The DOI matches its Crossref record; 151 of the 153 references it cites were found in a registry or an index.
Intracellular amyloid-β in Alzheimer's disease
Abstract
The primal role that the amyloid-beta (Abeta) peptide has in the development of Alzheimer's disease is now almost universally accepted. It is also well recognized that Abeta exists in multiple assembly states, which have different physiological or pathophysiological effects. Although the classical view is that Abeta is deposited extracellularly, emerging evidence from transgenic mice and human patients indicates that this peptide can also accumulate intraneuronally, which may contribute to disease progression.
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“verified that plaque deposition requires BACE1 activity, as previously shown [17-20].”
From Neuron loss in the 5XFAD mouse model of Alzheimer’s disease correlates with intraneuronal Aβ42 accumulation and Caspase-3 activation (2013) · cites this paper as [17]
In the citing paper
“In PD, intracellular inclusions of alpha-synuclein (αSYN) are found in neurons and glia, while both extracellular and intracellular deposits of amyloid-beta (Aβ) are present in the AD brain [2, 3].”
From Crosstalk between astrocytes and microglia results in increased degradation of α-synuclein and amyloid-β aggregates (2021) · cites this paper as [3]
In the citing paper
“A accumulation occurs prior to extracellular amyloid formation, has been implicated in the onset of early cognitive alterations, and may contribute to the pathological cascade of events that leads to neuronal dysfunction and, eventually, to AD (12,13).”
From Molecular Basis for Increased Risk for Late-onset Alzheimer Disease Due to the Naturally Occurring L28P Mutation in Apolipoprotein E4 (2014) · cites this paper as [12]
In the citing paper
“Furthermore, the 42-amino acid A (A42) constitutes the majority of intraneuronal A (12).”
From Molecular Basis for Increased Risk for Late-onset Alzheimer Disease Due to the Naturally Occurring L28P Mutation in Apolipoprotein E4 (2014) · cites this paper as [12]
In the citing paper
“Accumulation of A, the majority of which is A42, occurs prior to extracellular amyloid formation, has been implicated in the onset of early cognitive alterations, and may contribute to the pathological cascade of events that lead to neuronal dysfunction and, eventually, to AD (12,13).”
From Molecular Basis for Increased Risk for Late-onset Alzheimer Disease Due to the Naturally Occurring L28P Mutation in Apolipoprotein E4 (2014) · cites this paper as [12]
In the citing paper
“Since accumulation of Aβ42 within AD vulnerable neurons has been associated with physiological, pathological and behavioral abnormalities even prior to plaques [12, 140, 187, 188], the evidence is mounting that intraneuronal Aβ42 is the driving force in Aβ-related AD pathogenesis [9, 58, 92].”
From Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease (2010) · cites this paper as [92]
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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
RetractedGlenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
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-citationVassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876
Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676
Morris, R. G. M., Anderson, E., Lynch, G. S., & Baudry, M. (1986) · Nature · doi:10.1038/319774a0 · Cited by 3,640
Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1202-06.2006 · Cited by 3,530
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
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Astarita, G., Jung, K.-M., Berchtold, N. C., Nguyen, V. Q., Gillen, D. L., Head, E., Cotman, C. W., & Piomelli, D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012538 · Cited by 218
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Wessels, A. M., Tariot, P. N., Zimmer, J. A., Selzler, K. J., Bragg, S. M., Andersen, S. W., Landry, J., Krull, J. H., Downing, A. M., Willis, B. A., et al. (2020) · JAMA Neurology · doi:10.1001/jamaneurol.2019.3988 · Cited by 209
Mysterious oligomerization of the amyloidogenic proteins
Uversky, V. N. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07721.x · Cited by 219
The role of the immune system in Alzheimer disease: Etiology and treatment
Jevtic, S. D., Sengar, A. S., Salter, M. W., & McLaurin, J. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2017.08.005 · Cited by 224
Olfactory epithelium amyloid‐β and paired helical filament‐tau pathology in Alzheimer disease
Arnold, S. E., Lee, E. B., Moberg, P. J., Stutzbach, L., Kazi, H., Han, L., Lee, V. M. ‐., & Trojanowski, J. Q. (2009) · Annals of Neurology · doi:10.1002/ana.21910 · Cited by 215
Chen, H.-K., Ji, Z.-S., Dodson, S. E., Miranda, R. D., Rosenblum, C. I., Reynolds, I. J., Freedman, S. B., Weisgraber, K. H., Huang, Y., & Mahley, R. W. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.151084 · Cited by 209
Loss of O -GlcNAc glycosylation in forebrain excitatory neurons induces neurodegeneration
Wang, A. C., Jensen, E. H., Rexach, J. E., Vinters, H. V., & Hsieh-Wilson, L. C. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1606899113 · Cited by 211
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Grasso, M., Piscopo, P., Confaloni, A., & Denti, M. (2014) · Molecules · doi:10.3390/molecules19056891 · Cited by 208
Naert, G., & Rivest, S. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.0299-11.2011 · Cited by 207
“The significant correlation between cognitive deficit and intracellular A levels supports the hypothesis that intracellular A impairs neuronal functions (Wirths et al., 2004; LaFerla et al., 2007).”
BackgroundLiu, Y., Yoo, M.-J., Savonenko, A., Stirling, W., Price, D. L., Borchelt, D. R., Mamounas, L., Lyons, W. E., Blue, M. E., & Lee, M. K. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4218-08.2008 · Cited by 206
The Insulin/Akt Signaling Pathway Is Targeted by Intracellular β-Amyloid
Lee, H.-K., Kumar, P., Fu, Q., Rosen, K. M., & Querfurth, H. W. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-07-0777 · Cited by 185
Dual roles for autophagy: Degradation and secretion of Alzheimer's disease Aβ peptide
Nilsson, P., & Saido, T. C. (2014) · BioEssays · doi:10.1002/bies.201400002 · Cited by 206
Bee venom therapy: Potential mechanisms and therapeutic applications
Zhang, S., Liu, Y. F., Yang, Y., Wang, X., Lin, L.-T., Xiao, L., Zhou, P., Shi, G., & Liu, C. (2018) · Toxicon · doi:10.1016/j.toxicon.2018.04.012 · Cited by 203
Metadata
- Authors
- LaFerla, F. M., Green, K. N., & Oddo, S.
- Affiliations
- University of California, Irvine (US)
- Corresponding author
- LaFerla, Frank M.
- Venue
- Nature Reviews Neuroscience
- Published
- 2007-07
- Volume
- 8
- Issue
- 7
- Pages
- 499-509
- ISSN
- 1471-003X (ISSN-L)
- 1471-0048
- OpenAlex
- W1602771322
- Cited by
- 1,942
- References
- 153
- Citations by year
- 2026: 69 · 2025: 74 · 2024: 106 · 2023: 73 · 2022: 87 · 2021: 110 · 2020: 137 · 2019: 122 · 2018: 129 · 2017: 117 · 2016: 119 · 2015: 111 · 2014: 107 · 2013: 96 · 2012: 118
- FWCI
- 9.14
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature reviews. Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- 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, intraneuronal amyloid-beta, Alzheimer's disease, amyloid plaques, amyloid-beta production, neuronal pathology, transgenic mouse model
- MeSH terms
- Alzheimer Disease, Animals, Brain, Humans, Intracellular Fluid, Synaptic Transmission, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Extracellular Fluid, Proteasome Endopeptidase Complex, Plaque, Amyloid
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