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Vaccination with soluble Aβ oligomers generates toxicity‐neutralizing antibodies
Abstract
In recent studies of transgenic models of Alzheimer's disease (AD), it has been reported that antibodies to aged beta amyloid peptide 1-42 (Abeta(1-42)) solutions (mixtures of Abeta monomers, oligomers and amyloid fibrils) cause conspicuous reduction of amyloid plaques and neurological improvement. In some cases, however, neurological improvement has been independent of obvious plaque reduction, and it has been suggested that immunization might neutralize soluble, non-fibrillar forms of Abeta. It is now known that Abeta toxicity resides not only in fibrils, but also in soluble protofibrils and oligomers. The current study has investigated the immune response to low doses of Abeta(1-42) oligomers and the characteristics of the antibodies they induce. Rabbits that were injected with Abeta(1-42) solutions containing only monomers and oligomers produced antibodies that preferentially bound to assembled forms of Abeta in immunoblots and in physiological solutions. The antibodies have proven useful for assays that can detect inhibitors of oligomer formation, for immunofluorescence localization of cell-attached oligomers to receptor-like puncta, and for immunoblots that show the presence of SDS-stable oligomers in Alzheimer's brain tissue. The antibodies, moreover, were found to neutralize the toxicity of soluble oligomers in cell culture. Results support the hypothesis that immunizations of transgenic mice derive therapeutic benefit from the immuno-neutralization of soluble Abeta-derived toxins. Analogous immuno-neutralization of oligomers in humans may be a key in AD vaccines.
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“Dot immunoblots of soluble extracts from human brain show major increases in oligomers in AD-affected tissue (Gong et al., 2003; Kayed et al., 2003; Lambert et al., 2001).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lambert et al., 2001
Citations
Cites
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
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., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
Self-citationImmunization 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
Bard, F., Cannon, C., Barbour, R., Burke, R.-L., Games, D., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., et al. (2000) · Nature Medicine · doi:10.1038/78682 · Cited by 2,012
Mucke, L., Masliah, E., Yu, G.-Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., & McConlogue, L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-11-04050.2000 · Cited by 1,856
Harper, J. D., & Lansbury, P. T. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.385 · Cited by 1,652
Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease
Lue, L.-F., Kuo, Y.-M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., Beach, T., Kurth, J. H., Rydel, R. E., & Rogers, J. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65184-x · Cited by 1,530
Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease
Morgan, D., Diamond, D. M., Gottschall, P. E., Ugen, K. E., Dickey, C. A., Hardy, J., Duff, K., Jantzen, P. T., DiCarlo, G., Wilcock, D. M., et al. (2000) · Nature · doi:10.1038/35050116 · Cited by 1,506
Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
Janus, C., Pearson, J., McLaurin, J., Mathews, P. M., Jiang, Y., Schmidt, S. D., Chishti, M. A., Horne, P., Heslin, D., French, J., et al. (2000) · Nature · doi:10.1038/35050110 · Cited by 1,431
Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state
Pike, C., Burdick, D., Walencewicz, A., Glabe, C., & Cotman, C. (1993) · The Journal of Neuroscience · doi:10.1523/jneurosci.13-04-01676.1993 · Cited by 1,417
Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red.
