{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,9]],"date-time":"2026-09-09T11:51:25Z","timestamp":1788954685431,"version":"build-2803163510"},"reference-count":65,"publisher":"IMR Press","issue":"6","license":[{"start":{"date-parts":[[2023,11,6]],"date-time":"2023-11-06T00:00:00Z","timestamp":1699228800000},"content-version":"unspecified","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J. Integr. Neurosci."],"abstract":"<jats:p>Transthyretin (TTR) is secreted by hepatocytes, retinal pigment epithelial cells, pancreatic \u03b1 and \u03b2 cells, choroid plexus epithelium, and neurons under stress. The choroid plexus product is the main transporter of the thyroid hormone thyroxine (T4) to the brain during early development. TTR is one of three relatively abundant cerebrospinal fluid (CSF) proteins (Apolipoprotein J [ApoJ] (also known as clusterin), Apolipoprotein E [ApoE], and TTR) that interact with A\u03b2 peptides in vitro, in some instances inhibiting their aggregation and toxicity. It is now clear that clusterin functions as an extracellular, and perhaps intracellular, chaperone for many misfolded proteins and that variation in its gene (Clu) is associated with susceptibility to sporadic Alzheimer\u2019s disease (AD). The function of ApoE in AD is not yet completely understood, although the ApoE4 allele has the strongest genetic association with the development of sporadic late onset AD. Despite in vitro and in vivo evidence of the interaction between TTR and A\u03b2, genomewide association studies including large numbers of sporadic Alzheimer\u2019s disease patients have failed to show significant association between variation in the TTR gene and disease prevalence. Early clinical studies suggested an inverse relationship between CSF TTR levels and AD and the possibility of using the reduced CSF TTR concentration as a biomarker. Later, more extensive analyses indicated that CSF TTR concentrations may be increased in some patients with AD. While the observed changes in TTR may be pathogenetically or biologically interesting because of the inconsistency and lack of specificity, they offered no benefit diagnostically or prognostically either independently or when added to currently employed CSF biomarkers, i.e., decreased A\u03b21\u201342 and increased Tau and phospho-Tau. While some clinical data suggest that increases in CSF TTR may occur early in the disease with a significant decrease late in the course, without additional, more granular data, CSF TTR changes are neither consistent nor specific enough to warrant their use as a specific AD biomarker.<\/jats:p>","DOI":"10.31083\/j.jin2206158","type":"journal-article","created":{"date-parts":[[2023,11,9]],"date-time":"2023-11-09T08:45:55Z","timestamp":1699519555000},"source":"Crossref","is-referenced-by-count":8,"title":["The Role of CSF Transthyretin in Human Alzheimer's Disease: Offense, Defense, or not so Innocent Bystander"],"prefix":"10.31083","volume":"22","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5216-6414","authenticated-orcid":true,"given":"Joel N.","family":"Buxbaum","sequence":"first","affiliation":[{"name":"Scripps Research, La Jolla, CA 92037, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"16242","published-online":{"date-parts":[[2023,11,6]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","unstructured":"Kabat EA, Moore DH, Landow H. An electrophoretic study of the protein components in cerebrospinal fluid and their relationship to the serum proteins. The Journal of Clinical Investigation. 