A multidisciplinary approach for the early diagnosis of Alzheimer’s disease and potential therapeutic applications

2021 Alzheimer’s disease facts and figures. (2021). Alzheimer’s & Dementia: The Journal of the Alzheimer’s Association, 17(3), 327–406. DOI: 10.1002/alz.12328

2023 Alzheimer’s disease facts and figures. (2023). Alzheimer’s & Dementia: The Journal of the Alzheimer’s Association, 19(4), 1598–1695. DOI: 10.1002/alz.13016

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., & Biverstål, H. (2020). High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain. Scientific Reports, 10(1), 235. DOI: 10.1038/s41598-019-57143-x

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., & Keyaerts, M. (2021). Immunogenicity Risk Profile of Nanobodies. Frontiers in Immunology, 12, 632687. DOI: 10.3389/fimmu.2021.632687

M. Ahmed, J. Davis, D. Aucoin, T. Sato, S. Ahuja, S. Aimoto, J. I. Elliott, W. E. Van Nostrand, S. O. Smith. Nature Structural & Molecular Biology, 17(5):561-7 DOI: 10.1038/nsmb.1799

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

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., & 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 & Dementia, 7(3), 270–279. DOI: 10.1016/j.jalz.2011.03.008

Alonso, A. D., Cohen, L. S., Corbo, C., Morozova, V., ElIdrissi, A., Phillips, G., & Kleiman, F. E. (2018). Hyperphosphorylation of Tau Associates with Changes in Its Function Beyond Microtubule Stability. Frontiers in Cellular Neuroscience, 12, 338. DOI: 10.3389/fncel.2018.00338

Alzforum. (2023). Remternetug. alzforum.org/therapeutics/remternetug

Alzheimer, A., Stelzmann, R. A., Schnitzlein, H. N., & Murtagh, F. R. (1995). An English translation of Alzheimer’s 1907 paper, ‘Uber eine eigenartige Erkankung der Hirnrinde’. Clinical Anatomy, 8(6), 429–431. DOI: 10.1002/ca.980080612

Alzheimer Europe. (2020). Dementia in Europe Yearbook 2019: estimating the prevalence of dementia in Europe. ISBN: 978-99959-995-6-7

Amador-Ortiz, C., Lin, W.-L., Ahmed, Z., Personett, D., Davies, P., Duara, R., Graff-Radford, N. R., Hutton, M. L., & Dickson, D. W. (2007). TDP-43 immunoreactivity in hippocampal sclerosis and Alzheimer’s disease. Annals of Neurology, 61(5), 435–445. DOI: 10.1002/ana.21154

Amm, I., Sommer, T., & 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. DOI: 10.1016/j.bbamcr.2013.06.031

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., & Thambisetty, M. (2018). Evidence for brain glucose dysregulation in Alzheimer’s disease. Alzheimer’s & Dementia, 14(3), 318–329. DOI: 10.1016/j.jalz.2017.09.011

Andrews, S. J., Renton, A. E., Fulton-Howard, B., Podlesny-Drabiniok, A., Marcora, E., & Goate, A. M. (2023). The complex genetic architecture of Alzheimer’s disease: Novel insights and future directions. EBioMedicine, 90, 104511. DOI: 10.1016/j.ebiom.2023.104511

Angelova, P. R., & Abramov, A. Y. (2018). Role of mitochondrial ROS in the brain: From physiology to neurodegeneration. FEBS Letters, 592(5), 692–702. DOI: 10.1002/1873-3468.12964

Antonell, A., Mansilla, A., Rami, L., Lladó, A., Iranzo, A., Olives, J., Balasa, M., Sánchez-Valle, R., & 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. DOI: 10.3233/JAD-140624

Aprile, F. A., Sormanni, P., Perni, M., Arosio, P., Linse, S., Knowles, T. P. J., Dobson, C. M., & 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. DOI: 10.1126/sciadv.1700488

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., & 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. DOI: 10.1073/pnas.1919464117

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., & 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. DOI: 10.1186/s13024-017-0169-9

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. DOI: 10.1016/0022-2836(90)90085-Z

Ariga, T., Kobayashi, K., Hasegawa, A., Kiso, M., Ishida, H., & Miyatake, T. (2001). Characterization of high-affinity binding between gangliosides and amyloid beta-protein. Archives of Biochemistry and Biophysics, 388(2), 225–230. DOI: 10.1006/abbi.2001.2304

Arispe, N., Diaz, J. C., & Simakova, O. (2007). Abeta ion channels. Prospects for treating Alzheimer’s disease with Abeta channel blockers. Biochimica Et Biophysica Acta, 1768(8), 1952–1965. DOI: 10.1016/j.bbamem.2007.03.014

Arndt, J. W., Qian, F., Smith, B. A., Quan, C., Kilambi, K. P., Bush, M. W., Walz, T., Pepinsky, R. B., Bussière, T., Hamann, S., Cameron, T. O., & Weinreb, P. H. (2018). Structural and kinetic basis for the selectivity of aducanumab for aggregated forms of amyloid-β. Scientific Reports, 8(1), 6412. DOI: 10.1038/s41598-018-24501-0

Ashton, N. J., Pascoal, T. A., Karikari, T. K., Benedet, A. L., Lantero-Rodriguez, J., Brinkmalm, G., Snellman, A., Schöll, M., Troakes, C., Hye, A., Gauthier, S., Vanmechelen, E., Zetterberg, H., Rosa-Neto, P., & Blennow, K. (2021). Plasma p-tau231: A new biomarker for incipient Alzheimer’s disease pathology. Acta Neuropathologica, 141(5), 709–724. DOI: 10.1007/s00401-021-02275-6

Bäckman, L., Jones, S., Berger, A.-K., Laukka, E. J., & Small, B. J. (2005). Cognitive impairment in preclinical Alzheimer’s disease: A meta-analysis. Neuropsychology, 19(4), 520–531. DOI: 10.1037/0894-4105.19.4.520

Baghallab, I., Reyes-Ruiz, J. M., Abulnaja, K., Huwait, E., & 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. DOI: 10.3233/JAD-180582

Balchin, D., Hayer-Hartl, M., & Hartl, F. U. (2016). In vivo aspects of protein folding and quality control. Science (New York, N.Y.), 353(6294), aac4354. DOI: 10.1126/science.aac4354

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., & Matteini, P. (2020). Nanoscopic insights into the surface conformation of neurotoxic amyloid β oligomers. RSC Advances, 10(37), 21907–21913. DOI: 10.1039/d0ra03799k

Barenholz, Y. (2004). Sphingomyelin and cholesterol: From membrane biophysics and rafts to potential medical applications. Sub-Cellular Biochemistry, 37, 167–215. DOI: 10.1007/978-1-4757-5806-1_5

Barrera, N. P., Zhou, M., & 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. DOI: 10.1016/j.tcb.2012.08.007

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. DOI: 10.1056/NEJMoa1202753

Batko, J., Antosz, K., Miśków, W., Pszczołowska, M., Walczak, K., & Leszek, J. (2024). Chaperones-A New Class of Potential Therapeutic Targets in Alzheimer’s Disease. International Journal of Molecular Sciences, 25(6), 3401. DOI: 10.3390/ijms25063401

Bélanger, K., Iqbal, U., Tanha, J., MacKenzie, R., Moreno, M., & Stanimirovic, D. (2019). Single-Domain Antibodies as Therapeutic and Imaging Agents for the Treatment of CNS Diseases. Antibodies (Basel, Switzerland), 8(2), 27. DOI: 10.3390/antib8020027

Bellomo, G., Toja, A., Paolini Paoletti, F., Ma, Y., Farris, C. M., Gaetani, L., Salvadori, N., Chiasserini, D., Wojdaƚa, A. L., Concha-Marambio, L., & Parnetti, L. (2024). Investigating alpha-synuclein co-pathology in Alzheimer’s disease by means of cerebrospinal fluid alpha-synuclein seed amplification assay. Alzheimer’s & Dementia, 20(4), 2444–2452. DOI: 10.1002/alz.13658

Benedet, A. L., Brum, W. S., Hansson, O., Alzheimer’s Disease Neuroimaging Initiative, Karikari, T. K., Zimmer, E. R., Zetterberg, H., Blennow, K., & Ashton, N. J. (2022). The accuracy and robustness of plasma biomarker models for amyloid PET positivity. Alzheimer’s Research & Therapy, 14(1), 26. DOI: 10.1186/s13195-021-00942-0

Benilova, I., Karran, E., & De Strooper, B. (2012). The toxic Aβ oligomer and Alzheimer’s disease: An emperor in need of clothes. Nature Neuroscience, 15(3), 349–357. DOI: 10.1038/nn.3028

Bento, C. F., Renna, M., Ghislat, G., Puri, C., Ashkenazi, A., Vicinanza, M., Menzies, F. M., & Rubinsztein, D. C. (2016). Mammalian Autophagy: How Does It Work? Annual Review of Biochemistry, 85, 685–713. DOI: 10.1146/annurev-biochem-060815-014556

Berridge, M. J. (1998). Neuronal calcium signaling. Neuron, 21(1), 13–26. DOI: 10.1016/s0896-6273(00)80510-3

Berridge, M. J., Lipp, P., & Bootman, M. D. (2000). The versatility and universality of calcium signalling. Nature Reviews. Molecular Cell Biology, 1(1), 11–21. DOI: 10.1038/35036035

Bhatia, S., Rawal, R., Sharma, P., Singh, T., Singh, M., & Singh, V. (2022). Mitochondrial Dysfunction in Alzheimer’s Disease: Opportunities for Drug Development. Current Neuropharmacology, 20(4), 675–692. DOI: 10.2174/1570159X19666210517114016

Bigi, A., Cascella, R., Fani, G., Bernacchioni, C., Cencetti, F., Bruni, P., Chiti, F., Donati, C., & 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. DOI: 10.1111/febs.16579

Bigi, A., Fani, G., Bessi, V., Napolitano, L., Bagnoli, S., Ingannato, A., Neri, L., Cascella, R., Matteini, P., Sorbi, S., Nacmias, B., Cecchi, C., & 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. DOI: 10.1186/s40035-024-00405-0

Bigi, A., Loffredo, G., Cascella, R., & Cecchi, C. (2020). Targeting Pathological Amyloid Aggregates with Conformation-Sensitive Antibodies. Current Alzheimer Research, 17(8), 722–734. DOI: 10.2174/1567205017666201109093848

Bigi, A., Lombardo, E., Cascella, R., & Cecchi, C. (2023b). The Toxicity of Protein Aggregates: New Insights into the Mechanisms. International Journal of Molecular Sciences, 24(9), 7974. DOI: 10.3390/ijms24097974

Bigi, A., Napolitano, L., Vadukul, D. M., Chiti, F., Cecchi, C., Aprile, F. A., & Cascella, R. (2024a). A single-domain antibody detects and neutralises toxic Aβ42 oligomers in the Alzheimer’s disease CSF. Alzheimer’s Research & Therapy, 16(1), 13. DOI: 10.1186/s13195-023-01361-z

Biomarkers Definitions Working Group. (2001). Biomarkers and surrogate endpoints: Preferred definitions and conceptual framework. Clinical Pharmacology and Therapeutics, 69(3), 89–95. DOI: 10.1067/mcp.2001.113989

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., & Whitlow, M. (1988). Single-chain antigen-binding proteins. Science (New York, N.Y.), 242(4877), 423–426. DOI: 10.1126/science.3140379

Bitan, G., Kirkitadze, M. D., Lomakin, A., Vollers, S. S., Benedek, G. B., & 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. DOI: 10.1073/pnas.222681699

Blennow, K., Wallin, A., Agren, H., Spenger, C., Siegfried, J., & 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. DOI: 10.1007/BF02815140

Blessed, G., Tomlinson, B. E., & 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. DOI: 10.1192/bjp.114.512.797

Bode, D. C., Freeley, M., Nield, J., Palma, M., & 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. DOI: 10.1074/jbc.AC118.007195

Boess, F., Sakaoka, S., Abi-Saab, D., Scelsi, M., delmar, P., Hofmann, C., Klein, G., Baudler, M., Doody, R., & Kerchner, G. (2021). Graduation study design: Evaluation of once-weekly subcutaneous administration of gantenerumab on brain amyloid load. Alzheimer’s & Dementia, 17, e052060. DOI: 10.1002/alz.052060

