Journal
BIOCHEMISTRY
Volume 59, Issue 5, Pages 639-646Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.biochem.9b01069
Keywords
-
Categories
Funding
- Major State Basic Research Development Program [2016YFA0501902]
- National Natural Science Foundation (NSF) of China [91853113, 31872716]
- Science and Technology Commission of Shanghai Municipality [18JC1420500]
- Shanghai Municipal Education Commission
- Shanghai Pujiang Program [18PJ1404300]
- Shanghai Municipal Science and Technology Major Project [2019SHZDZX02]
- Eastern Scholar project
Ask authors/readers for more resources
Protein amyloid fibrils are originally identified as pathological entities in a variety of neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease. Recent studies have revealed that amyloid fibrils also serve as functional protein assemblies to fulfill a wide range of biological functions. Deciphering the molecular basis underlying the assembly of amyloid fibrils is essential for understanding their biological and pathological functions. Here, we summarize recent advances in the atomic structure determination of amyloid fibrils formed by both amyloidogenic peptides and full-length proteins. Furthermore, we demonstrate the diversity of amyloid fibrils, with a primary focus on the reversible fibrils, in sequence composition, self-assembled architecture, and physiochemical and pathological properties. Finally, we raise questions that will be answered by the future study of amyloid fibril structure.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available