.003</idno>
          </bibl>
          <bibl n="231128">
            <bibl>Simr&amp;#233;n, J., Elmgren, A., Blennow, K., &amp;amp; Zetterberg, H. (2023). Fluid biomarkers in Alzheimer’s disease. Advances in Clinical Chemistry, 112, 249–281.</bibl>
            <idno type="DOI">10.1016/bs.acc.2022.09.006</idno>
          </bibl>
          <bibl n="230781">
            <bibl>Sims, J. R., Zimmer, J. A., Evans, C. D., Lu, M., Ardayfio, P., Sparks, J., Wessels, A. M., Shcherbinin, S., Wang, H., Monkul Nery, E. S., Collins, E. C., Solomon, P., Salloway, S., Apostolova, L. G., Hansson, O., Ritchie, C., Brooks, D. A., Mintun, M., Skovronsky, D. M., &amp;amp; TRAILBLAZER-ALZ 2 Investigators. (2023). Donanemab in Early Symptomatic Alzheimer Disease: The TRAILBLAZER-ALZ 2 Randomized Clinical Trial. JAMA, 330(6), 512–527.</bibl>
            <idno type="DOI">10.1001/jama.2023.13239</idno>
          </bibl>
          <bibl n="231146">
            <bibl>Sims, R., Hill, M., &amp;amp; Williams, J. (2020). The multiplex model of the genetics of Alzheimer’s disease. Nature Neuroscience, 23(3), 311–322.</bibl>
            <idno type="DOI">10.1038/s41593-020-0599-5</idno>
          </bibl>
          <bibl n="231175">
            <bibl>Singer, S. J., &amp;amp; Nicolson, G. L. (1972). The fluid mosaic model of the structure of cell membranes. Science, 175(4023), 720–731.</bibl>
            <idno type="DOI">10.1126/science.175.4023.720</idno>
          </bibl>
          <bibl n="231137">
            <bibl>Singh, A., Kukreti, R., Saso, L., &amp;amp; Kukreti, S. (2019). Oxidative Stress: A Key Modulator in Neurodegenerative Diseases. Molecules, 24(8), 1583.</bibl>
            <idno type="DOI">10.3390/molecules24081583</idno>
          </bibl>
          <bibl n="231126">
            <bibl>Somavarapu, A. K., &amp;amp; Kepp, K. P. (2015). The Dependence of Amyloid-β Dynamics on Protein Force Fields and Water Models. Chemphyschem, 16(15), 3278–3289.</bibl>
            <idno type="DOI">10.1002/cphc.201500415</idno>
          </bibl>
          <bibl n="230887">
            <bibl>Song, S., Kim, S.-Y., Hong, Y.-M., Jo, D.-G., Lee, J.-Y., Shim, S. M., Chung, C.-W., Seo, S. J., Yoo, Y. J., Koh, J.-Y., Lee, M. C., Yates, A. J., Ichijo, H., &amp;amp; Jung, Y.-K. (2003). Essential role of E2-25K/Hip-2 in mediating amyloid-beta neurotoxicity. Molecular Cell, 12(3), 553–563.</bibl>
            <idno type="DOI">10.1016/j.molcel.2003.08.005</idno>
          </bibl>
          <bibl n="231100">
            <bibl>Sorbi, S., Bird, E. D., &amp;amp; Blass, J. P. (1983). Decreased pyruvate dehydrogenase complex activity in Huntington and Alzheimer brain. Annals of Neurology, 13(1), 72–78.</bibl>
            <idno type="DOI">10.1002/ana.410130116</idno>
          </bibl>
          <bibl n="230967">
            <bibl>Sorbi, S., Nacmias, B., Forleo, P., Latorraca, S., Gobbini, I., Bracco, L., Piacentini, S., &amp;amp; Amaducci, L. (1994). ApoE allele frequencies in Italian sporadic and familial Alzheimer’s disease. Neuroscience Letters, 177(1–2), 100–102.</bibl>
            <idno type="DOI">10.1016/0304-3940(94)90054-x</idno>
          </bibl>
          <bibl n="230987">
            <bibl>Sormanni, P., Aprile, F. A., &amp;amp; Vendruscolo, M. (2015). Rational design of antibodies targeting specific epitopes within intrinsically disordered proteins. Proceedings of the National Academy of Sciences, 112(32), 9902–9907.</bibl>