Bondi, M. W., Edmonds, E. C., & Salmon, D. P. (2017). Alzheimer’s Disease: Past, Present, and Future. Journal of the International Neuropsychological Society: JINS, 23(9–10), 818–831. DOI: 10.1017/S135561771700100X

Bondi, M. W., Monsch, A. U., Galasko, D., Butters, N., Salmon, D. P., & Delis, D. C. (1994). Preclinical cognitive markers of dementia of the Alzheimer type. Neuropsychology, 8(3), 374–384. DOI: 10.1037/0894-4105.8.3.374

Braak, H., & 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. DOI: 10.1016/0197-4580(94)90032-9

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. DOI: 10.1006/abio.1976.9999

Brehme, M., Voisine, C., Rolland, T., Wachi, S., Soper, J. H., Zhu, Y., Orton, K., Villella, A., Garza, D., Vidal, M., Ge, H., & Morimoto, R. I. (2014). A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease. Cell Reports, 9(3), 1135–1150. DOI: 10.1016/j.celrep.2014.09.042

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., & Pereira, S. D. S. (2021). Camelid Single-Domain Antibodies for the Development of Potent Diagnosis Platforms. Molecular Diagnosis & Therapy, 25(4), 439–456. DOI: 10.1007/s40291-021-00533-7

Brodaty, H., Heffernan, M., Kochan, N. A., Draper, B., Trollor, J. N., Reppermund, S., Slavin, M. J., & Sachdev, P. S. (2013). Mild cognitive impairment in a community sample: The Sydney Memory and Ageing Study. Alzheimer’s & Dementia, 9(3), 310-317.e1. DOI: 10.1016/j.jalz.2011.11.010

Brooks, W. H. (2024). Polyamine Dysregulation and Nucleolar Disruption in Alzheimer’s Disease. Journal of Alzheimer’s Disease, 98(3), 837. DOI: 10.3233/JAD-231184

Buchhave, P., Minthon, L., Zetterberg, H., Wallin, A. K., Blennow, K., & 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. DOI: 10.1001/archgenpsychiatry.2011.155

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. DOI: 10.14283/jpad.2022.30

Butterfield, D. A., & Halliwell, B. (2019). Oxidative stress, dysfunctional glucose metabolism, and Alzheimer disease. Nature Reviews. Neuroscience, 20(3), 148. DOI: 10.1038/s41583-019-0132-6

Cadonic, C., Sabbir, M. G., & Albensi, B. C. (2016). Mechanisms of Mitochondrial Dysfunction in Alzheimer’s Disease. Molecular Neurobiology, 53(9), 6078–6090. DOI: 10.1007/s12035-015-9515-5

Caillé, I., Allinquant, B., Dupont, E., Bouillot, C., Langer, A., Müller, U., & Prochiantz, A. (2004). Soluble form of amyloid precursor protein regulates proliferation of progenitors in the adult subventricular zone. Development, 131(9), 2173–2181. DOI: 10.1242/dev.01103

Camberg, J., Doyle, S., Johnston, D., & Wickner, S. (2013). Molecular Chaperones. In Brenner’s Encyclopedia of Genetics (pp. 456–460). DOI: 10.1016/B978-0-12-374984-0.00221-7

Canevari, L., Clark, J. B., & Bates, T. E. (1999). Beta-Amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria. FEBS Letters, 457(1), 131–134. DOI: 10.1016/s0014-5793(99)01028-5

Capitini, C., Conti, S., Perni, M., Guidi, F., Cascella, R., De Poli, A., Penco, A., Relini, A., Cecchi, C., & 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. DOI: 10.1371/journal.pone.0086720

Cardoso, F. M., Ibañez, L. I., Van den Hoecke, S., De Baets, S., Smet, A., Roose, K., Schepens, B., Descamps, F. J., Fiers, W., Muyldermans, S., Depicker, A., & Saelens, X. (2014). Single-domain antibodies targeting neuraminidase protect against an H5N1 influenza virus challenge. Journal of Virology, 88(15), 8278–8296. DOI: 10.1128/JVI.03178-13

Carmona, S., Hardy, J., & Guerreiro, R. (2018). The genetic landscape of Alzheimer disease. Handbook of Clinical Neurology, 148, 395–408. DOI: 10.1016/B978-0-444-64076-5.00026-0

Caroli, A., & Frisoni, G. B. (2010). The dynamics of Alzheimer's disease biomarkers in the Alzheimer's Disease Neuroimaging Initiative cohort. Neurobiology of Aging, 31(8), 1263–1274. DOI: 10.1016/j.neurobiolaging.2010.04.024

Cascella, R., Bigi, A., Riffert, D. G., Gagliani, M. C., Ermini, E., Moretti, M., Cortese, K., Cecchi, C., & Chiti, F. (2022). A quantitative biology approach correlates neuronal toxicity with the largest inclusions of TDP-43. Science Advances, 8(30), eabm6376. DOI: 10.1126/sciadv.abm6376

Cascella, R., & Cecchi, C. (2021). Calcium Dyshomeostasis in Alzheimer’s Disease Pathogenesis. International Journal of Molecular Sciences, 22(9), 4914. DOI: 10.3390/ijms22094914

Cascella, R., Chen, S. W., Bigi, A., Camino, J. D., Xu, C. K., Dobson, C. M., Chiti, F., Cremades, N., & Cecchi, C. (2021). The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells. Nature Communications, 12(1), 1814. DOI: 10.1038/s41467-021-21937-3

Cascella, R., Conti, S., Mannini, B., Li, X., Buxbaum, J. N., Tiribilli, B., Chiti, F., & Cecchi, C. (2013). Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro. Biochimica Et Biophysica Acta, 1832(12), 2302–2314. DOI: 10.1016/j.bbadis.2013.09.011

Cascella, R., Conti, S., Tatini, F., Evangelisti, E., Scartabelli, T., Casamenti, F., Wilson, M. R., Chiti, F., & Cecchi, C. (2013). Extracellular chaperones prevent Aβ42-induced toxicity in rat brains. Biochimica Et Biophysica Acta, 1832(8), 1217–1226. DOI: 10.1016/j.bbadis.2013.04.012

Cascella, R., Evangelisti, E., Bigi, A., Becatti, M., Fiorillo, C., Stefani, M., Chiti, F., & Cecchi, C. (2017). Soluble Oligomers Require a Ganglioside to Trigger Neuronal Calcium Overload. Journal of Alzheimer’s Disease: JAD, 60(3), 923–938. DOI: 10.3233/JAD-170340

Cecchi, C., Nichino, D., Zampagni, M., Bernacchioni, C., Evangelisti, E., Pensalfini, A., Liguri, G., Gliozzi, A., Stefani, M., & 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. DOI: 10.1016/j.bbamem.2009.07.019

Chasseigneaux, S., & Allinquant, B. (2012). Functions of Aβ, sAPPα and sAPPβ: Similarities and differences. Journal of Neurochemistry, 120 Suppl 1, 99–108. DOI: 10.1111/j.1471-4159.2011.07584.x

Chatani, E., Yuzu, K., Ohhashi, Y., & Goto, Y. (2021). Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils. International Journal of Molecular Sciences, 22(9), 4349. DOI: 10.3390/ijms22094349

Chatziefstathiou, A., Canaslan, S., Kanata, E., Vekrellis, K., Constantinides, V. C., Paraskevas, G. P., Kapaki, E., Schmitz, M., Zerr, I., Xanthopoulos, K., Sklaviadis, T., & Dafou, D. (2024). SIMOA Diagnostics on Alzheimer’s Disease and Frontotemporal Dementia. Biomedicines, 12(6), 1253. DOI: 10.3390/biomedicines12061253

Cheignon, C., Tomas, M., Bonnefont-Rousselot, D., Faller, P., Hureau, C., & Collin, F. (2018). Oxidative stress and the amyloid beta peptide in Alzheimer’s disease. Redox Biology, 14, 450–464. DOI: 10.1016/j.redox.2017.10.014

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., & Singhal, P. (2024). Results from the long-term extension of PRIME: A randomized Phase 1b trial of aducanumab. Alzheimer’s & Dementia, 20(5), 3406–3415. DOI: 10.1002/alz.13755

Chen, X., Zaro, J. L., & Shen, W.-C. (2013). Fusion protein linkers: Property, design and functionality. Advanced Drug Delivery Reviews, 65(10), 1357–1369. DOI: 10.1016/j.addr.2012.09.039

Chen, Y. R., & 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. DOI: 10.1074/jbc.M602363200

Cheng, B., Gong, H., Xiao, H., Petersen, R. B., Zheng, L., & Huang, K. (2013). Inhibiting Toxic Aggregation of Amyloidogenic Proteins: A Therapeutic Strategy for Protein Misfolding Diseases. Biochimica Et Biophysica Acta, 1830(10), 4860–4871. DOI: 10.1016/j.bbagen.2013.05.035

Chételat, 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. DOI: 10.1016/S1474-4422(20)30314-8

Chiti, F., & Dobson, C. M. (2006). Protein misfolding, functional amyloid, and human disease. Annual Review of Biochemistry, 75, 333–366. DOI: 10.1146/annurev.biochem.75.101304.123901

Chiti, F., & 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. DOI: 10.1146/annurev-biochem-061516-045115

Ciechanover, A., & Brundin, P. (2003). The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg. Neuron, 40(2), 427–446. DOI: 10.1016/s0896-6273(03)00606-8

Cinquanta, L., Fontana, D. E., & Bizzaro, N. (2017). Chemiluminescent immunoassay technology: What does it change in autoantibody detection? Auto-Immunity Highlights, 8(1), 9. DOI: 10.1007/s13317-017-0097-2

Clapham, D. E. (2007). Calcium signaling. Cell, 131(6), 1047–1058. DOI: 10.1016/j.cell.2007.11.028

Cline, E. N., Bicca, M. A., Viola, K. L., & Klein, W. L. (2018). The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade. Journal of Alzheimer’s Disease: JAD, 64(s1), S567–S610. DOI: 10.3233/JAD-179941

Cohen, S. I. A., Linse, S., Luheshi, L. M., Hellstrand, E., White, D. A., Rajah, L., Otzen, D. E., Vendruscolo, M., Dobson, C. M., & 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. DOI: 10.1073/pnas.1218402110

Colom-Cadena, M., Gelpi, E., Charif, S., Belbin, O., Blesa, R., Martí, M. J., Clarimón, J., & Lleó, 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. DOI: 10.1097/NEN.0000000000000018

Congdon, E. E., & Sigurdsson, E. M. (2018). Tau-targeting therapies for Alzheimer disease. Nature Reviews. Neurology, 14(7), 399–415. DOI: 10.1038/s41582-018-0013-z

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. DOI: 10.1017/s1041610203008664

Colvin, M. T., Silvers, R., Ni, Q. Z., Can, T. V., Sergeyev, I., Rosay, M., Donovan, K. J., Michael, B., Wall, J., Linse, S., & Griffin, R. G. (2016). Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils. Journal of the American Chemical Society, 138(30), 9663–9674. DOI: 10.1021/jacs.6b05129

Cummings, J., Osse, A. M. L., Cammann, D., Powell, J., & Chen, J. (2024). Anti-Amyloid Monoclonal Antibodies for the Treatment of Alzheimer’s Disease. BioDrugs, 38(1), 5–22. DOI: 10.1007/s40259-023-00633-2

Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., & LaDu, M. J. (2002). Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. Journal of Biological Chemistry, 277(35), 32046–32053. DOI: 10.1074/jbc.M201750200

Danis, C., Dupré, E., Zejneli, O., Caillierez, R., Arrial, A., Bégard, S., Mortelecque, J., Eddarkaoui, S., Loyens, A., Cantrelle, F.-X., Hanoulle, X., Rain, J.-C., Colin, M., Buée, L., & 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. DOI: 10.1016/j.ymthe.2022.01.009

David, M. A., Jones, D. R., & Tayebi, M. (2014). Potential candidate camelid antibodies for the treatment of protein-misfolding diseases. Journal of Neuroimmunology, 272(1-2), 76-85. DOI: 10.1016/j.jneuroim.2014.05.001

de la Monte, S. M., & Tong, M. (2014). Brain metabolic dysfunction at the core of Alzheimer's disease. Biochemical Pharmacology, 88(4), 548-559. DOI: 10.1016/j.bcp.2013.12.012

