Cryo-EM structures of amyloid-β 42 filaments from human brains-Reference-Cited by-同舟云学术

Cryo-EM structures of amyloid-β 42 filaments from human brains

Published:2022-01-14 Issue:6577 Volume:375 Page:167-172
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Yang Yang¹^ORCID,Arseni Diana¹^ORCID,Zhang Wenjuan¹^ORCID,Huang Melissa¹^ORCID,Lövestam Sofia¹^ORCID,Schweighauser Manuel¹,Kotecha Abhay²^ORCID,Murzin Alexey G.¹,Peak-Chew Sew Y.¹,Macdonald Jennifer¹^ORCID,Lavenir Isabelle¹^ORCID,Garringer Holly J.³^ORCID,Gelpi Ellen⁴^ORCID,Newell Kathy L.³^ORCID,Kovacs Gabor G.⁴⁵^ORCID,Vidal Ruben³^ORCID,Ghetti Bernardino³^ORCID,Ryskeldi-Falcon Benjamin¹^ORCID,Scheres Sjors H. W.¹^ORCID,Goedert Michel¹^ORCID

Affiliation:

1. Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.

2. Thermo Fisher Scientific, Eindhoven, Netherlands.

3. Department of Pathology and Laboratory Medicine, Indiana University, Indianapolis, IN, USA.

4. Institute of Neurology, Medical University, Vienna, Austria.

5. Tanz Centre and Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada.

Abstract

Hi-res view of human Aβ42 filaments Alzheimer’s disease is characterized by a loss of memory and other cognitive functions and the filamentous assembly of Aβ and tau in the brain. The assembly of Aβ peptides into filaments that end at residue 42 is a central event. Yang et al . used electron cryo–electron microscopy to determine the structures of Aβ42 filaments from human brain (see the Perspective by Willem and Fändrich). They identified two types of related S-shaped filaments, each consisting of two identical protofilaments. These structures will inform the development of better in vitro and animal models, inhibitors of Aβ42 assembly, and imaging agents with increased specificity and sensitivity. —SMH

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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