            <idno type="DOI">10.1073/pnas.1422401112</idno>
          </bibl>
          <bibl n="231084">
            <bibl>Sormanni, P., Aprile, F. A., &amp;amp; Vendruscolo, M. (2018). Third generation antibody discovery methods: In silico rational design. Chemical Society Reviews, 47(24), 9137–9157.</bibl>
            <idno type="DOI">10.1039/c8cs00523k</idno>
          </bibl>
          <bibl n="230764">
            <bibl>Sperling, R. A., Aisen, P. S., Beckett, L. A., Bennett, D. A., Craft, S., Fagan, A. M., Iwatsubo, T., Jack, C. R., Kaye, J., Montine, T. J., Park, D. C., Reiman, E. M., Rowe, C. C., Siemers, E., Stern, Y., Yaffe, K., Carrillo, M. C., Thies, B., Morrison-Bogorad, M., … Phelps, C. H. (2011). Toward defining the preclinical stages of Alzheimer’s disease: Recommendations from the National Institute on Aging-Alzheimer’s Association workgroups on diagnostic guidelines for Alzheimer’s disease. Alzheimer’s &amp;amp; Dementia, 7(3), 280–292.</bibl>
            <idno type="DOI">10.1016/j.jalz.2011.03.003</idno>
          </bibl>
          <bibl n="231152">
            <bibl>Stewart, M. D., Ritterhoff, T., Klevit, R. E., &amp;amp; Brzovic, P. S. (2016). E2 enzymes: More than just middle men. Cell Research, 26(4), 423.</bibl>
            <idno type="DOI">10.1038/cr.2016.35</idno>
          </bibl>
          <bibl n="231194">
            <bibl>Strimbu, K., &amp;amp; Tavel, J. A. (2010). What are biomarkers? Current Opinion in HIV and AIDS, 5(6), 463–466.</bibl>
            <idno type="DOI">10.1097/COH.0b013e32833ed177</idno>
          </bibl>
          <bibl n="231124">
            <bibl>Sunde, M., &amp;amp; Blake, C. (1997). The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Advances in Protein Chemistry, 50, 123–159.</bibl>
            <idno type="DOI">10.1016/s0065-3233(08)60320-4</idno>
          </bibl>
          <bibl n="230796">
            <bibl>Sutphen, C. L., Jasielec, M. S., Shah, A. R., Macy, E. M., Xiong, C., Vlassenko, A. G., Benzinger, T. L. S., Stoops, E. E. J., Vanderstichele, H. M. J., Brix, B., Darby, H. D., Vandijck, M. L. J., Ladenson, J. H., Morris, J. C., Holtzman, D. M., &amp;amp; Fagan, A. M. (2015). Longitudinal Cerebrospinal Fluid Biomarker Changes in Preclinical Alzheimer Disease During Middle Age. JAMA Neurology, 72(9), 1029–1042.</bibl>
            <idno type="DOI">10.1001/jamaneurol.2015.1285</idno>
          </bibl>
          <bibl n="230793">
            <bibl>Swanson, C. J., Zhang, Y., Dhadda, S., Wang, J., Kaplow, J., Lai, R. Y. K., Lannfelt, L., Bradley, H., Rabe, M., Koyama, A., Reyderman, L., Berry, D. A., Berry, S., Gordon, R., Kramer, L. D., &amp;amp; Cummings, J. L. (2021). A randomized, double-blind, phase 2b proof-of-concept clinical trial in early Alzheimer’s disease with lecanemab, an anti-Aβ protofibril antibody. Alzheimer’s Research &amp;amp; Therapy, 13(1), 80.</bibl>
            <idno type="DOI">10.1186/s13195-021-00813-8</idno>
          </bibl>
          <bibl n="231169">
            <bibl>Sewell, R. D. E. (Ed.). (2007). Protein Misfolding in Neurodegenerative Diseases: Mechanisms and Therapeutic Strategies. CRC Press.</bibl>
            <idno type="DOI">10.1201/9781420007145</idno>
          </bibl>
          <bibl n="231142">
