ReviewNature reviews. Chemistry2026
Targeting soluble misfolded oligomers in anti-amyloid research.
Review in Nature reviews. Chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
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
No grant is acknowledged in the PubMed record.
Abstract
Protein misfolding drives a range of non-curable diseases, such as Alzheimer disease, Parkinson disease, type 2 diabetes and Huntington disease, that devastate tens of millions of patients each year. The pathological proteins are misfolded into soluble oligomers, which eventually evolve into insoluble amyloid plaques. Increasing evidence suggests that soluble oligomers are the primary cytotoxic species leading to amyloidoses. However, the transient, heterogeneous and low-abundance nature of soluble oligomers makes it extremely challenging to study these species using conventional methods. This Review surveys emerging chemical tools developed for in vitro detection, separation and analysis of soluble amyloid oligomers. We exemplify how the present arsenal can be extended to construct individual amyloid oligomers as potential drug targets. Finally, we summarize their technical limits and discuss possibilities of adapting these chemical tools to target specific soluble oligomers in the fight against amyloidoses.
Identifiers
42624989What OpenQuestion holds
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.