The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Acetylcholinesterase Accelerates Assembly of Amyloid-β-Peptides into Alzheimer's Fibrils: Possible Role of the Peripheral Site of the Enzyme
Open accessAbstract
Acetylcholinesterase (AChE), an important component of cholinergic synapses, colocalizes with amyloid-beta peptide (A beta) deposits of Alzheimer's brain. We report here that bovine brain AChE, as well as the human and mouse recombinant enzyme, accelerates amyloid formation from wild-type A beta and a mutant A beta peptide, which alone produces few amyloid-like fibrils. The action of AChE was independent of the subunit array of the enzyme, was not affected by edrophonium, an active site inhibitor, but it was affected by propidium, a peripheral anionic binding site ligand. Butyrylcholinesterase, an enzyme that lacks the peripheral site, did not affect amyloid formation. Furthermore, AChE is a potent amyloid-promoting factor when compared with other A beta-associated proteins. Thus, in addition to its role in cholinergic synapses, AChE may function by accelerating A beta formation and could play a role during amyloid deposition in Alzheimer's brain.
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Cites
Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022
Molecular and cellular biology of cholinesterases
Massoulié, J., Pezzementi, L., Bon, S., Krejci, E., & Vallette, F.-M. (1993) · Progress in Neurobiology · doi:10.1016/0301-0082(93)90040-y · Cited by 1,214
Ma, J., Yee, A., Brewer, H. B., Das, S., & Potter, H. (1994) · Nature · doi:10.1038/372092a0 · Cited by 871
Evans, K. C., Berger, E. P., Cho, C. G., Weisgraber, K. H., & Lansbury, P. T. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.3.763 · Cited by 333
Arendt, T., Brückner, M. K., Lange, M., & Bigl, V. (1992) · Neurochemistry International · doi:10.1016/0197-0186(92)90189-x · Cited by 314
Ghiso, J., Matsubara, E., Koudinov, A., Choi-Miura, N. H., Tomita, M., Wisniewski, T., & Frangione, B. (1993) · Biochemical Journal · doi:10.1042/bj2930027 · Cited by 304
Cited by
Gaggelli, E., Kozlowski, H., Valensin, D., & Valensin, G. (2006) · Chemical Reviews · doi:10.1021/cr040410w · Cited by 1,729
Harper, J. D., & Lansbury, P. T. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.385 · Cited by 1,652
Targeting acetylcholinesterase and butyrylcholinesterase in dementia
Lane, R. M., Potkin, S. G., & Enz, A. (2005) · The International Journal of Neuropsychopharmacology · doi:10.1017/s1461145705005833 · Cited by 654
Cholinergic system during the progression of Alzheimer’s disease: therapeutic implications
Mufson, E. J., Counts, S. E., Perez, S. E., & Ginsberg, S. D. (2008) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.8.11.1703 · Cited by 587
El-Husseiny, H. M., Mady, E. A., Hamabe, L., Abugomaa, A., Shimada, K., Yoshida, T., Tanaka, T., Yokoi, A., Elbadawy, M., & Tanaka, R. (2022) · Materials Today Bio · doi:10.1016/j.mtbio.2021.100186 · Cited by 533
Metadata
- Authors
- Inestrosa, N. C., Alvarez, A., Pérez, C. A., Moreno, R. D., Vicente, M., Linker, C., Casanueva, O. I., Soto, C., & Garrido, J.
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1996-04
- Volume
- 16
- Issue
- 4
- Pages
- 881-891
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2084107396
- Cited by
- 1,101
- References
- 6
- FWCI
- 13.82
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Acetylcholinesterase Accelerates Assembly of Amyloid-β-Peptides into Alzheimer's Fibrils: Possible Role of the Peripheral Site of the Enzyme. https://app.cochat.ai/papers/10.1016/s0896-6273(00)80108-7
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- Inestrosa, N. C., Alvarez, A., Pérez, C. A., Moreno, R. D., Vicente, M., Linker, C., Casanueva, O. I., Soto, C., & Garrido, J. (1996). Acetylcholinesterase Accelerates Assembly of Amyloid-β-Peptides into Alzheimer's Fibrils: Possible Role of the Peripheral Site of the Enzyme. Neuron. https://doi.org/10.1016/s0896-6273(00)80108-7
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.