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Neuroprotective natural antibodies to assemblies of amyloidogenic peptides decrease with normal aging and advancing Alzheimer's disease
Open accessAbstract
A number of distinct β-amyloid (Aβ) variants or multimers have been implicated in Alzheimer's disease (AD), and antibodies recognizing such peptides are in clinical trials. Humans have natural Aβ-specific antibodies, but their diversity, abundance, and function in the general population remain largely unknown. Here, we demonstrate with peptide microarrays the presence of natural antibodies against known toxic Aβ and amyloidogenic non-Aβ species in plasma samples and cerebrospinal fluid of AD patients and healthy controls aged 21–89 years. Antibody reactivity was most prominent against oligomeric assemblies of Aβ and pyroglutamate or oxidized residues, and IgGs specific for oligomeric preparations of Aβ1-42 in particular declined with age and advancing AD. Most individuals showed unexpected antibody reactivities against peptides unique to autosomal dominant forms of dementia (mutant Aβ, ABri, ADan) and IgGs isolated from plasma of AD patients or healthy controls protected primary neurons from Aβ toxicity. Aged vervets showed similar patterns of plasma IgG antibodies against amyloid peptides, and after immunization with Aβ the monkeys developed high titers not only against Aβ peptides but also against ABri and ADan peptides. Our findings support the concept of conformation-specific, cross-reactive antibodies that may protect against amyloidogenic toxic peptides. If a therapeutic benefit of Aβ antibodies can be confirmed in AD patients, stimulating the production of such neuroprotective antibodies or passively administering them to the elderly population may provide a preventive measure toward AD.
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“their level inversely correlate with the number of amyloid plaques [97,98].”
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“These antibodies to toxic forms of A β are present in the plasma and CSF of patients and healthy controls”
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1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
RetractedRegularization and Variable Selection Via the Elastic Net
Zou, H., & Hastie, T. (2005) · Journal of the Royal Statistical Society Series B: Statistical Methodology · doi:10.1111/j.1467-9868.2005.00503.x · Cited by 20,957
Cluster analysis and display of genome-wide expression patterns
Eisen, M. B., Spellman, P. T., Brown, P. O., & Botstein, D. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.25.14863 · Cited by 16,184
In silico prediction of protein-protein interactions in human macrophages
Souiai, O., Guerfali, F. Z., Miled, S. B., Brun, C., & Benkahla, A. (2014) · BMC Research Notes · doi:10.1186/1756-0500-7-157 · Cited by 10,785
Significance analysis of microarrays applied to the ionizing radiation response
Tusher, V. G., Tibshirani, R., & Chu, G. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.091062498 · Cited by 10,568
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160
Java Treeview—extensible visualization of microarray data
Saldanha, A. J. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bth349 · Cited by 2,991
Holmes, C., Boche, D., Wilkinson, D., Yadegarfar, G., Hopkins, V., Bayer, A., Jones, R. W., Bullock, R., Love, S., Neal, J. W., et al. (2008) · The Lancet · doi:10.1016/s0140-6736(08)61075-2 · Cited by 1,416
Amyloid pores from pathogenic mutations
Lashuel, H. A., Hartley, D. M., Petre, B. M., Walz, T., & Lansbury, P. T. (2002) · Nature · doi:10.1038/418291a · Cited by 1,307
DeMattos, R. B., Bales, K. R., Cummins, D. J., Dodart, J.-C., Paul, S. M., & Holtzman, D. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151261398 · Cited by 1,298
Self-citationClassification and prediction of clinical Alzheimer's diagnosis based on plasma signaling proteins