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., & 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. DOI: 10.1186/s40478-019-0777-4

De Strooper, B. (2003). Aph-1, Pen-2, and Nicastrin with Presenilin generate an active gamma-Secretase complex. Neuron, 38(1), 9–12. DOI: 10.1016/s0896-6273(03)00205-8

De Strooper, B., & Karran, E. (2016). The Cellular Phase of Alzheimer’s Disease. Cell, 164(4), 603–615. DOI: 10.1016/j.cell.2015.12.056

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., & Hutton, M. L. (2012). A plaque-specific antibody clears existing β-amyloid plaques in Alzheimer’s disease mice. Neuron, 76(5), 908–920. DOI: 10.1016/j.neuron.2012.10.029

Demuro, A., Mina, E., Kayed, R., Milton, S. C., Parker, I., & 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. DOI: 10.1074/jbc.M500997200

Deng, J., Habib, A., Obregon, D. F., Barger, S. W., Giunta, B., Wang, Y.-J., Hou, H., Sawmiller, D., & Tan, J. (2015). Soluble amyloid precursor protein alpha inhibits tau phosphorylation through modulation of GSK3β signaling pathway. Journal of Neurochemistry, 135(3), 630–637. DOI: 10.1111/jnc.13351

B. C. Dickerson, & D. A. Wolk. Neurology, 78(2):84-90 DOI: 10.1212/WNL.0b013e31823efc6c

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., & 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. DOI: 10.1073/pnas.0709180105

Ding, Q., Markesbery, W. R., Chen, Q., Li, F., & Keller, J. N. (2005). Ribosome dysfunction is an early event in Alzheimer’s disease. Journal of Neuroscience, 25(40), 9171–9175. DOI: 10.1523/JNEUROSCI.3040-05.2005

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., & Klenerman, D. (2017). Inhibiting the Ca2+ Influx Induced by Human CSF. Cell Reports, 21(11), 3310–3316. DOI: 10.1016/j.celrep.2017.11.057

Dufour-Rainfray, D., Beaufils, E., Vourc’h, P., Vierron, E., Mereghetti, L., Gendrot, C., Hommet, C., Andres, C. R., Guilloteau, D., & Mondon, K. (2013). Total protein level in cerebrospinal fluid is stable in elderly adults. Journal of the American Geriatrics Society, 61(10), 1819–1821. DOI: 10.1111/jgs.12489

Edelman, G. M. (1970). The structure and function of antibodies. Scientific American, 223(2), 34–42. DOI: 10.1038/scientificamerican0870-34

Eisenberg, D., & Jucker, M. (2012). The amyloid state of proteins in human diseases. Cell, 148(6), 1188–1203. DOI: 10.1016/j.cell.2012.02.022

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

Engelman, D. M. (2005). Membranes are more mosaic than fluid. Nature, 438(7068), 578–580. DOI: 10.1038/nature04394

Englund, H., Sehlin, D., Johansson, A. S., Nilsson, L. N., Gellerfors, P., Paulie, S., Lannfelt, L., & Pettersson, F. E. (2007). Sensitive ELISA detection of amyloid-beta protofibrils in biological samples. Journal of Neurochemistry, 103(1), 334-45. DOI: 10.1111/j.1471-4159.2007.04759.x

Esteves, A., Arduíno, D., Silva, D. F., Martins-Branco, D., Oliveira, C., & Cardoso, S. (2009). Mitochondrial Metabolism in Age-Related Neurodegenerative Disorders: Alzheimer's and Parkinson's Revisited. DOI: 10.1007/978-0-387-84835-8_7

Evangelisti, E., Cascella, R., Becatti, M., Marrazza, G., Dobson, C. M., Chiti, F., Stefani, M., & 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. DOI: 10.1038/srep32721

Evangelisti, E., Wright, D., Zampagni, M., Cascella, R., Fiorillo, C., Bagnoli, S., Relini, A., Nichino, D., Scartabelli, T., Nacmias, B., Sorbi, S., & Cecchi, C. (2013). Lipid rafts mediate amyloid-induced calcium dyshomeostasis and oxidative stress in Alzheimer's disease. Current Alzheimer Research, 10(2), 143-53. DOI: 10.2174/1567205011310020004

Evangelisti, E., Zampagni, M., Cascella, R., Becatti, M., Fiorillo, C., Caselli, A., Bagnoli, S., Nacmias, B., & Cecchi, C. (2014). Plasma membrane injury depends on bilayer lipid composition in Alzheimer's disease. Journal of Alzheimer's Disease, 41(1), 289-300. DOI: 10.3233/JAD-131406

Ewers, M., Mattsson, N., Minthon, L., Molinuevo, J. L., Antonell, A., Popp, J., Jessen, F., Herukka, S.-K., Soininen, H., Maetzler, W., Leyhe, T., Bürger, K., Taniguchi, M., Urakami, K., Lista, S., Dubois, B., Blennow, K., & Hampel, H. (2015). CSF biomarkers for the differential diagnosis of Alzheimer’s disease: A large-scale international multicenter study. Alzheimer’s & Dementia, 11(11), 1306–1315. DOI: 10.1016/j.jalz.2014.12.006

Fabiani, C., & 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. DOI: 10.3389/fncel.2019.00309

Fagan, A. M., Mintun, M. A., Shah, A. R., Aldea, P., Roe, C. M., Mach, R. H., Marcus, D., Morris, J. C., & 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. DOI: 10.1002/emmm.200900048

Fani, G., La Torre, C. E., Cascella, R., Cecchi, C., Vendruscolo, M., & 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. DOI: 10.1007/s00018-022-04513-w

Fani, G., Mannini, B., Vecchi, G., Cascella, R., Cecchi, C., Dobson, C. M., Vendruscolo, M., & Chiti, F. (2021). Aβ Oligomers Dysregulate Calcium Homeostasis by Mechanosensitive Activation of AMPA and NMDA Receptors. ACS Chemical Neuroscience, 12(4), 766–781. DOI: 10.1021/acschemneuro.0c00811

FDA Office of the Commissioner. (2023). FDA Grants Accelerated Approval for Alzheimer’s Disease Treatment. fda.gov

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. DOI: 10.1046/j.1365-2990.2002.t01-1-00410.x

Ferrer, I., Blanco, R., Carmona, M., Puig, B., Barrachina, M., Gómez, C., & 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. DOI: 10.1007/s007020100015

Finder, V. H., Vodopivec, I., Nitsch, R. M., & 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. DOI: 10.1016/j.jmb.2009.12.016

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., Müller, 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., & 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. DOI: 10.1073/pnas.1219476110

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., & Reiman, E. M. (2012). Florbetapir PET analysis of amyloid-β deposition in the presenilin 1 E280A autosomal dominant Alzheimer's disease kindred: a cross-sectional study. Lancet Neurology, 11(12), 1057-65. DOI: 10.1016/S1474-4422(12)70227-2

Fletcher, J. (2023). Lilly’s Donanemab Significantly Slowed Cognitive and Functional Decline in Phase 3 Study of Early Alzheimer’s Disease.

Förster, S., Grimmer, T., Miederer, I., Henriksen, G., Yousefi, B. H., Graner, P., Wester, H.-J., Förstl, H., Kurz, A., Dickerson, B. C., Bartenstein, P., & Drzezga, A. (2012). Regional expansion of hypometabolism in Alzheimer’s disease follows amyloid deposition with temporal delay. Biological Psychiatry, 71(9), 792–797. DOI: 10.1016/j.biopsych.2011.04.023

Friede, R. L., & 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. DOI: 10.1002/ar.1091670402

Frisoni, G. B., Fox, N. C., Jack, C. R., Scheltens, P., & Thompson, P. M. (2010). The clinical use of structural MRI in Alzheimer disease. Nature Reviews. Neurology, 6(2), 67–77. DOI: 10.1038/nrneurol.2009.215

Frost, D., Gorman, P. M., Yip, C. M., & 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. DOI: 10.1046/j.1432-1033.2003.03415.x

Fukuchi, K., Accavitti-Loper, M. A., Kim, H.-D., Tahara, K., Cao, Y., Lewis, T. L., Caughey, R. C., Kim, H., & 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. DOI: 10.1016/j.bbrc.2006.03.145

Fukuchi, K., Tahara, K., Kim, H.-D., Maxwell, J. A., Lewis, T. L., Accavitti-Loper, M. A., Kim, H., Ponnazhagan, S., & 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. DOI: 10.1016/j.nbd.2006.04.012

Fukumoto, H., Tokuda, T., Kasai, T., Ishigami, N., Hidaka, H., Kondo, M., Allsop, D., & Nakagawa, M. (2010). High-molecular-weight beta-amyloid oligomers are elevated in cerebrospinal fluid of Alzheimer patients. FASEB Journal, 24(8), 2716–2726. DOI: 10.1096/fj.09-150359

Fukunaga, S., Ueno, H., Yamaguchi, T., Yano, Y., Hoshino, M., & Matsuzaki, K. (2012). GM1 cluster mediates formation of toxic Aβ fibrils by providing hydrophobic environments. Biochemistry, 51(41), 8125–8131. DOI: 10.1021/bi300839u

Georganopoulou, D. G., Chang, L., Nam, J.-M., Thaxton, C. S., Mufson, E. J., Klein, W. L., & 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. DOI: 10.1073/pnas.0409336102

Giacomucci, G., Mazzeo, S., Bagnoli, S., Ingannato, A., Leccese, D., Berti, V., Padiglioni, S., Galdo, G., Ferrari, C., Sorbi, S., Bessi, V., & 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. DOI: 10.1007/s00415-022-11055-5

Gibbs, E., Silverman, J. M., Zhao, B., Peng, X., Wang, J., Wellington, C. L., Mackenzie, I. R., Plotkin, S. S., Kaplan, J. M., & Cashman, N. R. (2019). A Rationally Designed Humanized Antibody Selective for Amyloid Beta Oligomers in Alzheimer’s Disease. Scientific Reports, 9(1), 9870. DOI: 10.1038/s41598-019-46306-5

Gill, S. C., & von Hippel, P. H. (1989). Calculation of protein extinction coefficients from amino acid sequence data. Analytical Biochemistry, 182(2), 319–326. DOI: 10.1016/0003-2697(89)90602-7

Ginsberg, S. D., Galvin, J. E., Chiu, T. S., Lee, V. M., Masliah, E., & Trojanowski, J. Q. (1998). RNA sequestration to pathological lesions of neurodegenerative diseases. Acta Neuropathologica, 96(5), 487-94. DOI: 10.1007/s004010050923

Gisslén, M., Price, R. W., Andreasson, U., Norgren, N., Nilsson, S., Hagberg, L., Fuchs, D., Spudich, S., Blennow, K., & 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. DOI: 10.1016/j.ebiom.2015.11.036

Glenner, G. G., & 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. DOI: 10.1016/0006-291x(84)91209-9

Goedert, M., Masuda-Suzukake, M., & Falcon, B. (2017). Like prions: the propagation of aggregated tau and α-synuclein in neurodegeneration. Brain, 140(2), 266-278. DOI: 10.1093/brain/aww230

Golde, T. E., Eckman, C. B., & 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. DOI: 10.1016/s0925-4439(00)00043-0

Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., Krafft, G. A., & 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. DOI: 10.1073/pnas.1834302100

Gorantla, N. V., & Chinnathambi, S. (2018). Tau Protein Squired by Molecular Chaperones During Alzheimer’s Disease. Journal of Molecular Neuroscience, 66(3), 356–368. DOI: 10.1007/s12031-018-1174-3

N. J. Greenfield. Nature Protocols, 1, 2733–2741 DOI: 10.1038/nprot.2006.202

Greenough, M. A., Camakaris, J., & Bush, A. I. (2013). Metal dyshomeostasis and oxidative stress in Alzheimer’s disease. Neurochemistry International, 62(5), 540–555. DOI: 10.1016/j.neuint.2012.08.014

Guerreiro, R. J., Gustafson, D. R., & Hardy, J. (2012). The genetic architecture of Alzheimer’s disease: Beyond APP, PSENs and APOE. Neurobiology of Aging, 33(3), 437–456. DOI: 10.1016/j.neurobiolaging.2010.03.025

Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020). Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease. Molecular Neurodegeneration, 15(1), 40. DOI: 10.1186/s13024-020-00391-7

