ReviewFEBS letters2025
Making tau amyloid models in vitro: a crucial and underestimated challenge.
Review in FEBS letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed.
- Protocol for efficient purification of endotoxin-free human recombinant tau protein.STAR protocols · 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
- DEER of Singly Labelled Proteins to Evaluate Supramolecular Packing of Amyloid Fibrils.bioRxiv : the preprint server for biology · 2025Article
- Structure-specific Mini-Prion Model for Alzheimer's Disease Tau Fibrils.bioRxiv : the preprint server for biology · 2025Article
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
The protein Tau accumulates in the brain as insoluble deposits in a number of neurodegenerative diseases called tauopathies. In vitro work studying the properties of reconstituted tau assemblies has played a major role in understanding the fundamental mechanisms underlying tauopathies. Yet, in our view, the extent to which tau in vitro models represent the assemblies found in the brain is not sufficiently addressed. Here, we provide an overview of the procedures used to form tau amyloids in vitro and we discuss their similarities and differences with brain deposits. We emphasize that, to date, further work is needed to establish how to form accurate models of tau deposits with recombinant protein, let alone how to represent disease-specific properties that discriminate tauopathies.
Indexed as
Identifiers
What 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.