Lorenzo, A., & Yankner, B. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12243 · Cited by 1,324
Research works printed but not linked: 5
- Guerette P. A., 2000, Oligomeric Aβ in PBS‐soluble extracts of human Alzheimer brain, Socneurosci. Abstract., 25, 2129
- Kim K. S., 1990, Quantitation of amyloid β‐protein with two monoclonal antibodies, Neurosci. Res. Commun, 7, 113
- Klein W. L., 2001, Molecular Mechanisms of Neurodegenerative Diseases, 1
- Stine W. B., 2000, Amyloid beta 1–40 and 1–42: solubilization parameters and structural outcomes, Soc. Neurosci. Abstract., 26, 800
- Terry R. D., 1999, Alzheimer Disease
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Hawkes, C. A., & McLaurin, J. (2007) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.7.11.1535 · Cited by 33
Reelin reverts biochemical, physiological and cognitive alterations in mouse models of Tauopathy
Rossi, D., Gruart, A., Contreras-Murillo, G., Muhaisen, A., Ávila, J., Delgado-García, J. M., Pujadas, L., & Soriano, E. (2020) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2019.101743 · Cited by 30
Protective effect of new S-acylglutathione derivatives against amyloid-induced oxidative stress
Pensalfini, A., Cecchi, C., Zampagni, M., Becatti, M., Favilli, F., Paoli, P., Catarzi, S., Bagnoli, S., Nacmias, B., Sorbi, S., et al. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.01.025 · Cited by 32
Chen, P.-Z., Jiang, H., Wen, B., Ren, S., Chen, Y., Ji, W.-G., Hu, B., Zhang, J., Xu, F., & Zhu, Z.-R. (2014) · Neural Plasticity · doi:10.1155/2014/320937 · Cited by 32
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Dimakopoulos, A. C. (2005) · Current Alzheimer Research · doi:10.2174/1567205052772795 · Cited by 33
Kim, H., Maxwell, J. A., Kong, F.-K., Tang, D.-C. C., & Fukuchi, K.-I. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.08.044 · Cited by 32
Marciani, D. J. (2019) · Research · doi:10.34133/2019/5341375 · Cited by 33
Desai, A. A., Smith, M. D., Zhang, Y., Makowski, E. K., Gerson, J. E., Ionescu, E., Starr, C. G., Zupancic, J. M., Moore, S. J., Sutter, A. B., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100508 · Cited by 31
O’Nuallain, B., Klyubin, I. V., Donald, J. M. M., Foster, J. S., Welzel, A. T., Barry, A. E., Dykoski, R. K., Cleary, J. P., Gebbink, M. F. B. G., Rowan, M. J., et al. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07389.x · Cited by 33
Kabir, M. T., Uddin, M. S., Mathew, B., Das, P. K., Perveen, A., & Ashraf, G. M. (2020) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026620666200422105156 · Cited by 32
Narendran, S., Pereira, F., Yerramothu, P., Apicella, I., Wang, S.-B., Ambati, K., Hirahara, S., Kim, Y., Ambati, M., Ambati, V. L., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00537-z · Cited by 31
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Bigi, A., Loffredo, G., Cascella, R., & Cecchi, C. (2020) · Current Alzheimer Research · doi:10.2174/1567205017666201109093848 · Cited by 29
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Ishizuka, Y., Shimizu, H., Takagi, E., Kato, M., Yamagata, H., Mikuni, M., & Shirao, T. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.07.005 · Cited by 26
Alzheimer’s protection effect of A673T mutation may be driven by lower Aβ oligomer binding affinity
Limegrover, C. S., LeVine, H., Izzo, N. J., Yurko, R., Mozzoni, K., Rehak, C., Sadlek, K., Safferstein, H., & Catalano, S. M. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15212 · Cited by 24
Logan, S. M., Sarkar, S. N., Zhang, Z., & Simpkins, J. W. (2011) · Brain Research · doi:10.1016/j.brainres.2011.01.038 · Cited by 27
Elucidating Molecular Mass and Shape of a Neurotoxic Aβ Oligomer
Sebollela, A. S., Mustata, G.-M., Luo, K., Velasco, P. T., Viola, K. L., Cline, E. N., Shekhawat, G. S., Wilcox, K. C., Dravid, V. P., & Klein, W. L. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500156r · Cited by 25
Self-citationMeng, X., Fink, A. L., & Uversky, V. N. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.06.062 · Cited by 25
Small Molecules and Alzheimer’s Disease: Misfolding, Metabolism and Imaging
Patel, V., Zhang, X., Tautiva, N., Nyabera, A., Owa, O., Baidya, M., Sung, H., Taunk, P., Abdollahi, S., Charles, S., et al. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666150504145646 · Cited by 25