Ray, S., Britschgi, M., Herbert, C., Takeda-Uchimura, Y., Boxer, A., Blennow, K., Friedman, L. F., Galasko, D. R., Jutel, M., Karydas, A., et al. (2007) · Nature Medicine · doi:10.1038/nm1653 · Cited by 1,048
Self-citationIn vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
Stine, W. B., Dahlgren, K. N., Krafft, G. A., & LaDu, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210207200 · Cited by 1,015
Amyloid ion channels: A common structural link for protein-misfolding disease
Quist, A. P., Doudevski, I., Lin, H., Azimova, R., Ng, D., Frangione, B., Kagan, B. L., Ghiso, J. A., & Lal, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502066102 · Cited by 985
Self-citationAntibodies against β-Amyloid Slow Cognitive Decline in Alzheimer's Disease
Höck, C., Konietzko, U., Streffer, J. R., Tracy, J., Signorell, A., Müller-Tillmanns, B., Lemke, U., Henke, K., Moritz, E., Garcia, E., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00294-0 · Cited by 786
Autoantigen microarrays for multiplex characterization of autoantibody responses
Robinson, W. H., DiGennaro, C., Hueber, W., Haab, B. B., Kamachi, M., Dean, E. J., Fournel, S., Fong, D., Genovese, M. C., de Vegvar, H. E. N., et al. (2002) · Nature Medicine · doi:10.1038/nm0302-295 · Cited by 673
Self-citationSaido, T. C., Iwatsubo, T., Mann, D. M. A., Shimada, H., Ihara, Y., & Kawashima, S. (1995) · Neuron · doi:10.1016/0896-6273(95)90301-1 · Cited by 587
Cerebral Hemorrhage After Passive Anti-Aβ Immunotherapy
Pfeifer, M., Boncristiano, S., Bondolfi, L., Stalder, A., Deller, T., Staufenbiel, M., Mathews, P. M., & Jucker, M. (2002) · Science · doi:10.1126/science.1078259 · Cited by 511
Mass spectrometry of purified amyloid beta protein in Alzheimer's disease.
Mori, H., Takio, K., OGAWARA, M., & Selkoe, D. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41896-0 · Cited by 486
Autoreactivity in Human IgG+ Memory B Cells
Tiller, T., Tsuiji, M., Yurasov, S., Velinzon, K., Nussenzweig, M. C., & Wardemann, H. (2007) · Immunity · doi:10.1016/j.immuni.2007.01.009 · Cited by 477
Näslund, J., Schierhorn, A., Hellman, U., Lannfelt, L., Roses, A. D., Tjernberg, L. O., Silberring, J., Gandy, S. E., Winblad, B., & Greengard, P. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8378 · Cited by 468
A stop-codon mutation in the BRI gene associated with familial British dementia
Vidal, R., Frangione, B., Rostagno, A., Mead, S., Révész, T., Plant, G., & Ghiso, J. (1999) · Nature · doi:10.1038/21637 · Cited by 466
Self-citationSparks, D. L., & Schreurs, B. G. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1832769100 · Cited by 455
McLaurin, J., Cecal, R., Kierstead, M. E., Tian, X., Phinney, A. L., Manea, M., French, J. E., Lambermon, M. H. L., Darabie, A. A., Brown, M. E., et al. (2002) · Nature Medicine · doi:10.1038/nm790 · Cited by 415
Bard, F., Barbour, R., Cannon, C., Carretto, R., Fox, M., Games, D., Guido, T., Hoenow, K., Hu, K., Johnson-Wood, K., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0436286100 · Cited by 411
Copper Mediates Dityrosine Cross-Linking of Alzheimer's Amyloid-β
Atwood, C., Perry, G. L., Zeng, H., Kato, Y., Jones, W. D., Ling, K.-Q., Huang, X., Moir, R. D., Wang, D., Sayre, L. M., et al. (2003) · Biochemistry · doi:10.1021/bi0358824 · Cited by 371
Different Mechanisms of Oxidative Stress and Neurotoxicity for Alzheimer‘s Aβ(1−42) and Aβ(25−35)
Varadarajan, S., Kanski, J., Aksenova, M., Lauderback, C., & Butterfield, D. A. (2001) · Journal of the American Chemical Society · doi:10.1021/ja010452r · Cited by 346
18-Month study of intravenous immunoglobulin for treatment of mild Alzheimer disease
Relkin, N. R., Szabo, P., Adamiak, B., Burgut, T., Monthé, C., Lent, R. W., Younkin, S. G., Younkin, L. H., Schiff, R. I., & Weksler, M. E. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.12.021 · Cited by 305