            <bibl>Swerdlow, R. H. (2018). Mitochondria and Mitochondrial Cascades in Alzheimer’s Disease. Journal of Alzheimer’s Disease: JAD, 62(3), 1403–1416.</bibl>
            <idno type="DOI">10.3233/JAD-170585</idno>
          </bibl>
          <bibl n="231067">
            <bibl>Taipale, M., Jarosz, D. F., &amp;amp; Lindquist, S. (2010). HSP90 at the hub of protein homeostasis: Emerging mechanistic insights. Nature Reviews. Molecular Cell Biology, 11(7), 515–528.</bibl>
            <idno type="DOI">10.1038/nrm2918</idno>
          </bibl>
          <bibl n="231120">
            <bibl>Tcw, J., &amp;amp; Goate, A. M. (2017). Genetics of β-Amyloid Precursor Protein in Alzheimer’s Disease. Cold Spring Harbor Perspectives in Medicine, 7(6), a024539.</bibl>
            <idno type="DOI">10.1101/cshperspect.a024539</idno>
          </bibl>
          <bibl n="230792">
            <bibl>Thompson, A. J., Banwell, B. L., Barkhof, F., Carroll, W. M., Coetzee, T., Comi, G., Correale, J., Fazekas, F., Filippi, M., Freedman, M. S., Fujihara, K., Galetta, S. L., Hartung, H. P., Kappos, L., Lublin, F. D., Marrie, R. A., Miller, A. E., Miller, D. H., Montalban, X., … Cohen, J. A. (2018). Diagnosis of multiple sclerosis: 2017 revisions of the McDonald criteria. The Lancet Neurology, 17(2), 162–173.</bibl>
            <idno type="DOI">10.1016/S1474-4422(17)30470-2</idno>
          </bibl>
          <bibl n="231079">
            <bibl>Tokunaga, Y., &amp;amp; Takeuchi, K. (2020). Role of NMR in High Ordered Structure Characterization of Monoclonal Antibodies. International Journal of Molecular Sciences, 22(1), 46.</bibl>
            <idno type="DOI">10.3390/ijms22010046</idno>
          </bibl>
          <bibl n="230854">
            <bibl>Toledo, J. B., Arnold, S. E., Raible, K., Brettschneider, J., Xie, S. X., Grossman, M., Monsell, S. E., Kukull, W. A., &amp;amp; Trojanowski, J. Q. (2013). Contribution of cerebrovascular disease in autopsy confirmed neurodegenerative disease cases in the National Alzheimer’s Coordinating Centre. Brain, 136, 2697–2706.</bibl>
            <idno type="DOI">10.1093/brain/awt188</idno>
          </bibl>
          <bibl n="231121">
            <bibl>Tu, S., Okamoto, S., Lipton, S. A., &amp;amp; Xu, H. (2014). Oligomeric Aβ-induced synaptic dysfunction in Alzheimer’s disease. Molecular Neurodegeneration, 9, 48.</bibl>
            <idno type="DOI">10.1186/1750-1326-9-48</idno>
          </bibl>
          <bibl n="231157">
            <bibl>Twohig, D., &amp;amp; Nielsen, H. M. (2019). α-synuclein in the pathophysiology of Alzheimer’s disease. Molecular Neurodegeneration, 14(1), 23.</bibl>
            <idno type="DOI">10.1186/s13024-019-0320-x</idno>
          </bibl>
          <bibl n="230921">
            <bibl>Vadukul, D. M., Papp, M., Thrush, R. J., Wang, J., Jin, Y., Arosio, P., &amp;amp; Aprile, F. A. (2023). α-Synuclein Aggregation Is Triggered by Oligomeric Amyloid-β 42 via Heterogeneous Primary Nucleation. Journal of the American Chemical Society, 145(33), 18276–18285.</bibl>
            <idno type="DOI">10.1021/jacs.3c03212</idno>
          </bibl>
          <bibl n="230868">
            <bibl>Valdor, R., Mocholi, E., Botbol, Y., Guerrero-Ros, I., Chandra, D., Koga, H., Gravekamp, C., Cuervo, A. M., &amp;amp; Macian, F. (2014). Chaperone-mediated autophagy regulates T cell responses through targeted degradation of negative regulators of T cell activation. Nature Immunology, 15(11), 1046–1054.</bibl>
