ReviewCurrent opinion in chemical biology2021
Exploring amyloid oligomers with peptide model systems.
Review in Current opinion in chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 36 citations in OpenAlex.
- Leveraging Glycan-Glycan Interactions to Tune the Conformation of Glycan Hairpins and Build Rigid 3D Architectures.Journal of the American Chemical Society · 2026Article
- Endogenous Aβ and Exogenous Wheat Gluten Nanostructures: Understanding Peptide Self-Assembly in Disease.ACS nano · 2025Review
- Rational Design of a Foldon-Derived Heterotrimer Guided by Quantitative Native Mass Spectrometry.Journal of the American Chemical Society · 2025Article
- Application of modular isoxazoline-βiScience · 2025Article
- α-Methylation Enables the X-ray Crystallographic Observation of Oligomeric Assemblies Formed by a β-Hairpin Peptide Derived from Aβ.The Journal of organic chemistry · 2025Article
- Article
- A turn for the worse: Aβ β-hairpins in Alzheimer's disease.Bioorganic & medicinal chemistry · 2024Review
- Dissecting the Conformational Stability of a Glycan Hairpin.Journal of the American Chemical Society · 2024Article
- Antibodies Raised Against an Aβ Oligomer Mimic Recognize Pathological Features in Alzheimer's Disease and Associated Amyloid-Disease Brain Tissue.ACS central science · 2024Article
- β-Hairpin Alignment Alters Oligomer Formation in Aβ-Derived Peptides.Biochemistry · 2024Article
- A β-barrel-like tetramer formed by a β-hairpin derived from Aβ.Chemical science · 2023Article
- Synthesis of a glycan hairpin.Nature chemistry · 2023Article
- Probing differences among Aβ oligomers with two triangular trimers derived from Aβ.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Aggregation of Amyloidogenic Peptide Uperin-Molecular Dynamics Simulations.Molecules (Basel, Switzerland) · 2023Article
- Mismatched covalent and noncovalent templating leads to large coiled coil-templated macrocycles.Chemical science · 2023Article
- The manifold role of octapeptide repeats in prion protein assembly.Peptide science (Hoboken, N.J.) · 2023Article
- Current Peptide Vaccine and Immunotherapy Approaches Against Alzheimer's Disease.Peptide science (Hoboken, N.J.) · 2023Article
- Pathway Dependence of the Formation and Development of Prefibrillar Aggregates in Insulin B Chain.Molecules (Basel, Switzerland) · 2022Article
- Impact of Electronic Polarization on Preformed, β-Strand Rich Homogenous and Heterogenous Amyloid Oligomers.Journal of computational biophysics and chemistry · 2022Article
- A Disulfide-Stabilized Aβ that Forms Dimers but Does Not Form Fibrils.Biochemistry · 2022Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The assembly of amyloidogenic peptides and proteins, such as the β-amyloid peptide, α-synuclein, huntingtin, tau, and islet amyloid polypeptide, into amyloid fibrils and oligomers is directly linked to amyloid diseases, such as Alzheimer's, Parkinson's, and Huntington's diseases, frontotemporal dementias, and type II diabetes. Although amyloid oligomers have emerged as especially important in amyloid diseases, high-resolution structures of the oligomers formed by full-length amyloidogenic peptides and proteins have remained elusive. Investigations of oligomers assembled from fragments or stabilized β-hairpin segments of amyloidogenic peptides and proteins have allowed investigators to illuminate some of the structural, biophysical, and biological properties of amyloid oligomers. Here, we summarize recent advances in the application of these peptide model systems to investigate and understand the structures, biological properties, and biophysical properties of amyloid oligomers.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.