1942; 21: 571\u2013577.","DOI":"10.1172\/JCI101335"},{"key":"ref2","doi-asserted-by":"crossref","unstructured":"Ingbar SH. Pre-albumin: a thyroxinebinding protein of human plasma. Endocrinology. 1958; 63: 256\u2013259.","DOI":"10.1210\/endo-63-2-256"},{"key":"ref3","doi-asserted-by":"crossref","unstructured":"Nomenclature Committee of IUB (NC-IUB) IUB-IUPAC Joint Commission on Biochemical Nomenclature (JCBN). Newsletter 1981. The Journal of Biological Chemistry. 1981; 256: 12\u201314.","DOI":"10.1016\/S0021-9258(19)70086-6"},{"key":"ref4","doi-asserted-by":"crossref","unstructured":"Dickson PW, Schreiber G. High levels of messenger RNA for transthyretin (prealbumin) in human choroid plexus. Neuroscience Letters. 1986; 66: 311\u2013315.","DOI":"10.1016\/0304-3940(86)90037-6"},{"key":"ref5","doi-asserted-by":"crossref","unstructured":"Dickson PW, Aldred AR, Marley PD, Bannister D, Schreiber G. Rat choroid plexus specializes in the synthesis and the secretion of transthyretin (prealbumin). Regulation of transthyretin synthesis in choroid plexus is independent from that in liver. The Journal of Biological Chemistry. 1986; 261: 3475\u20133478.","DOI":"10.1016\/S0021-9258(17)35671-5"},{"key":"ref6","doi-asserted-by":"crossref","unstructured":"Costa RH, Lai E, Grayson DR, Darnell JE Jr. The cell-specific enhancer of the mouse transthyretin (prealbumin) gene binds a common factor at one site and a liver-specific factor(s) at two other sites. Molecular and Cellular Biology. 1988; 8: 81\u201390.","DOI":"10.1128\/mcb.8.1.81-90.1988"},{"key":"ref7","doi-asserted-by":"crossref","unstructured":"Herbert J, Wilcox JN, Pham KT, Fremeau RT Jr, Zeviani M, Dwork A, et al. Transthyretin: a choroid plexus-specific transport protein in human brain. The 1986 S. Weir Mitchell award. Neurology. 1986; 36: 900\u2013911.","DOI":"10.1212\/WNL.36.7.900"},{"key":"ref8","doi-asserted-by":"crossref","unstructured":"Wang X, Cattaneo F, Ryno L, Hulleman J, Reixach N, Buxbaum JN. The systemic amyloid precursor transthyretin (TTR) behaves as a neuronal stress protein regulated by HSF1 in SH-SY5Y human neuroblastoma cells and APP23 Alzheimer\u2019s disease model mice. The Journal of Neuroscience. 2014; 34: 7253\u20137265.","DOI":"10.1523\/JNEUROSCI.4936-13.2014"},{"key":"ref9","doi-asserted-by":"crossref","unstructured":"Elovaara I, Ic\u00e9n A, Palo J, Erkinjuntti T. CSF in Alzheimer\u2019s disease. Studies on blood-brain barrier function and intrathecal protein synthesis. Journal of the Neurological Sciences. 1985; 70: 73\u201380.","DOI":"10.1016\/0022-510X(85)90189-3"},{"key":"ref10","doi-asserted-by":"crossref","unstructured":"Elovaara I, Palo J, Erkinjuntti T, Sulkava R. Serum and cerebrospinal fluid proteins and the blood-brain barrier in Alzheimer\u2019s disease and multi-infarct dementia. European Neurology. 1987; 26: 229\u2013234.","DOI":"10.1159\/000116341"},{"key":"ref11","unstructured":"Blessed G, Tomlinson BE, Roth M. Blessed-Roth Dementia Scale (DS). Psychopharmacology Bulletin. 1988; 24: 705\u2013708."},{"key":"ref12","doi-asserted-by":"crossref","unstructured":"Riis\u00f8en H. Reduced prealbumin (transthyretin) in CSF of severely demented patients with Alzheimer\u2019s disease. Acta Neurologica Scandinavica. 