            <idno type="DOI">10.1038/ni.3003</idno>
          </bibl>
          <bibl n="230828">
            <bibl>van Dyck, C. H., Swanson, C. J., Aisen, P., Bateman, R. J., Chen, C., Gee, M., Kanekiyo, M., Li, D., Reyderman, L., Cohen, S., Froelich, L., Katayama, S., Sabbagh, M., Vellas, B., Watson, D., Dhadda, S., Irizarry, M., Kramer, L. D., &amp;amp; Iwatsubo, T. (2023). Lecanemab in Early Alzheimer’s Disease. The New England Journal of Medicine, 388(1), 9–21.</bibl>
            <idno type="DOI">10.1056/NEJMoa2212948</idno>
          </bibl>
          <bibl n="230846">
            <bibl>Veerabhadrappa, B., Delaby, C., Hirtz, C., Vialaret, J., Alcolea, D., Lle&amp;#243;, A., Fortea, J., Santosh, M. S., Choubey, S., &amp;amp; Lehmann, S. (2020). Detection of amyloid beta peptides in body fluids for the diagnosis of alzheimer’s disease: Where do we stand? Critical Reviews in Clinical Laboratory Sciences, 57(2), 99–113.</bibl>
            <idno type="DOI">10.1080/10408363.2019.1678011</idno>
          </bibl>
          <bibl n="230825">
            <bibl>Vemuri, P., Weigand, S. D., Przybelski, S. A., Knopman, D. S., Smith, G. E., Trojanowski, J. Q., Shaw, L. M., Decarli, C. S., Carmichael, O., Bernstein, M. A., Aisen, P. S., Weiner, M., Petersen, R. C., &amp;amp; Jack, C. R. (2011). Cognitive reserve and Alzheimer’s disease biomarkers are independent determinants of cognition. Brain, 134(Pt 5), 1479–1492.</bibl>
            <idno type="DOI">10.1093/brain/awr049</idno>
          </bibl>
          <bibl n="230917">
            <bibl>Vemuri, P., Wiste, H. J., Weigand, S. D., Shaw, L. M., Trojanowski, J. Q., Weiner, M. W., Knopman, D. S., Petersen, R. C., &amp;amp; Jack, C. R. (2009). MRI and CSF biomarkers in normal, MCI, and AD subjects: Predicting future clinical change. Neurology, 73(4), 294–301.</bibl>
            <idno type="DOI">10.1212/WNL.0b013e3181af79fb</idno>
          </bibl>
          <bibl n="230770">
            <bibl>Vermunt, L., Sikkes, S. A. M., van den Hout, A., Handels, R., Bos, I., van der Flier, W. M., Kern, S., Ousset, P.-J., Maruff, P., Skoog, I., Verhey, F. R. J., Freund-Levi, Y., Tsolaki, M., Wallin, &amp;#197;. K., Olde Rikkert, M., Soininen, H., Spiru, L., Zetterberg, H., Blennow, K., … ICTUS/DSA study groups. (2019). Duration of preclinical, prodromal, and dementia stages of Alzheimer’s disease in relation to age, sex, and APOE genotype. Alzheimer’s &amp;amp; Dementia, 15(7), 888–898.</bibl>
            <idno type="DOI">10.1016/j.jalz.2019.04.001</idno>
          </bibl>
          <bibl n="230790">
            <bibl>Villemagne, V. L., Burnham, S., Bourgeat, P., Brown, B., Ellis, K. A., Salvado, O., Szoeke, C., Macaulay, S. L., Martins, R., Maruff, P., Ames, D., Rowe, C. C., Masters, C. L., &amp;amp; Australian Imaging Biomarkers and Lifestyle (AIBL) Research Group. (2013). Amyloid β deposition, neurodegeneration, and cognitive decline in sporadic Alzheimer’s disease: A prospective cohort study. The Lancet Neurology, 12(4), 357–367.</bibl>
            <idno type="DOI">10.1016/S1474-4422(13)70044-9</idno>
          </bibl>
          <bibl n="230820">