Alzheimer vaccine: amyloid‐β on trial
Robinson, S. R., Bishop, G. M., & Münch, G. W. (2003) · BioEssays · doi:10.1002/bies.10236 · Cited by 25
Wen, J., Fang, F., Guo, S., Zhang, Y., Peng, X.-L., Sun, W., Wei, X., He, J., & Hung, T. (2017) · Journal of Molecular Neuroscience · doi:10.1007/s12031-017-1015-9 · Cited by 25
Yu, J., Bakhos, L., Chang, L., Holterman, M., Klein, W. L., & Venton, D. L. (2002) · Journal of Molecular Neuroscience · doi:10.1007/s12031-002-0010-x · Cited by 24
Self-citationTargeting soluble amyloid-beta oligomers with a novel nanobody
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Funke, S. A. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/151645 · Cited by 23
Klein, W. L., Lacor, P. N., Felice, F. G. D., & Ferreira, S. T. (2007) · Research and perspectives in neurosciences · doi:10.1007/978-3-540-45702-2_11 · Cited by 23
Self-citationColvin, B. A., Rogers, V. A., Kulas, J. A., Ridgway, E. A., Amtashar, F. S., Combs, C. K., & Nichols, M. R. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14211 · Cited by 21
Chattopadhyay, S., Sarkar, A., Chatterjee, S., & Dey, A. (2017) · Journal of Materials Chemistry A · doi:10.1039/c7ta09179f · Cited by 21
Thomas, R. S., Liddell, J. E., Murphy, L. S., Pache, D. M., & Kidd, E. J. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-10406 · Cited by 21
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Park, S.-K., Ratia, K. M., Ba, M. A., Valencik, M. L., & Liebman, S. W. (2016) · Microbial Cell · doi:10.15698/mic2016.02.476 · Cited by 21
Vahed, M., Sweeney, A., Shirasawa, H., & Vahed, M. (2019) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2019.107128 · Cited by 19
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Fu, L., Li, Y., Hu, Y., Yu, B., Zhang, H., Wu, J., Wu, H., Yu, X., & Kong, W. (2015) · Immunology Letters · doi:10.1016/j.imlet.2015.09.002 · Cited by 18
Caballero, E., Calvo-Rodríguez, M., Gonzalo‐Ruiz, A., Villalobos, C., & Núñez, L. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.11.041 · Cited by 20
Chuang, W.-H., Chou, Y.-T., Chen, Y.-H., Kuo, T.-H., Liaw, W., Lu, T., Kao, C.-F., & Wang, Y. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00348 · Cited by 17
Venkataramani, V., Wirths, O., Budka, H., Härtig, W., Kovács, G. G., & Bayer, T. A. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111379 · Cited by 17
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Leite, D. M., Seifi, M., Ruiz‐Pérez, L., Nguemo, F., Plomann, M., Swinny, J. D., & Battaglia, G. (2022) · Brain Communications · doi:10.1093/braincomms/fcac039 · Cited by 16
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Zhang, D. Y., Wang, J., Fleeman, R. M., Kuhn, M. K., Swulius, M. T., Proctor, E. A., & Dokholyan, N. V. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00221 · Cited by 14
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Wacker, J., Rönicke, R., Westermann, M., Wulff, M., Reymann, K. G., Dobson, C. M., Horn, U., Crowther, D. C., Luheshi, L. M., & Fändrich, M. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-43 · Cited by 14
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Xue, C., Lee, Y. K., Tran, J., Chang, D., & Guo, Z. (2017) · Royal Society Open Science · doi:10.1098/rsos.170325 · Cited by 13
Forner, S., Martini, A. C., Prieto, G. A., Dang, C. T., Rodríguez‐Ortiz, C. J., Reyes‐Ruiz, J. M., Trujillo‐Estrada, L., da Cunha, C., Andrews, E. J., Phan, J., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-52324-0 · Cited by 15
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Fu, L., Zhang, Y., Zhang, X., Tian, W., Zhang, W., Jia, Y. X., & Zhang, L. (2020) · Immunology Letters · doi:10.1016/j.imlet.2020.07.009 · Cited by 13
Wang, J., Ikonen, S., Gurevicius, K., Groen, T. V., & Tanila, H. (2003) · Neuroscience · doi:10.1016/s0306-4522(02)00714-5 · Cited by 13
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Kou, J., Song, M., Pattanayak, A., Lim, J. E., Yang, J., Cao, D., Li, L., & Fukuchi, K. (2012) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2012.01.008 · Cited by 12
Ren, S., Shao, H., Ji, W.-G., Jiang, H., Xu, F., Chen, P.-Z., Mi, Z., Wen, B., Zhu, G.-X., & Zhu, Z.-R. (2014) · Amyloid · doi:10.3109/13506129.2014.990558 · Cited by 12
