ReviewBiophysics reviews2025
On the reversibility of amyloid fibril formation.
Review in Biophysics reviews, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed.
- Cofactor-Free Tau Filaments Are Dynamic and Undergo Structural Evolution Driven by Thermodynamic Control.Journal of the American Chemical Society · 2026Article
- Synaptic vesicle architecture modulates α-synuclein conformation and pathogenic transitions in Parkinson's disease.Bioscience reports · 2026Review
- Fragmentation-Induced Disassembly and Reaggregation of α-Synuclein Amyloid Fibrils.ACS chemical neuroscience · 2026Article
- Amyloid fibril polymorphism: Structural mechanisms of assembly and the links to disease.Current opinion in structural biology · 2026Review
- Charge-Balanced Design for Redox-Responsive Disassembly of Ampholytic β-Sheet Peptide Nanofibers.Polymers · 2026Article
- The temperature dependence of amyloidProceedings of the National Academy of Sciences of the United States of America · 2026Article
- From Pathology to Materials Science and Engineering: Harnessing the Amyloid State for Biotechnological Applications.ACS applied materials & interfaces · 2025Review
- Experimental methods for studying amyloid cross-interactions.Protein science : a publication of the Protein Society · 2025Review
- Converging frontiers in biomolecular condensate and synthetic cell research.npj biomedical innovations · 2025Review
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloids are elongated supramolecular protein self-assemblies. Their formation is a non-covalent assembly process and as such is fully reversible. Amyloid formation is associated with several neurodegenerative diseases, and the reversibility is key to maintaining the healthy state. Reversibility is also key to the performance of fibril-based biomaterials and functional amyloids. The reversibility can be observed by a range of spectroscopic, calorimetric, or surface-based techniques using as a starting state either a supersaturated monomer solution or diluted fibrils. Amyloid formation has the characteristics of a phase transition, and we provide some basic formalism for the reversibility and the derivation of the solubility/critical concentration. We also discuss conditions under which the dissociation of amyloids may be so slow that the process can be viewed as practically irreversible, for example, because it is slow relative to the experimental time frame or because the system at hand contains a source for constant monomer addition.
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.