The DOI matches its Crossref record; 44 of the 45 references it cites were found in a registry or an index.
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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
Cited by
Sorted by citations
Items 101–200 of 349
Aβ40 Oligomers Identified as a Potential Biomarker for the Diagnosis of Alzheimer's Disease
Gao, C. M., Yam, A. Y., Wang, X., Magdangal, E., Salisbury, C., Peretz, D., Zuckermann, R. N., Connolly, M. D., Hansson, O., Minthon, L., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015725 · Cited by 105
“However, recent reports suggest that smaller, soluble Ab oligomers are more likely to be the pathogenic agents of disease [3,4,7–10].”
BackgroundFani, G., Mannini, B., Vecchi, G., Cascella, R., Cecchi, C., Dobson, C. M., Vendruscolo, M., & Chiti, F. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00811 · Cited by 106
Izzo, N. J., Yuede, C. M., LaBarbera, K. M., Limegrover, C. S., Rehak, C., Yurko, R., Waybright, L., Look, G., Rishton, G., Safferstein, H., et al. (2021) · Alzheimer's & Dementia · doi:10.1002/alz.12302 · Cited by 95
Immunotherapy for Alzheimer's disease
Dodel, R. C., Hampel, H. J., & Du, Y. (2003) · The Lancet Neurology · doi:10.1016/s1474-4422(03)00349-1 · Cited by 102
Chemical sensing platforms for detecting trace-level Alzheimer's core biomarkers
Kim, K., Lee, C. H., & Park, C. B. (2020) · Chemical Society Reviews · doi:10.1039/d0cs00107d · Cited by 101
Ryan, D. A., Narrow, W. C., Federoff, H. J., & Bowers, W. J. (2010) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2010.05.001 · Cited by 102
Fukuchi, K.-I., Tahara, K., Kim, H., Maxwell, J. A., Lewis, T. L., Accavitti-Loper, M. A., Kim, H., Ponnazhagan, S., & Lalonde, R. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.04.012 · Cited by 100
Cellular Receptors of Amyloid β Oligomers (AβOs) in Alzheimer’s Disease
Mroczko, B., Groblewska, M., Litman-Zawadzka, A., Kornhuber, J., & Lewczuk, P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19071884 · Cited by 97
A neurodegenerative cellular stress response linked to dark microglia and toxic lipid secretion
Flury, A. G., Aljayousi, L., Park, H.-J., Khakpour, M., Mechler, J., Aziz, S., McGrath, J. D., Deme, P., Sandberg, C., Ibáñez, F. G., et al. (2024) · Neuron · doi:10.1016/j.neuron.2024.11.018 · Cited by 102
Why Alzheimer's is a disease of memory: The attack on synapses by Aß oligomers (ADDLs)
Viola, K. L., Velasco, P. T., & Klein, W. L. (2008) · The journal of nutrition health & aging · doi:10.1007/bf02982587 · Cited by 97
Self-citationA Ganglioside-induced Toxic Soluble Aβ Assembly
Yamamoto, N., Matsubara, E., Maeda, S., Minagawa, H., Takashima, A., Maruyama, W., Michikawa, M., & Yanagisawa, K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606202200 · Cited by 96
Mice as models: Transgenic approaches and Alzheimer's disease
Games, D., Buttini, M., Kobayashi, D. T., Schenk, D., & Seubert, P. A. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s316 · Cited by 93
Leshchyns’ka, I., Liew, H. T., Shepherd, C. E., Halliday, G. M., Stevens, C. H., Ke, Y. D., Ittner, L. M., & Sytnyk, V. (2015) · Nature Communications · doi:10.1038/ncomms9836 · Cited by 94
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
Poduslo, J. F., Ramakrishnan, M., Holasek, S. S., Ramı́rez-Alvarado, M., Kandimalla, K. K., Gilles, E. J., Curran, G. L., & Wengenack, T. M. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04591.x · Cited by 91
Capitini, C., Conti, S., Perni, M., Guidi, F., Cascella, R., Poli, A. D., Penco, A., Relini, A., Cecchi, C., & Chiti, F. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086720 · Cited by 88
Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro
Cascella, R., Conti, S., Mannini, B., Li, X., Buxbaum, J. N., Tiribilli, B., Chiti, F., & Cecchi, C. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.09.011 · Cited by 86
Rahimi, F., Shanmugam, A., & Bitan, G. (2008) · Current Alzheimer Research · doi:10.2174/156720508784533358 · Cited by 88
Kurji, K. H., Cui, J. Z., Lin, T. R., Harriman, D. I., Prasad, S. S., Kojic, L., & Matsubara, J. A. (2010) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.09-3622 · Cited by 90
Jang, H., Arce, F. T., Ramachandran, S., Kagan, B. L., Lal, R., & Nussinov, R. (2014) · Chemical Society Reviews · doi:10.1039/c3cs60459d · Cited by 85
Evangelisti, E., Cecchi, C., Cascella, R., Sgromo, C., Becatti, M., Dobson, C. M., Chiti, F., & Stefani, M. (2012) · Journal of Cell Science · doi:10.1242/jcs.098434 · Cited by 84
Hickman, D. T., López-Deber, M. P., Ndao, D. M., Silva, A. B., Nand, D., Pihlgren, M., Giriens, V., Madani, R., St-Pierre, A., Karastaneva, H., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.186338 · Cited by 84
Cecchi, C., Nichino, D., Zampagni, M., Bernacchioni, C., Evangelisti, E., Pensalfini, A., Liguri, G., Gliozzi, A., Stefani, M., & Relini, A. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2009.07.019 · Cited by 82
Amyloid beta acts synergistically as a pro-inflammatory cytokine
LaRocca, T. J., Cavalier, A. N., Roberts, C. M., Lemieux, M. R., Ramesh, P., Garcia, M. A., & Link, C. D. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105493 · Cited by 83
Chang, L., Bakhos, L., Wang, Z., Venton, D. L., & Klein, W. L. (2003) · Journal of Molecular Neuroscience · doi:10.1385/jmn:20:3:305 · Cited by 81
Self-citationGhadami, S. A., Chia, S., Ruggeri, F. S., Meisl, G., Bemporad, F., Habchi, J., Cascella, R., Dobson, C. M., Vendruscolo, M., Knowles, T. P. J., et al. (2020) · Biomacromolecules · doi:10.1021/acs.biomac.9b01475 · Cited by 79
ADDLs & protofibrils —the missing links?
Klein, W. L. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00312-8 · Cited by 77
Self-citationScreening for Inhibitors of Tau Polymerization
Pickhardt, M., von Bergen�, M., Gažová, Z., Hascher, A., Biernat, J., Mandelkow, E., & Mandelkow�, E. (2005) · Current Alzheimer Research · doi:10.2174/1567205053585891 · Cited by 74
Marutle, A., Gillberg, P.-G., Bergfors, A., Yu, W., Ni, R., Nennesmo, I., Voytenko, L., & Nordberg, A. (2013) · Journal of Neuroinflammation · doi:10.1186/1742-2094-10-90 · Cited by 70
Johnson, E. C. B., Ho, K., Yu, G.-Q., Das, M., Sanchez, P. E., Djukic, B., Lopez, I., Yu, X., Gill, M., Zhang, W., et al. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00393-5 · Cited by 73
Rukhsana Sultana, A., Marzia Perluigi, A., & Butterfield, D. A. (2005) · Journal of Chromatography B · doi:10.1016/j.jchromb.2005.09.024 · Cited by 72
Moretto, N., Bolchi, A., Rivetti, C., Imbimbo, B. P., Villetti, G., Pietrini, V., Polonelli, L., Signore, S. J. D., Smith, K. M., Ferrante, R. J., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609690200 · Cited by 69
Hamley, I. W. (2007) · Angewandte Chemie · doi:10.1002/ange.200700861 · Cited by 69
Extracellular chaperones prevent Aβ42-induced toxicity in rat brains
Cascella, R., Conti, S., Tatini, F., Evangelisti, E., Scartabelli, T., Casamenti, F., Wilson, M. R., Chiti, F., & Cecchi, C. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.04.012 · Cited by 70
“Click Peptide“: pH‐Triggered in Situ Production and Aggregation of Monomer Aβ1–42