Wilcock, D. M., Rojiani, A. M., Rosenthal, A., Levkowitz, G., Subbarao, S., Alamed, J., Wilson, D. H., Wilson, N., Freeman, M. J., Gordon, M. N., et al. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1090-04.2004 · Cited by 302
Vidal, R., Révész, T., Rostagno, A., Kim, E., Holton, J. L., Bek, T., Bojsen-Møller, M., Braendgaard, H., Plant, G., Ghiso, J., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.080076097 · Cited by 300
Self-citationOn the Seeding and Oligomerization of pGlu-Amyloid Peptides (in vitro)
Schilling, S., Lauber, T., Schaupp, M., Manhart, S., Scheel, E., Böhm, G., & Demuth, H.-U. (2006) · Biochemistry · doi:10.1021/bi0612667 · Cited by 254
Iwatsubo, T., Saido, T. C., Mann, D. M. A., Lee, V. M.-Y., & Trojanowski, J. Q. (1996) · Europe PMC (PubMed Central) · Cited by 248
Quintana, F. J., Farez, M., Viglietta, V., Iglesias, A. H., Merbl, Y., Izquierdo, G., Lucas, M., Basso, A. S., Khoury, S. J., Lucchinetti, C. F., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806310105 · Cited by 243
Reduced levels of amyloid β-peptide antibody in Alzheimer disease
Du, Y., Dodel, R. C., Hampel, H. J., Büerger, K., Lin, S., Eastwood, B. J., Bales, K. R., Gao, F., Moeller, H. –., Oertel, W. H., et al. (2001) · Neurology · doi:10.1212/wnl.57.5.801 · Cited by 236
Lemere, C. A., Beierschmitt, A., Iglesias, M., Spooner, E. T., Bloom, J. K., Leverone, J. F., Zheng, J. B., Seabrook, T. J., Louard, D., Li, D., et al. (2004) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63296-8 · Cited by 230
Self-citationPodlisny, M. B., Tolan, D. R., & Selkoe, D. J. (1991) · PubMed Central · Cited by 217
Systemic Catabolism of Alzheimer's Aβ40 and Aβ42
Ghiso, J., Shayo, M., Calero, M., Ng, D., Tomidokoro, Y., Gandy, S., Rostagno, A., & Frangione, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407668200 · Cited by 209
Self-citationLevites, Y. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25410 · Cited by 209
Russo, C., Violani, E., Salis, S., Venezia, V., Dolcini, V., Damonte, G., Benatti, U., D’Arrigo, C., Patrone, E., Carlo, P., et al. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01107.x · Cited by 204
Weksler, M. E., Relkin, N. R., Turkenich, R., LaRusse, S., Zhou, L., & Szabo, P. (2002) · Experimental Gerontology · doi:10.1016/s0531-5565(02)00029-3 · Cited by 200
β-Amyloid Is Different in Normal Aging and in Alzheimer Disease
Piccini, A., Russo, C., Gliozzi, A., Relini, A., Vitali, A., Borghi, R., Giliberto, L., Armirotti, A., D’Arrigo, C., Bachi, A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501694200 · Cited by 192
Barnham, K. J., Ciccotosto, G. D., Tickler, A. K., Ali, F. E. A., Smith, D. G., Williamson, N. A., Lam, Y.-H., Carrington, D., Tew, D. J., Kocak, G., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305494200 · Cited by 191
Naturally occurring auto-antibodies in homeostasis and disease
Lutz, H. U., Binder, C. J., & Kaveri, S. V. (2008) · Trends in Immunology · doi:10.1016/j.it.2008.10.002 · Cited by 182
Kuo, Y.-M., Emmerling, M. R., Woods, A. S., Cotter, R. J., & Roher, A. E. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7083 · Cited by 178
β-Amyloid Immunotherapy Prevents Synaptic Degeneration in a Mouse Model of Alzheimer's Disease
Buttini, M., Masliah, E., Barbour, R., Grajeda, H., Motter, R., Johnson-Wood, K., Khan, K., Seubert, P., Freedman, S., Schenk, D., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1697-05.2005 · Cited by 176
Peripheral clearance of amyloid β peptide by complement C3-dependent adherence to erythrocytes
Rogers, J., Li, R., Mastroeni, D., Grover, A., Leonard, B., Ahern, G., Cao, P., Kolody, H., Vedders, L., Kolb, W. P., et al. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.09.043 · Cited by 175
RECIPROCAL CHANGE WITH AGE IN ANTIBODY TO EXTRINSIC AND INTRINSIC ANTIGENS
Rowley, M. J., Buchanan, H., & Mackay, I. R. (1968) · The Lancet · doi:10.1016/s0140-6736(68)92893-6 · Cited by 170
ENZYMATIC OR PHARMACOLOGICAL FIBRINOLYSIS?
