The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Temporal Profile of Amyloid-β (Aβ) Oligomerization in an in Vivo Model of Alzheimer Disease
Open accessAbstract
Accumulation of amyloid-beta (Abeta) is one of the earliest molecular events in Alzheimer disease (AD), whereas tau pathology is thought to be a later downstream event. It is now well established that Abeta exists as monomers, oligomers, and fibrils. To study the temporal profile of Abeta oligomer formation in vivo and to determine their interaction with tau pathology, we used the 3xTg-AD mice, which develop a progressive accumulation of plaques and tangles and cognitive impairments. We show that SDS-resistant Abeta oligomers accumulate in an age-dependent fashion, and we present evidence to show that oligomerization of Abeta appears to first occur intraneuronally. Finally, we show that a single intrahippocampal injection of a specific oligomeric antibody is sufficient to clear Abeta pathology, and more importantly, tau pathology. Therefore, Abeta oligomers may play a role in the induction of tau pathology, making the interference of Abeta oligomerization a valid therapeutic target.
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“Both Aβ and tau exhibit age- and region-dependent formation in these mice, with Aβ plaques appearing prior to tangles, which are extensive in older transgenic mice.”
From Brain microstructure abnormalities in the 3xTg-AD mouse – A diffusion MRI and morphology correlation study (2022) · cites this paper as [4]
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“In our morphological analysis (Fig. 2 and 3), as previously described [3–6, 28], Aβ plaque and tau pathology are evident in 15-month-old TG mice, and significantly increased with age (online supplementary Fig.1 and 2).”
From Brain microstructure abnormalities in the 3xTg-AD mouse – A diffusion MRI and morphology correlation study (2022) · cites this paper as [4]
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“It develops both amyloid-β (Aβ) and neurofibrillary tangles in a temporal and spatial pattern similar to human AD pathology [3–6].”
From Brain microstructure abnormalities in the 3xTg-AD mouse – A diffusion MRI and morphology correlation study (2022) · cites this paper as [4]
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“Additionally, due to the variability of the degree of AD pathology described in this model [4, 6, 26], large ROIs, as used for the HD and HV, may have attenuated some effects.”
From Brain microstructure abnormalities in the 3xTg-AD mouse – A diffusion MRI and morphology correlation study (2022) · cites this paper as [4]
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“the ability of antibodies to reverse intracellular tau and synapse pathology (Chauhan et al., 2008; Oddo et al., 2006) and to provide cognitive benefits (Hillen et al., 2010; Takamura et al., 2011).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Oddo et al., 2006
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“Synapse deterioration in tg-mice is prevented by ICV injections of oligomer-specific antibodies (Chauhan, 2007; Oddo et al., 2006).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Oddo et al., 2006
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Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles
Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126
Self-citationCommon 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
Self-citationDiffusible, 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-citationAlzheimer Disease in the US Population: Prevalence Estimates Using the 2000 Census
Hebert, L. E., Scherr, P. A., Bienias, J. L., Bennett, D. A., & Evans, D. A. (2003) · Archives of Neurology · doi:10.1001/archneur.60.8.1119 · Cited by 2,168
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,722
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Lewis, J., Dickson, D. W., Lin, W.-L., Chisholm, L., Corral, A., Jones, G., Yen, S.-H., Sahara, N., Skipper, L., Yager, D., et al. (2001) · Science · doi:10.1126/science.1058189 · Cited by 1,611
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- Oddo, 2006, Am. J. Pathol.
