The DOI matches its Crossref record; 69 of the 69 references it cites were found in a registry or an index.
Lack of BACE1 S-palmitoylation reduces amyloid burden and mitigates memory deficits in transgenic mouse models of Alzheimer’s disease
Abstract
Significance: Alzheimer’s disease (AD) is a devastating neurodegenerative disorder for which no preventative drug or cure is currently available. BACE1 is a key enzyme that initiates the production of β-amyloid peptides (Aβ), which accumulate in AD brain and contribute to cognitive decline. BACE1 undergoes S-palmitoylation, a lipid modification that is known to regulate neuronal protein trafficking. We investigated the in vivo significance of BACE1 S-palmitoylation by generating knock-in mice selectively lacking this modification. The lack of BACE1 S-palmitoylation impaired synaptic activity-induced Aβ production, significantly reduced cerebral amyloid burden in AD mouse models, and mitigated cognitive deficits. Using transgenic mouse models, our results demonstrate that intrinsic posttranslational S-palmitoylation of BACE1 has a significant impact on amyloid pathogenesis and the consequent cognitive decline.
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“Dystrophic neurites are found in a halo around fibrillar plaques and are characterized by the accumulation of LAMP1 and APP32–34.”
From Sustained microglial depletion with CSF1R inhibitor impairs parenchymal plaque development in an Alzheimer’s disease model (2019) · cites this paper as [32]
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“As expected (42), 5XFAD mice showed a significant decrease in the percentage of spontaneous alternation.”
BackgroundMethodInfluentialAlzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
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A mutation in APP protects against Alzheimer’s disease and age-related cognitive decline
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Synaptic Activity Regulates Interstitial Fluid Amyloid-β Levels In Vivo
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Self-citationPalmitoylation: policing protein stability and traffic
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Amyloid Precursor Protein Trafficking, Processing, and Function
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Self-citationEndoproteolysis of Presenilin 1 and Accumulation of Processed Derivatives In Vivo
Thinakaran, G., Borchelt, D. R., Lee, M. K., Slunt, H. H., Spitzer, L., Kim, G., Ratovitsky, T., Davenport, F., Nordstedt, C., Seeger, M., et al. (1996) · Neuron · doi:10.1016/s0896-6273(00)80291-3 · Cited by 1,013
Self-citationRelease of Excess Amyloid β Protein from a Mutant Amyloid β Protein Precursor
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Cited by
Spangenberg, E., Severson, P. L., Hohsfield, L. A., Crapser, J., Zhang, J., Burton, E. A., Zhang, Y., Spevak, W., Lin, J., Phan, N. Y., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11674-z · Cited by 939
Practical considerations for choosing a mouse model of Alzheimer’s disease
Jankowsky, J. L., & Zheng, H. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0231-7 · Cited by 449
PSD-95 protects synapses from β-amyloid
Dore, K., Carrico, Z., Alfonso, S., Marino, M., Koymans, K., Kessels, H. W., & Malinow, R. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109194 · Cited by 149
Amyloid Precursor Protein and Alzheimer’s Disease
Orobets, K. S., & Karamyshev, A. L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914794 · Cited by 141
Andrew, R. J., De Rossi, P., Nguyen, P., Kowalski, H. R., Recupero, A. J., Guerbette, T., Krause, S. V., Rice, R. C., Laury-Kleintop, L., Wagner, S. L., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006379 · Cited by 55
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Metadata
- Authors
- Andrew, R. J., Fernandez, C. G., Stanley, M., Jiang, H., Nguyen, P., Rice, R. C., Buggia-Prévot, V., De Rossi, P., Vetrivel, K. S., Lamb, R., Argemi, A., Allaert, E. S., Rathbun, E. M., Krause, S. V., Wagner, S. L., Parent, A. T., Holtzman, D. M., & Thinakaran, G.
- Affiliations
- Department of Neurobiology, The University of Chicago, Chicago, IL 60637;
- Hope Center for Neurological Disorders, Department of Neurology, Washington University School of Medicine, St. Louis, MO 63110;
- Department of Neurosciences, University of California, San Diego, La Jolla, CA 92093
- ORCID
- Thinakaran, Gopal
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2017-10-23
- Volume
- 114
- Issue
- 45
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 69
- References
- 69
- Language
- en
- Funders
- HHS | NIH | National Institute on Aging (AG019070, AG051230, AG046710)
- HHS | NIH | National Institute of Neurological Disorders and Stroke (P01 NS080675, NS055223)
- Cure Alzheimer's Fund (NA)
- HHS | NIH | National Institute of General Medical Sciences (GM07839-30)
- BrightFocus Foundation (NA)
- HHS | National Institutes of Health (S10OD010649)
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- CoChat. (2026). Citation check: Lack of BACE1 S-palmitoylation reduces amyloid burden and mitigates memory deficits in transgenic mouse models of Alzheimer’s disease. https://app.cochat.ai/papers/10.1073/pnas.1708568114
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- Andrew, R. J., Fernandez, C. G., Stanley, M., Jiang, H., Nguyen, P., Rice, R. C., Buggia-Prévot, V., De Rossi, P., Vetrivel, K. S., Lamb, R., Argemi, A., Allaert, E. S., Rathbun, E. M., Krause, S. V., Wagner, S. L., Parent, A. T., Holtzman, D. M., & Thinakaran, G. (2017). Lack of BACE1 S-palmitoylation reduces amyloid burden and mitigates memory deficits in transgenic mouse models of Alzheimer’s disease. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1708568114
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