Marshall, M. (1964) · PubMed · Cited by 154
Autoantibodies to amyloid-? and Alzheimer's disease
Hyman, B. T., Smith, C. R., Buldyrev, I., Whelan, C. M., Brown, H., Tang, M., & Mayeux, R. P. (2001) · Annals of Neurology · doi:10.1002/ana.1061 · Cited by 144
Insights into the mechanisms of action of anti‐Aβ antibodies in Alzheimer's disease mouse models
Levites, Y., Smithson, L. A., Price, R. W., Dakin, R. S., Yuan, B., Sierks, M. R., Kim, J., McGowan, E., Kim Reed, D., Rosenberry, T. L., et al. (2006) · The FASEB Journal · doi:10.1096/fj.06-6463fje · Cited by 113
Алексеевна, Г. М., Davidova, T. B., Mališauskas, M., Sewell, R. D. E., Voskresenskaya, N. I., Wilhelm, K., Elistratova, E. I., Sherstnev, V. V., & Morozova‐Roche, L. A. (2007) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2007.03.023 · Cited by 112
Natural human antibodies to amyloid beta peptide
Szabo, P., Relkin, N. R., & Weksler, M. E. (2008) · Autoimmunity Reviews · doi:10.1016/j.autrev.2008.03.007 · Cited by 109
Nath, A., Hall, E., Tuzova, M., Dobbs, M., Jones, M., Anderson, C., Woodward, J. G., Guo, Z., Fu, W., Kryscio, R. J., et al. (2003) · NeuroMolecular Medicine · doi:10.1385/nmm:3:1:29 · Cited by 107
Mamikonyan, G., Necula, M., Mkrtichyan, M., Ghochikyan, A., Petrushina, I., Movsesyan, N., Mina, E. W., Kiyatkin, A. B., Glabe, C. G., Cribbs, D. H., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700088200 · Cited by 95
Moir, R. D., Tseitlin, K. A., Soscia, S. J., Hyman, B. T., Irizarry, M. C., & Tanzi, R. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414176200 · Cited by 88
Human antibodies reactive with beta-amyloid protein in Alzheimer's disease.
Gaskin, F., Finley, J., Fang, Q., Xu, S., & Fu, S. M. (1993) · The Journal of Experimental Medicine · doi:10.1084/jem.177.4.1181 · Cited by 82
Antigen–antibody dissociation in Alzheimer disease: a novel approach to diagnosis
Gustaw, K. A., Garrett, M. R., Lee, H., Castellani, R. J., Zagorski, M. G., Prakasam, A., Siedlak, S. L., Zhu, X., Perry, G. L., Petersen, R. B., et al. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05477.x · Cited by 59
Li, Q., Gordon, M. N., Cao, C., Ugen, K. E., & Morgan, D. (2007) · BMC Neuroscience · doi:10.1186/1471-2202-8-22 · Cited by 48
Strain specific recombinant antibodies to potato virus Y potyvirus
Boonham, N., & Barker, I. (1998) · Journal of Virological Methods · doi:10.1016/s0166-0934(98)00097-4 · Cited by 37
Zhou, J., Fonseca, M. I., Kayed, R., Hernandez, I., Webster, S. D., Yazan, O., Cribbs, D. H., Glabe, C. G., & Tenner, A. J. (2005) · Journal of Neuroinflammation · doi:10.1186/1742-2094-2-28 · Cited by 34
Antibodies to Potato Virus Y Bind the Amyloid β Peptide
Friedland, R. P., Tedesco, J. M., Wilson, A. C., Atwood, C., Smith, M. A., Perry, G. L., & Zagorski, M. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802088200 · Cited by 28
Henkel, A. W., Dittrich, P. S., Groemer, T. W., Lemke, E. A., Klingauf, J., Klafki, H., Lewczuk, P., Esselmann, H., Schwille, P., Kornhuber, J., et al. (2007) · Molecular Psychiatry · doi:10.1038/sj.mp.4001947 · Cited by 21
Reduced serum level of antibodies against amyloid β peptide is associated with aging in Tg2576 mice
Sohn, J.-H., So, J. O., Kim, H. J., Nam, E. J., Ha, H. J., Kim, Y. H., & Mook‐Jung, I. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.07.107 · Cited by 13
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Blennow, K., Hampel, H., Weiner, M., & Zetterberg, H. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2010.4 · Cited by 1,863
Immune activation in brain aging and neurodegeneration: too much or too little?
