ReviewProtein science : a publication of the Protein Society2026
In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances.
Review in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
3 citing papers in PubMed.
- Dual Targeted Far-Red Emissive Small Molecules for Mitochondrial Imaging and Multifunctional Modulation in Alzheimer's Disease.Advanced healthcare materials · 2026Article
- SEC Purified Monomeric Aβ42 Produces Reproducible and Reliable Aggregation Measurements.bioRxiv : the preprint server for biology · 2026Article
- In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances.Protein science : a publication of the Protein Society · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Oligomeric assemblies of amyloidogenic proteins, such as Aβ, tau, α-synuclein, amylin, transthyretin, and TDP-43, are increasingly recognized as key drivers of cellular dysfunction across a range of neurodegenerative and systemic disorders. However, their molecular properties remain poorly understood due to their low abundance, structural heterogeneity, and transient nature. This review outlines current methods for studying amyloid oligomers, including biophysical (NMR, cryo-EM, HS-AFM, mass spectrometry), computational (molecular dynamics simulations), and biological (cellular assays, organoids, and animal models) approaches. This review also covers emerging methods for detecting misfolded proteins within complex biological environments and live-cell systems. Furthermore, we discuss recent advances that specifically address the challenges of studying oligomers, which are yielding crucial data on how these pathogenic species impair cellular homeostasis. Given the heterogeneity and transient nature of the oligomers, it is essential to utilize findings across diverse experimental platforms that yield complementary data and apply methods that also ensure reproducibility and mechanistic clarity with the goal of translating these findings into effective therapeutic strategies.
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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.