eprintid: 10077293
rev_number: 20
eprint_status: archive
userid: 608
dir: disk0/10/07/72/93
datestamp: 2019-07-03 09:49:19
lastmod: 2021-09-19 23:01:22
status_changed: 2020-03-06 17:48:23
type: article
metadata_visibility: show
creators_name: Fitzpatrick, AW
creators_name: Saibil, HR
title: Cryo-EM of amyloid fibrils and cellular aggregates
ispublished: pub
divisions: UCL
divisions: B02
divisions: C08
divisions: D09
divisions: G03
note: This is an open access article under the CC BY license (http://creativecommons.
org/licenses/by/4.0/).
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.
date: 2019-10
date_type: published
official_url: https://doi.org/10.1016/j.sbi.2019.05.003
oa_status: green
full_text_type: pub
language: eng
primo: open
primo_central: open_green
verified: verified_manual
elements_id: 1668050
doi: 10.1016/j.sbi.2019.05.003
pii: S0959-440X(18)30209-4
lyricists_name: Saibil, Helen
lyricists_id: HRSAI29
actors_name: Flynn, Bernadette
actors_id: BFFLY94
actors_role: owner
full_text_status: public
publication: Current Opinion in Structural Biology
volume: 58
pagerange: 34-42
event_location: England
issn: 1879-033X
citation:        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 <https://doi.org/10.1016/j.sbi.2019.05.003>.       Green open access   
 
document_url: https://discovery.ucl.ac.uk/id/eprint/10077293/1/1-s2.0-S0959440X18302094-main.pdf