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Oligomerization of Alzheimer's β-Amyloid within Processes and Synapses of Cultured Neurons and Brain
Open accessAbstract
Multiple lines of evidence implicate β-amyloid (Aβ) in the pathogenesis of Alzheimer's disease (AD), but the mechanisms whereby Aβ is involved remain unclear. Addition of Aβ to the extracellular space can be neurotoxic. Intraneuronal Aβ42 accumulation is also associated with neurodegeneration. We reported previously that in Tg2576 amyloid precursor protein mutant transgenic mice, brain Aβ42 localized by immunoelectron microscopy to, and accumulated with aging in, the outer membranes of multivesicular bodies, especially in neuronal processes and synaptic compartments. We now demonstrate that primary neurons from Tg2576 mice recapitulate the in vivo localization and accumulation of Aβ42 with time in culture. Furthermore, we demonstrate that Aβ42 aggregates into oligomers within endosomal vesicles and along microtubules of neuronal processes, both in Tg2576 neurons with time in culture and in Tg2576 and human AD brain. These Aβ42 oligomer accumulations are associated with pathological alterations within processes and synaptic compartments in Tg2576 mouse and human AD brains.
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“Intraneuronal Ab is derived from Ab internalized by neurons from the extracellular space through ApoE-dependent and ApoE-independent uptakes and from intrinsic Ab that escapes exocytosis after APP cleavage that takes place in the endocytic compartment.34”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [34]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Intraneuronal accumulation of Ab is a potentially important aspect of AD pathogenesis.”
From Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration (2013) · cites this paper as [34]
In the citing paper
“a subsequent immuno-EM study demonstrated that intraneuronal accumulation of higher molecular weight Aβ42 oligomers (antibody M16; [210]) was invariably associated with neuritic degeneration, even prior to plaques, in vulnerable distal neurites and synaptic compartments in brains of AD transgenic mice and human AD [187].”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [187]
In the citing paper
“C-terminal specific Aβ42 antibodies typically are best at detecting Aβ42 monomers, and have minimal reactivity against oligomers larger than trimers [187].”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [187]
In the citing paper
“Emerging data, such as FAD mutations noted above, and the direct association of intraneuronal Aβ42 with subcellular pathology [187, 188], cell death [23, 167], and behavioral and physiological abnormalities, even prior to plaques, in AD transgenic mouse models [140], are providing increasing evidence for the importance of intraneuronal Aβ.”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [187]
In the citing paper
“Immuno-EM images of completely abnormal Aβ42 accumulating dystrophic neurites [187, 188], lacking the normal microtubule tracks required for organelle trafficking, secretion and exocytosis, argue against the active secretion of aggregating Aβ42 from neuritis prior to the dissolution of the plasma membrane [95].”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [187]
In the citing paper
“It needs to be stressed again that by immuno-EM high molecular weight Aβ42 oligomers are consistently associated with pathology within neurites even prior to plaques [187].”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [187]
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Citations
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
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
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
Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210
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
Holcomb, L., Gordon, M. N., McGowan, E., Yu, X., Benkovic, S., Jantzen, P., Wright, K., Saad, I., Mueller, R., Morgan, D., et al. (1998) · Nature Medicine · doi:10.1038/nm0198-097 · Cited by 1,386
Correlation Between Elevated Levels of Amyloid β-Peptide in the Brain and Cognitive Decline
Näslund, J. (2000) · JAMA · doi:10.1001/jama.283.12.1571 · Cited by 1,268
Receptor downregulation and multivesicular-body sorting
Katzmann, D. J., Odorizzi, G., & Emr, S. D. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm973 · Cited by 1,201
Kawarabayashi, T., Younkin, L. H., Saido, T. C., Shoji, M., Ashe, K. H., & Younkin, S. G. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-02-00372.2001 · Cited by 1,053 · cited 1×
“A 42 oligomerization in Tg2576 mouse brain with aging A previous report showed that microdeposits of A 42 appear as early as 7– 8 months in Tg2576 brain (Kawarabayashi et al., 2001).”
MethodIntraneuronal Aβ42 Accumulation in Human Brain
Gouras, G. K., Tsai, J., Naslund, J., Vincent, B., Edgar, M., Checler, F., Greenfield, J. P., Haroutunian, V., Buxbaum, J. D., Xu, H., et al. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64700-1 · Cited by 991
Self-citation
Research works printed but not linked: 1
- Peters A, Palay SL, Webster Hd (1991) The fine structure of nervous system. Oxford: Oxford UP.
