Evidence map›Paper›PMID 24681687›Full record

ArticleEukaryotic cell2014

Role of force-sensitive amyloid-like interactions in fungal catch bonding and biofilms.

Cho X J Chan, Peter N Lipke

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

25 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. Functional Amyloids in Adhesion of Non-Pathogens (Basel, Switzerland) · 2025
    Article
  4. Review
  5. Article
  6. What makes functional amyloids work?Critical reviews in biochemistry and molecular biology · 2022
    Review
  7. Structure and Conservation of Amyloid Spines From theFrontiers in molecular biosciences · 2022
    Article
  8. Review
  9. Article
  10. Article
  11. Functional Amyloids.Cold Spring Harbor perspectives in biology · 2019
    Review
  12. Article
  13. Article
  14. Impact of Fungal MAPK Pathway Targets on the Cell Wall.Journal of fungi (Basel, Switzerland) · 2018
    Article
  15. What We Do Not Know about Fungal Cell Adhesion Molecules.Journal of fungi (Basel, Switzerland) · 2018
    Review
  16. Article
  17. Review
  18. Fungal Biofilms: Inside Out.Microbiology spectrum · 2017
    Review
  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 1 country.

Cho X J ChanBiology Department, City University of New York Brooklyn College and Biochemistry Program, Graduate Center of the City University of New York, New York, New York, USA.
Peter N LipkeBiology Department, City University of New York Brooklyn College and Biochemistry Program, Graduate Center of the City University of New York, New York, New York, USA plipke@brooklyn.cuny.edu.
City University of New York · USThe Graduate Center, CUNY · US

Funding

Amyloid-like Interactions in Yeast Cell AdhesionSC1GM083756 · NIGMS · BROOKLYN COLLEGE · PI LIPKE, PETER N · 2008 to 2011
$1.7M
Diversity Supplement to R01 GM 098616 for Ivor JosephR01GM098616 · NIGMS · BROOKLYN COLLEGE · PI LIPKE, PETER N · 2012 to 2015
$1.5M
NIGMS NIH HHS R01 GM098616NIGMS NIH HHS SC1 GM083756
6 · The paper itself

Abstract

The Candida albicans Als adhesin Als5p has an amyloid-forming sequence that is required for aggregation and formation of model biofilms on polystyrene. Because amyloid formation can be triggered by force, we investigated whether laminar flow could activate amyloid formation and increase binding to surfaces. Shearing Saccharomyces cerevisiae cells expressing Als5p or C. albicans at 0.8 dyne/cm(2) increased the quantity and strength of cell-to-surface and cell-to-cell binding compared to that at 0.02 dyne/cm(2). Thioflavin T fluorescence showed that the laminar flow also induced adhesin aggregation into surface amyloid nanodomains in Als5p-expressing cells. Inhibitory concentrations of the amyloid dyes thioflavin S and Congo red or a sequence-specific anti-amyloid peptide decreased binding and biofilm formation under flow. Shear-induced binding also led to formation of robust biofilms. There was less shear-activated increase in adhesion, thioflavin fluorescence, and biofilm formation in cells expressing the amyloid-impaired V326N-substituted Als5p. Similarly, S. cerevisiae cells expressing Flo1p or Flo11p flocculins also showed shear-dependent binding, amyloid formation, biofilm formation, and inhibition by anti-amyloid compounds. Together, these results show that laminar flow activated amyloid formation and led to enhanced adhesion of yeast cells to surfaces and to biofilm formation.

Indexed as

Amino Acid SequenceAmyloidBiofilmsCandida albicansCell AdhesionCell Adhesion MoleculesFluorescenceFungal ProteinsPolystyrenesSaccharomyces cerevisiaeALA1 protein, Candida albicansAmyloidCell Adhesion MoleculesFungal ProteinsPolystyrenes

Identifiers

PMID24681687
PMCPMC4187618
OpenAlexW2139097235

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.