ReviewBiomolecules2017
Why are Functional Amyloids Non-Toxic in Humans?
Review in Biomolecules, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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
38 citing papers in PubMed, 101 citations in OpenAlex.
- Enzymes of physiological amyloidogenesis control pathological amyloid toxicity.Life science alliance · 2026Article
- Amelogenin proteolysis orchestrates functional amyloid pathways in enamel development.Matrix biology : journal of the International Society for Matrix Biology · 2026Article
- Membrane charge primes the necroptotic kinase RIPK3 for amyloid assembly.Communications chemistry · 2025Article
- Cryo-EM of wild-type and mutant PMEL amyloid cores reveals structural mechanism of pigment dispersion syndrome.Nature communications · 2025Article
- Functional constraints of wtf killer meiotic drivers.PLoS genetics · 2025Article
- Structural commonalities determined by physicochemical principles in the complex polymorphism of the amyloid state of proteins.The Biochemical journal · 2025Article
- Functional constraints ofbioRxiv : the preprint server for biology · 2025Article
- Hybrid Micro-/Nanoprotein Platform Provides Endocrine-like and Extracellular Matrix-like Cell Delivery of Growth Factors.ACS applied materials & interfaces · 2024Article
- Rationally Designed Peptoid Inhibitors of Amyloid-β Oligomerization.Chembiochem : a European journal of chemical biology · 2024Article
- Human Platelet Lysate-Derived Nanofibrils as Building Blocks to Produce Free-Standing Membranes for Cell Self-Aggregation.ACS nano · 2024Article
- Observation of pH-Dependent Residual Structure in the Pmel17 Repeat Domain and the Implication for Its Amyloid Formation.Biochemistry · 2023Article
- Controversial Properties of Amyloidogenic Proteins and Peptides: New Data in the COVID Era.Biomedicines · 2023Review
- Neutrophil extracellular traps in central nervous system pathologies: A mini review.Frontiers in medicine · 2023Review
- Comparative Study of the Solid-Liquid Interfacial Adsorption of Proteins in Their Native and Amyloid Forms.International journal of molecular sciences · 2022Article
- Variability of Amyloid Propensity in Imperfect Repeats of CsgA Protein ofInternational journal of molecular sciences · 2021Article
- Amyloids: The History of Toxicity and Functionality.Biology · 2021Review
- The role of CPEB family proteins in the nervous system function in the norm and pathology.Cell & bioscience · 2021Review
- Mechanisms and therapeutic potential of interactions between human amyloids and viruses.Cellular and molecular life sciences : CMLS · 2021Review
- Amyloid Aggregation under the Lens of Liquid-Liquid Phase Separation.The journal of physical chemistry letters · 2021Article
- Visualizing and trapping transient oligomers in amyloid assembly pathways.Biophysical chemistry · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Amyloids were first identified in association with amyloidoses, human diseases in which proteins and peptides misfold into amyloid fibrils. Subsequent studies have identified an array of functional amyloid fibrils that perform physiological roles in humans. Given the potential for the production of toxic species in amyloid assembly reactions, it is remarkable that cells can produce these functional amyloids without suffering any obvious ill effect. Although the precise mechanisms are unclear, there are a number of ways in which amyloid toxicity may be prevented. These include regulating the level of the amyloidogenic peptides and proteins, minimising the production of prefibrillar oligomers in amyloid assembly reactions, sequestrating amyloids within membrane bound organelles, controlling amyloid assembly by other molecules, and disassembling the fibrils under physiological conditions. Crucially, a better understanding of how toxicity is avoided in the production of functional amyloids may provide insights into the prevention of amyloid toxicity in amyloidoses.
Indexed as
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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.