            <bibl>Villemagne, V. L., Pike, K. E., Ch&amp;#233;telat, G., Ellis, K. A., Mulligan, R. S., Bourgeat, P., Ackermann, U., Jones, G., Szoeke, C., Salvado, O., Martins, R., O’Keefe, G., Mathis, C. A., Klunk, W. E., Ames, D., Masters, C. L., &amp;amp; Rowe, C. C. (2011). Longitudinal assessment of Aβ and cognition in aging and Alzheimer disease. Annals of Neurology, 69(1), 181–192.</bibl>
            <idno type="DOI">10.1002/ana.22248</idno>
          </bibl>
          <bibl n="230992">
            <bibl>Vivekanandan, S., Brender, J. R., Lee, S. Y., &amp;amp; Ramamoorthy, A. (2011). A partially folded structure of amyloid-beta(1-40) in an aqueous environment. Biochemical and Biophysical Research Communications, 411(2), 312–316.</bibl>
            <idno type="DOI">10.1016/j.bbrc.2011.06.133</idno>
          </bibl>
          <bibl n="230918">
            <bibl>Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., &amp;amp; Selkoe, D. J. (2002). Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature, 416(6880), 535–539.</bibl>
            <idno type="DOI">10.1038/416535a</idno>
          </bibl>
          <bibl n="231158">
            <bibl>Walsh, D. M., &amp;amp; Selkoe, D. J. (2004). Deciphering the molecular basis of memory failure in Alzheimer’s disease. Neuron, 44(1), 181–193.</bibl>
            <idno type="DOI">10.1016/j.neuron.2004.09.010</idno>
          </bibl>
          <bibl n="230993">
            <bibl>Walsh, D. M., Tseng, B. P., Rydel, R. E., Podlisny, M. B., &amp;amp; Selkoe, D. J. (2000). The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain. Biochemistry, 39(35), 10831–10839.</bibl>
            <idno type="DOI">10.1021/bi001048s</idno>
          </bibl>
          <bibl n="230851">
            <bibl>Wang, H.-W., Pasternak, J. F., Kuo, H., Ristic, H., Lambert, M. P., Chromy, B., Viola, K. L., Klein, W. L., Stine, W. B., Krafft, G. A., &amp;amp; Trommer, B. L. (2002). Soluble oligomers of beta amyloid (1-42) inhibit long-term potentiation but not long-term depression in rat dentate gyrus. Brain Research, 924(2), 133–140.</bibl>
            <idno type="DOI">10.1016/s0006-8993(01)03058-x</idno>
          </bibl>
          <bibl n="231051">
            <bibl>Wang, X., Wang, W., Li, L., Perry, G., Lee, H., &amp;amp; Zhu, X. (2014). Oxidative stress and mitochondrial dysfunction in Alzheimer’s disease. Biochimica Et Biophysica Acta, 1842(8), 1240–1247.</bibl>
            <idno type="DOI">10.1016/j.bbadis.2013.10.015</idno>
          </bibl>
          <bibl n="230832">
            <bibl>Wasik, U., Schneider, G., Mietelska-Porowska, A., Mazurkiewicz, M., Fabczak, H., Weis, S., Zabke, C., Harrington, C. R., Filipek, A., &amp;amp; Niewiadomska, G. (2013). Calcyclin binding protein and Siah-1 interacting protein in Alzheimer’s disease pathology: Neuronal localization and possible function. Neurobiology of Aging, 34(5), 1380–1388.</bibl>
            <idno type="DOI">10.1016/j.neurobiolaging.2012.11.007</idno>
          </bibl>
          <bibl n="230988">
            <bibl>Wasmer, C., Lange, A., Van Melckebeke, H., Siemer, A. B., Riek, R., &amp;amp; Meier, B. H. (2008). Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core. Science, 319(5869), 1523–1526.</bibl>
            <idno type="DOI">10.1126/science.1151839</idno>
          </bibl>
          <bibl n="231091">
            <bibl>Weintraub, S., Wicklund, A. H., &amp;amp; Salmon, D. P. (2012). The neuropsychological profile of Alzheimer disease. Cold Spring Harbor Perspectives in Medicine, 2(4), a006171.</bibl>