Habiba, U., Descallar, J., Kreilaus, F., Adhikari, U. K., Kumar, S., Morley, J. W., Bui, B. V., Koronyo-Hamaoui, M., & Tayebi, M. (2021). Detection of retinal and blood Aβ oligomers with nanobodies. Alzheimer’s & Dementia (Amsterdam, Netherlands), 13(1), e12193. DOI: 10.1002/dad2.12193

Halliwell, B., & Gutteridge, J. M. C. (2015). Free Radicals in Biology and Medicine. Oxford University Press. DOI: 10.1093/acprof:oso/9780198717478.001.0001

Hamers-Casterman, C., Atarhouch, T., Muyldermans, S., Robinson, G., Hamers, C., Songa, E. B., Bendahman, N., & Hamers, R. (1993). Naturally occurring antibodies devoid of light chains. Nature, 363(6428), 446–448. DOI: 10.1038/363446a0

Hampel, H., Cummings, J., Blennow, K., Gao, P., Jack, C. R., & Vergallo, A. (2021a). Developing the ATX(N) classification for use across the Alzheimer disease continuum. Nature Reviews. Neurology, 17(9), 580–589. DOI: 10.1038/s41582-021-00520-w

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., & Vergallo, A. (2021b). The Amyloid-β Pathway in Alzheimer’s Disease. Molecular Psychiatry, 26(10), 5481–5503. DOI: 10.1038/s41380-021-01249-0

Hansen, D. V., Hanson, J. E., & Sheng, M. (2018). Microglia in Alzheimer’s disease. Journal of Cell Biology, 217(2), 459–472. DOI: 10.1083/jcb.201709069

Hansson, O., Janelidze, S., Hall, S., Magdalinou, N., Lees, A. J., Andreasson, U., Norgren, N., Linder, J., Forsgren, L., Constantinescu, R., Zetterberg, H., & Blennow, K. (2017). Blood-based NfL: A biomarker for differential diagnosis of parkinsonian disorder. Neurology, 88(10), 930–937. DOI: 10.1212/WNL.0000000000003680

Hansson, O., Lehmann, S., Otto, M., Zetterberg, H., & 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 & Therapy, 11(1), 34. DOI: 10.1186/s13195-019-0485-0

Hardy, J., & Allsop, D. (1991). Amyloid deposition as the central event in the aetiology of Alzheimer’s disease. Trends in Pharmacological Sciences, 12(10), 383–388. DOI: 10.1016/0165-6147(91)90609-v

Hardy, J., & Selkoe, D. J. (2002). The amyloid hypothesis of Alzheimer’s disease: Progress and problems on the road to therapeutics. Science, 297(5580), 353–356. DOI: 10.1126/science.1072994

Hashimoto, M., Rockenstein, E., Crews, L., & 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. DOI: 10.1385/NMM:4:1-2:21

Hebda, J. A., & 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. DOI: 10.1146/annurev.biophys.050708.133641

Hefti, F., Goure, W. F., Jerecic, J., Iverson, K. S., Walicke, P. A., & 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. DOI: 10.1016/j.tips.2013.03.002

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. DOI: 10.1016/S1474-4422(15)70016-5

Hepp, D. H., Vergoossen, D. L. E., Huisman, E., Lemstra, A. W., Berendse, H. W., Rozemuller, A. J., Foncke, E. M. J., & 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. DOI: 10.1093/jnen/nlw070

Hernández-Ortega, K., Garcia-Esparcia, P., Gil, L., Lucas, J. J., & Ferrer, I. (2016). Altered Machinery of Protein Synthesis in Alzheimer’s: From the Nucleolus to the Ribosome. Brain Pathology, 26(5), 593–605. DOI: 10.1111/bpa.12335

Herring, W. L., Gould, I. G., Fillit, H., Lindgren, P., Forrestal, F., Thompson, R., & Pemberton-Ross, P. (2021). Predicted Lifetime Health Outcomes for Aducanumab in Patients with Early Alzheimer’s Disease. Neurology and Therapy, 10(2), 919–940. DOI: 10.1007/s40120-021-00273-0

Hershko, A., & Ciechanover, A. (1998). The ubiquitin system. Annual Review of Biochemistry, 67, 425–479. DOI: 10.1146/annurev.biochem.67.1.425

Herskovits, A. Z., Locascio, J. J., Peskind, E. R., Li, G., & Hyman, B. T. (2013). A Luminex assay detects amyloid β oligomers in Alzheimer’s disease cerebrospinal fluid. PloS One, 8(7), e67898. DOI: 10.1371/journal.pone.0067898

Heyman, A., Peterson, B., Fillenbaum, G., & 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. DOI: 10.1212/wnl.46.3.656

Hillen, H., Barghorn, S., Striebinger, A., Labkovsky, B., Müller, 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., & Ebert, U. (2010). Generation and therapeutic efficacy of highly oligomer-specific beta-amyloid antibodies. Journal of Neuroscience, 30(31), 10369–10379. DOI: 10.1523/JNEUROSCI.5721-09.2010

Hipp, M. S., Park, S.-H., & Hartl, F. U. (2014). Proteostasis impairment in protein-misfolding and -aggregation diseases. Trends in Cell Biology, 24(9), 506–514. DOI: 10.1016/j.tcb.2014.05.003

Hodges, J. R., Graham, N., & Patterson, K. (1995). Charting the progression in semantic dementia: Implications for the organisation of semantic memory. Memory, 3(3–4), 463–495. DOI: 10.1080/09658219508253161

Hof, P. R., Vogt, B. A., Bouras, C., & 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. DOI: 10.1016/S0042-6989(96)00240-4

Hölttä, M., Hansson, O., Andreasson, U., Hertze, J., Minthon, L., Nägga, K., Andreasen, N., Zetterberg, H., & Blennow, K. (2013). Evaluating amyloid-β oligomers in cerebrospinal fluid as a biomarker for Alzheimer’s disease. PloS One, 8(6), e66381. DOI: 10.1371/journal.pone.0066381

Hong, S., Ostaszewski, B. L., Yang, T., O’Malley, T. T., Jin, M., Yanagisawa, K., Li, S., Bartels, T., & 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. DOI: 10.1016/j.neuron.2014.02.027

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. DOI: 10.1126/science.aad8373

Huang, W.-J., Zhang, X., & Chen, W.-W. (2016). Role of oxidative stress in Alzheimer’s disease. Biomedical Reports, 4(5), 519–522. DOI: 10.3892/br.2016.630

Huang, Y. R., & Liu, R.-T. (2020). The Toxicity and Polymorphism of β-Amyloid Oligomers. International Journal of Molecular Sciences, 21(12), 4477. DOI: 10.3390/ijms21124477

Hubin, E., van Nuland, N. a. J., Broersen, K., & Pauwels, K. (2014). Transient dynamics of Aβ contribute to toxicity in Alzheimer’s disease. Cellular and Molecular Life Sciences, 71(18), 3507–3521. DOI: 10.1007/s00018-014-1634-z

Hultberg, A., Temperton, N. J., Rosseels, V., Koenders, M., Gonzalez-Pajuelo, M., Schepens, B., Ibañez, L. I., Vanlandschoot, P., Schillemans, J., Saunders, M., Weiss, R. A., Saelens, X., Melero, J. A., Verrips, C. T., Van Gucht, S., & 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. DOI: 10.1371/journal.pone.0017665

Huston, J. S., Levinson, D., Mudgett-Hunter, M., Tai, M. S., Novotný, J., Margolies, M. N., Ridge, R. J., Bruccoleri, R. E., Haber, E., & 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. DOI: 10.1073/pnas.85.16.5879

Hyman, B. T., Van Hoesen, G. W., Damasio, A. R., & Barnes, C. L. (1984). Alzheimer’s disease: Cell-specific pathology isolates the hippocampal formation. Science, 225(4667), 1168–1170. DOI: 10.1126/science.6474172

Iadecola, C. (2017). The Neurovascular Unit Coming of Age: A Journey through Neurovascular Coupling in Health and Disease. Neuron, 96(1), 17-42. DOI: 10.1016/j.neuron.2017.07.030

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 & Dementia, 14(4), 535–562. DOI: 10.1016/j.jalz.2018.02.018

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., & Petersen, R. C. (2002). Antemortem MRI findings correlate with hippocampal neuropathology in typical aging and dementia. Neurology, 58(5), 750–757. DOI: 10.1212/wnl.58.5.750

Jack, C. R., & Holtzman, D. M. (2013). Biomarker modeling of Alzheimer’s disease. Neuron, 80(6), 1347–1358. DOI: 10.1016/j.neuron.2013.12.003

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., & 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. DOI: 10.1016/S1474-4422(12)70291-0

Jack, C. R., Knopman, D. S., Jagust, W. J., Shaw, L. M., Aisen, P. S., Weiner, M. W., Petersen, R. C., & Trojanowski, J. Q. (2010a). Hypothetical model of dynamic biomarkers of the Alzheimer’s pathological cascade. The Lancet Neurology, 9(1), 119–128. DOI: 10.1016/S1474-4422(09)70299-6

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., & 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. DOI: 10.1093/brain/awm336

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., & 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. DOI: 10.1093/brain/awp062

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., & Knopman, D. S. (2012). Shapes of the trajectories of 5 major biomarkers of Alzheimer disease. Archives of Neurology, 69(7), 856–867. DOI: 10.1001/archneurol.2011.3405

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., & 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. DOI: 10.1093/brain/awq277

Jackson, R. J., Hellen, C. U. T., & Pestova, T. V. (2010). The mechanism of eukaryotic translation initiation and principles of its regulation. Nature Reviews. Molecular Cell Biology, 11(2), 113–127. DOI: 10.1038/nrm2838

Jagust, W. J. (2010). Amyloid imaging: Coming to a PET scanner near you. Annals of Neurology, 68(3), 277–278. DOI: 10.1002/ana.22144

Jakob-Roetne, R., & Jacobsen, H. (2009). Alzheimer’s disease: From pathology to therapeutic approaches. Angewandte Chemie (International Ed. in English), 48(17), 3030–3059. DOI: 10.1002/anie.200802808

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., & 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. DOI: 10.1038/s41591-020-0755-1

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., & Hansson, O. (2016). Plasma β-amyloid in Alzheimer’s disease and vascular disease. Scientific Reports, 6, 26801. DOI: 10.1038/srep26801

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. DOI: 10.1001/jama.2015.4668

Jarrett, J. T., Berger, E. P., & 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. DOI: 10.1021/bi00069a001

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., Nygård, L., Olde-Rikkert, M. G., Orgogozo, J.-M., Pasquier, F., Peres, K., … Frölich, L. (2015). Mild cognitive impairment and deficits in instrumental activities of daily living: A systematic review. Alzheimer’s Research & Therapy, 7(1), 17. DOI: 10.1186/s13195-015-0099-0

Ji, S. R., Wu, Y., & 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. DOI: 10.1074/jbc.M104146200

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., & Dickey, C. A. (2011). The Hsp90 kinase co-chaperone Cdc37 regulates tau stability and phosphorylation dynamics. Journal of Biological Chemistry, 286(19), 16976–16983. DOI: 10.1074/jbc.M110.182493

Johnson, J. K., Head, E., Kim, R., Starr, A., & Cotman, C. W. (1999). Clinical and pathological evidence for a frontal variant of Alzheimer disease. Archives of Neurology, 56(10), 1233–1239. DOI: 10.1001/archneur.56.10.1233

Kagan, B. L., Azimov, R., & Azimova, R. (2004). Amyloid peptide channels. Journal of Membrane Biology, 202(1), 1–10. DOI: 10.1007/s00232-004-0709-4

Kakio, A., Nishimoto, S. I., Yanagisawa, K., Kozutsumi, Y., & 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. DOI: 10.1074/jbc.M100252200

Kakio, A., Nishimoto, S., Yanagisawa, K., Kozutsumi, Y., & 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. DOI: 10.1021/bi0255874

Kamat, P. K., Kalani, A., Rai, S., Swarnkar, S., Tota, S., Nath, C., & 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. DOI: 10.1007/s12035-014-9053-6

Kaneko, M., Koike, H., Saito, R., Kitamura, Y., Okuma, Y., & 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. DOI: 10.1523/JNEUROSCI.2422-09.2010

Kaneko, M., Saito, R., Okuma, Y., & Nomura, Y. (2012). Possible involvement of ubiquitin ligase HRD1 insolubilization in amyloid β generation. Biological & Pharmaceutical Bulletin, 35(2), 269–272. DOI: 10.1248/bpb.35.269