Taniguchi, A., Sohma, Y., Hirayama, Y., Mukai, H., Kimura, T., Hayashi, Y., Matsuzaki, K., & Kiso, Y. (2009) · ChemBioChem · doi:10.1002/cbic.200800765 · Cited by 68
Ding, Y. J., Zhao, J., Zhang, X., Wang, S., Viola, K. L., Chow, F. E., Zhang, Y., Lippa, C. F., Klein, W. L., & Gong, Y. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.01140 · Cited by 68
Self-citationMiao, J., Vitek, M. P., Xu, F., Previti, M. L., Davis, J., & Nostrand, W. E. V. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.1306-05.2005 · Cited by 64
Sivilia, S., Lorenzini, L., Giuliani, A., Gusciglio, M., Fernández, M., Baldassarro, V. A., Mangano, C., Ferraro, L., Pietrini, V., Baroc, M. F., et al. (2013) · BMC Neuroscience · doi:10.1186/1471-2202-14-44 · Cited by 65
Neutralization of Soluble, Synaptotoxic Amyloid β Species by Antibodies Is Epitope Specific
Zago, W., Buttini, M., Comery, T. A., Nishioka, C., Gardai, S. J., Seubert, P., Games, D., Bard, F., Schenk, D., & Kinney, G. G. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.1676-11.2012 · Cited by 62
Targets for AD treatment: conflicting messages from γ-secretase inhibitors
Sambamurti, K., Greig, N. H., Utsuki, T., Barnwell, E., Sharma, E., Mazell, C., Bhat, N. R., Kindy, M. S., Lahiri, D. K., & Pappolla, M. A. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07213.x · Cited by 62
The Amyloid-Beta Clearance: From Molecular Targets to Glial and Neural Cells
Cai, W., Wu, T., & Chen, N. (2023) · Biomolecules · doi:10.3390/biom13020313 · Cited by 69
Wang, X.-P., Zhang, J.-H., Wang, Y.-J., Feng, Y. N., Zhang, X., Sun, X.-X., Li, J.-L., Du, X.-T., Lambert, M. P., Yang, S.-G., et al. (2009) · FEBS Letters · doi:10.1016/j.febslet.2008.12.064 · Cited by 62
Self-citationYang, Y., Ji, W.-G., Zhu, Z.-R., Wu, Y.-L., Zhang, Z., & Qu, S.-C. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.03.007 · Cited by 62
Meli, G., Visintin, M., Cannistraci, I., & Cattaneo, A. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.01.061 · Cited by 64
Tetrahydrocurcumin confers protection against amyloid β-induced toxicity
Mishra, S., Mishra, M., Seth, P., & Sharma, S. K. (2010) · Neuroreport · doi:10.1097/wnr.0b013e328341e141 · Cited by 61
Nanoscience enables ultrasensitive detection of Alzheimer's biomarker
Keating, C. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500024102 · Cited by 61
Small molecule inhibitors of Abetaassembly
LeVine, H. (2007) · Amyloid · doi:10.1080/13506120701461020 · Cited by 58
Antibody-based therapy in Alzheimer's disease
Pul, R., Dodel, R. C., & Stangel, M. (2011) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2011.552884 · Cited by 59
Nanobody specific for oligomeric beta-amyloid stabilizes nontoxic form
Kasturirangan, S., Li, L., Emadi, S., Boddapati, S. P., Schulz, P., & Sierks, M. R. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.09.020 · Cited by 57
Lindhagen‐Persson, M., Brännström, K., Vestling, M., Steinitz, M. O., & Olofsson, A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013928 · Cited by 57
Velasco, P. T., Heffern, M. C., Sebollela, A. S., Popova, I. A., Lacor, P. N., Lee, K. B., Sun, X., Tiano, B. N., Viola, K. L., Eckermann, A. L., et al. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn300122k · Cited by 57
Self-citationSoluble Oligomers Require a Ganglioside to Trigger Neuronal Calcium Overload
Cascella, R., Evangelisti, E., Bigi, A., Becatti, M., Fiorillo, C., Stefani, M., Chiti, F., & Cecchi, C. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170340 · Cited by 57
Limbocker, R., Staats, R., Chia, S., Ruggeri, F. S., Mannini, B., Xu, C. K., Perni, M., Cascella, R., Bigi, A., Sasser, L. R., et al. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.680026 · Cited by 54
