Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids.
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Summary
A partially hypothetic fibril selection model will be described that may be suitable to explain why amyloid fibrils look the way they do, in particular, why at least all so far reported high resolution cryo-electron microscopy obtained fibrIL structures are in register, parallel, cross-β-sheetfibrils that mostly consist of two protofilaments twisted around each other.
- Type
- review
- Published
- 2021-06-17
- Cited by
- 187
- References
- 0
- Access
- Open access
- OpenAlex
- https://openalex.org/W3168207341
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:235462564
Keywords
Fibril, Chemistry, Amyloid (mycology), Amyloid fibril, Protein aggregation
References
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