Kapasi, A., DeCarli, C., & Schneider, J. A. (2017). Impact of multiple pathologies on the threshold for clinically overt dementia. Acta Neuropathologica, 134, 171–186. DOI: 10.1007/s00401-017-1717-7

Karch, C. M., Cruchaga, C., & Goate, A. M. (2014). Alzheimer’s disease genetics: From the bench to the clinic. Neuron, 83(1), 11–26. DOI: 10.1016/j.neuron.2014.05.041

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., Schöll, M., Massarweh, G., Soucy, J.-P., Höglund, 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. DOI: 10.1016/S1474-4422(20)30071-5

Karran, E., & De Strooper, B. (2022). The amyloid hypothesis in Alzheimer disease: New insights from new therapeutics. Nature Reviews. Drug Discovery, 21(4), 306–318. DOI: 10.1038/s41573-022-00391-w

Kasturirangan, S., Li, L., Emadi, S., Boddapati, S., Schulz, P., & Sierks, M. R. (2012). Nanobody specific for oligomeric β-amyloid stabilizes nontoxic form. Neurobiology of Aging, 33(7), 1320–1328. DOI: 10.1016/j.neurobiolaging.2010.09.020

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., & 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. DOI: 10.1186/1750-1326-2-18

Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003). Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science, 300(5618), 486–489. DOI: 10.1126/science.1079469

Kayed, R., Sokolov, Y., Edmonds, B., McIntire, T. M., Milton, S. C., Hall, J. E., & 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. DOI: 10.1074/jbc.C400260200

Kaushik, S., & Cuervo, A. M. (2015). Proteostasis and aging. Nature Medicine, 21(12), 1406-15. DOI: 10.1038/nm.4001

Keck, S., Nitsch, R., Grune, T., & 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. DOI: 10.1046/j.1471-4159.2003.01642.x

Khachaturian, Z. S. (1989). The role of calcium regulation in brain aging: Reexamination of a hypothesis. Aging (Milan), 1(1), 17–34. DOI: 10.1007/BF03323872

Kim, S., Sharma, C., Jung, U. J., & Kim, S. R. (2023). Pathophysiological Role of Microglial Activation Induced by Blood-Borne Proteins in Alzheimer’s Disease. Biomedicines, 11(5), 1383. DOI: 10.3390/biomedicines11051383

Kim, S. I., Yi, J. S., & Ko, Y. G. (2006). Amyloid beta oligomerization is induced by brain lipid rafts. Journal of Cellular Biochemistry, 99(3), 878–889. DOI: 10.1002/jcb.20978

Kim, Y. E., Hipp, M. S., Bracher, A., Hayer-Hartl, M., & Hartl, F. U. (2013). Molecular chaperone functions in protein folding and proteostasis. Annual Review of Biochemistry, 82, 323–355. DOI: 10.1146/annurev-biochem-060208-092442

Kim, K. S., Wen, G. Y., Bancher, C., Chen, C. M. J., Sapienza, V., Hong, H., & Wisniewski, H. M. (1990). Detection and quantification of amyloid β-peptide with two monoclonal antibodies. Neuroscience Research Communications, 7, 113–122.

Kinger, S., Jagtap, Y. A., Kumar, P., Choudhary, A., Prasad, A., Prajapati, V. K., Kumar, A., Mehta, G., & Mishra, A. (2024). Proteostasis in neurodegenerative diseases. Advances in Clinical Chemistry, 121, 270–333. DOI: 10.1016/bs.acc.2024.04.002

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. DOI: 10.1111/j.1749-6632.1997.tb48473.x

Kleiger, G., & Mayor, T. (2014). Perilous journey: A tour of the ubiquitin-proteasome system. Trends in Cell Biology, 24(6), 352–359. DOI: 10.1016/j.tcb.2013.12.003

Klement, M., Liu, C., Loo, B. L. W., Choo, A. B.-H., Ow, D. S.-W., & 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. DOI: 10.1016/j.jbiotec.2015.02.008

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., & 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. DOI: 10.1523/JNEUROSCI.5161-07.2008

Knopman, D. S., Amieva, H., Petersen, R. C., Chételat, G., Holtzman, D. M., Hyman, B. T., Nixon, R. A., & Jones, D. T. (2021). Alzheimer disease. Nature Reviews. Disease Primers, 7(1), 33. DOI: 10.1038/s41572-021-00269-y

Kollmer, M., Close, W., Funk, L., Rasmussen, J., Bsoul, A., Schierhorn, A., Schmidt, M., Sigurdson, C. J., Jucker, M., & Fändrich, M. (2019). Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue. Nature Communications, 10(1), 4760. DOI: 10.1038/s41467-019-12683-8

Kosik, K. S., Joachim, C. L., & 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. DOI: 10.1073/pnas.83.11.4044

Kravats, A. N., Wickner, S., & Camberg, J. L. (2022). Molecular Chaperones. Reference Module in Life Sciences. DOI: 10.1016/B978-0-12-809633-8.21045-8

Kremer, J. J., Pallitto, M. M., Sklansky, D. J., & Murphy, R. M. (2000). Correlation of beta-amyloid aggregate size and hydrophobicity with decreased bilayer fluidity of model membranes. Biochemistry, 39(33), 10309–10318. DOI: 10.1021/bi0001980

Kulichikhin, K. Y., Fedotov, S. A., Rubel, M. S., Zalutskaya, N. M., Zobnina, A. E., Malikova, O. A., Neznanov, N. G., Chernoff, Y. O., & 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. DOI: 10.1080/19336896.2021.1917289

Labbadia, J., & Morimoto, R. I. (2015). The biology of proteostasis in aging and disease. Annual Review of Biochemistry, 84, 435–464. DOI: 10.1146/annurev-biochem-060614-033955

Ladiwala, A. R. A., Litt, J., Kane, R. S., Aucoin, D. S., Smith, S. O., Ranjan, S., Davis, J., Van Nostrand, W. E., & 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. DOI: 10.1074/jbc.M111.329763

Lafaye, P., Achour, I., England, P., Duyckaerts, C., & 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. DOI: 10.1016/j.molimm.2008.09.008

LaFerla, F. M., Green, K. N., & Oddo, S. (2007). Intracellular amyloid-beta in Alzheimer’s disease. Nature Reviews. Neuroscience, 8(7), 499–509. DOI: 10.1038/nrn2168

Lafleche, G., & Albert, M. S. (1995). Executive function deficits in mild Alzheimer’s disease. Neuropsychology, 9(3), 313–320. DOI: 10.1037/0894-4105.9.3.313

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., & 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. DOI: 10.1073/pnas.95.11.6448

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., & Klein, W. L. (2001). Vaccination with soluble Abeta oligomers generates toxicity-neutralizing antibodies. Journal of Neurochemistry, 79(3), 595–605. DOI: 10.1046/j.1471-4159.2001.00592.x

Landau, S. M., Mintun, M. A., Joshi, A. D., Koeppe, R. A., Petersen, R. C., Aisen, P. S., Weiner, M. W., & Jagust, W. J. (2012). Amyloid deposition, hypometabolism, and longitudinal cognitive decline. Annals of Neurology, 72(4), 578–586. DOI: 10.1002/ana.23650

Lardinois, O., Kirby, P. J., Morgan, D. L., Sills, R. C., Tomer, K. B., & 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. DOI: 10.1002/rcm.7046

Le Bastard, N., Coart, E., Vanderstichele, H., Vanmechelen, E., Martin, J. J., & Engelborghs, S. (2013). Comparison of two analytical platforms for the clinical qualification of Alzheimer's disease biomarkers in pathologically-confirmed dementia. Journal of Alzheimer's Disease, 33(1), 117-31. DOI: 10.3233/JAD-2012-121246

Lee, A. G. (2003). Lipid-protein interactions in biological membranes: A structural perspective. Biochimica Et Biophysica Acta, 1612(1), 1–40. DOI: 10.1016/s0005-2736(03)00056-7

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., & Nixon, R. A. (2010). Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations. Cell, 141(7), 1146–1158. DOI: 10.1016/j.cell.2010.05.008

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. DOI: 10.1038/s41598-019-38752-y

Leuzy, A., Mattsson-Carlgren, N., Palmqvist, S., Janelidze, S., Dage, J. L., & Hansson, O. (2022). Blood-based biomarkers for Alzheimer’s disease. EMBO Molecular Medicine, 14(1), e14408. DOI: 10.15252/emmm.202114408

Lewczuk, P., Matzen, A., Blennow, K., Parnetti, L., Molinuevo, J. L., Eusebi, P., Kornhuber, J., Morris, J. C., & Fagan, A. M. (2017). Cerebrospinal Fluid Aβ42/40 Corresponds Better than Aβ42 to Amyloid PET in Alzheimer's Disease. Journal of Alzheimer's Disease, 55(2), 813-822. DOI: 10.3233/JAD-160722

Li, G., Bien-Ly, N., Andrews-Zwilling, Y., Xu, Q., Bernardo, A., Ring, K., Halabisky, B., Deng, C., Mahley, R. W., & Huang, Y. (2009). GABAergic interneuron dysfunction impairs hippocampal neurogenesis in adult apolipoprotein E4 knockin mice. Cell Stem Cell, 5(6), 634–645. DOI: 10.1016/j.stem.2009.10.015

Li, S., Hong, S., Shepardson, N. E., Walsh, D. M., Shankar, G. M., & Selkoe, D. (2009). Soluble oligomers of amyloid Beta protein facilitate hippocampal long-term depression by disrupting neuronal glutamate uptake. Neuron, 62(6), 788–801. DOI: 10.1016/j.neuron.2009.05.012

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., & 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. DOI: 10.1016/j.jconrel.2016.09.019

Li, X., An, W.-L., Alafuzoff, I., Soininen, H., Winblad, B., & Pei, J.-J. (2004). Phosphorylated eukaryotic translation factor 4E is elevated in Alzheimer brain. Neuroreport, 15(14), 2237–2240. DOI: 10.1097/00001756-200410050-00019

Lin, H., Bhatia, R., & Lal, R. (2001). Amyloid beta protein forms ion channels: Implications for Alzheimer’s disease pathophysiology. FASEB Journal, 15(13), 2433–2444. DOI: 10.1096/fj.01-0377com

Lin, M. S., Chen, L. Y., Wang, S. S. S., Chang, Y., & 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. DOI: 10.1016/j.colsurfb.2008.03.012

Liu, C. C., Liu, C. C., Kanekiyo, T., Xu, H., & Bu, G. (2013). Apolipoprotein E and Alzheimer disease: Risk, mechanisms and therapy. Nature Reviews. Neurology, 9(2), 106–118. DOI: 10.1038/nrneurol.2012.263

Liu, P., Li, L., He, F., Meng, F., Liu, X., Su, Y., Su, X., Luo, B., & 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. DOI: 10.3390/ijms241814225

Lo, R. Y., Hubbard, A. E., Shaw, L. M., Trojanowski, J. Q., Petersen, R. C., Aisen, P. S., Weiner, M. W., & Jagust, W. J. (2011). Longitudinal change of biomarkers in cognitive decline. Archives of Neurology, 68(10), 1257–1266. DOI: 10.1001/archneurol.2011.123

Lopez Salon, M., Pasquini, L., Besio Moreno, M., Pasquini, J. M., & Soto, E. (2003). Relationship between beta-amyloid degradation and the 26S proteasome in neural cells. Experimental Neurology, 180(2), 131–143. DOI: 10.1016/s0014-4886(02)00060-2

Löppönen, M., Räihä, I., Isoaho, R., Vahlberg, T., & Kivelä, S.-L. (2003). Diagnosing cognitive impairment and dementia in primary healthcare—A more active approach is needed. Age and Ageing, 32(6), 606–612. DOI: 10.1093/ageing/afg097

Love, S., & Miners, J. S. (2016). Cerebrovascular disease in ageing and Alzheimer’s disease. Acta Neuropathologica, 131, 645–658. DOI: 10.1007/s00401-015-1522-0

Lu, R. C., Tan, M. S., Wang, H., Xie, A. M., Yu, J. T., & Tan, L. (2014). Heat shock protein 70 in Alzheimer’s disease. BioMed Research International, 2014, 435203. DOI: 10.1155/2014/435203

