Evidence map›Paper›PMID 29886539›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2018

Bacterial Amyloids.

Margery L Evans, Elizabeth Gichana, Yizhou Zhou, Matthew R Chapman

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
7.3field-weighted citation impact, top 3% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Detection of an ExPEC-likeBiotech (Basel (Switzerland)) · 2026
    Article
  2. Article
  3. Review
  4. Review
  5. CsgA gatekeeper residues control nucleation but not stability of functional amyloid.Protein science : a publication of the Protein Society · 2024
    Article
  6. Article
  7. Review
  8. Article
  9. Structure and Conservation of Amyloid Spines From theFrontiers in molecular biosciences · 2022
    Article
  10. CRISPRiFrontiers in nutrition · 2022
    Article
  11. Review
  12. Article
  13. Review
  14. Repertoire of theToxins · 2019
    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

4 authors at 1 institution in 1 country.

Margery L EvansDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.
Elizabeth GichanaDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.
Yizhou ZhouDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.
Matthew R ChapmanDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI, USA. chapmanm@umich.edu.
University of Michigan–Ann Arbor · 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
Cellular Biotechnology Training Program (CBTP) - Years 31-35T32GM145304 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Guizhi Zhu · 2022 to 2026
$2.6M
NIGMS NIH HHS R01 GM118651NIGMS NIH HHS T32 GM145304
6 · The paper itself

Abstract

Many bacteria can assemble functional amyloid fibers on their cell surface. Most bacterial amyloids contribute to biofilm or other community behaviors where cells interact with a surface or with other cells. Bacterial amyloids, like all functional amyloids, share structural and biochemical properties with disease-associated eukaryotic amyloids. The general ability of amyloids to bind specific dyes, like Congo red and Thioflavin T, and their resistance to denaturation have provided useful tools for scoring and quantifying bacterial amyloid formation. Here, we present basic approaches to study bacterial amyloids by focusing on the well-studied curli amyloid fibers expressed by Enterobacteriaceae. These methods exploit the specific tinctorial and biophysical properties of amyloids. The methods described here are straightforward and can be easily applied by any modern molecular biology lab for the study of other bacterial amyloids.

Indexed as

Bacterial ProteinsBenzothiazolesBiofilmsCongo RedEscherichia coliEscherichia coli ProteinsProtein MultimerizationBacterial ProteinsBenzothiazolesCongo RedCrl protein, BacteriaEscherichia coli Proteinsthioflavin TBacterial amyloidsCongo red dyeCurliInterbacterial complementationOverlay assayPlug Western blot analysisWestern blot analysis

Identifiers

PMID29886539
PMCPMC6447394
OpenAlexW4255402238

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.