            <idno type="DOI">10.1101/cshperspect.a006171</idno>
          </bibl>
          <bibl n="231181">
            <bibl>Westermark, P. (2005). Aspects on human amyloid forms and their fibril polypeptides. The FEBS Journal, 272(23), 5942–5949.</bibl>
            <idno type="DOI">10.1111/j.1742-4658.2005.05024.x</idno>
          </bibl>
          <bibl n="230994">
            <bibl>Westin, K., Buchhave, P., Nielsen, H., Minthon, L., Janciauskiene, S., &amp;amp; Hansson, O. (2012). CCL2 is associated with a faster rate of cognitive decline during early stages of Alzheimer’s disease. PloS One, 7(1), e30525.</bibl>
            <idno type="DOI">10.1371/journal.pone.0030525</idno>
          </bibl>
          <bibl n="230880">Whitehouse, P. J., Orgogozo, J. M., Becker, R. E., Gauthier, S., Pontecorvo, M., Erzigkeit, H., Rogers, S., Mohs, R. C., Bodick, N., Bruno, G., &amp;amp; Dal-Bianco, P. (1997). Quality-of-life assessment in dementia drug development. Alzheimer Disease and Associated Disorders, 11 Suppl 3, 56–60.</bibl>
          <bibl n="231075">
            <bibl>Wiatrak, B., Piasny, J., Kuźniarski, A., &amp;amp; Gąsiorowski, K. (2021). Interactions of Amyloid-β with Membrane Proteins. International Journal of Molecular Sciences, 22(11), 6075.</bibl>
            <idno type="DOI">10.3390/ijms22116075</idno>
          </bibl>
          <bibl n="230841">
            <bibl>Wiedrick, J. T., Phillips, J. I., Lusardi, T. A., McFarland, T. J., Lind, B., Sandau, U. S., Harrington, C. A., Lapidus, J. A., Galasko, D. R., Quinn, J. F., &amp;amp; Saugstad, J. A. (2019). Validation of MicroRNA Biomarkers for Alzheimer’s Disease in Human Cerebrospinal Fluid. Journal of Alzheimer’s Disease: JAD, 67(3), 875–891.</bibl>
            <idno type="DOI">10.3233/JAD-180539</idno>
          </bibl>
          <bibl n="231159">
            <bibl>Wilkins, H. M., &amp;amp; Swerdlow, R. H. (2017). Amyloid precursor protein processing and bioenergetics. Brain Research Bulletin, 133, 71–79.</bibl>
            <idno type="DOI">10.1016/j.brainresbull.2016.08.009</idno>
          </bibl>
          <bibl n="230788">
            <bibl>Winblad, B., Amouyel, P., Andrieu, S., Ballard, C., Brayne, C., Brodaty, H., Cedazo-Minguez, A., Dubois, B., Edvardsson, D., Feldman, H., Fratiglioni, L., Frisoni, G. B., Gauthier, S., Georges, J., Graff, C., Iqbal, K., Jessen, F., Johansson, G., J&amp;#246;nsson, L., … Zetterberg, H. (2016). Defeating Alzheimer’s disease and other dementias: A priority for European science and society. The Lancet Neurology, 15(5), 455–532.</bibl>
            <idno type="DOI">10.1016/S1474-4422(16)00062-4</idno>
          </bibl>
          <bibl n="230872">
            <bibl>Wojdała, A. L., Bellomo, G., Toja, A., Gaetani, L., Parnetti, L., &amp;amp; Chiasserini, D. (2024). CSF and plasma Aβ42/40 across Alzheimer’s disease continuum: Comparison of two ultrasensitive Simoa&amp;#174; assays targeting distinct amyloid regions. Clinical Chemistry and Laboratory Medicine, 62(2), 332–340.</bibl>
            <idno type="DOI">10.1515/cclm-2023-0659</idno>
          </bibl>
          <bibl n="231206">World Health Organization. (2021). Fact sheets of dementia. who.int</bibl>
          <bibl n="231031">
            <bibl>Yamamoto, N., Fukata, Y., Fukata, M., &amp;amp; Yanagisawa, K. (2007). GM1-ganglioside-induced Abeta assembly on synaptic membranes of cultured neurons. Biochimica Et Biophysica Acta, 1768(5), 1128–1137.</bibl>
