Fitzpatrick, AW;
Saibil, HR;
(2019)
Cryo-EM of amyloid fibrils and cellular aggregates.
Current Opinion in Structural Biology
, 58
pp. 34-42.
10.1016/j.sbi.2019.05.003.
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Abstract
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.
| Type: | Article |
|---|---|
| Title: | Cryo-EM of amyloid fibrils and cellular aggregates |
| Location: | England |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1016/j.sbi.2019.05.003 |
| Publisher version: | https://doi.org/10.1016/j.sbi.2019.05.003 |
| Language: | English |
| Additional information: | This is an open access article under the CC BY license (http://creativecommons. org/licenses/by/4.0/). |
| UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology |
| URI: | https://discovery.ucl.ac.uk/id/eprint/10077293 |
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