Lusardi, T. A., Phillips, J. I., Wiedrick, J. T., Harrington, C. A., Lind, B., Lapidus, J. A., Quinn, J. F., & 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. DOI: 10.3233/JAD-160835

Manoutcharian, K., Acero, G., Munguia, M. E., Becerril, B., Massieu, L., Govezensky, T., Ortiz, E., Marks, J. D., Cao, C., Ugen, K., & 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. DOI: 10.1016/j.nbd.2004.06.005

Marín-Argany, M., Rivera-Hernández, G., Martí, J., & 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. DOI: 10.1042/BJ20101712

Martinez-Lopez, N., Athonvarangkul, D., & Singh, R. (2015). Autophagy and aging. Advances in Experimental Medicine and Biology, 847, 73–87. DOI: 10.1007/978-1-4939-2404-2_3

Mason, R. P., Shoemaker, W. J., Shajenko, L., Chambers, T. E., & 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. DOI: 10.1016/0197-4580(92)90116-f

Mastrogiacoma, F., Lindsay, J. G., Bettendorff, L., Rice, J., & Kish, S. J. (1996). Brain protein and alpha-ketoglutarate dehydrogenase complex activity in Alzheimer’s disease. Annals of Neurology, 39(5), 592–598. DOI: 10.1002/ana.410390508

Matsuzaki, K. (2007). Physicochemical interactions of amyloid beta-peptide with lipid bilayers. Biochimica Et Biophysica Acta, 1768(8), 1935–1942. DOI: 10.1016/j.bbamem.2007.02.009

Matsuzaki, K., Kato, K., & Yanagisawa, K. (2010). Abeta polymerization through interaction with membrane gangliosides. Biochimica Et Biophysica Acta, 1801(8), 868–877. DOI: 10.1016/j.bbalip.2010.01.008

Mattson, M. P. (2004). Pathways towards and away from Alzheimer’s disease. Nature, 430(7000), 631–639. DOI: 10.1038/nature02621

Mattson, M. P., Cheng, B., Davis, D., Bryant, K., Lieberburg, I., & 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. DOI: 10.1523/JNEUROSCI.12-02-00376.1992

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., Rosén, E., Aarsland, D., Visser, P. J., Schröder, J., … Blennow, K. (2009). CSF biomarkers and incipient Alzheimer disease in patients with mild cognitive impairment. JAMA, 302(4), 385–393. DOI: 10.1001/jama.2009.1064

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. DOI: 10.1212/WNL.0000000000004058

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, & C. H. Phelps. Alzheimer’s & Dementia, 7(3):263-9 DOI: 10.1016/j.jalz.2011.03.005

McKinnon, C., & Tabrizi, S. J. (2014). The ubiquitin-proteasome system in neurodegeneration. Antioxidants & Redox Signaling, 21(17), 2302–2321. DOI: 10.1089/ars.2013.5802

McLaurin, J., Franklin, T., Fraser, P. E., & Chakrabartty, A. (1998). Structural transitions associated with the interaction of Alzheimer beta-amyloid peptides with gangliosides. Journal of Biological Chemistry, 273(8), 4506–4515. DOI: 10.1074/jbc.273.8.4506

Mendez, M. F. (2017). Early-Onset Alzheimer Disease. Neurologic Clinics, 35(2), 263–281. DOI: 10.1016/j.ncl.2017.01.005

Miao, J., Ma, H., Yang, Y., Liao, Y., Lin, C., Zheng, J., Yu, M., & Lan, J. (2023). Microglia in Alzheimer’s disease: Pathogenesis, mechanisms, and therapeutic potentials. Frontiers in Aging Neuroscience, 15, 1201982. DOI: 10.3389/fnagi.2023.1201982

Miao, W. (2008). Electrogenerated chemiluminescence and its biorelated applications. Chemical Reviews, 108(7), 2506–2553. DOI: 10.1021/cr068083a

Micsonai, A., Wien, F., Bulyáki, É., Kun, J., Moussong, É., Lee, Y.-H., Goto, Y., Réfrégiers, M., & 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. DOI: 10.1093/nar/gky497

Mielke, M. M., & Fowler, N. R. (2024). Alzheimer disease blood biomarkers: Considerations for population-level use. Nature Reviews. Neurology, 20(8), 495–504. DOI: 10.1038/s41582-024-00989-1

Milstein, C. (1980). Monoclonal antibodies. Scientific American, 243(4), 66–74. DOI: 10.1038/scientificamerican1080-66

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., & Jagust, W. J. (2009). Episodic memory loss is related to hippocampal-mediated beta-amyloid deposition in elderly subjects. Brain, 132(Pt 5), 1310–1323. DOI: 10.1093/brain/awn320

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. DOI: 10.1016/0022-1759(83)90303-4

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. DOI: 10.1080/09168451.2014.940275

Muyldermans, S. (2013). Nanobodies: Natural single-domain antibodies. Annual Review of Biochemistry, 82, 775–797. DOI: 10.1146/annurev-biochem-063011-092449

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. DOI: 10.1007/s00401-007-0261-2

Nalivaeva, N. N., & Turner, A. J. (2013). The amyloid precursor protein: A biochemical enigma in brain development, function and disease. FEBS Letters, 587(13), 2046–2054. DOI: 10.1016/j.febslet.2013.05.010

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., & Benson, D. F. (1998). Frontotemporal lobar degeneration: A consensus on clinical diagnostic criteria. Neurology, 51(6), 1546–1554. DOI: 10.1212/wnl.51.6.1546

Nebes, R. D. (1989). Semantic memory in Alzheimer’s disease. Psychological Bulletin, 106(3), 377–394. DOI: 10.1037/0033-2909.106.3.377

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. DOI: 10.1016/j.bbamem.2013.10.019

Nikolaev, A., McLaughlin, T., O’Leary, D. D. M., & Tessier-Lavigne, M. (2009). APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature, 457(7232), 981–989. DOI: 10.1038/nature07767

Nisbet, R. M., Nigro, J., Breheney, K., Caine, J., Hattarki, M. K., & Nuttall, S. D. (2013). Central amyloid-β-specific single chain variable fragment ameliorates Aβ aggregation and neurotoxicity. Protein Engineering, Design & Selection, 26(10), 571–580. DOI: 10.1093/protein/gzt025

Nonaka, T., Masuda-Suzukake, M., & Hasegawa, M. (2018). Molecular mechanisms of the co-deposition of multiple pathological proteins in neurodegenerative diseases. Neuropathology, 38(1), 64–71. DOI: 10.1111/neup.12427

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., & Smith, M. A. (2001). Oxidative damage is the earliest event in Alzheimer disease. Journal of Neuropathology and Experimental Neurology, 60(8), 759–767. DOI: 10.1093/jnen/60.8.759

Nyhus, C., Pihl, M., Hyttel, P., & Hall, V. (2019). Evidence for nucleolar dysfunction in Alzheimer’s disease. Reviews in the Neurosciences, 30(7), 685–700. DOI: 10.1515/revneuro-2018-0104

Obregon, D., Hou, H., Deng, J., Giunta, B., Tian, J., Darlington, D., Shahaduzzaman, M., Zhu, Y., Mori, T., Mattson, M. P., & Tan, J. (2012). Soluble amyloid precursor protein-α modulates β-secretase activity and amyloid-β generation. Nature Communications, 3, 777. DOI: 10.1038/ncomms1781

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. DOI: 10.1038/s41380-020-0838-x

Olsson, B., Alberg, L., Cullen, N. C., Michael, E., Wahlgren, L., Kroksmark, A.-K., Rostasy, K., Blennow, K., Zetterberg, H., & Tulinius, M. (2019). NFL is a marker of treatment response in children with SMA treated with nusinersen. Journal of Neurology, 266(9), 2129–2136. DOI: 10.1007/s00415-019-09389-8

Olsson, B., Lautner, R., Andreasson, U., Öhrfelt, A., Portelius, E., Bjerke, M., Hölttä, M., Rosén, C., Olsson, C., Strobel, G., Wu, E., Dakin, K., Petzold, M., Blennow, K., & 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. DOI: 10.1016/S1474-4422(16)00070-3

Ossenkoppele, R., Rabinovici, G. D., Smith, R., Cho, H., Schöll, M., Strandberg, O., Palmqvist, S., Mattsson, N., Janelidze, S., Santillo, A., Ohlsson, T., Jögi, 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. DOI: 10.1001/jama.2018.12917

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. DOI: 10.1001/jamaneurol.2022.2909

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, & L. Santarelli. Archives of Neurology, 69(2):198-207 DOI: 10.1001/archneurol.2011.1538

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., & Bateman, R. J. (2017). Amyloid β concentrations and stable isotope labeling kinetics of human plasma specific to central nervous system amyloidosis. Alzheimer’s & Dementia, 13(8), 841–849. DOI: 10.1016/j.jalz.2017.06.2266

Pain, C., Dumont, J., & 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. DOI: 10.1016/j.biochi.2015.01.012

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. DOI: 10.1001/jama.2020.12134

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., Allué, 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 & Dementia (Amsterdam, Netherlands), 13(1), e12242. DOI: 10.1002/dad2.12242

Panza, F., Lozupone, M., Seripa, D., & Imbimbo, B. P. (2019). Amyloid-β immunotherapy for alzheimer disease: Is it now a long shot? Annals of Neurology, 85(3), 303–315. DOI: 10.1002/ana.25410

Paravastu, A. K., Leapman, R. D., Yau, W.-M., & 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. DOI: 10.1073/pnas.0806270105

Parker, W. D., Filley, C. M., & Parks, J. K. (1990). Cytochrome oxidase deficiency in Alzheimer’s disease. Neurology, 40(8), 1302–1303. DOI: 10.1212/wnl.40.8.1302

Perchiacca, J. M., Ladiwala, A. R. A., Bhattacharya, M., & 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. DOI: 10.1073/pnas.1111232108

Pereira, C., Santos, M. S., & Oliveira, C. (1998). Mitochondrial function impairment induced by amyloid beta-peptide on PC12 cells. Neuroreport, 9(8), 1749–1755. DOI: 10.1097/00001756-199806010-00015

Perrin, R. J., Fagan, A. M., & Holtzman, D. M. (2009). Multimodal techniques for diagnosis and prognosis of Alzheimer’s disease. Nature, 461(7266), 916–922. DOI: 10.1038/nature08538

Perry, R. J., & Hodges, J. R. (1999). Attention and executive deficits in Alzheimer’s disease. A critical review. Brain, 122 ( Pt 3), 383–404. DOI: 10.1093/brain/122.3.383

Peters, C., Espinoza, M. P., Gallegos, S., Opazo, C., & 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. DOI: 10.1016/j.neurobiolaging.2014.11.019

Pickford, F., Masliah, E., Britschgi, M., Lucin, K., Narasimhan, R., Jaeger, P. A., Small, S., Spencer, B., Rockenstein, E., Levine, B., & 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. DOI: 10.1172/JCI33585

Pietrzak, M., Rempala, G., Nelson, P. T., Zheng, J.-J., & Hetman, M. (2011). Epigenetic silencing of nucleolar rRNA genes in Alzheimer’s disease. PloS One, 6(7), e22585. DOI: 10.1371/journal.pone.0022585

Pollard, H. B., Rojas, E., & 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. DOI: 10.1111/j.1749-6632.1993.tb23044.x

Popugaeva, E., Pchitskaya, E., & Bezprozvanny, I. (2018). Dysregulation of Intracellular Calcium Signaling in Alzheimer’s Disease. Antioxidants & Redox Signaling, 29(12), 1176–1188. DOI: 10.1089/ars.2018.7506

Praticò, D. (2008). Oxidative stress hypothesis in Alzheimer’s disease: A reappraisal. Trends in Pharmacological Sciences, 29(12), 609–615. DOI: 10.1016/j.tips.2008.09.001

Rabinovici, G. D. (2019). Late-onset Alzheimer Disease. Continuum (Minneapolis, Minn.), 25(1), 14–33. DOI: 10.1212/CON.0000000000000700

Rai, S. N., Singh, C., Singh, A., Singh, M. P., & Singh, B. K. (2020). Mitochondrial Dysfunction: A Potential Therapeutic Target to Treat Alzheimer’s Disease. Molecular Neurobiology, 57(7), 3075–3088. DOI: 10.1007/s12035-020-01945-y

