Evidence map›Paper›PMID 22099004›Full record

ArticleTrends in microbiology2012

Strengthening relationships: amyloids create adhesion nanodomains in yeasts.

Peter N Lipke, Melissa C Garcia, David Alsteens, Caleen B Ramsook, Stephen A Klotz, Yves F Dufrêne

Open access · greenAbstract read
In one paragraph

Article in Trends in microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

60 citing papers in PubMed, 103 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Assessing Als3 Peptide-Binding Cavity and Amyloid-Forming Region Contributions toFrontiers in cellular and infection microbiology · 2022
    Article
  7. Frontiers in cellular and infection microbiology · 2022
    Article
  8. Review
  9. Article
  10. Review
  11. Critical reviews in microbiology · 2021
    Review
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Pathogens (Basel, Switzerland) · 2019
    Review
  19. Article
  20. Adhesins of Yeasts: Protein Structure and Interactions.Journal of fungi (Basel, Switzerland) · 2018
    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

6 authors at 3 institutions in 2 countries.

Peter N LipkeDepartment of Biology, Brooklyn College of the City University of New York, New York, NY, USA. plipke@brooklyn.cuny.edu
Melissa C Garcia
David Alsteens
Caleen B Ramsook
Stephen A Klotz
Yves F Dufrêne
City University of New York · USUCLouvain · BEUniversity of Arizona · 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 GM 083756NIGMS NIH HHS SC1 GM083756
6 · The paper itself

Abstract

Budding yeasts adhere to biotic or abiotic surfaces and aggregate to form biofilms, using wall-anchored glycoprotein adhesins. The process is paradoxical: adhesins often show weak binding to specific ligands, yet mediate remarkably strong adherence. Single-molecule atomic force microscopy (AFM), genomics, biochemistry and cell biology have recently explained the puzzle, with Candida albicans Als adhesins as the paradigm. The strength of adhesion results partly from force-activated amyloid-like clustering of hundreds of adhesin molecules to form arrays of ordered multimeric binding sites. The various protein domains of eukaryotic adhesins cooperate to facilitate this fascinating new mechanism of activation.

Indexed as

Amino Acid SequenceAmyloidBinding SitesBiofilmsCandida albicansCell AdhesionCell Adhesion MoleculesFungal ProteinsMicroscopy, Atomic ForceMolecular Sequence DataOligosaccharidesProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationSaccharomyces cerevisiae(6-O-aminoethylphosphonato-mannopyranosyl)-(1-2)-mannopyranosyl-(1-6)-mannopyranosyl-(1-4)-(2-amino-2-deoxyglucopyranosyl)-(1-6)-1-O-(1,2-di-O-octadecanoyl-sn-glyceryl-phosphonato)-myo-inositolALA1 protein, Candida albicansAmyloidCell Adhesion MoleculesFungal ProteinsOligosaccharides

Identifiers

PMID22099004
PMCPMC3278544
OpenAlexW2166344331

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.