ArticleACS chemical neuroscience2015
Azaphilones inhibit tau aggregation and dissolve tau aggregates in vitro.
Article in ACS chemical neuroscience, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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.
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Who cites it
20 citing papers in PubMed.
- Covalent Modulation of Protein Misfolding and Aggregation Processes in the Context of Neurodegenerative Diseases.Archiv der Pharmazie · 2026Review
- Transcription Factor Engineering inJournal of natural products · 2024Article
- Sedimentation and Laser Light Scattering Methods for Quantifying Synthetic Tau Aggregation Propensity.Methods in molecular biology (Clifton, N.J.) · 2024Article
- The screening for marine fungal strains with high potential in alkaloids production byFrontiers in microbiology · 2023Article
- Combining OSMAC, metabolomic and genomic methods for the production and annotation of halogenated azaphilones and ilicicolins in termite symbiotic fungi.Scientific reports · 2022Article
- Characterization of a silent azaphilone biosynthesis gene cluster in Aspergillus terreus NIH 2624.Fungal genetics and biology : FG & B · 2022Article
- Fungally Derived Isoquinoline Demonstrates Inducer-Specific Tau Aggregation Inhibition.Biochemistry · 2021Article
- Pharmacological Modulators of Tau Aggregation and Spreading.Brain sciences · 2020Review
- Fungal Pigments and Their Roles Associated with Human Health.Journal of fungi (Basel, Switzerland) · 2020Review
- The multifunctional dopamine DBioorganic & medicinal chemistry · 2020Article
- Recent advances in the chemistry and biology of azaphilones.RSC advances · 2020Review
- Basic Limonoid modulates Chaperone-mediated Proteostasis and dissolve Tau fibrils.Scientific reports · 2020Article
- Muyocopronones A and B: azaphilones from the endophytic fungusBeilstein journal of organic chemistry · 2020Article
- Article
- Neem Derivatives Inhibits Tau Aggregation.Journal of Alzheimer's disease reports · 2019Article
- Hybrid Transcription Factor Engineering Activates the Silent Secondary Metabolite Gene Cluster for (+)-Asperlin in Aspergillus nidulans.ACS chemical biology · 2018Article
- Mechanistic insights into remodeled Tau-derived PHF6 peptide fibrils by Naphthoquinone-Tryptophan hybrids.Scientific reports · 2018Article
- Therapeutic Strategies for Restoring Tau Homeostasis.Cold Spring Harbor perspectives in medicine · 2018Review
- The fungal natural product azaphilone-9 binds to HuR and inhibits HuR-RNA interaction in vitro.PloS one · 2017Article
- New Features about Tau Function and Dysfunction.Biomolecules · 2016Review
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 aggregation of the microtubule-associated protein tau is a seminal event in many neurodegenerative diseases, including Alzheimer's disease. The inhibition or reversal of tau aggregation is therefore a potential therapeutic strategy for these diseases. Fungal natural products have proven to be a rich source of useful compounds having wide varieties of biological activities. We have previously screened Aspergillus nidulans secondary metabolites for their ability to inhibit tau aggregation in vitro using an arachidonic acid polymerization protocol. One aggregation inhibitor identified was asperbenzaldehyde, an intermediate in azaphilone biosynthesis. We therefore tested 11 azaphilone derivatives to determine their tau assembly inhibition properties in vitro. All compounds tested inhibited tau filament assembly to some extent, and four of the 11 compounds had the advantageous property of disassembling preformed tau aggregates in a dose-dependent fashion. The addition of these compounds to the tau aggregates reduced both the total length and number of tau polymers. The most potent compounds were tested in in vitro reactions to determine whether they interfere with tau's normal function of stabilizing microtubules (MTs). We found that they did not completely inhibit MT assembly in the presence of tau. These derivatives are very promising lead compounds for tau aggregation inhibitors and, more excitingly, for compounds that can disassemble pre-existing tau filaments. They also represent a new class of anti-tau aggregation compounds with a novel structural scaffold.
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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.