Discover Community Create You

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

Anti-Parallel β-Hairpin Structure in Soluble Aβ Oligomers of Aβ40-Dutch and Aβ40-Iowa.

International journal of molecular sciences - 27 Jan 2021

Fu Ziao, Van Nostrand William E, Smith Steven O

Abstract excerpt

The amyloid-β (Aβ) peptides are associated with two prominent diseases in the brain, Alzheimer's disease (AD) and cerebral amyloid angiopathy (CAA). Aβ42 is the dominant component of cored parenchymal plaques associated with AD, while Aβ40 is the predominant component of vascular amyloid associated with CAA. There are familial CAA mutations at positions Glu22 and Asp23 that lead to aggressive Aβ aggregation,...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Benzothiazoles
Share to Cerebral Amyloid Angiopathy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluorescence

Share to Microscopy, Atomic Force

Share to Plaque, Amyloid

Share to Protein Conformation, beta-Strand

Share to Spectroscopy, Fourier Transform Infrared

Source

Open in PubMed Open full text

Identifiers

PMID: 33513738
DOI: 10.3390/ijms22031225
PMCID: PMC7865275

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Anti-Parallel β-Hairpin Structure in Soluble Aβ Oligomers of Aβ40-Dutch and Aβ40-Iowa.PMID 33513738Read ↗

Intermediate Antiparallel Fibrils in Aβ40 Dutch Mutant Aggregation: Insights from Nanoscale Infrared Spectroscopy.Semantic proximity Read ↗

Intermediate antiparallel fibrils in Aβ40 Dutch mutant aggregation: nanoscale insights from AFM-IRSemantic proximity Read ↗

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

An electrostatic cluster guides Aβ40 fibril formation in sporadic and Dutch-type cerebral amyloid angiopathy.Semantic proximity Read ↗

A turn for the worse: Aβ β-hairpins in Alzheimer’s diseaseSemantic proximity Read ↗

An electrostatic cluster guides Aβ40 fibril formation in cerebral amyloid angiopathySemantic proximity Read ↗

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

Structural evolution of Iowa mutant β-amyloid fibrils from polymorphic to homogeneous states under repeated seeded growth.Semantic proximity Read ↗

Exploring the complexity of amyloid-beta fibrils: structural polymorphisms and molecular interactions.Semantic proximity Read ↗

Heterotypic Seeding Generates Mixed Amyloid PolymorphsSemantic proximity Read ↗

Two distinct β-sheet structures in Italian-mutant amyloid-beta fibrils: a potential link to different clinical phenotypes.Semantic proximity Read ↗

Stability of Iowa mutant and wild type Aβ-peptide aggregates.Semantic proximity Read ↗

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