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Creed, M. C., & Milgram, N. W. (2010) · AGE · doi:10.1007/s11357-010-9142-z · Cited by 10
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Pluta, R. M., & Jaboski, M. (2012) · InTech eBooks · doi:10.5772/27205 · Cited by 9
Min-Kaung-Wint-Mon, Kida, H., Kanehisa, I., Kurose, M., Ishikawa, J., Sakimoto, Y., Paw-Min-Thein-Oo, Kimura, R., & Mitsushima, D. (2024) · Biomolecules · doi:10.3390/biom14111425 · Cited by 8
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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
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Falangola, M. F., Nie, X., Voltin, J., Ward, R., Dhiman, S., Nietert, P. J., & Jensen, J. H. (2022) · Magnetic Resonance Imaging · doi:10.1016/j.mri.2022.09.002 · Cited by 6
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Gatz, M., Jang, J. Y., Karlsson, I., & Pedersen, N. L. (2013) · Springer eBooks · doi:10.1007/978-1-4614-7447-0_7 · Cited by 3
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Serpente, M. (2013) · Archivio Istituzionale della Ricerca (Universita Degli Studi Di Milano) · doi:10.13130/serpente-maria_phd2013-02-12
Yanos, M. E. (2014) · ResearchWorks at the University of Washington (University of Washington)
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Lee, Y. (2012) · Georgetown University-Graduate School of Arts & Sciences
Luo, Y. (2008) · Oxidative stress and disease · doi:10.1201/9780849381492.ch18
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Tian, H. (2014)
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Mels, J. (2018) · Scholarship@Western (Western University)
Yates, J. R. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.727680133.793557922
Gonzalo‐Ruiz, A., Delso, M., Carrero, I., Vicente, P. G., Anquela, J. M. S., Rodríguez, M. J., & Arévalo‐Serrano, J. (2011) · European Journal of Anatomy
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Koike, M. A., Myczek, K., Green, K. N., & LaFerla, F. M. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-422-3_6
Self-citationViana, R. J. S. (2010) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT)
Indenkleef, L. S. A. (2015) · Utrecht University Repository (Utrecht University)
Li, W., Fu, H., Youdim, M. B. H., Pang, Y., & Han, Y. (2010) · Springer eBooks · doi:10.1007/978-90-481-8553-5_7
Kapadia, M., Mian, M. F., Ma, D., Hutton, C. P., Azam, A. B., Narkaj, K., Cao, C., Brown, B., Michalski, B., Morgan, D., et al. (2021) · Figshare · doi:10.6084/m9.figshare.13619932
Giménez‐Llort, L., Vida, C., Félix, J., Quer-Palomas, S., Manassra, R., & la Fuente, M. D. (2026) · Diseases · doi:10.3390/diseases14020061
Falangola, M. F., Voltin, J. R., Cole, M., Nietert, P., Liu, F., Iqbal, K., & Jensen, J. H. (2026) · Magnetic Resonance Imaging · doi:10.1016/j.mri.2026.110641
Souchet, B. (2018) · theses.fr (ABES) · doi:10.70675/5510ef76zecf1z41f2z9496z015aa6a093be
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Metadata
- Authors
- Oddo, S., Caccamo, A., Tran, L., Lambert, M. P., Glabe, C. G., Klein, W. L., & LaFerla, F. M.
- Affiliations
- University of California, Irvine (US)
- Northwestern University (US)
- Corresponding author
- LaFerla, Frank M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-01
- Volume
- 281
- Issue
- 3
- Pages
- 1599-1604
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2020497815
- Cited by
- 379
- References
- 41
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 8 · 2023: 5 · 2022: 9 · 2021: 8 · 2020: 12 · 2019: 13 · 2018: 14 · 2017: 16 · 2016: 17 · 2015: 15 · 2014: 21 · 2013: 21 · 2012: 22
- FWCI
- 18.98
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Larry L. Hillblom Foundation
- National Institutes of Health (AG00538)
- National Institute on Aging (AG-11385, AG18877, AG0212982, AG 00538, AG 22547, R01AG022547, R01AG018877)
- 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
- amyloid-beta oligomers, Alzheimer's disease, 3xTg-AD mice, tau pathology, age-dependent accumulation, intrahippocampal injection, amyloid plaques, cognitive impairment, therapeutic target
- MeSH terms
- Aging, Alzheimer Disease, Animals, Disease Models, Animal, Hippocampus, Humans, Functional Laterality, Mice, Transgenic, Neurons, Recombinant Proteins, Amyloid beta-Peptides, tau Proteins, Macromolecular Substances, Mice
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