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Lee, H., Moreira, P. I., Zhu, X., Smith, M. A., & Perry, G. L. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63404-9 · Cited by 19
Vrancx, C., & Annaert, W. G. (2025) · Trends in Neurosciences · doi:10.1016/j.tins.2025.05.007 · Cited by 18
Joshi, P., Riffel, F., Kumar, S., Villacampa, N., Theil, S., Parhizkar, S., Haass, C., Colonna, M., Heneka, M. T., Arzberger, T., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01263-x · Cited by 18
Sethiya, N. K., Ghiloria, N., Srivastav, A., Bisht, D., Chaudhary, S. K., Walia, V., & Alam, M. S. (2023) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527322666230718105358 · Cited by 20
Ovsepian, S. V., & Herms, J. W. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.05.005 · Cited by 19
Chaves, E. (2012) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y2012-076 · Cited by 18
Roy, A., Chandra, K., Dolui, S., & Maiti, N. C. (2017) · ACS Omega · doi:10.1021/acsomega.7b00522 · Cited by 18
Tettevi, E. J., Maina, M. B., Simpong, D. L., Osei-Atweneboana, M. Y., & Ocloo, A. (2022) · Journal of Evidence-Based Integrative Medicine · doi:10.1177/2515690x221114657 · Cited by 19
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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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Mondragón‐Rodríguez, S., Basurto‐Islas, G., Binder, L. I., & García‐Sierra, F. (2008) · Future Neurology · doi:10.2217/14796708.4.1.39 · Cited by 17
Ray, S., Howells, C., Eaton, E. D., Butler, C., Shabala, L., Adlard, P. A., West, A. K., Bennett, W. R., Guillemin, G. J., & Chung, R. S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019026 · Cited by 16
Cheng, F., Ruscher, K., Fransson, L., & Mani, K. (2013) · Glycobiology · doi:10.1093/glycob/cwt079 · Cited by 17
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Sun, A. Y., Wang, Q., Simonyi, Á., & Sun, G. Y. (2011) · Oxidative stress and disease · doi:10.1201/b10787-16 · Cited by 15
Critical thinking of Alzheimer’s transgenic mouse model: current research and future perspective
Li, X., Quan, M., Wei, Y., Wang, W., Xu, L., Wang, Q., & Jia, J. (2023) · Science China Life Sciences · doi:10.1007/s11427-022-2357-x · Cited by 14
Sun, L., Guo, C., Wang, T., Li, X., Li, G., Luo, Y., & Xiao, S. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140231 · Cited by 14
Synapsin 1 promotes Aβ generation via BACE1 modulation
Maesako, M., Zoltowska, K. M., & Berezovska, O. (2019) · PLoS ONE · doi:10.1371/journal.pone.0226368 · Cited by 14
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Konings, S. C., Nyberg, E., Martinsson, I., Torres-Garcia, L., Klementieva, O. L., Almeida, C. G., & Gouras, G. K. (2023) · Life Science Alliance · doi:10.26508/lsa.202201887 · Cited by 12
Self-citationKuszczyk, M. A., Sadowski, M. J., Antkiewicz‐Michaluk, L., & Łazarewicz, J. W. (2013) · Neurotoxicity Research · doi:10.1007/s12640-013-9440-1 · Cited by 13
He, P., Schulz, P., & Sierks, M. R. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.015327 · Cited by 11
Das, H., Sarkar, S., Paidi, R. K., & Biswas, S. C. (2021) · The FASEB Journal · doi:10.1096/fj.202001676rr · Cited by 12
Willis, M., Prokesch, M., Hutter‐Paier, B., Windisch, M., Stridsberg, M., Mahata, S. K., Kirchmair, R., Wietzorrek, G., Knaus, H., Jellinger, K. A., et al. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-13202 · Cited by 12
Actor-Engel, H. S., Schwartz, S. L., Crosby, K. C., Sinnen, B. L., Prikhodko, O., Ramsay, H. J., Bourne, J. N., Winborn, C. S., Lucas, A., Smith, K. R., et al. (2021) · eNeuro · doi:10.1523/eneuro.0416-21.2021 · Cited by 11
Wang, B.-Y., Gu, B.-C., Wang, G., Yang, Y., & Wu, C.-C. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.853947 · Cited by 15
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Tan, S., Ma, G., Li, Y., Li, J., Yao, W., Ren, X., Liu, X., & Gao, J. (2012) · Neurological Research · doi:10.1179/1743132812y.0000000069 · Cited by 11
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Lin, L., Petralia, R. S., Lake, R. G., Wang, Y., & Hoffman, D. A. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01065-7 · Cited by 11
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Mirfakhar, F. S., Castanheira, J., Domingues, R., Ramalho, J. S., & Almeida, C. G. (2024) · Journal of Neuroscience · doi:10.1523/jneurosci.1734-23.2024 · Cited by 10
Self-citationNonhuman Amyloid Oligomer Epitope Reduces Alzheimer’s-Like Neuropathology in 3xTg-AD Transgenic Mice
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Allen, P. B., & Chiu, D. T. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.02.002 · Cited by 10
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Borutaite, V., Morkuniene, R., & Valincius, G. (2011) · bmc · doi:10.1515/bmc.2011.019 · Cited by 9
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Self-citationRammohan, A., Bhaskar, B. V., & Zyryanov, G. V. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91221-1.00009-9 · Cited by 8
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Gouras, G. K. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00185 · Cited by 10
Self-citationCulturing adult rat hippocampal neurons with long-interval changing media.
