Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

E22G Aβ40 fibril structure and kinetics illuminate how Aβ40 rather than Aβ42 triggers familial Alzheimer's.

Nature communications - 15 Aug 2024

Tehrani Mohammad Jafar, Matsuda Isamu, Yamagata Atsushi, Kodama Yu, Matsunaga Tatsuya, Sato Mayuko, Toyooka Kiminori, McElheny Dan, Kobayashi Naohiro, Shirouzu Mikako, Ishii Yoshitaka

Abstract excerpt

Arctic (E22G) mutation in amyloid-β (Aβ enhances Aβ40 fibril accumulation in Alzheimer's disease (AD). Unlike sporadic AD, familial AD (FAD) patients with the mutation exhibit more Aβ40 in the plaque core. However, structural details of E22G Aβ40 fibrils remain elusive, hindering therapeutic progress. Here, we determine a distinctive W-shaped parallel β-sheet structure through co-analysis by cryo-electron...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Kinetics
Share to Alzheimer Disease

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Amyloid

Share to Amyloid beta-Peptides

Share to Cryoelectron Microscopy

Share to Molecular Dynamics Simulation

Share to Peptide Fragments

Share to Protein Folding

Source

Open in PubMed Open full text

Identifiers

PMID: 39147751
DOI: 10.1038/s41467-024-51294-w
PMCID: PMC11327332

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

E22G Aβ40 fibril structure and kinetics illuminate how Aβ40 rather than Aβ42 triggers familial Alzheimer's.PMID 39147751Read ↗

E22G Pathogenic Mutation of β-Amyloid (Aβ) Enhances Misfolding of Aβ40 by Unexpected Prion-like Cross Talk between Aβ42 and Aβ40.Semantic proximity Read ↗

Structural Polymorphism of Alzheimer's β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study.Semantic proximity Read ↗

Cross-seeding of WT amyloid-β with Arctic but not Italian familial mutants accelerates fibril formation in Alzheimer's disease.Semantic proximity Read ↗

Cryo-EM structures of amyloid-β filaments with the Arctic mutation (E22G) from human and mouse brains.Semantic proximity Read ↗

Cryo-EM Structures of Amyloid-β Filaments With the Arctic Mutation (E22G) From Human and Mouse BrainsSemantic proximity Read ↗

The in-tissue molecular architecture of β-amyloid pathology in the mammalian brain.Semantic proximity Read ↗

Mixtures of wild-type and a pathogenic (E22G) form of Abeta40 in vitro accumulate protofibrils, including amyloid pores.Semantic proximity Read ↗

The Structures of the E22Δ Mutant-Type Amyloid-β Alloforms and the Impact of E22Δ Mutation on the Structures of the Wild-Type Amyloid-β AlloformsSemantic proximity Read ↗

Modulating Amyloid-β Toxicity: In Vitro Analysis of Aβ42(G37V) Variant Impact on Aβ42 Aggregation and CytotoxicitySemantic proximity Read ↗

Antiparallel β-sheet architecture in Iowa-mutant β-amyloid fibrils.Semantic proximity Read ↗

Alzheimer's Protective Cross-Interaction between Wild-Type and A2T Variants Alters Aβ42 Dimer Structure.Semantic proximity Read ↗

Accelerating amyloid-beta fibrillization reduces oligomer levels and functional deficits in Alzheimer disease mouse models.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.