Evidence map›Paper›PMID 18083824›Full record

ArticleEukaryotic cell2008

Candida albicans Als adhesins have conserved amyloid-forming sequences.

Henry N Otoo, Kyeng Gea Lee, Weigang Qiu, Peter N Lipke

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

76 citing papers in PubMed, 130 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Functional Amyloids in Adhesion of Non-Pathogens (Basel, Switzerland) · 2025
    Article
  6. Development of Miniprotein-Type Inhibitors of Biofilm Formation inJournal of microbiology and biotechnology · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Structure and Conservation of Amyloid Spines From theFrontiers in molecular biosciences · 2022
    Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. Article

16 more citing papers are in PubMed but not listed here.

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 3 institutions in 1 country.

Henry N OtooDepartment of Biology, Brooklyn College, 2900 Bedford Avenue, Brooklyn, NY 11210, USA.
Kyeng Gea Lee
Weigang Qiu
Peter N Lipke
City University of New York · USBrooklyn College · USHunter College · US

Funding

PHS HHS S06 70758
6 · The paper itself

Abstract

The cell wall-bound Als adhesins of Candida albicans mediate both yeast-to-host tissue adherence and yeast aggregation. This aggregation is amyloid-like, with self-propagating secondary-structure changes, amyloid-characteristic dye binding, and induced birefringence (J. M. Rauceo, N. K. Gaur, K. G. Lee, J. E. Edwards, S. A. Klotz, and P. N. Lipke, Infect. Immun. 72:4948-4955, 2004). Therefore, we determined whether Als proteins could form amyloid fibers with properties like those in cellular aggregation. The beta-aggregation predictor TANGO identified a heptapeptide sequence present in a highly conserved sequence with amyloid-forming potential in Als1p, Als3p, and Als5p. A tridecapeptide containing this sequence formed fibers that bound Congo red and thioflavin T and had characteristic amyloid morphology. Als5p(20-431) and Als5p(20-664), large fragments of Als5p containing the amyloid sequence, also formed amyloid-like fibers and bound Congo red under native conditions. K(a)/K(s) analysis showed that the amyloid-forming sequences are highly conserved in Als proteins and evolve more slowly than other regions of the proteins. Therefore, amyloid-forming ability itself is conserved in these proteins.

Indexed as

Amino Acid SequenceAmyloidCandida albicansCell Adhesion MoleculesConserved SequenceEvolution, MolecularFungal ProteinsMicroscopy, Electron, TransmissionPeptidesProtein FoldingRecombinant ProteinsALA1 protein, Candida albicansALS1 protein, Candida albicansALS3 protein, Candida albicansAmyloidCell Adhesion MoleculesFungal ProteinsPeptidesRecombinant Proteins

Identifiers

PMID18083824
PMCPMC2394976
OpenAlexW2113757561

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.