1988; 78: 455\u2013459.","DOI":"10.1111\/j.1600-0404.1988.tb03687.x"},{"key":"ref13","unstructured":"Shirahama T, Skinner M, Westermark P, Rubinow A, Cohen AS, Brun A, et al. Senile cerebral amyloid. Prealbumin as a common constituent in the neuritic plaque, in the neurofibrillary tangle, and in the microangiopathic lesion. The American Journal of Pathology. 1982; 107: 41\u201350."},{"key":"ref14","doi-asserted-by":"crossref","unstructured":"Eikelenboom P, Stam FC. An immunohistochemical study on cerebral vascular and senile plaque amyloid in Alzheimer\u2019s dementia. Virchows Archiv. B, Cell Pathology Including Molecular Pathology. 1984; 47: 17\u201325.","DOI":"10.1007\/BF02890185"},{"key":"ref15","doi-asserted-by":"crossref","unstructured":"Glenner GG, Wong CW. Alzheimer\u2019s disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochemical and Biophysical Research Communications. 1984; 120: 885\u2013890.","DOI":"10.1016\/S0006-291X(84)80190-4"},{"key":"ref16","doi-asserted-by":"crossref","unstructured":"Wong CW, Quaranta V, Glenner GG. Neuritic plaques and cerebrovascular amyloid in Alzheimer disease are antigenically related. Proceedings of the National Academy of Sciences of the United States of America. 1985; 82: 8729\u20138732.","DOI":"10.1073\/pnas.82.24.8729"},{"key":"ref17","doi-asserted-by":"crossref","unstructured":"Masters CL, Simms G, Weinman NA, Multhaup G, McDonald BL, Beyreuther K. Amyloid plaque core protein in Alzheimer disease and Down syndrome. Proceedings of the National Academy of Sciences of the United States of America. 1985; 82: 4245\u20134249.","DOI":"10.1073\/pnas.82.12.4245"},{"key":"ref18","doi-asserted-by":"crossref","unstructured":"Hardy JA, Higgins GA. Alzheimer\u2019s disease: the amyloid cascade hypothesis. Science. 1992; 256: 184\u2013185.","DOI":"10.1126\/science.1566067"},{"key":"ref19","doi-asserted-by":"crossref","unstructured":"Hardy J, Selkoe DJ. The amyloid hypothesis of Alzheimer\u2019s disease: progress and problems on the road to therapeutics. Science. 2002; 297: 353\u2013356.","DOI":"10.1126\/science.1072994"},{"key":"ref20","doi-asserted-by":"crossref","unstructured":"Kosik KS, Joachim CL, Selkoe DJ. Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proceedings of the National Academy of Sciences of the United States of America. 1986; 83: 4044\u20134048.","DOI":"10.1073\/pnas.83.11.4044"},{"key":"ref21","doi-asserted-by":"crossref","unstructured":"Grundke-Iqbal I, Iqbal K, Quinlan M, Tung YC, Zaidi MS, Wisniewski HM. Microtubule-associated protein tau. A component of Alzheimer paired helical filaments. The Journal of Biological Chemistry. 1986; 261: 6084\u20136089.","DOI":"10.1016\/S0021-9258(17)38495-8"},{"key":"ref22","doi-asserted-by":"crossref","unstructured":"Strozyk D, Blennow K, White LR, Launer LJ. CSF Abeta 42 levels correlate with amyloid-neuropathology in a population-based autopsy study. Neurology. 2003; 60: 652\u2013656.","DOI":"10.1212\/01.WNL.0000046581.81650.D0"},{"key":"ref23","doi-asserted-by":"crossref","unstructured":"Vandermeeren M, Mercken M, Vanmechelen E, Six J, van de Voorde A, Martin JJ, et al. Detection of tau proteins in normal and Alzheimer\u2019s disease cerebrospinal fluid with a sensitive sandwich enzyme-linked immunosorbent assay. Journal of Neurochemistry. 1993; 61: 1828\u20131834.","DOI":"10.1111\/j.1471-4159.1993.tb09823.x"},{"key":"ref24","doi-asserted-by":"crossref","unstructured":"Blennow K, Wallin A, Agren H, Spenger C, Siegfried J, Vanmechelen E. Tau protein in cerebrospinal fluid: a biochemical marker for axonal degeneration in Alzheimer disease? Molecular and Chemical Neuropathology. 