The DOI matches its Crossref record; 65 of the 65 references it cites were found in a registry or an index.
Amyloid β-Protein Fibrillogenesis
Open accessAbstract
Alzheimer's disease is characterized by extensive cerebral amyloid deposition. Amyloid deposits associated with damaged neuropil and blood vessels contain abundant fibrils formed by the amyloid beta-protein (Abeta). Fibrils, both in vitro and in vivo, are neurotoxic. For this reason, substantial effort has been expended to develop therapeutic approaches to control Abeta production and amyloidogenesis. Achievement of the latter goal is facilitated by a rigorous mechanistic understanding of the fibrillogenesis process. Recently, we discovered a novel intermediate in the pathway of Abeta fibril formation, the amyloid protofibril (Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., and Teplow, D. B. (1997) J. Biol. Chem. 272, 22364-22372). We report here results of studies of the assembly, structure, and biological activity of these polymers. We find that protofibrils: 1) are in equilibrium with low molecular weight Abeta (monomeric or dimeric); 2) have a secondary structure characteristic of amyloid fibrils; 3) appear as beaded chains in rotary shadowed preparations examined electron microscopically; 4) give rise to mature amyloid-like fibrils; and 5) affect the normal metabolism of cultured neurons. The implications of these results for the development of therapies for Alzheimer's disease and for our understanding of fibril assembly are discussed.
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“oligomeric Aβ rather than fibril Aβ is regarded as the toxic species of this peptide [143,144,145,146].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [144]
Citations
Cites
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Research works printed but not linked: 4
- Alzheimer, 1906, Neurol. Centr., 23, 1129
- Lomakin, 1999, Methods Enzymol., 309
- Naiki, 1996, Lab. Invest., 74, 374
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Sorted by citations
Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,497
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
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Self-citationWalsh, 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
Self-citationInherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
Aβ Oligomers – a decade of discovery
Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938
Self-citation
Metadata
- Authors
- Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B.
- Affiliations
- Brigham and Women's Hospital (US)
- Massachusetts Institute of Technology (US)
- Corresponding author
- Teplow, David B.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-09
- Volume
- 274
- Issue
- 36
- Pages
- 25945-25952
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2073516240
- Cited by
- 1,046
- References
- 65
- Citations by year
- 2026: 5 · 2025: 10 · 2024: 14 · 2023: 15 · 2022: 18 · 2021: 20 · 2020: 24 · 2019: 13 · 2018: 23 · 2017: 26 · 2016: 39 · 2015: 43 · 2014: 38 · 2013: 34 · 2012: 58
- FWCI
- 21.57
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- Amgen
- Brigham and Women's Hospital
- Foundation for Neurologic Diseases
- National Institutes of Health (5p01ag014366-05)
- National Institute on Aging (1PO1 AG14366, 1RO1 AG12749, R01AG012749)
- National Institute of Neurological Disorders and Stroke (R01NS038328, 1RO1 NS38328)
- 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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- amyloid-beta, fibril formation, amyloid protofibrils, Alzheimer's disease, amyloid deposition, neurotoxicity, secondary structure, neuronal metabolism, amyloid fibril formation, Alzheimer's disease treatment
- MeSH terms
- Alzheimer Disease, Humans, Amyloid beta-Peptides, Protein Structure, Secondary, Protein Folding, Dimerization
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