Matsubara, E., Takamura, A., Okamoto, Y., Oono, H., Nakata, T., Wakasaya, Y., Kawarabayashi, T., & Shoji, M. (2013) · BioMed Research International · doi:10.1155/2013/984041 · Cited by 12
A novel Aβ epitope vaccine based on bacterium-like particle against Alzheimer’s disease
Fu, L., Guo, Y., Sun, Y., Dong, Y., Wu, J., Yu, B., Zhang, H., Yu, X., Wu, H., & Kong, W. (2018) · Molecular Immunology · doi:10.1016/j.molimm.2018.07.019 · Cited by 12
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Dong, J., Apkarian, R. P., & Lynn, D. G. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.05.052 · Cited by 12
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Simmons, M. K., Manjeshwar, R. M., Agdeppa, E. D., Mattheyses, R. M., Kiehl, T. R., & Montalto, M. (2004) · Molecular Imaging and Biology · doi:10.1007/s11307-005-0952-9 · Cited by 11
Pande, V. S. (2004) · Nature Biotechnology · doi:10.1038/nbt1004-1240 · Cited by 12
Errico, S., Lucchesi, G., Odino, D., Osman, E. Y., Cascella, R., Neri, L., Capitini, C., Calamai, M., Bemporad, F., Cecchi, C., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00182 · Cited by 12
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Breydo, L., & Uversky, V. N. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-394431-3.00001-8 · Cited by 11
Klein, W. L. (2007) · Springer eBooks · doi:10.1007/0-387-25919-8_4 · Cited by 11
Self-citationCattepoel, S., Schaub, A., Ender, M., Gaida, A., Kropf, A., Guggisberg, U., Nolte, M. W., Fabri, L., Adlard, P. A., Finkelstein, D. I., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063162 · Cited by 11
Sánchez-García, M. A., Lara-Ureña, N., March‐Díaz, R., Luis, C. O. S., Quiñones-Cañete, S., Mora-Romero, B., Cabello-Rivera, D., Cabello-Rivera, D., Romero‐Molina, C., Romero‐Molina, C., et al. (2025) · Science Advances · doi:10.1126/sciadv.adu2244 · Cited by 10
Cecchi, C., Evangelisti, E., Cascella, R., Zampagni, M., Benvenuti, S., Luciani, P., Deledda, C., Cellai, I., Wright, D., Saccardi, R., et al. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110590 · Cited by 10
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Morgan, D. (2003) · Expert Review of Vaccines · doi:10.1586/14760584.2.1.53 · Cited by 10
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Lana, E., Gellerbring, A., Jung, S., Nordberg, A. K., Lithner, C. U., & Darreh‐Shori, T. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00176 · Cited by 10
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Cowan, C. B., Patel, D. A., & Good, T. A. (2009) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2009.02.003 · Cited by 9
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LeVine, H. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(03)00322-9 · Cited by 8
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Innocent, N., Evans, N. A., Hille, C. J., & Wonnacott, S. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.04.003 · Cited by 7
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Klein, W. L., Felice, F. G. D., Lacor, P. N., Lambert, M. P., & Zhao, W.-Q. (2008) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-540-76330-7_9 · Cited by 7
Self-citationβ‐Amyloid Therapeutic Strategies for Alzheimer's Disease
Imbimbo, B. P., & Speroni, F. (2005) · Wiley eBooks · doi:10.1002/0471266949.bmc112 · Cited by 6
Tsai, Y.-C., Luo, J.-C., Liu, T., Lu, I.-L., Shen, M., Chuang, C., Chern, C., & Chiu, H. (2020) · Nanomaterials · doi:10.3390/nano10071284 · Cited by 6
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Yeh, C., Chang, H., Hsu, W., Huang, S., Wu, M., Tu, L., Lee, M., & Chan, J. C. C. (2023) · Chemistry - A European Journal · doi:10.1002/chem.202301879 · Cited by 6
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Zhou, Y., & Klein, W. L. (2012) · Neurotoxicity Research · doi:10.1007/s12640-012-9318-7 · Cited by 6
Self-citationSpecific and efficient anti-Aβ42 antibodies induced by sixteen tandem repeats of Aβ9
Cui, L., Huang, X., Wang, J., & Zhang, Y. (2010) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2010.06.004 · Cited by 6
Boroujeni, E. R., Hosseini, S. M., Fani, G., Cecchi, C., & Chiti, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197273 · Cited by 7