1995; 26: 231\u2013245.","DOI":"10.1007\/BF02815140"},{"key":"ref25","doi-asserted-by":"crossref","unstructured":"Wisniewski T, Castano E, Ghiso J, Frangione B. Cerebrospinal fluid inhibits Alzheimer beta-amyloid fibril formation in vitro. Annals of Neurology. 1993; 34: 631\u2013633.","DOI":"10.1002\/ana.410340422"},{"key":"ref26","doi-asserted-by":"crossref","unstructured":"Schwarzman AL, Gregori L, Vitek MP, Lyubski S, Strittmatter WJ, Enghilde JJ, et al. Transthyretin sequesters amyloid beta protein and prevents amyloid formation. Proceedings of the National Academy of Sciences of the United States of America. 1994; 91: 8368\u20138372.","DOI":"10.1073\/pnas.91.18.8368"},{"key":"ref27","doi-asserted-by":"crossref","unstructured":"Ghiso J, Matsubara E, Koudinov A, Choi-Miura NH, Tomita M, Wisniewski T, et al. The cerebrospinal-fluid soluble form of Alzheimer\u2019s amyloid beta is complexed to SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex. The Biochemical Journal. 1993; 293: 27\u201330.","DOI":"10.1042\/bj2930027"},{"key":"ref28","doi-asserted-by":"crossref","unstructured":"Wisniewski T, Golabek A, Matsubara E, Ghiso J, Frangione B. Apolipoprotein E: binding to soluble Alzheimer\u2019s beta-amyloid. Biochemical and Biophysical Research Communications. 1993; 192: 359\u2013365.","DOI":"10.1006\/bbrc.1993.1423"},{"key":"ref29","doi-asserted-by":"crossref","unstructured":"Adams D, Ando Y, Beir\u00e3o JM, Coelho T, Gertz MA, Gillmore JD, et al. Expert consensus recommendations to improve diagnosis of ATTR amyloidosis with polyneuropathy. Journal of Neurology. 2021; 268: 2109\u20132122.","DOI":"10.1007\/s00415-019-09688-0"},{"key":"ref30","doi-asserted-by":"crossref","unstructured":"Connors LH, Doros G, Sam F, Badiee A, Seldin DC, Skinner M. Clinical features and survival in senile systemic amyloidosis: comparison to familial transthyretin cardiomyopathy. Amyloid. 2011; 18: 157\u2013159.","DOI":"10.3109\/13506129.2011.574354059"},{"key":"ref31","doi-asserted-by":"crossref","unstructured":"Westermark GT, F\u00e4ndrich M, Lundmark K, Westermark P. Noncerebral Amyloidoses: Aspects on Seeding, Cross-Seeding, and Transmission. Cold Spring Harbor Perspectives in Medicine. 2018; 8: a024323.","DOI":"10.1101\/cshperspect.a024323"},{"key":"ref32","doi-asserted-by":"crossref","unstructured":"Serot JM, Christmann D, Dubost T, Couturier M. Cerebrospinal fluid transthyretin: aging and late onset Alzheimer\u2019s disease. Journal of Neurology, Neurosurgery, and Psychiatry. 1997; 63: 506\u2013508.","DOI":"10.1136\/jnnp.63.4.506"},{"key":"ref33","doi-asserted-by":"crossref","unstructured":"Kunicki S, Richardson J, Mehta PD, Kim KS, Zorychta E. The effects of age, apolipoprotein E phenotype and gender on the concentration of amyloid-beta (A beta) 40, A beta 42, apolipoprotein E and transthyretin in human cerebrospinal fluid. Clinical Biochemistry. 1998; 31: 409\u2013415.","DOI":"10.1016\/S0009-9120(98)00027-7"},{"key":"ref34","doi-asserted-by":"crossref","unstructured":"Davidsson P, Ekman R, Blennow K. A new procedure for detecting brain-specific proteins in cerebrospinal fluid. Journal of Neural Transmission. 1997; 104: 711\u2013720.","DOI":"10.1007\/BF01291888"},{"key":"ref35","doi-asserted-by":"crossref","unstructured":"Merched A, Serot JM, Visvikis S, Aguillon D, Faure G, Siest G. Apolipoprotein E, transthyretin and actin in the CSF of Alzheimer\u2019s patients: relation with the senile plaques and cytoskeleton biochemistry. FEBS Letters. 