The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
Open accessAbstract
BACKGROUND: Brain amyloid plaque, a diagnostic feature of Alzheimer's disease (AD), contains an insoluble fibrillar core that is composed primarily of variants of the beta-amyloid protein (Abeta). As Abeta amyloid fibrils may initiate neurodegeneration, the inhibition of fibril formation is a possible therapeutic strategy. Very little is known about the early steps of the process, however. RESULTS: Atomic force microscopy was used to follow amyloid fibril formation in vitro by the Abeta variants Abeta1-40 and Abeta1-42. Both variants first form small ordered aggregates that grow slowly and then rapidly disappear, while prototypical amyloid fibrils of two discrete morphologies appear. Abeta1-42 aggregates much more rapidly than Abeta1-40, which is consistent with its connection to early-onset AD. We propose that the metastable intermediate species be called Abeta amyloid protofibrils. CONCLUSIONS: Abeta protofibrils are likely to be intermediates in the in vitro assembly of Abeta amyloid fibrils, but their in vivo role has yet to be determined. Numerous reports of a nonfibrillar form of Abeta aggregate in the brains of individuals who are predisposed to AD suggest the existence of a precursor form, possibly the protofibril. Thus, stabilization of Abeta protofibrils may be a useful therapeutic strategy.
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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
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
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Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
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The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes
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Amyloid Beta: Structure, Biology and Structure-Based Therapeutic Development
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Metadata
- Authors
- Harper, J. D., Wong, S. S., Lieber, C. M., & Lansbury, P. T.
- Venue
- Chemistry & Biology
- Publisher
- Elsevier BV
- Published
- 1997
- Volume
- 4
- Issue
- 2
- Pages
- 119-125
- ISSN
- 1074-5521 (ISSN-L)
- OpenAlex
- W2033847972
- Cited by
- 697
- References
- 9
- FWCI
- 13.39
- Type
- journal article
- Language
- en
- Open access
- hybrid
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