ArticleMolecular cell2015
The bacterial curli system possesses a potent and selective inhibitor of amyloid formation.
Article in Molecular cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
128 citing papers in PubMed.
- The protease code of the bacterial gut microbiota: ecological regulation, barrier disruption, and rewiring host defense and signaling.Gut microbes · 2026Review
- From Helicobacter pylori CagA to Cross-Kingdom Amyloid Control: Emerging Anti-amyloid Biology, Mechanistic Paradoxes, and Translational Opportunities.The protein journal · 2026Review
- 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
- Gut Dysbiosis and Microbiota-Derived Metabolites in Neurodegenerative Diseases: Molecular and Biochemical Mechanisms Along the Gut-Brain Axis.Molecules (Basel, Switzerland) · 2026Review
- Transient binding facilitates super-resolution imaging of functional amyloid fibrils on living bacteria.Protein science : a publication of the Protein Society · 2026Article
- The Many Lives of a Single Sequence: Functional Plasticity Through Amyloid Polymorphism.Sub-cellular biochemistry · 2026Review
- Synthetic deformylated α-helical PSMα3 as a selective inhibitor of human amyloid aggregation.Scientific reports · 2025Article
- Programming cellular condensates for living materials using an intrinsically disordered protein display platform.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- RcsB and H-NS Both Contribute to the Repression the Expression of theMicroorganisms · 2025Article
- Article
- The Small Intestinal Microbiota and the Gut-Brain Axis in Parkinson's Disease: A Narrative Review.Biomedicines · 2025Review
- Article
- The Curli Accessory Protein CsgF ofmicroPublication biology · 2025Article
- Identification of Amino Acid Conservation in The Curli Accessory Protein CsgF.microPublication biology · 2025Article
- Parkinson's disease beyond the brain: implications for treatments.Frontiers in aging neuroscience · 2025Review
- Gut microbiome features and resistome elements associated with colonization and infection with antibiotic-resistance threats.Gut microbes reports · 2025Article
68 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
Authors and funding
12 authors.
Funding
Abstract
Curli are extracellular functional amyloids that are assembled by enteric bacteria during biofilm formation and host colonization. An efficient secretion system and chaperone network ensures that the major curli fiber subunit, CsgA, does not form intracellular amyloid aggregates. We discovered that the periplasmic protein CsgC was a highly effective inhibitor of CsgA amyloid formation. In the absence of CsgC, CsgA formed toxic intracellular aggregates. In vitro, CsgC inhibited CsgA amyloid formation at substoichiometric concentrations and maintained CsgA in a non-β-sheet-rich conformation. Interestingly, CsgC inhibited amyloid assembly of human α-synuclein, but not Aβ42, in vitro. We identified a common D-Q-Φ-X0,1-G-K-N-ζ-E motif in CsgC client proteins that is not found in Aβ42. CsgC is therefore both an efficient and selective amyloid inhibitor. Dedicated functional amyloid inhibitors may be a key feature that distinguishes functional amyloids from disease-associated amyloids.
Indexed as
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.