ArticleScientific reports2019
RNA-binding protein FXR1 is presented in rat brain in amyloid form.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 40 citations in OpenAlex.
- The prion-like characteristic of ORF3 contributes to virion release and pathogenesis of hepatitis E virus.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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- Amyloid fibrils of the myelin basic protein are an integral component of myelin in the vertebrate brain.Scientific reports · 2025Article
- Amyloid Fibrils of the s36 Protein Modulate the Morphogenesis ofInternational journal of molecular sciences · 2024Article
- Active regulation of amyloidosis.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Sodium Dodecyl Sulfate Analogs as a Potential Molecular Biology Reagent.Current issues in molecular biology · 2024Review
- Amyloids and prions in the light of evolution.Current genetics · 2023Review
- Stress Granules as Causes and Consequences of Translation Suppression.Antioxidants & redox signaling · 2023Review
- ARL6IP1 mediates small-molecule-induced alleviation of Alzheimer pathology through FXR1-dependent BACE1 translation initiation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Identification of New FG-Repeat Nucleoporins with Amyloid Properties.International journal of molecular sciences · 2023Article
- Search and Identification of Amyloid Proteins.Methods and protocols · 2023Article
- The Effect of a Rotating Cone on Horseradish Peroxidase Aggregation on Mica Revealed by Atomic Force Microscopy.Micromachines · 2022Article
- Human RAD51 Protein Forms Amyloid-like AggregatesInternational journal of molecular sciences · 2022Article
- Amyloid Properties of the FXR1 Protein Are Conserved in Evolution of Vertebrates.International journal of molecular sciences · 2022Article
- Article
- AFM and FTIR Investigation of the Effect of Water Flow on Horseradish Peroxidase.Molecules (Basel, Switzerland) · 2021Article
- Search for functional amyloid structures in chicken and fruit fly female reproductive cells.Prion · 2020Article
- Functional amyloids of eukaryotes: criteria, classification, and biological significance.Current genetics · 2020Review
- A simple procedure for bacterial expression and purification of the fragile X protein family.Scientific reports · 2020Article
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Authors and funding
13 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloids are β-sheets-rich protein fibrils that cause neurodegenerative and other incurable human diseases affecting millions of people worldwide. However, a number of proteins is functional in the amyloid state in various organisms from bacteria to humans. Using an original proteomic approach, we identified a set of proteins forming amyloid-like aggregates in the brain of young healthy rats. One of them is the FXR1 protein, which is known to regulate memory and emotions. We showed that FXR1 clearly colocalizes in cortical neurons with amyloid-specific dyes Congo-Red, Thioflavines S and T. FXR1 extracted from brain by immunoprecipitation shows yellow-green birefringence after staining with Congo red. This protein forms in brain detergent-resistant amyloid oligomers and insoluble aggregates. RNA molecules that are colocalized with FXR1 in cortical neurons are insensitive to treatment with RNase A. All these data suggest that FXR1 functions in rat brain in amyloid form. The N-terminal amyloid-forming fragment of FXR1 is highly conserved across mammals. We assume that the FXR1 protein may be presented in amyloid form in brain of different species of mammals, including humans.
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