ReviewCold Spring Harbor perspectives in biology2019
Functional Amyloids.
Review in Cold Spring Harbor perspectives in biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 166 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
166 citing papers in PubMed, 306 citations in OpenAlex.
- From Helicobacter pylori CagA to Cross-Kingdom Amyloid Control: Emerging Anti-amyloid Biology, Mechanistic Paradoxes, and Translational Opportunities.The protein journal · 2026Review
- Structural Hierarchy and Maturation of Amyloid Fibrils Revealed by Interface Descriptor Analysis.Journal of chemical information and modeling · 2026Article
- Functional amyloids as molecular switches: emerging roles in diverse signalling pathways.Biochemical Society transactions · 2026Review
- Bioinformatic assessment of the potential amyloidogenicity of the human and evolutionarily more ancient proteomes.The Biochemical journal · 2026Article
- The impact of physiological oxidants on triggering amyloid formation of the cell cycle regulator protein p16Protein science : a publication of the Protein Society · 2026Article
- Helical reconstruction of amyloids in cryoSPARC.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Article
- A functional amyloid scaffold shapes insect egg coats.bioRxiv : the preprint server for biology · 2026Article
- Standardization of cross-site biophysical studies of bovine insulin amyloids is challenged by structural polymorphism.European biophysics journal : EBJ · 2026Article
- Enzymes of physiological amyloidogenesis control pathological amyloid toxicity.Life science alliance · 2026Article
- Uncovering a previously unknown function of polyphosphate in polyadenylated RNA-induced amyloidogenesis of Hfq.The FEBS journal · 2026Article
- Aggregation in gut: on the link between neurodegeneration and bacterial functional amyloids.NPJ biofilms and microbiomes · 2026Article
- Fluorescent non-canonical amino acid as a site-specific conformational probe of prion formation.bioRxiv : the preprint server for biology · 2026Article
- Self-Assembly of Amyloid Fibrils into Fibrillar Superstructure Monitored with Thioflavin T.Biomolecules · 2026Article
- Rapid elongation drives the exceptionally fast aggregation of the most common localized human amyloid medin.Communications chemistry · 2026Article
- Amelogenin proteolysis orchestrates functional amyloid pathways in enamel development.Matrix biology : journal of the International Society for Matrix Biology · 2026Article
- CAR Treg therapies for neurodegenerative diseases.iScience · 2026Review
- Catalytic Amyloids: Turning Fibrils Into Biocatalysts.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Elucidating β-Sheet Ordering in Lipopeptides Bearing Lysine-Rich Tripeptide Sequences: Fibrils versus Nanotapes.The journal of physical chemistry. B · 2026Article
- The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
106 more citing papers are in PubMed but not listed here.
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 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
When protein/peptides aggregate, they usually form the amyloid state consisting of cross β-sheet structure built by repetitively stacked β-strands forming long fibrils. Amyloids are usually associated with disease including Alzheimer's. However, amyloid has many useful features. It efficiently transforms protein from the soluble to the insoluble state in an essentially two-state process, while its repetitive structure provides high stability and a robust prion-like replication mechanism. Accordingly, amyloid is used by nature in multifaceted and ingenious ways of life, ranging from bacteria and fungi to mammals. These include (1) Structure: Templating for small chemical molecules (Pmel17), biofilm formation in bacteria (curli), assisting aerial hyphae formation in streptomycetes (chaplins) or monolayer formation at a surface (hydrophobins). (2) Reservoirs: A storage state for peptide/proteins to protect them from their surroundings or vice versa (storage of peptide hormones in mammalian secretory granules or major basic protein in eosinophils). (3) Information carriers: The fungal immune system (HET-s prion in
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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.