TY  - JOUR
TI  - Cryo-EM of amyloid fibrils and cellular aggregates
UR  - https://doi.org/10.1016/j.sbi.2019.05.003
SP  - 34
JF  - Current Opinion in Structural Biology
EP  - 42
AV  - public
ID  - discovery10077293
SN  - 1879-033X
N1  - This is an open access article under the CC BY license (http://creativecommons.
org/licenses/by/4.0/).
VL  - 58
Y1  - 2019/10//
A1  - Fitzpatrick, AW
A1  - Saibil, HR
N2  - Neurodegenerative and other protein misfolding diseases are associated with the aggregation of a protein, which may be mutated in genetic forms of disease, or the wild type form in late onset sporadic disease. A wide variety of proteins and peptides can be involved, with aggregation originating from a natively folded or a natively unstructured species. Large deposits of amyloid fibrils are typically associated with cell death in late stage pathology. In this review, we illustrate the contributions of cryo-EM and related methods to the structure determination of amyloid fibrils extracted post mortem from patient brains or formed in vitro. We also discuss cell models of protein aggregation and the contributions of electron tomography to understanding the cellular context of aggregation.
ER  -