Rasmussen, M. K., Mestre, H., & Nedergaard, M. (2018). The glymphatic pathway in neurological disorders. The Lancet Neurology, 17(11), 1016–1024. DOI: 10.1016/S1474-4422(18)30318-1

Reed, B. R., Mungas, D., Farias, S. T., Harvey, D., Beckett, L., Widaman, K., Hinton, L., & DeCarli, C. (2010). Measuring cognitive reserve based on the decomposition of episodic memory variance. Brain, 133(Pt 8), 2196–2209. DOI: 10.1093/brain/awq154

Reese, L. C., & Taglialatela, G. A. (2011). Role for calcineurin in Alzheimer’s disease. Current Neuropharmacology, 9(4), 685–692. DOI: 10.2174/156802611798192661

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. DOI: 10.1016/S1474-4422(12)70228-4

Reiss, A. B., Arain, H. A., Stecker, M. M., Siegart, N. M., & Kasselman, L. J. (2018). Amyloid toxicity in Alzheimer’s disease. Reviews in the Neurosciences, 29(6), 613–627. DOI: 10.1515/revneuro-2017-0063

Relkin, N., Marmarou, A., Klinge, P., Bergsneider, M., & Black, P. M. (2005). Diagnosing idiopathic normal-pressure hydrocephalus. Neurosurgery, 57(3 Suppl), S4-16. DOI: 10.1227/01.neu.0000168185.29659.c5

Renner, J. A., Burns, J. M., Hou, C. E., McKeel, D. W., Storandt, M., & Morris, J. C. (2004). Progressive posterior cortical dysfunction: A clinicopathologic series. Neurology, 63(7), 1175–1180. DOI: 10.1212/01.wnl.0000140290.80962.bf

Revi, M. (2020). Alzheimer’s Disease Therapeutic Approaches. Advances in Experimental Medicine and Biology, 1195, 105–116. DOI: 10.1007/978-3-030-32633-3_15

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., & Duffy, D. C. (2010). Single-molecule enzyme-linked immunosorbent assay detects serum proteins at subfemtomolar concentrations. Nature Biotechnology, 28(6), 595–599. DOI: 10.1038/nbt.1641

Robertson, D. S. (2010). The physical chemistry of brain and neural cell membranes: An overview. Neurochemical Research, 35(5), 681–687. DOI: 10.1007/s11064-010-0121-7

Roychaudhuri, R., Yang, M., Hoshi, M. M., & Teplow, D. B. (2009). Amyloid beta-protein assembly and Alzheimer disease. Journal of Biological Chemistry, 284(8), 4749–4753. DOI: 10.1074/jbc.R800036200

Rudajev, V., & Novotny, J. (2020). The Role of Lipid Environment in Ganglioside GM1-Induced Amyloid β Aggregation. Membranes, 10(9), 226. DOI: 10.3390/membranes10090226

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., & 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. DOI: 10.1097/WAD.0000000000000034

Saido, T., & Leissring, M. A. (2012). Proteolytic degradation of amyloid β-protein. Cold Spring Harbor Perspectives in Medicine, 2(6), a006379. DOI: 10.1101/cshperspect.a006379

Saito, R., Kaneko, M., Kitamura, Y., Takata, K., Kawada, K., Okuma, Y., & 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. DOI: 10.1371/journal.pone.0094576

Saito, R., Kaneko, M., Okuma, Y., & 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. DOI: 10.1254/jphs.10118sc

Sajdel-Sulkowska, E. M., & Marotta, C. A. (1984). Alzheimer’s disease brain: Alterations in RNA levels and in a ribonuclease-inhibitor complex. Science, 225(4665), 947–949. DOI: 10.1126/science.6206567

Sakono, M., & Zako, T. (2010). Amyloid oligomers: Formation and toxicity of Abeta oligomers. The FEBS Journal, 277(6), 1348–1358. DOI: 10.1111/j.1742-4658.2010.07568.x

Samad, N., Ishaq, S., Bano, S., & 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.

Santoro, M. M. & 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). DOI: 10.1021/bi00421a014

Santos, A. N., Torkler, S., Nowak, D., Schlittig, C., Goerdes, M., Lauber, T., Trischmann, L., Schaupp, M., Penz, M., Tiller, F.-W., & Böhm, 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. DOI: 10.3233/jad-2007-11114

Santos, R. X., Correia, S. C., Wang, X., Perry, G., Smith, M. A., Moreira, P. I., & 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. DOI: 10.3233/JAD-2010-100666

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., & McCampbell, A. (2014). A sensitive aβ oligomer assay discriminates Alzheimer’s and aged control cerebrospinal fluid. Journal of Neuroscience, 34(8), 2884–2897. DOI: 10.1523/JNEUROSCI.1675-13.2014

Scalia, F., Vitale, A. M., Santonocito, R., Conway de Macario, E., Macario, A. J. L., & Cappello, F. (2021). The Neurochaperonopathies: Anomalies of the Chaperone System with Pathogenic Effects in Neurodegenerative and Neuromuscular Disorders. Applied Sciences, 11(3), 898. DOI: 10.3390/app11030898

Schengrund, C. L. (2010). Lipid rafts: Keys to neurodegeneration. Brain Research Bulletin, 82(1–2), 7–17. DOI: 10.1016/j.brainresbull.2010.02.013

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. DOI: 10.1038/nm0896-864

Schneider, J. A., Arvanitakis, Z., Bang, W., & Bennett, D. A. (2007). Mixed brain pathologies account for most dementia cases in community-dwelling older persons. Neurology, 69(24), 2197–2204. DOI: 10.1212/01.wnl.0000271090.28148.24

Schwab, C., Arai, T., Hasegawa, M., Yu, S., & 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. DOI: 10.1097/NEN.0b013e31818e8951

Sciacca, M. F. M., La Rosa, C., & Milardi, D. (2021). Amyloid-Mediated Mechanisms of Membrane Disruption. Biophysica, 1(2), 137-156. DOI: 10.3390/biophysica1020011

Selkoe, D. J. (1999). Translating cell biology into therapeutic advances in Alzheimer’s disease. Nature, 399(6738 Suppl), A23-31. DOI: 10.1038/399a023

Selkoe, D. J. (2019). Alzheimer disease and aducanumab: Adjusting our approach. Nature Reviews. Neurology, 15(7), 365–366. DOI: 10.1038/s41582-019-0205-1

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. DOI: 10.1016/j.ymthe.2022.11.002

Sengupta, U., Guerrero-Muñoz, M. J., Castillo-Carranza, D. L., Lasagna-Reeves, C. A., Gerson, J. E., Paulucci-Holthauzen, A. A., Krishnamurthy, S., Farhed, M., Jackson, G. R., & Kayed, R. (2015). Pathological interface between oligomeric alpha-synuclein and tau in synucleinopathies. Biological Psychiatry, 78(10), 672–683. DOI: 10.1016/j.biopsych.2014.12.019

Senjem, M. L., Gunter, J. L., Shiung, M. M., Petersen, R. C., & Jack, C. R. (2005). Comparison of different methodological implementations of voxel-based morphometry in neurodegenerative disease. NeuroImage, 26(2), 600–608. DOI: 10.1016/j.neuroimage.2005.02.005

Sevigny, J., Chiao, P., Bussière, 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. DOI: 10.1038/nature19323

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., & Alzheimer’s Disease Neuroimaging Initiative. (2009). Cerebrospinal fluid biomarker signature in Alzheimer’s disease neuroimaging initiative subjects. Annals of Neurology, 65(4), 403–413. DOI: 10.1002/ana.21610

Sheu, K. F., Cooper, A. J., Koike, K., Koike, M., Lindsay, J. G., & 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. DOI: 10.1002/ana.410350311

Sheu, K. F., Kim, Y. T., Blass, J. P., & Weksler, M. E. (1985). An immunochemical study of the pyruvate dehydrogenase deficit in Alzheimer’s disease brain. Annals of Neurology, 17(5), 444–449. DOI: 10.1002/ana.410170505

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., & Kinney, G. G. (2010). Anti-ADDL antibodies differentially block oligomer binding to hippocampal neurons. Neurobiology of Aging, 31(2), 189–202. DOI: 10.1016/j.neurobiolaging.2008.04.003

Simrén, J., Elmgren, A., Blennow, K., & Zetterberg, H. (2023). Fluid biomarkers in Alzheimer’s disease. Advances in Clinical Chemistry, 112, 249–281. DOI: 10.1016/bs.acc.2022.09.006

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., & TRAILBLAZER-ALZ 2 Investigators. (2023). Donanemab in Early Symptomatic Alzheimer Disease: The TRAILBLAZER-ALZ 2 Randomized Clinical Trial. JAMA, 330(6), 512–527. DOI: 10.1001/jama.2023.13239

Sims, R., Hill, M., & Williams, J. (2020). The multiplex model of the genetics of Alzheimer’s disease. Nature Neuroscience, 23(3), 311–322. DOI: 10.1038/s41593-020-0599-5

Singer, S. J., & Nicolson, G. L. (1972). The fluid mosaic model of the structure of cell membranes. Science, 175(4023), 720–731. DOI: 10.1126/science.175.4023.720

Singh, A., Kukreti, R., Saso, L., & Kukreti, S. (2019). Oxidative Stress: A Key Modulator in Neurodegenerative Diseases. Molecules, 24(8), 1583. DOI: 10.3390/molecules24081583

Somavarapu, A. K., & Kepp, K. P. (2015). The Dependence of Amyloid-β Dynamics on Protein Force Fields and Water Models. Chemphyschem, 16(15), 3278–3289. DOI: 10.1002/cphc.201500415

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., & Jung, Y.-K. (2003). Essential role of E2-25K/Hip-2 in mediating amyloid-beta neurotoxicity. Molecular Cell, 12(3), 553–563. DOI: 10.1016/j.molcel.2003.08.005

Sorbi, S., Bird, E. D., & Blass, J. P. (1983). Decreased pyruvate dehydrogenase complex activity in Huntington and Alzheimer brain. Annals of Neurology, 13(1), 72–78. DOI: 10.1002/ana.410130116

Sorbi, S., Nacmias, B., Forleo, P., Latorraca, S., Gobbini, I., Bracco, L., Piacentini, S., & Amaducci, L. (1994). ApoE allele frequencies in Italian sporadic and familial Alzheimer’s disease. Neuroscience Letters, 177(1–2), 100–102. DOI: 10.1016/0304-3940(94)90054-x

Sormanni, P., Aprile, F. A., & 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. DOI: 10.1073/pnas.1422401112

Sormanni, P., Aprile, F. A., & Vendruscolo, M. (2018). Third generation antibody discovery methods: In silico rational design. Chemical Society Reviews, 47(24), 9137–9157. DOI: 10.1039/c8cs00523k

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 & Dementia, 7(3), 280–292. DOI: 10.1016/j.jalz.2011.03.003

Stewart, M. D., Ritterhoff, T., Klevit, R. E., & Brzovic, P. S. (2016). E2 enzymes: More than just middle men. Cell Research, 26(4), 423. DOI: 10.1038/cr.2016.35

Strimbu, K., & Tavel, J. A. (2010). What are biomarkers? Current Opinion in HIV and AIDS, 5(6), 463–466. DOI: 10.1097/COH.0b013e32833ed177

Sunde, M., & Blake, C. (1997). The structure of amyloid fibrils by electron microscopy and X-ray diffraction. Advances in Protein Chemistry, 50, 123–159. DOI: 10.1016/s0065-3233(08)60320-4

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., & Fagan, A. M. (2015). Longitudinal Cerebrospinal Fluid Biomarker Changes in Preclinical Alzheimer Disease During Middle Age. JAMA Neurology, 72(9), 1029–1042. DOI: 10.1001/jamaneurol.2015.1285

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., & 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 & Therapy, 13(1), 80. DOI: 10.1186/s13195-021-00813-8

Sewell, R. D. E. (Ed.). (2007). Protein Misfolding in Neurodegenerative Diseases: Mechanisms and Therapeutic Strategies. CRC Press. DOI: 10.1201/9781420007145

Swerdlow, R. H. (2018). Mitochondria and Mitochondrial Cascades in Alzheimer’s Disease. Journal of Alzheimer’s Disease: JAD, 62(3), 1403–1416. DOI: 10.3233/JAD-170585

Taipale, M., Jarosz, D. F., & Lindquist, S. (2010). HSP90 at the hub of protein homeostasis: Emerging mechanistic insights. Nature Reviews. Molecular Cell Biology, 11(7), 515–528. DOI: 10.1038/nrm2918

