The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Structural Studies of Amyloid Proteins at the Molecular Level
Open accessAbstract
Dozens of proteins are known to convert to the aggregated amyloid state. These include fibrils associated with systemic and neurodegenerative diseases and cancer, functional amyloid fibrils in microorganisms and animals, and many denatured proteins. Amyloid fibrils can be much more stable than other protein assemblies. In contrast to globular proteins, a single protein sequence can aggregate into several distinctly different amyloid structures, termed polymorphs, and a given polymorph can reproduce itself by seeding. Amyloid polymorphs may be the molecular basis of prion strains. Whereas the Protein Data Bank contains some 100,000 globular protein and 3,000 membrane protein structures, only a few dozen amyloid protein structures have been determined, and most of these are short segments of full amyloid-forming proteins. Regardless, these amyloid structures illuminate the architecture of the amyloid state, including its stability and its capacity for formation of polymorphs.
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Cites
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Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
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“The suggestion that amyloid oligomers have common structural features regardless of constituent amyloid protein was based on the production of an antibody termed A11 that was reported to bind to all oligomers (92).”
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Self-citationThe toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes
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Multimodal techniques for diagnosis and prognosis of Alzheimer's disease
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Cited by
Fibril structure of amyloid-β(1–42) by cryo–electron microscopy
Gremer, L., Schölzel, D., Schenk, C., Reinartz, E., Labahn, J., Ravelli, R. B. G., Tusche, M., Lopez-Iglesias, C., Hoyer, W., Heise, H., et al. (2017) · Science · doi:10.1126/science.aao2825 · Cited by 1,041
Cao, Y., & Mezzenga, R. (2019) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2019.05.002 · Cited by 649
The expanding amyloid family: Structure, stability, function, and pathogenesis
Sawaya, M. R., Hughes, M. P., Rodriguez, J. A., Riek, R., & Eisenberg, D. S. (2021) · Cell · doi:10.1016/j.cell.2021.08.013 · Cited by 475
Self-citationAmyloid Polymorphism in the Protein Folding and Aggregation Energy Landscape
Adamcik, J., & Mezzenga, R. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201713416 · Cited by 346
Structure-based inhibitors of tau aggregation
Seidler, P. M., Boyer, D. R., Rodriguez, J. A., Sawaya, M. R., Cascio, D., Murray, K., Gonen, T., & Eisenberg, D. S. (2018) · Nature Chemistry · doi:10.1038/nchem.2889 · Cited by 339
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Metadata
- Authors
- Eisenberg, D. S., & Sawaya, M. R.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2017-06-20
- Volume
- 86
- Issue
- 1
- Pages
- 69-95
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2560598375
- Cited by
- 523
- References
- 12
- FWCI
- 3.90
- Type
- journal article
- Language
- en
- Open access
- bronze
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