            <idno type="DOI">10.1016/j.bbamem.2007.01.009</idno>
          </bibl>
          <bibl n="230998">
            <bibl>Yamazaki, T., Koo, E. H., &amp;amp; Selkoe, D. J. (1997). Cell surface amyloid beta-protein precursor colocalizes with beta 1 integrins at substrate contact sites in neural cells. Journal of Neuroscience, 17(3), 1004–1010.</bibl>
            <idno type="DOI">10.1523/JNEUROSCI.17-03-01004.1997</idno>
          </bibl>
          <bibl n="231183">
            <bibl>Yanagisawa, K. (2007). Role of gangliosides in Alzheimer’s disease. Biochimica Et Biophysica Acta, 1768(8), 1943–1951.</bibl>
            <idno type="DOI">10.1016/j.bbamem.2007.01.018</idno>
          </bibl>
          <bibl n="230862">
            <bibl>Yang, T., O’Malley, T. T., Kanmert, D., Jerecic, J., Zieske, L. R., Zetterberg, H., Hyman, B. T., Walsh, D. M., &amp;amp; Selkoe, D. J. (2015). A highly sensitive novel immunoassay specifically detects low levels of soluble Aβ oligomers in human cerebrospinal fluid. Alzheimer’s Research &amp;amp; Therapy, 7(1), 14.</bibl>
            <idno type="DOI">10.1186/s13195-015-0100-y</idno>
          </bibl>
          <bibl n="231015">
            <bibl>Yerbury, J. J., &amp;amp; Wilson, M. R. (2010). Extracellular chaperones modulate the effects of Alzheimer’s patient cerebrospinal fluid on Abeta(1-42) toxicity and uptake. Cell Stress &amp;amp; Chaperones, 15(1), 115–121.</bibl>
            <idno type="DOI">10.1007/s12192-009-0122-0</idno>
          </bibl>
          <bibl n="230847">
            <bibl>Yoshihara, T., Takiguchi, S., Kyuno, A., Tanaka, K., Kuba, S., Hashiguchi, S., Ito, Y., Hashimoto, T., Iwatsubo, T., Tsuyama, S., Nakashima, T., &amp;amp; Sugimura, K. (2008). Immunoreactivity of phage library-derived human single-chain antibodies to amyloid beta conformers in vitro. Journal of Biochemistry, 143(4), 475–486.</bibl>
            <idno type="DOI">10.1093/jb/mvm239</idno>
          </bibl>
          <bibl n="230980">
            <bibl>Young-Pearse, T. L., Chen, A. C., Chang, R., Marquez, C., &amp;amp; Selkoe, D. J. (2008). Secreted APP regulates the function of full-length APP in neurite outgrowth through interaction with integrin beta1. Neural Development, 3, 15.</bibl>
            <idno type="DOI">10.1186/1749-8104-3-15</idno>
          </bibl>
          <bibl n="231176">
            <bibl>Younkin, S. G. (1995). Evidence that A beta 42 is the real culprit in Alzheimer’s disease. Annals of Neurology, 37(3), 287–288.</bibl>
            <idno type="DOI">10.1002/ana.410370303</idno>
          </bibl>
          <bibl n="231164">
            <bibl>Yu, Y. J., &amp;amp; Watts, R. J. (2013). Developing therapeutic antibodies for neurodegenerative disease. Neurotherapeutics, 10(3), 459–472.</bibl>
            <idno type="DOI">10.1007/s13311-013-0187-4</idno>
          </bibl>
          <bibl n="231133">
            <bibl>Yuan, S., Zhou, G., &amp;amp; Xu, G. (2024). Translation machinery: The basis of translational control. Journal of Genetics and Genomics, 51(4), 367–378.</bibl>
            <idno type="DOI">10.1016/j.jgg.2023.07.009</idno>
          </bibl>
          <bibl n="230906">
