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