Ladiwala, A. R. A., Mora‐Pale, M., Lin, J. C., Bale, S. S., Fishman, Z. S., Dordick, J. S., & Tessier, P. M. (2011) · ChemBioChem · doi:10.1002/cbic.201100123 · Cited by 54
Apolipoprotein J (clusterin) activates rodent microglia in vivo and in vitro
Xie, Z., Harris‐White, M. E., Wals, P. A., Frautschy, S. A., Finch, C. E., & Morgan, T. E. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03065.x · Cited by 53
Self-citationAnti-ADDL antibodies differentially block oligomer binding to hippocampal neurons
Shughrue, P. J., Acton, P. J., Breese, R., Zhao, W., Chen-Dodson, E., Hepler, R. W., Wolfe, A. L., Matthews, M., Heidecker, G. J., Joyce, J. G., et al. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.04.003 · Cited by 53
ACU193: An Immunotherapeutic Poised to Test the Amyloid β Oligomer Hypothesis of Alzheimer’s Disease
Krafft, G. A., Jerecı̀ć, J., Siemers, E., & Cline, E. N. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.848215 · Cited by 54
Self-citationMitochondria in Aging and Alzheimer's Disease
Crouch, P. J., Cimdins, K., Duce, J. A., Bush, A. I., & Trounce, I. A. (2007) · Rejuvenation Research · doi:10.1089/rej.2007.0592 · Cited by 54
Expression and Localization of Mitochondrial Ferritin mRNA in Alzheimer's Disease Cerebral Cortex
Wang, L., Yang, H., Zhao, S., Sato, H., Konishi, Y., Beach, T. G., Abdelalim, E. M., Bisem, N. J., & Tooyama, I. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022325 · Cited by 51
Rózga, M., & Bal, W. (2009) · Chemical Research in Toxicology · doi:10.1021/tx900358j · Cited by 54
Ashley, R. H., Harroun, T. A., Hauß, T., Breen, K. C., & Bradshaw, J. P. (2006) · BMC Structural Biology · doi:10.1186/1472-6807-6-21 · Cited by 52
A review on protein misfolding, aggregation and strategies to prevent related ailments
Shamsi, T. N., Athar, T., Parveen, R., & Fatima, S. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.07.116 · Cited by 56
Ostrovskaya, R. U., Алексеевна, Г. М., Bobkova, N. A., Sewell, R. D. E., Гудашева, Т. А., Samokhin, A. N., Seredinin, S. B., Noppe, W., Sherstnev, V. V., & Morozova‐Roche, L. A. (2006) · Journal of Psychopharmacology · doi:10.1177/0269881106071335 · Cited by 55
An ultra‐sensitive immunoassay detects and quantifies soluble Aβ oligomers in human plasma
Liu, L., Kwak, H., Lawton, T., Jin, S., Meunier, A. L., Dang, Y., Ostaszewski, B. L., Pietras, A., Stern, A. M., & Selkoe, D. J. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12457 · Cited by 49
Development and validation of a yeast high-throughput screen for inhibitors of Aβ42 oligomerization
Park, S.-K., Pegan, S. D., Mesecar, A. D., Jungbauer, L. M., LaDu, M. J., & Liebman, S. W. (2011) · Disease Models & Mechanisms · doi:10.1242/dmm.007963 · Cited by 50
Single Chain Fv Antibodies against the 25−35 Aβ Fragment Inhibit Aggregation and Toxicity of Aβ42
Zameer, A., Schulz, P., Wang, M. S., & Sierks, M. R. (2006) · Biochemistry · doi:10.1021/bi060601o · Cited by 48
Wälti, M. A., Orts, J., Vögeli, B., Campioni, S., & Riek, R. (2015) · ChemBioChem · doi:10.1002/cbic.201402595 · Cited by 49
Synthetic dityrosine-linked β-amyloid dimers form stable, soluble, neurotoxic oligomers
Kok, W. M., Cottam, J. M., Ciccotosto, G. D., Miles, L. A., Karas, J. A., Scanlon, D. B., Roberts, B. R., Parker, M. W., Cappai, R., Barnham, K. J., et al. (2013) · Chemical Science · doi:10.1039/c3sc22295k · Cited by 46
Therapeutic Strategies to Reduce the Toxicity of Misfolded Protein Oligomers
