Evidence map›Paper›PMID 28628096›Full record

ArticleNature chemical biology2017

Nucleation and growth of a bacterial functional amyloid at single-fiber resolution.

Mike Sleutel, Imke Van den Broeck, Nani Van Gerven, Cécile Feuillie, Wim Jonckheere, Claire Valotteau, Yves F Dufrêne, Han Remaut

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
5.3field-weighted citation impact, top 4% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  5. The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023
    Review
  11. Article
  12. Time-Resolved In Situ AFM Measurement of Growth Rates of Aβ40 Fibrils.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  13. Article
  14. Article
  15. Review
  16. Frustrated peptide chains at the fibril tip control the kinetics of growth of amyloid-β fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. Article
  18. Article
  19. Review
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Mike SleutelStructural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium.ORCID http://orcid.org/0000-0003-3247-2187
Imke Van den BroeckStructural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium.
Nani Van GervenStructural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium.
Cécile FeuillieInstitute of Life Sciences, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.
Wim JonckheereStructural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium.
Claire ValotteauInstitute of Life Sciences, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.
Yves F DufrêneInstitute of Life Sciences, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.
Han RemautStructural Biology Brussels, Vrije Universiteit Brussel, Brussels, Belgium.
Vrije Universiteit Brussel · BEUCLouvain · BEWalloon Excellence in Lifesciences and Biotechnology · BE

Funding

European Research Council 649082
6 · The paper itself

Abstract

Curli are functional amyloids produced by proteobacteria like Escherichia coli as part of the extracellular matrix that holds cells together into biofilms. The molecular events that occur during curli nucleation and fiber extension remain largely unknown. Combining observations from curli amyloidogenesis in bulk solutions with real-time in situ nanoscopic imaging at the single-fiber level, we show that curli display polar growth, and we detect two kinetic regimes of fiber elongation. Single fibers exhibit stop-and-go dynamics characterized by bursts of steady-state growth alternated with periods of stagnation. At high subunit concentrations, fibers show constant, unperturbed burst growth. Curli follow a one-step nucleation process in which monomers contemporaneously fold and oligomerize into minimal fiber units that have growth characteristics identical to those of the mature fibrils. Kinetic data and interaction studies of curli fibrillation in the presence of the natural inhibitor CsgC show that the inhibitor binds curli fibers and predominantly acts at the level of fiber elongation.

Indexed as

AmyloidBacterial ProteinsEscherichia coliAmyloidBacterial ProteinsCrl protein, Bacteria

Identifiers

PMID28628096
PMCPMC5580806
OpenAlexW2625601114

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.