Evidence map›Paper›PMID 30622185›Full record

ArticlemBio2019

Physical Determinants of Amyloid Assembly in Biofilm Formation.

Maria Andreasen, Georg Meisl, Jonathan D Taylor, Thomas C T Michaels, Aviad Levin, Daniel E Otzen, Matthew R Chapman, Christopher M Dobson, Steve J Matthews, Tuomas P J Knowles

Open access · goldAbstract read
In one paragraph

Article in mBio, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
4.5field-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

47 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
  2. The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Structural basis ofScience advances · 2025
    Article
  7. Article
  8. Advance in identified targets of berberine.Frontiers in pharmacology · 2025
    Review
  9. CsgA gatekeeper residues control nucleation but not stability of functional amyloid.Protein science : a publication of the Protein Society · 2024
    Article
  10. Structure of biofilm-forming functional amyloid PSMα1 fromProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Gut dysbiosis in autoimmune diseases: Association with mortality.Frontiers in cellular and infection microbiology · 2023
    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

10 authors at 5 institutions in 3 countries.

Maria Andreasen *Department of Chemistry, University of Cambridge, Cambridge, United Kingdom.ORCID 0000-0002-6096-2995
Georg Meisl *Department of Chemistry, University of Cambridge, Cambridge, United Kingdom.
Jonathan D TaylorDepartment of Life Sciences, Imperial College London, London, United Kingdom.
Thomas C T MichaelsDepartment of Chemistry, University of Cambridge, Cambridge, United Kingdom.
Aviad LevinDepartment of Chemistry, University of Cambridge, Cambridge, United Kingdom.
Daniel E OtzenInterdisciplinary Nanoscience Center (iNANO), Aarhus University, Aarhus, Denmark.
Matthew R ChapmanDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan College of Literature, Science, and the Arts, Ann Arbor, Michigan, USA.
Christopher M DobsonDepartment of Chemistry, University of Cambridge, Cambridge, United Kingdom.
Steve J MatthewsPaulson School of Engineering and Applied Sciences, Harvard University, Cambridge, Massachusetts, USA.
Tuomas P J KnowlesDepartment of Chemistry, University of Cambridge, Cambridge, United Kingdom tpjk2@cam.ac.uk.
University of Cambridge · GBHarvard University · USAarhus University · DKImperial College London · GBUniversity of Michigan · US

Funding

Protein and Chemical Modulation of Curli Amyloid BiogenesisR01GM118651 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Matthew Richard Chapman · 2016 to 2026
$3.0M
Medical Research Council MR/P028225/1NIGMS NIH HHS R01 GM118651Wellcome Trust
6 · The paper itself

Abstract

A wide range of bacterial pathogens have been shown to form biofilms, which significantly increase their resistance to environmental stresses, such as antibiotics, and are thus of central importance in the context of bacterial diseases. One of the major structural components of these bacterial biofilms are amyloid fibrils, yet the mechanism of fibril assembly and its importance for biofilm formation are currently not fully understood. By studying fibril formation

Indexed as

Protein MultimerizationAmyloidBiofilmsChemical PhenomenaEscherichia coliEscherichia coli ProteinsMacromolecular SubstancesProtein AggregatesPseudomonas fluorescensAmyloidcsgA protein, E coliEscherichia coli ProteinsMacromolecular SubstancesProtein Aggregatesbiofilmsfunctional bacterial amyloidsprotein aggregation

Identifiers

PMID30622185
PMCPMC6325246
OpenAlexW2909879374

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.