Kreiser, R. P., Wright, A. K., Block, N. R., Hollows, J. E., Nguyen, L. T., LeForte, K., Mannini, B., Vendruscolo, M., & Limbocker, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228651 · Cited by 48
Sehlin, D., Hedlund, M., Lord, A., Englund, H., Gellerfors, P., Paulie, S., Lannfelt, L., & Pettersson, F. E. (2010) · Neurodegenerative Diseases · doi:10.1159/000316530 · Cited by 47
Probing the origins, diagnosis and treatment of amyloid diseases using antibodies
Dumoulin, M., & Dobson, C. M. (2004) · Biochimie · doi:10.1016/j.biochi.2004.09.012 · Cited by 45
Qahwash, I. M., Weiland, K. L., Lu, Y., Sarver, R. W., Kletzien, R. F., & Yan, R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213298200 · Cited by 45
Shah, P., Lal, N., Leung, E., Traul, D., Gonzalo‐Ruiz, A., & Geula, C. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.090937 · Cited by 48
Amyloid-β Oligomers: Multiple Moving Targets
Shea, D. W., & Daggett, V. (2022) · Biophysica · doi:10.3390/biophysica2020010 · Cited by 43
Helmond, Z. V., Heesom, K. J., & Love, S. (2008) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2008.09.002 · Cited by 44
Genetic Alterations of the BRI2 gene: Familial British and Danish Dementias
J, G., A, R., Y, T., T, L., M, B.-M., H, B., G, P., J, H., R, L., T, R., et al. (2006) · Brain Pathology · doi:10.1111/j.1750-3639.2006.tb00563.x · Cited by 44
Ren, S., Chen, P.-Z., Jiang, H., Mi, Z., Xu, F., Hu, B., Zhang, J., & Zhu, Z.-R. (2014) · Neuroscience Letters · doi:10.1016/j.neulet.2014.07.050 · Cited by 43
PGH2‐derived levuglandin adducts increase the neurotoxicity of amyloid β1–42
Boutaud, O. G., Montine, T. J., Chang, L., Klein, W. L., & Oates, J. A. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03586.x · Cited by 44
Self-citationFani, G., Torre, C. E. L., Cascella, R., Cecchi, C., Vendruscolo, M., & Chiti, F. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04513-w · Cited by 44
Membrane cholesterol enrichment prevents Aβ-induced oxidative stress in Alzheimer's fibroblasts
Pensalfini, A., Zampagni, M., Liguri, G., Becatti, M., Evangelisti, E., Fiorillo, C., Bagnoli, S., Cellini, E., Nacmias, B., Sorbi, S., et al. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.02.010 · Cited by 43
Targeted Drug Delivery Across the Blood Brain Barrier in Alzheimer’s Disease
Rocha, S. (2013) · Current Pharmaceutical Design · doi:10.2174/13816128113199990613 · Cited by 42
In vivo induction of membrane damage by β-amyloid peptide oligomers
Julien, C., Tomberlin, C., Roberts, C. M., Akram, A., Stein, G. H., Silverman, M. A., & Link, C. D. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0634-x · Cited by 39
Lee, C. C., Julian, M. C., Tiller, K. E., Meng, F., DuConge, S. E., Akter, R., Raleigh, D. P., & Tessier, P. M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.682336 · Cited by 41
A glycine zipper motif mediates the formation of toxic β-amyloid oligomers in vitro and in vivo
Fonte, V. G., Dostal, V., Roberts, C. M., Gonzales, P. K., Lacor, P. N., Magrané, J., Dingwell, N., Fan, E. Y., Silverman, M. A., Stein, G. H., et al. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-61 · Cited by 37
Microglia activation mediates fibrillar amyloid-β toxicity in the aged primate cortex
Leung, E., Guo, L., Bu, J., Maloof, M. E., Khoury, J. B. E., & Geula, C. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.02.025 · Cited by 40
Kim, H., Cao, Y., Kong, F.-K., Kampen, K. R. V., Lewis, T. L., Ma, Z., Tang, D.-C. C., & Fukuchi, K.-I. (2005) · Vaccine · doi:10.1016/j.vaccine.2004.12.015 · Cited by 39
Is there a future for vaccination as a treatment for Alzheimer's disease?