Tcw, J., & Goate, A. M. (2017). Genetics of β-Amyloid Precursor Protein in Alzheimer’s Disease. Cold Spring Harbor Perspectives in Medicine, 7(6), a024539. DOI: 10.1101/cshperspect.a024539

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. DOI: 10.1016/S1474-4422(17)30470-2

Tokunaga, Y., & Takeuchi, K. (2020). Role of NMR in High Ordered Structure Characterization of Monoclonal Antibodies. International Journal of Molecular Sciences, 22(1), 46. DOI: 10.3390/ijms22010046

Toledo, J. B., Arnold, S. E., Raible, K., Brettschneider, J., Xie, S. X., Grossman, M., Monsell, S. E., Kukull, W. A., & 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. DOI: 10.1093/brain/awt188

Tu, S., Okamoto, S., Lipton, S. A., & Xu, H. (2014). Oligomeric Aβ-induced synaptic dysfunction in Alzheimer’s disease. Molecular Neurodegeneration, 9, 48. DOI: 10.1186/1750-1326-9-48

Twohig, D., & Nielsen, H. M. (2019). α-synuclein in the pathophysiology of Alzheimer’s disease. Molecular Neurodegeneration, 14(1), 23. DOI: 10.1186/s13024-019-0320-x

Vadukul, D. M., Papp, M., Thrush, R. J., Wang, J., Jin, Y., Arosio, P., & 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. DOI: 10.1021/jacs.3c03212

Valdor, R., Mocholi, E., Botbol, Y., Guerrero-Ros, I., Chandra, D., Koga, H., Gravekamp, C., Cuervo, A. M., & 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. DOI: 10.1038/ni.3003

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., & Iwatsubo, T. (2023). Lecanemab in Early Alzheimer’s Disease. The New England Journal of Medicine, 388(1), 9–21. DOI: 10.1056/NEJMoa2212948

Veerabhadrappa, B., Delaby, C., Hirtz, C., Vialaret, J., Alcolea, D., Lleó, A., Fortea, J., Santosh, M. S., Choubey, S., & 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. DOI: 10.1080/10408363.2019.1678011

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., & Jack, C. R. (2011). Cognitive reserve and Alzheimer’s disease biomarkers are independent determinants of cognition. Brain, 134(Pt 5), 1479–1492. DOI: 10.1093/brain/awr049

Vemuri, P., Wiste, H. J., Weigand, S. D., Shaw, L. M., Trojanowski, J. Q., Weiner, M. W., Knopman, D. S., Petersen, R. C., & Jack, C. R. (2009). MRI and CSF biomarkers in normal, MCI, and AD subjects: Predicting future clinical change. Neurology, 73(4), 294–301. DOI: 10.1212/WNL.0b013e3181af79fb

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, Å. 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 & Dementia, 15(7), 888–898. DOI: 10.1016/j.jalz.2019.04.001

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., & 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. DOI: 10.1016/S1474-4422(13)70044-9

Villemagne, V. L., Pike, K. E., Chételat, 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., & Rowe, C. C. (2011). Longitudinal assessment of Aβ and cognition in aging and Alzheimer disease. Annals of Neurology, 69(1), 181–192. DOI: 10.1002/ana.22248

Vivekanandan, S., Brender, J. R., Lee, S. Y., & 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. DOI: 10.1016/j.bbrc.2011.06.133

Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002). Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature, 416(6880), 535–539. DOI: 10.1038/416535a

Walsh, D. M., & Selkoe, D. J. (2004). Deciphering the molecular basis of memory failure in Alzheimer’s disease. Neuron, 44(1), 181–193. DOI: 10.1016/j.neuron.2004.09.010

Walsh, D. M., Tseng, B. P., Rydel, R. E., Podlisny, M. B., & Selkoe, D. J. (2000). The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain. Biochemistry, 39(35), 10831–10839. DOI: 10.1021/bi001048s

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., & 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. DOI: 10.1016/s0006-8993(01)03058-x

Wang, X., Wang, W., Li, L., Perry, G., Lee, H., & Zhu, X. (2014). Oxidative stress and mitochondrial dysfunction in Alzheimer’s disease. Biochimica Et Biophysica Acta, 1842(8), 1240–1247. DOI: 10.1016/j.bbadis.2013.10.015

Wasik, U., Schneider, G., Mietelska-Porowska, A., Mazurkiewicz, M., Fabczak, H., Weis, S., Zabke, C., Harrington, C. R., Filipek, A., & 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. DOI: 10.1016/j.neurobiolaging.2012.11.007

Wasmer, C., Lange, A., Van Melckebeke, H., Siemer, A. B., Riek, R., & 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. DOI: 10.1126/science.1151839

Weintraub, S., Wicklund, A. H., & Salmon, D. P. (2012). The neuropsychological profile of Alzheimer disease. Cold Spring Harbor Perspectives in Medicine, 2(4), a006171. DOI: 10.1101/cshperspect.a006171

Westermark, P. (2005). Aspects on human amyloid forms and their fibril polypeptides. The FEBS Journal, 272(23), 5942–5949. DOI: 10.1111/j.1742-4658.2005.05024.x

Westin, K., Buchhave, P., Nielsen, H., Minthon, L., Janciauskiene, S., & 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. DOI: 10.1371/journal.pone.0030525

Whitehouse, P. J., Orgogozo, J. M., Becker, R. E., Gauthier, S., Pontecorvo, M., Erzigkeit, H., Rogers, S., Mohs, R. C., Bodick, N., Bruno, G., & Dal-Bianco, P. (1997). Quality-of-life assessment in dementia drug development. Alzheimer Disease and Associated Disorders, 11 Suppl 3, 56–60.

Wiatrak, B., Piasny, J., Kuźniarski, A., & Gąsiorowski, K. (2021). Interactions of Amyloid-β with Membrane Proteins. International Journal of Molecular Sciences, 22(11), 6075. DOI: 10.3390/ijms22116075

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., & 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. DOI: 10.3233/JAD-180539

Wilkins, H. M., & Swerdlow, R. H. (2017). Amyloid precursor protein processing and bioenergetics. Brain Research Bulletin, 133, 71–79. DOI: 10.1016/j.brainresbull.2016.08.009

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., Jönsson, 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. DOI: 10.1016/S1474-4422(16)00062-4

Wojdała, A. L., Bellomo, G., Toja, A., Gaetani, L., Parnetti, L., & Chiasserini, D. (2024). CSF and plasma Aβ42/40 across Alzheimer’s disease continuum: Comparison of two ultrasensitive Simoa® assays targeting distinct amyloid regions. Clinical Chemistry and Laboratory Medicine, 62(2), 332–340. DOI: 10.1515/cclm-2023-0659

World Health Organization. (2021). Fact sheets of dementia. who.int

Yamamoto, N., Fukata, Y., Fukata, M., & Yanagisawa, K. (2007). GM1-ganglioside-induced Abeta assembly on synaptic membranes of cultured neurons. Biochimica Et Biophysica Acta, 1768(5), 1128–1137. DOI: 10.1016/j.bbamem.2007.01.009

Yamazaki, T., Koo, E. H., & 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. DOI: 10.1523/JNEUROSCI.17-03-01004.1997

Yanagisawa, K. (2007). Role of gangliosides in Alzheimer’s disease. Biochimica Et Biophysica Acta, 1768(8), 1943–1951. DOI: 10.1016/j.bbamem.2007.01.018

Yang, T., O’Malley, T. T., Kanmert, D., Jerecic, J., Zieske, L. R., Zetterberg, H., Hyman, B. T., Walsh, D. M., & Selkoe, D. J. (2015). A highly sensitive novel immunoassay specifically detects low levels of soluble Aβ oligomers in human cerebrospinal fluid. Alzheimer’s Research & Therapy, 7(1), 14. DOI: 10.1186/s13195-015-0100-y

Yerbury, J. J., & Wilson, M. R. (2010). Extracellular chaperones modulate the effects of Alzheimer’s patient cerebrospinal fluid on Abeta(1-42) toxicity and uptake. Cell Stress & Chaperones, 15(1), 115–121. DOI: 10.1007/s12192-009-0122-0

Yoshihara, T., Takiguchi, S., Kyuno, A., Tanaka, K., Kuba, S., Hashiguchi, S., Ito, Y., Hashimoto, T., Iwatsubo, T., Tsuyama, S., Nakashima, T., & 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. DOI: 10.1093/jb/mvm239

Young-Pearse, T. L., Chen, A. C., Chang, R., Marquez, C., & 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. DOI: 10.1186/1749-8104-3-15

Younkin, S. G. (1995). Evidence that A beta 42 is the real culprit in Alzheimer’s disease. Annals of Neurology, 37(3), 287–288. DOI: 10.1002/ana.410370303

Yu, Y. J., & Watts, R. J. (2013). Developing therapeutic antibodies for neurodegenerative disease. Neurotherapeutics, 10(3), 459–472. DOI: 10.1007/s13311-013-0187-4

Yuan, S., Zhou, G., & Xu, G. (2024). Translation machinery: The basis of translational control. Journal of Genetics and Genomics, 51(4), 367–378. DOI: 10.1016/j.jgg.2023.07.009

Yusakul, G., Sakamoto, S., Pongkitwitoon, B., Tanaka, H., & 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. DOI: 10.1080/09168451.2016.1156482

Zameer, A., Kasturirangan, S., Emadi, S., Nimmagadda, S. V., & 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. DOI: 10.1016/j.jmb.2008.09.068

Zampagni, M., Cascella, R., Casamenti, F., Grossi, C., Evangelisti, E., Wright, D., Becatti, M., Liguri, G., Mannini, B., Campioni, S., Chiti, F., & 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. DOI: 10.1111/j.1582-4934.2010.01239.x

Zandomeneghi, G., Krebs, M. R. H., McCammon, M. G., & Fändrich, M. (2004). FTIR reveals structural differences between native beta-sheet proteins and amyloid fibrils. Protein Science, 13(12), 3314–3321. DOI: 10.1110/ps.041024904

Zetterberg, H., & Bendlin, B. B. (2021). Biomarkers for Alzheimer’s disease-preparing for a new era of disease-modifying therapies. Molecular Psychiatry, 26(1), 296–308. DOI: 10.1038/s41380-020-0721-9

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., & Schott, J. M. (2020). Blood Tests for Alzheimer Disease. Practical Neurology. practicalneurology.com

Zha, J., Liu, X.-M., Zhu, J., Liu, S.-Y., Lu, S., Xu, P.-X., Yu, X.-L., & Liu, R.-T. (2016). A scFv antibody targeting common oligomeric epitope has potential for treating several amyloidoses. Scientific Reports, 6, 36631. DOI: 10.1038/srep36631

Zhao, Y., & Zhao, B. (2013). Oxidative stress and the pathogenesis of Alzheimer’s disease. Oxidative Medicine and Cellular Longevity, 2013, 316523. DOI: 10.1155/2013/316523

Zheng, F., Pang, Y., Li, L., Pang, Y., Zhang, J., Wang, X., & Raes, G. (2022). Applications of nanobodies in brain diseases. Frontiers in Immunology, 13, 978513. DOI: 10.3389/fimm u.2022.978513

Zhu, X., Perry, G., Smith, M. A., & Wang, X. (2013). Abnormal mitochondrial dynamics in the pathogenesis of Alzheimer’s disease. Journal of Alzheimer’s Disease: JAD, 33 Suppl 1, S253-262. DOI: 10.3233/JAD-2012-129005

A multidisciplinary approach for the early diagnosis of Alzheimer’s disease and potential therapeutic applications

Purchase

Bibliographic Information

News and Events

Views

Export Citation

Suggested Books

1,791

Books in the Catalogue

1,492

Open Access Books

3,300

Book Chapters

5,736,013

Fulltext
downloads

5,556

Authors

77

scientific boards

1,316

Referees

Catalogue

Scientific Cloud

Best Practice

A multidisciplinary approach for the early diagnosis of Alzheimer’s disease and potential therapeutic applications

Purchase

Bibliographic Information

News and Events

Views

Export Citation

Suggested Books

1,791

Books in the Catalogue

1,492

Open Access Books

3,300

Book Chapters

5,736,013

Fulltextdownloads

5,556

Authors

77

scientific boards

1,316

Referees

Fulltext
downloads