1998; 425: 225\u2013228.","DOI":"10.1016\/S0014-5793(98)00234-8"},{"key":"ref36","doi-asserted-by":"crossref","unstructured":"Gloeckner SF, Meyne F, Wagner F, Heinemann U, Krasnianski A, Meissner B, et al. Quantitative analysis of transthyretin, tau and amyloid-beta in patients with dementia. Journal of Alzheimer\u2019s Disease. 2008; 14: 17\u201325.","DOI":"10.3233\/JAD-2008-14102"},{"key":"ref37","doi-asserted-by":"crossref","unstructured":"Hansson SF, Andr\u00e9asson U, Wall M, Skoog I, Andreasen N, Wallin A, et al. Reduced levels of amyloid-beta-binding proteins in cerebrospinal fluid from Alzheimer\u2019s disease patients. Journal of Alzheimer\u2019s Disease. 2009; 16: 389\u2013397.","DOI":"10.3233\/JAD-2009-0966"},{"key":"ref38","doi-asserted-by":"crossref","unstructured":"Davidsson P, Westman-Brinkmalm A, Nilsson CL, Lindbjer M, Paulson L, Andreasen N, et al. Proteome analysis of cerebrospinal fluid proteins in Alzheimer patients. Neuroreport. 2002; 13: 611\u2013615.","DOI":"10.1097\/00001756-200204160-00015"},{"key":"ref39","doi-asserted-by":"crossref","unstructured":"Puchades M, Hansson SF, Nilsson CL, Andreasen N, Blennow K, Davidsson P. Proteomic studies of potential cerebrospinal fluid protein markers for Alzheimer\u2019s disease. Brain Research. Molecular Brain Research. 2003; 118: 140\u2013146.","DOI":"10.1016\/j.molbrainres.2003.08.005"},{"key":"ref40","doi-asserted-by":"crossref","unstructured":"Casta\u00f1o EM, Roher AE, Esh CL, Kokjohn TA, Beach T. Comparative proteomics of cerebrospinal fluid in neuropathologically-confirmed Alzheimer\u2019s disease and non-demented elderly subjects. Neurological Research. 2006; 28: 155\u2013163.","DOI":"10.1179\/016164106X98035"},{"key":"ref41","doi-asserted-by":"crossref","unstructured":"Roher AE, Maarouf CL, Sue LI, Hu Y, Wilson J, Beach TG. Proteomics-derived cerebrospinal fluid markers of autopsy-confirmed Alzheimer\u2019s disease. Biomarkers. 2009; 14: 493\u2013501.","DOI":"10.3109\/13547500903108423"},{"key":"ref42","doi-asserted-by":"crossref","unstructured":"Maarouf CL, Andacht TM, Kokjohn TA, Casta\u00f1o EM, Sue LI, Beach TG, et al. Proteomic analysis of Alzheimer\u2019s disease cerebrospinal fluid from neuropathologically diagnosed subjects. Current Alzheimer Research. 2009; 6: 399\u2013406.","DOI":"10.2174\/156720509788929318"},{"key":"ref43","doi-asserted-by":"crossref","unstructured":"Jung SM, Lee K, Lee JW, Namkoong H, Kim HK, Kim S, et al. Both plasma retinol-binding protein and haptoglobin precursor allele 1 in CSF: candidate biomarkers for the progression of normal to mild cognitive impairment to Alzheimer\u2019s disease. Neuroscience Letters. 2008; 436: 153\u2013157.","DOI":"10.1016\/j.neulet.2008.03.010"},{"key":"ref44","doi-asserted-by":"crossref","unstructured":"Perrin RJ, Craig-Schapiro R, Malone JP, Shah AR, Gilmore P, Davis AE, et al. Identification and validation of novel cerebrospinal fluid biomarkers for staging early Alzheimer\u2019s disease. PLoS ONE. 2011; 6: e16032.","DOI":"10.1371\/journal.pone.0016032"},{"key":"ref45","doi-asserted-by":"crossref","unstructured":"Wildsmith KR, Schauer SP, Smith AM, Arnott D, Zhu Y, Haznedar J, et al. Identification of longitudinally dynamic biomarkers in Alzheimer\u2019s disease cerebrospinal fluid by targeted proteomics. Molecular Neurodegeneration. 