Cryo-EM structures of amyloid-β 42 filaments from human brains.
Aged
Aged, 80 and over
Alzheimer Disease
/ metabolism
Amino Acid Sequence
Amyloid beta-Peptides
/ chemistry
Animals
Brain Chemistry
Cryoelectron Microscopy
Female
Gene Knock-In Techniques
Humans
Male
Mice
Middle Aged
Models, Animal
Models, Molecular
Peptide Fragments
/ chemistry
Protein Conformation
Protein Conformation, beta-Strand
Protein Domains
Protein Folding
Journal
Science (New York, N.Y.)
ISSN: 1095-9203
Titre abrégé: Science
Pays: United States
ID NLM: 0404511
Informations de publication
Date de publication:
14 Jan 2022
14 Jan 2022
Historique:
entrez:
13
1
2022
pubmed:
14
1
2022
medline:
29
1
2022
Statut:
ppublish
Résumé
Filament assembly of amyloid-β peptides ending at residue 42 (Aβ42) is a central event in Alzheimer’s disease. Here, we report the cryo–electron microscopy (cryo-EM) structures of Aβ42 filaments from human brains. Two structurally related S-shaped protofilament folds give rise to two types of filaments. Type I filaments were found mostly in the brains of individuals with sporadic Alzheimer’s disease, and type II filaments were found in individuals with familial Alzheimer’s disease and other conditions. The structures of Aβ42 filaments from the brain differ from those of filaments assembled in vitro. By contrast, in
Identifiants
pubmed: 35025654
doi: 10.1126/science.abm7285
pmc: PMC7612234
mid: EMS140501
doi:
Substances chimiques
Amyloid beta-Peptides
0
Peptide Fragments
0
amyloid beta-protein (1-42)
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
167-172Subventions
Organisme : Medical Research Council
ID : MC_U105184326
Pays : United Kingdom
Organisme : NINDS NIH HHS
ID : U01 NS110437
Pays : United States
Organisme : Medical Research Council
ID : MC_U105184291
Pays : United Kingdom
Organisme : Medical Research Council
ID : MC_UP_1201/25
Pays : United Kingdom
Organisme : Medical Research Council
ID : MC_U105192716
Pays : United Kingdom
Organisme : NIA NIH HHS
ID : P30 AG010133
Pays : United States
Organisme : NIA NIH HHS
ID : RF1 AG071177
Pays : United States
Organisme : Medical Research Council
ID : MC_UP_A025_1013
Pays : United Kingdom
Commentaires et corrections
Type : CommentIn
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