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Structures for amyloid fibrils (mini-review)
journal contribution
posted on 2023-06-08, 07:38 authored by O Sumner Makin, Louise SerpellLouise SerpellAlzheimer's disease and Creutzfeldt¿Jakob disease are the best-known examples of a group of diseases known as the amyloidoses. They are characterized by the extracellular deposition of toxic, insoluble amyloid fibrils. Knowledge of the structure of these fibrils is essential for understanding the process of pathology of the amyloidoses and for the rational design of drugs to inhibit or reverse amyloid formation. Structural models have been built using information from a wide variety of techniques, including X-ray diffraction, electron microscopy, solid state NMR and EPR. Recent advances have been made in understanding the architecture of the amyloid fibril. Here, we describe and compare postulated structural models for the mature amyloid fibril and discuss how the ordered structure of amyloid contributes to its stability
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Publication status
- Published
Journal
FEBS JournalISSN
1742-464XExternal DOI
Issue
23Volume
272Page range
5950-5961Department affiliated with
- Biochemistry Publications
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- No
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- Yes
Legacy Posted Date
2012-02-06Usage metrics
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