            <bibl>Yusakul, G., Sakamoto, S., Pongkitwitoon, B., Tanaka, H., &amp;amp; Morimoto, S. (2016). Effect of linker length between variable domains of single chain variable fragment antibody against daidzin on its reactivity. Bioscience, Biotechnology and Biochemistry, 80(7), 1306–1312.</bibl>
            <idno type="DOI">10.1080/09168451.2016.1156482</idno>
          </bibl>
          <bibl n="230930">
            <bibl>Zameer, A., Kasturirangan, S., Emadi, S., Nimmagadda, S. V., &amp;amp; Sierks, M. R. (2008). Anti-oligomeric Abeta single-chain variable domain antibody blocks Abeta-induced toxicity against human neuroblastoma cells. Journal of Molecular Biology, 384(4), 917–928.</bibl>
            <idno type="DOI">10.1016/j.jmb.2008.09.068</idno>
          </bibl>
          <bibl n="230835">
            <bibl>Zampagni, M., Cascella, R., Casamenti, F., Grossi, C., Evangelisti, E., Wright, D., Becatti, M., Liguri, G., Mannini, B., Campioni, S., Chiti, F., &amp;amp; Cecchi, C. (2011). A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells. Journal of Cellular and Molecular Medicine, 15(10), 2106–2116.</bibl>
            <idno type="DOI">10.1111/j.1582-4934.2010.01239.x</idno>
          </bibl>
          <bibl n="231020">
            <bibl>Zandomeneghi, G., Krebs, M. R. H., McCammon, M. G., &amp;amp; F&amp;#228;ndrich, M. (2004). FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils. Protein Science, 13(12), 3314–3321.</bibl>
            <idno type="DOI">10.1110/ps.041024904</idno>
          </bibl>
          <bibl n="231087">
            <bibl>Zetterberg, H., &amp;amp; Bendlin, B. B. (2021). Biomarkers for Alzheimer’s disease-preparing for a new era of disease-modifying therapies. Molecular Psychiatry, 26(1), 296–308.</bibl>
            <idno type="DOI">10.1038/s41380-020-0721-9</idno>
          </bibl>
          <bibl n="230952">Zetterberg, H., Alawode, D. O. T., Keshavan, A., O’Connor, A, Weston, P. S. J., Paterson, R. W., Heslegrave, A., Fox, N. C. Fox, Lunn, M. P., &amp;amp; Schott, J. M. (2020). Blood Tests for Alzheimer Disease. Practical Neurology. practicalneurology.com</bibl>
          <bibl n="230989">
            <bibl>Zha, J., Liu, X.-M., Zhu, J., Liu, S.-Y., Lu, S., Xu, P.-X., Yu, X.-L., &amp;amp; Liu, R.-T. (2016). A scFv antibody targeting common oligomeric epitope has potential for treating several amyloidoses. Scientific Reports, 6, 36631.</bibl>
            <idno type="DOI">10.1038/srep36631</idno>
          </bibl>
          <bibl n="231130">
            <bibl>Zhao, Y., &amp;amp; Zhao, B. (2013). Oxidative stress and the pathogenesis of Alzheimer’s disease. Oxidative Medicine and Cellular Longevity, 2013, 316523.</bibl>
            <idno type="DOI">10.1155/2013/316523</idno>
          </bibl>
          <bibl n="231109">
            <bibl>Zheng, F., Pang, Y., Li, L., Pang, Y., Zhang, J., Wang, X., &amp;amp; Raes, G. (2022). Applications of nanobodies in brain diseases. Frontiers in Immunology, 13, 978513.</bibl>
            <idno type="DOI">10.3389/fimm u.2022.978513</idno>
          </bibl>
          <bibl n="231052">
            <bibl>Zhu, X., Perry, G., Smith, M. A., &amp;amp; Wang, X. (2013). Abnormal mitochondrial dynamics in the pathogenesis of Alzheimer’s disease. Journal of Alzheimer’s Disease: JAD, 33 Suppl 1, S253-262.</bibl>
            <idno type="DOI">10.3233/JAD-2012-129005</idno>
          </bibl>
        </listBibl>
      </div>
    </body>
  </text>
</TEI>