Evidence map›Paper›PMID 18373633›Full record

ReviewCellular microbiology2008

Polymerizing the fibre between bacteria and host cells: the biogenesis of functional amyloid fibres.

Elisabeth Ashman Epstein, Matthew R Chapman

Open access · bronzeAbstract readReview
In one paragraph

Review in Cellular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

43 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Gallibacterium anatis infection in poultry: a comprehensive review.Tropical animal health and production · 2023
    Review
  7. Article
  8. Antibiofilm properties of cathelicidin LL-37: an in-depth review.World journal of microbiology & biotechnology · 2023
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Lectins ofBeilstein journal of organic chemistry · 2019
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

2 authors at 2 institutions in 2 countries.

Elisabeth Ashman EpsteinDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 830 North University, Ann Arbor, MI 48109, USA.
Matthew R Chapman
Institut thématique Génétique, génomique et bioinformatique · FRUniversity of Michigan–Ann Arbor · US

Funding

PREDOCTORAL TRAINING IN GENETICST32GM007544 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MORAN, JOHN V. · 1985 to 2022
$11.3M
Assembly of Curli Fibers by Escherichia coliR01AI073847 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CHAPMAN, MATTHEW RICHARD · 2007 to 2011
$1.8M
NIAID NIH HHS R01 AI073847NIAID NIH HHS R01AI073847NIGMS NIH HHS T32 GM007544NIGMS NIH HHS T32GM07544
6 · The paper itself

Abstract

Amyloid fibres are proteinaceous aggregates associated with several human diseases, including Alzheimer's, Huntington's and Creutzfeldt Jakob's. Disease-associated amyloid formation is the result of proteins that misfold and aggregate into beta sheet-rich fibre polymers. Cellular toxicity is readily associated with amyloidogenesis, although the molecular mechanism of toxicity remains unknown. Recently, a new class of 'functional' amyloid fibres was discovered that demonstrates that amyloids can be utilized as a productive part of cellular biology. These functional amyloids will provide unique insights into how amyloid formation can be controlled and made less cytotoxic. Bacteria produce some of the best-characterized functional amyloids, including a surface amyloid fibre called curli. Assembled by enteric bacteria, curli fibres mediate attachment to surfaces and host tissues. Some bacterial amyloids, like harpins and microcinE492, have exploited amyloid toxicity in a directed and functional manner. Here, we review and discuss the functional amyloids assembled by bacteria. Special emphasis will be paid to the biology of functional amyloid synthesis and the connections between bacterial physiology and pathology.

Indexed as

Protein FoldingAmyloidAnimalsBacteriaBacterial Outer Membrane ProteinsBacterial ProteinsBacteriocinsHumansProtein ConformationAmyloidBacterial Outer Membrane ProteinsBacterial ProteinsBacteriocinsharpin protein, Erwinia amylovoramicrocin

Identifiers

PMID18373633
PMCPMC2674401
OpenAlexW2025221802

What OpenQuestion holds

Textmetadata
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.