2014; 9: 22.","DOI":"10.1186\/1750-1326-9-22"},{"key":"ref46","doi-asserted-by":"crossref","unstructured":"Wang J, Cunningham R, Zetterberg H, Asthana S, Carlsson C, Okonkwo O, et al. Label-free quantitative comparison of cerebrospinal fluid glycoproteins and endogenous peptides in subjects with Alzheimer\u2019s disease, mild cognitive impairment, and healthy individuals. Proteomics. Clinical Applications. 2016; 10: 1225\u20131241.","DOI":"10.1002\/prca.201600009"},{"key":"ref47","doi-asserted-by":"crossref","unstructured":"Schultz K, Nilsson K, Nielsen JE, Lindquist SG, Hjermind LE, Andersen BB, et al. Transthyretin as a potential CSF biomarker for Alzheimer\u2019s disease and dementia with Lewy bodies: effects of treatment with cholinesterase inhibitors. European Journal of Neurology. 2010; 17: 456\u2013460.","DOI":"10.1111\/j.1468-1331.2009.02841.x"},{"key":"ref48","doi-asserted-by":"crossref","unstructured":"Heywood WE, Galimberti D, Bliss E, Sirka E, Paterson RW, Magdalinou NK, et al. Identification of novel CSF biomarkers for neurodegeneration and their validation by a high-throughput multiplexed targeted proteomic assay. Molecular Neurodegeneration. 2015; 10: 64.","DOI":"10.1186\/s13024-015-0059-y"},{"key":"ref49","doi-asserted-by":"crossref","unstructured":"Alzate O, Osorio C, DeKroon RM, Corcimaru A, Gunawardena HP. Differentially charged isoforms of apolipoprotein E from human blood are potential biomarkers of Alzheimer\u2019s disease. Alzheimer\u2019s Research & Therapy. 2014; 6: 43.","DOI":"10.1186\/alzrt273"},{"key":"ref50","doi-asserted-by":"crossref","unstructured":"Biroccio A, Del Boccio P, Panella M, Bernardini S, Di Ilio C, Gambi D, et al. Differential post-translational modifications of transthyretin in Alzheimer\u2019s disease: a study of the cerebral spinal fluid. Proteomics. 2006; 6: 2305\u20132313.","DOI":"10.1002\/pmic.200500285"},{"key":"ref51","doi-asserted-by":"crossref","unstructured":"Poulsen K, Bahl JM, Simonsen AH, Hasselbalch SG, Heegaard NH. Distinct transthyretin oxidation isoform profile in spinal fluid from patients with Alzheimer\u2019s disease and mild cognitive impairment. Clinical Proteomics. 2014; 11: 12.","DOI":"10.1186\/1559-0275-11-12"},{"key":"ref52","doi-asserted-by":"crossref","unstructured":"Korolainen MA, Nyman TA, Nyyss\u00f6nen P, Hartikainen ES, Pirttil\u00e4 T. Multiplexed proteomic analysis of oxidation and concentrations of cerebrospinal fluid proteins in Alzheimer disease. Clinical Chemistry. 2007; 53: 657\u2013665.","DOI":"10.1373\/clinchem.2006.078014"},{"key":"ref53","doi-asserted-by":"crossref","unstructured":"Bastos P, Ferreira R, Manadas B, Moreira PI, Vitorino R. Insights into the human brain proteome: Disclosing the biological meaning of protein networks in cerebrospinal fluid. Critical Reviews in Clinical Laboratory Sciences. 2017; 54: 185\u2013204.","DOI":"10.1080\/10408363.2017.1299682"},{"key":"ref54","doi-asserted-by":"crossref","unstructured":"Portelius E, Brinkmalm G, Pannee J, Zetterberg H, Blennow K, Dahl\u00e9n R, et al. Proteomic studies of cerebrospinal fluid biomarkers of Alzheimer\u2019s disease: an update. Expert Review of Proteomics. 2017; 14: 1007\u20131020.","DOI":"10.1080\/14789450.2017.1384697"},{"key":"ref55","doi-asserted-by":"crossref","unstructured":"Pedrero-Prieto CM, Garc\u00eda-Carpintero S, Fronti\u00f1\u00e1n-Rubio J, Llanos-Gonz\u00e1lez E, Aguilera Garc\u00eda C, Alca\u00edn FJ, et al. A comprehensive systematic review of CSF proteins and peptides that define Alzheimer\u2019s disease. Clinical Proteomics. 