Majd, S., Zarifkar, A., Rastegar, K., & Takhshid, M. A. (2008) · PubMed · Cited by 9
Gunawardena, S. (2013) · Pharmaceutical Research · doi:10.1007/s11095-013-1037-0 · Cited by 8
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Bhaskar, K., & Lamb, B. T. (2011) · Springer eBooks · doi:10.1007/978-94-007-2774-8_5 · Cited by 8
Pascual, A. C., Gaveglio, V. L., Giusto, N. M., & Pasquaré, S. J. (2017) · Neuroscience · doi:10.1016/j.neuroscience.2017.08.042 · Cited by 8
Chakraborty, H., Devi, P. G., Sarkar, M., & Dasgupta, D. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-803961-8.50001-4 · Cited by 8
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Goldsbury, C. S., Thies, E., Konzack, S., & Mandelkow, E. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.5024-06.2007 · Cited by 8
Sui, H. X., Zhan, L., Niu, X., Liang, L., & Li, X. (2017) · Neuropeptides · doi:10.1016/j.npep.2017.03.001 · Cited by 8
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Imbimbo, B. P., & Speroni, F. (2005) · Wiley eBooks · doi:10.1002/0471266949.bmc112 · Cited by 6
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Kim, M. J., Huh, Y. H., Choi, K. J., Jun, S., Je, A. R., Chae, H., Lee, C., & Kweon, H. (2012) · Han-guk hyeonmigyeong hakoeji/Applied microscopy · doi:10.9729/am.2012.42.4.179 · Cited by 6
Harris, J. R. (2006) · Springer eBooks · doi:10.1007/0-387-23226-5_1 · Cited by 6
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Garcia, M. G., Paulus, A., Vázquez‐Reyes, S., Klementieva, O. L., Gouras, G. K., Bachiller, S., & Deierborg, T. (2023) · Brain Behavior & Immunity - Health · doi:10.1016/j.bbih.2023.100663 · Cited by 5
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Suenaga, M., Furuta, A., Wakabayashi, K., Saibara, T., & Matsunaga, Y. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2015.04.028 · Cited by 4
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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Androuin, A., Thierry, M., Boluda, S., Baskaran, A., Langui, D., Duyckaerts, C., Potier, M., Hachimi, K. E., Delatour, B., & Marty, S. (2022) · Journal of Alzheimer's Disease · doi:10.3233/jad-215692 · Cited by 4
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Borchelt, D., & Savonenko, A. V. (2008) · Handbook of behavioral neuroscience · doi:10.1016/s1569-7339(08)00230-0 · Cited by 4
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Tampellini, D., & Gouras, G. K. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-328-8_22 · Cited by 4
Self-citationNeuronal aging potentiates beta-amyloid generation via amyloid precursor protein endocytosisPreprint
Burrinha, T., Gomes, R. A., Terrasso, A. P., & Almeida, C. G. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/616540 · Cited by 4
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Mondal, M., Bali, J., Tzioras, M., Paolicelli, R. C., Jawaid, A., Malnar, M., Dominko, K., Udayar, V., Halima, S. B., Vadodaria, K. C., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.13.381186 · Cited by 3
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Wen, G., Lindblom, N., Zhan, X., Garcia, M. G., Deierborg, T., Kobro‐Flatmoen, A., & Gouras, G. K. (2026) · Alzheimer s & Dementia · doi:10.1002/alz.71121 · Cited by 2
Self-citationHeat Shock Proteins, Unfolded Protein Response Chaperones and Alzheimer’s Disease
Magrané, J., & Querfurth, H. W. (2008) · Springer eBooks · doi:10.1007/978-1-4020-8231-3_2 · Cited by 2
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Shamchuk, A. L., & Tierney, K. B. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-415894-8.00027-0 · Cited by 2
Sun, J., Shao, X., Wang, X. L., Yin, X., Qiu, W., Qian, X., Liu, F., Chen, Y., & Ma, C. (2025) · Molecular Brain · doi:10.1186/s13041-025-01226-6 · Cited by 4
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Ross, J. A., Mathews, P. M., & Bockstaele, E. J. V. (2018) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2018.10.032 · Cited by 2
Cole, G. M., & Frautschy, S. A. (2006) · Neuron · doi:10.1016/j.neuron.2006.09.005 · Cited by 2
Early Intraneuronal β-Amyloid Pathology: Do Transgenic Mice Represent Valid Model Systems?