Lucin, K. M., & Wyss-Coray, T. (2009) · Neuron · doi:10.1016/j.neuron.2009.08.039 · Cited by 679
Self-citationBohrmann, B., Baumann, K., Benz, J., Gerber, F., Huber, W., Knoflach, F., Messer, J., Oroszlan, K., Rauchenberger, R., Richter, W. F., et al. (2012) · Journal of Alzheimer's Disease · doi:10.3233/jad-2011-110977 · Cited by 448
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Lemere, C. A., & Masliah, E. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2009.219 · Cited by 351
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Metadata
- Authors
- Britschgi, M., Olin, C. E., Johns, H. T., Takeda-Uchimura, Y., LeMieux, M. C., Rufibach, K., Rajadas, J., Zhang, H., Tomooka, B., Robinson, W. H., Clark, C. M., Fagan, A. M., Galasko, D. R., Holtzman, D. M., Jutel, M., Kaye, J. A., Lemere, C. A., Leszek, J., Li, G., Peskind, E. R., Quinn, J. F., Yesavage, J. A., Ghiso, J. A., & Wyss-Coray, T.
- Affiliations
- Stanford Medicine (US)
- Stanford University (US)
- Departments of aNeurology and Neurological Sciences and
- University of Zurich (CH)
- VA Palo Alto Health Care System (US)
- University of Pennsylvania (US)
- Washington University in St. Louis (US)
- University of California San Diego (US)
- Wroclaw Medical University (PL)
- Oregon Health & Science University (US)
- Brigham and Women's Hospital (US)
- University of Washington (US)
- NYU Langone Health (US)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2009-07-21
- Volume
- 106
- Issue
- 29
- Pages
- 12145-12150
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2715538
- OpenAlex
- W2132576841
- Cited by
- 201
- References
- 65
- Citations by year
- 2026: 8 · 2025: 12 · 2024: 8 · 2023: 11 · 2022: 16 · 2021: 9 · 2020: 15 · 2019: 7 · 2018: 5 · 2017: 4 · 2016: 16 · 2015: 12 · 2014: 10 · 2013: 12 · 2012: 20
- FWCI
- 12.41
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Zurich Open Repository and Archive (University of Zurich) (acceptedVersion, other-oa)
- Zurich Open Repository and Archive (University of Zurich) (submittedVersion, other-oa)
- Zurich Open Repository and Archive (University of Zurich)
- Funders
- National Institute on Aging (P01AG010491, AG10491, AG 08017, AG20603, R01AG020603, P30AG008017, R01AG030539, AG030539, P50AG005136)
- National Institute of Neurological Disorders and Stroke (R01NS136122)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, natural antibodies, amyloid-beta, amyloid oligomers, neuroprotection, aging, cerebrospinal fluid, plasma IgG, pyroglutamic acid, ABRI, Adán, conformation-specific antibodies, vervet monkey, immunization, passive immunotherapy, peptide microarrays
- MeSH terms
- Aging, Alzheimer Disease, Animals, Antibodies, Dementia, Genes, Dominant, Immunoglobulin G, Immunization, Molecular Weight, Neurons, Peptides, Primates, Protein Processing, Post-Translational, Amyloid beta-Peptides, Disease Progression, Neuroprotective Agents, Cytoprotection, Protein Structure, Quaternary, Mice
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