ArticleNature chemical biology2025
Interactions with tau's microtubule-binding repeats modulate amyloid-β aggregation and toxicity.
Article in Nature chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed.
- Strategic physicochemical tuning: amphiphilic polymers as molecular regulators of amyloid aggregation and cytotoxicity.Chemical science · 2026Article
- Thermodynamic Frontiers in Hemoglobin-Inspired Polymer Science for Diagnosis and Modulation of Neurodegenerative Diseases.Cell biochemistry and function · 2026Review
- A Prodrug Approach for Activity-Based Chemical Modulation toward Multiple Pathological Targets in Alzheimer's Disease.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- The microtubule nexus linking amyloid beta and tau: A simple and unifying theory for the underlying cause of Alzheimer's disease.PNAS nexus · 2026Article
- Disease-disease interactions: molecular links of neurodegenerative diseases with cancer, viral infections, and type 2 diabetes.Translational neurodegeneration · 2025Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
The complicated pathogenesis of Alzheimer's disease (AD) is characterized by the accumulation of neurofibrillary tangles and senile plaques, primarily composed of tau and amyloid-β (Aβ) aggregates, respectively. While substantial efforts have focused on unraveling the individual roles of tau and Aβ in AD development, the intricate interplay between these components remains elusive. Here we report how the microtubule-binding repeats of tau engage with Aβ in a distinct manner. Crucially, this interaction notably modifies Aβ aggregation behavior, thereby altering Aβ-associated toxicity within both extracellular and intracellular milieus. Our mechanistic investigations at the molecular level manifest specific fragments within tau's microtubule-binding domain that possess a balance of hydrophobic and hydrophilic properties, promoting the formation of hetero-adducts with Aβ peptides. These findings offer avenues for understanding and treating AD by emphasizing the tau-Aβ interplay in the pathogenesis.
Indexed as
Identifiers
40846995What 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.