ArticleScientific reports2016
Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 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.
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Who cites it
43 citing papers in PubMed, 66 citations in OpenAlex.
- The Microglial Protein sTREM2 Inhibits the Bacterial Functional Amyloid CsgA and Suppresses Amyloid-Dependent Biofilm Formation.bioRxiv : the preprint server for biology · 2026Article
- From Environmental Persistence to Host Adaptation: Differential Curli Regulation inMicroorganisms · 2026Review
- The cytoplasmic protein YedX is a potent inhibitor of CsgA amyloid assembly in E. coli.The Journal of biological chemistry · 2026Article
- βProceedings of the National Academy of Sciences of the United States of America · 2026Article
- The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Structural basis ofScience advances · 2025Article
- Bacterial Species in Engineered Living Materials: Strategies and Future Directions.Microbial biotechnology · 2025Review
- Revealing systematic changes in the transcriptome during the transition from exponential growth to stationary phase.mSystems · 2025Article
- Structural insight intomBio · 2024Article
- Designed α-sheet peptides disrupt uropathogenic E. coli biofilms rendering bacteria susceptible to antibiotics and immune cells.Scientific reports · 2023Article
- LL-37 and CsgC exemplify the crosstalk between anti-amyloid, antimicrobial, and anti-biofilm protein activities.Neural regeneration research · 2023Article
- CsgI (YccT) Is a Novel Inhibitor of Curli Fimbriae Formation inInternational journal of molecular sciences · 2023Article
- Molecular-level insights into the surface-induced assembly of functional bacterial amyloid.Biophysical journal · 2022Article
- Functional Bacterial Amyloids: Understanding Fibrillation, Regulating Biofilm Fibril Formation and Organizing Surface Assemblies.Molecules (Basel, Switzerland) · 2022Review
- Chaperones mainly suppress primary nucleation during formation of functional amyloid required for bacterial biofilm formation.Chemical science · 2022Article
- Anti-Biofilm Molecules Targeting Functional Amyloids.Antibiotics (Basel, Switzerland) · 2021Review
- Half a century of amyloids: past, present and future.Chemical Society reviews · 2020Review
- Force spectra of single bacterial amyloid CsgA nanofibers.RSC advances · 2020Article
- Cryo-EM structure of the nonameric CsgG-CsgF complex and its implications for controlling curli biogenesis in Enterobacteriaceae.PLoS biology · 2020Article
- NMR insights into the pre-amyloid ensemble and secretion targeting of the curli subunit CsgA.Scientific reports · 2020Article
Corrections and comments
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Authors and funding
24 authors at 3 institutions in 2 countries.
Funding
Abstract
Polypeptide aggregation into amyloid is linked with several debilitating human diseases. Despite the inherent risk of aggregation-induced cytotoxicity, bacteria control the export of amyloid-prone subunits and assemble adhesive amyloid fibres during biofilm formation. An Escherichia protein, CsgC potently inhibits amyloid formation of curli amyloid proteins. Here we unlock its mechanism of action, and show that CsgC strongly inhibits primary nucleation via electrostatically-guided molecular encounters, which expands the conformational distribution of disordered curli subunits. This delays the formation of higher order intermediates and maintains amyloidogenic subunits in a secretion-competent form. New structural insight also reveal that CsgC is part of diverse family of bacterial amyloid inhibitors. Curli assembly is therefore not only arrested in the periplasm, but the preservation of conformational flexibility also enables efficient secretion to the cell surface. Understanding how bacteria safely handle amyloidogenic polypeptides contribute towards efforts to control aggregation in disease-causing amyloids and amyloid-based biotechnological applications.
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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.