McGeer, P. L. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00157-4 · Cited by 39
Advances on the Understanding of the Origins of Synaptic Pathology in AD
Lacor, P. N. (2007) · Current Genomics · doi:10.2174/138920207783769530 · Cited by 40
Plasma Membrane Injury Depends on Bilayer Lipid Composition in Alzheimer's Disease
Evangelisti, E., Zampagni, M., Cascella, R., Becatti, M., Fiorillo, C., Caselli, A., Bagnoli, S., Nacmias, B., & Cecchi, C. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131406 · Cited by 37
Overcoming synthetic Aβ peptide aging: a new approach to an age-old problem
Manzoni, C., Colombo, L., Messa, M., Cagnotto, A., Cantú, L., Favero, E. D., & Salmona, M. (2009) · Amyloid · doi:10.1080/13506120902879848 · Cited by 37
Wang, Z., Chang, L., Klein, W. L., Thatcher, G. R. J., & Venton, D. L. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm034224e · Cited by 37
Self-citationVattemi, G. N. A., Engel, W. K., McFerrin, J., & Askanas, V. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01798.x · Cited by 37
Bateman, D. A., McLaurin, J., & Chakrabartty, A. (2007) · BMC Neuroscience · doi:10.1186/1471-2202-8-29 · Cited by 36
Costantini, C., Bianca, V. D., Formaggio, E., Chiamulera, C., Montresor, A., & Rossi, F. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.09.004 · Cited by 36
Sebollela, A. S., Cline, E. N., Popova, I. A., Luo, K., Sun, X., Ahn, J., Barcelos, M. A., Bezerra, V. N., Silva, N. M. L. E., Patel, J., et al. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14118 · Cited by 38
Self-citationMolecular basis of selective amyloid‐β degrading enzymes in Alzheimer's disease
Żukowska, J., Moss, S. J., Subramanian, V., & Acharya, K. R. (2023) · FEBS Journal · doi:10.1111/febs.16939 · Cited by 36
Wilcox, K. C., Marunde, M. R., Das, A., Velasco, P. T., Kuhns, B. D., Marty, M. T., Haoming, J., Luan, C.-H., Sligar, S. G., & Klein, W. L. (2015) · PLoS ONE · doi:10.1371/journal.pone.0125263 · Cited by 37
Self-citationTakamura, A., Okamoto, Y., Kawarabayashi, T., Yokoseki, T., Shibata, M. S., Mouri, A., Nabeshima, T., Sun, H., Abe, K., Urisu, T., et al. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-20 · Cited by 34
Soluble amyloid β oligomers may contribute to apoptosis of retinal ganglion cells in glaucoma
Yin, H., Chen, L., Chen, X., & Liu, X. (2008) · Medical Hypotheses · doi:10.1016/j.mehy.2008.01.030 · Cited by 34
Wang, T., Xie, X.-X., Ji, M., Wang, S., Zha, J., Zhou, W.-W., Yu, X., Chen, W., Ma, S., Xi, Z.-Y., et al. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.02.015 · Cited by 34
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review