Oligomerization and toxicity of Aβ fusion proteins
Caine, J. M., Bharadwaj, P. R., Sankovich, S. E., Ciccotosto, G. D., Streltsov, V. A., & Varghese, J. N. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.05.029 · Cited by 6
Zhu, S., Du, C., Fu, Y., Deng, Q., & Shi, L. (2009) · Plasmonics · doi:10.1007/s11468-009-9084-4 · Cited by 6
Johnson, E. A., Nowar, R., Viola, K. L., Huang, W., Zhou, S., Bicca, M. A., Zhu, W., Kranz, D. L., Klein, W. L., & Silverman, R. B. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2402117122 · Cited by 5
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Finch, C. E., & Stanford, C. B. (2003) · Springer eBooks · doi:10.1007/978-3-642-59356-7_3 · Cited by 5
Self-citationJohn, P. A. S. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21251 · Cited by 5
Sabu, A., Huang, Y. C., Sharmila, R., Sun, C.-Y., Shen, M.-Y., & Chiu, H. (2024) · Materials Today Bio · doi:10.1016/j.mtbio.2024.101213 · Cited by 4
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Errico, S., Fani, G., Gennari, M., Mastricci, A., Neri, L., Odino, D., Canale, C., Relini, A., Vendruscolo, M., Mannini, B., et al. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.146398 · Cited by 4
Grover, S., Pham, T., Jones, A., Pereira, C. S., Maurino, M. V. D., Garrad, E. C., Makoni, N. J., Parks, A., Domalewski, R. J., Riggio, G., et al. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15817 · Cited by 5
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Bitan, F. R. A. G. (2014) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9781608058525114020014 · Cited by 4
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Gold, M. (2002) · Journal of Molecular Neuroscience · doi:10.1385/jmn:19:3:329 · Cited by 4
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Yu, L., Wang, X., Doan, T. H., Fan, Y., Bussière, T., Bacskai, B. J., & Kastanenka, K. V. (2025) · Alzheimer s Research & Therapy · doi:10.1186/s13195-025-01812-9 · Cited by 3
Piccialli, I., Greco, F., Roviello, G. N., Sisalli, M. J., Tedeschi, V., Mola, A. D., Borbone, N., Oliviero, G., Feo, V. D., Secondo, A., et al. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115745 · Cited by 3
Reporters of Amyloid Structural Polymorphism
LeVine, H., Nilsson, K. P. R., Nilsson, R., & Hammarström, P. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-394431-3.00007-9 · Cited by 3
Ma, Q., Lim, G. P., Harris‐White, M. E., Yang, F., Ambegaokar, S. S., Ubeda, O. J., Glabe, C. G., Teter, B., Frautschy, S. A., & Cole, G. M. (2006) · Cited by 3
Imaging of Amyloid-β Aggregation Using a Novel Quantum dot Nanoprobe and its Advanced Applications
Tokuraku, K., & Ikezu, T. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-394431-3.00011-0 · Cited by 3
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Physiological factors could enhance amyloid-beta toxicity
Hunya, Á. G. (2013) · SZTE Repository of Dissertations (University of Szeged) · doi:10.14232/phd.1674 · Cited by 3
Metadata
- Authors
- 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.
- Affiliations
- Northwestern University (US)
- University of Southern California (US)
- University of Illinois Chicago (US)
- Corresponding author
- Klein, William L.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2001-11
- Volume
- 79
- Issue
- 3
- Pages
- 595-605
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W1857351893
- Cited by
- 349
- References
- 45
- Citations by year
- 2026: 12 · 2025: 8 · 2024: 4 · 2023: 11 · 2022: 6 · 2021: 8 · 2020: 15 · 2019: 10 · 2018: 5 · 2017: 11 · 2016: 6 · 2015: 10 · 2014: 18 · 2013: 20 · 2012: 20
- FWCI
- 8.37
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (AG-13499, P01 AG13138, R01AG013499)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, amyloid-beta oligomers, amyloid-beta 42, immunization, neutralizing antibodies, amyloid plaques, amyloid protofibrils, oligomer toxicity, Alzheimer's disease vaccine, transgenic mice
- MeSH terms
- Alzheimer Disease, Animals, Antibody Specificity, Epitopes, Fluorescent Antibody Technique, Hippocampus, Humans, Neurons, Peptide Fragments, Solubility, Vaccination, Amyloid beta-Peptides, PC12 Cells, Neuroprotective Agents, Rats
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