2020; 17: 21.","DOI":"10.1186\/s12014-020-09276-9"},{"key":"ref56","doi-asserted-by":"crossref","unstructured":"Simr\u00e9n J, Leuzy A, Karikari TK, Hye A, Benedet AL, Lantero-Rodriguez J, et al. The diagnostic and prognostic capabilities of plasma biomarkers in Alzheimer\u2019s disease. Alzheimer\u2019s & Dementia. 2021; 17: 1145\u20131156.","DOI":"10.1002\/alz.12283"},{"key":"ref57","doi-asserted-by":"crossref","unstructured":"Simr\u00e9n J, Elmgren A, Blennow K, Zetterberg H. Fluid biomarkers in Alzheimer\u2019s disease. Advances in Clinical Chemistry. 2023; 112: 249\u2013281.","DOI":"10.1016\/bs.acc.2022.09.006"},{"key":"ref58","doi-asserted-by":"crossref","unstructured":"Li X, Masliah E, Reixach N, Buxbaum JN. Neuronal production of transthyretin in human and murine Alzheimer\u2019s disease: is it protective? The Journal of Neuroscience. 2011; 31: 12483\u201312490.","DOI":"10.1523\/JNEUROSCI.2417-11.2011"},{"key":"ref59","doi-asserted-by":"crossref","unstructured":"Li X, Zhang X, Ladiwala ARA, Du D, Yadav JK, Tessier PM, et al. Mechanisms of transthyretin inhibition of \u03b2-amyloid aggregation in vitro. The Journal of Neuroscience. 2013; 33: 19423\u201319433.","DOI":"10.1523\/JNEUROSCI.2561-13.2013"},{"key":"ref60","doi-asserted-by":"crossref","unstructured":"Pate KM, Kim BJ, Shusta EV, Murphy RM. Transthyretin Mimetics as Anti-\u03b2-Amyloid Agents: A Comparison of Peptide and Protein Approaches. ChemMedChem. 2018; 13: 968\u2013979.","DOI":"10.1002\/cmdc.201800031"},{"key":"ref61","doi-asserted-by":"crossref","unstructured":"Ghadami SA, Chia S, Ruggeri FS, Meisl G, Bemporad F, Habchi J, et al. Transthyretin Inhibits Primary and Secondary Nucleations of Amyloid-\u03b2 Peptide Aggregation and Reduces the Toxicity of Its Oligomers. Biomacromolecules. 2020; 21: 1112\u20131125.","DOI":"10.1021\/acs.biomac.9b01475"},{"key":"ref62","doi-asserted-by":"crossref","unstructured":"Nilsson L, Pamr\u00e9n A, Islam T, Br\u00e4nnstr\u00f6m K, Golchin SA, Pettersson N, et al. Transthyretin Interferes with A\u03b2 Amyloid Formation by Redirecting Oligomeric Nuclei into Non-Amyloid Aggregates. Journal of Molecular Biology. 2018; 430: 2722\u20132733.","DOI":"10.1016\/j.jmb.2018.06.005"},{"key":"ref63","doi-asserted-by":"crossref","unstructured":"Silva CS, Eira J, Ribeiro CA, Oliveira \u00c2, Sousa MM, Cardoso I, et al. Transthyretin neuroprotection in Alzheimer\u2019s disease is dependent on proteolysis. Neurobiology of Aging. 2017; 59: 10\u201314.","DOI":"10.1016\/j.neurobiolaging.2017.07.002"},{"key":"ref64","doi-asserted-by":"crossref","unstructured":"Buxbaum JN, Ye Z, Reixach N, Friske L, Levy C, Das P, et al. Transthyretin protects Alzheimer\u2019s mice from the behavioral and biochemical effects of Abeta toxicity. Proceedings of the National Academy of Sciences of the United States of America. 2008; 105: 2681\u20132686.","DOI":"10.1073\/pnas.0712197105"},{"key":"ref65","doi-asserted-by":"crossref","unstructured":"Stein TD, Anders NJ, DeCarli C, Chan SL, Mattson MP, Johnson JA. Neutralization of transthyretin reverses the neuroprotective effects of secreted amyloid precursor protein (APP) in APPSW mice resulting in tau phosphorylation and loss of hippocampal neurons: support for the amyloid hypothesis. 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