Wirths, O., & Bayer, T. A. (2008) · Open Longevity Science · doi:10.2174/1874369200802010007 · Cited by 2
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LEUVEN, F. V. (2006) · Behavioural Pharmacology · doi:10.1097/00008877-200609000-00033 · Cited by 2
Adams, D. J., Shen, C., Levenga, J., Basta, T., Eisenberg, S. P., Mapes, J., Hampton, L., Grounds, K. M., Hoeffer, C. A., & Stowell, M. H. B. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/129551 · Cited by 2
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Matsubara, E. (2013) · Journal of Gerontology & Geriatric Research · doi:10.4172/2167-7182.s2-001 · Cited by 1
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Cole, G. M., Ma, Q., Yang, F., Deshpande, A. M., Ubeda, O. J., & Frautschy, S. A. (2010) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-04300-0_11 · Cited by 1
Amyloid β-protein oligomers and Alzheimer's
Hayden, E. Y., & Teplow, D. B. (2013) · Cited by 1
Bansal, V. A., Tan, J. M., Soon, H. R., Zainolabidin, N., Saido, T. C., & Ch’ng, T. H. (2024) · eLife · doi:10.7554/elife.92069.3 · Cited by 4
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Lippa, C. F., & Rosso, A. L. (2012) · American Journal of Alzheimer s Disease & Other Dementias® · doi:10.1177/1533317512446187 · Cited by 1
Caprelli, M. T. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.1260-17.2017 · Cited by 1
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Zhang, Y. (2011) · Wiley eBooks · doi:10.1002/9783527634323.ch6 · Cited by 1
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Lord, A. (2009) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
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Metadata
- Authors
- Takahashi, R. H., Almeida, C. G., Kearney, P. F., Yu, F., Lin, M. T., Milner, T. A., & Gouras, G. K.
- Affiliations
- Cornell University (US)
- Corresponding author
- Gouras, Gunnar K.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2004-04-07
- Volume
- 24
- Issue
- 14
- Pages
- 3592-3599
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6729733
- OpenAlex
- W2128779293
- Cited by
- 445
- References
- 48
- Citations by year
- 2026: 9 · 2025: 9 · 2024: 10 · 2023: 10 · 2022: 18 · 2021: 18 · 2020: 9 · 2019: 16 · 2018: 13 · 2017: 19 · 2016: 14 · 2015: 12 · 2014: 18 · 2013: 22 · 2012: 26
- FWCI
- 22.01
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Funders
- American Academy of Neurology
- National Institutes of Health (2k08ns002037-04, HL18974)
- National Heart, Lung, and Blood Institute (HL-18974, P01HL018974)
- National Institute of Neurological Disorders and Stroke (NS02037, R01NS045677, NS 045677)
- 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, neural processes, synapses, multivesicular bodies, endosomal vesicles, microtubules, Tg2576 mice, amyloid precursor protein, neurodegeneration, primary neurons
- MeSH terms
- Adult, Aging, Alzheimer Disease, Animals, Brain, Cells, Cultured, Disease Models, Animal, Fluorescent Antibody Technique, Humans, Mice, Transgenic, Microtubules, Middle Aged, Neurons, Peptide Fragments, Endosomes, Synapses, Organelles, Amyloid beta-Peptides, Macromolecular Substances, Mice
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