ArticlePloS one2011
A role for amyloid in cell aggregation and biofilm formation.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
What it found
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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.
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.
Who cites it
61 citing papers in PubMed, 120 citations in OpenAlex.
- Cell Adhesion and Biofilm Development via Force-Sensitive Mechanisms: A Perspective.ACS biomaterials science & engineering · 2026Review
- Amyloid fibrils of the Als5p-derived peptide NHVirulence · 2025Article
- Functional Amyloids in Adhesion of Non-Pathogens (Basel, Switzerland) · 2025Article
- Review
- Insights into Candida auris dispersal cells and their impact on antifungal resistance.BMC microbiology · 2025Article
- Conserved signaling modules regulate filamentous growth in fungi: a model for eukaryotic cell differentiation.Genetics · 2024Review
- The Pga59 cell wall protein is an amyloid forming protein involved in adhesion and biofilm establishment in the pathogenic yeast Candida albicans.NPJ biofilms and microbiomes · 2023Article
- What makes functional amyloids work?Critical reviews in biochemistry and molecular biology · 2022Review
- Structure and Conservation of Amyloid Spines From theFrontiers in molecular biosciences · 2022Article
- FLO11, a Developmental Gene Conferring Impressive Adaptive Plasticity to the YeastPathogens (Basel, Switzerland) · 2021Review
- A New Function for Amyloid-Like Interactions: Cross-Beta Aggregates of Adhesins form Cell-to-Cell Bonds.Pathogens (Basel, Switzerland) · 2021Review
- From Protein Building Blocks to Functional Materials.ACS nano · 2021Review
- Review
- Deciphering Streptococcal Biofilms.Microorganisms · 2020Review
- Functional amyloids of eukaryotes: criteria, classification, and biological significance.Current genetics · 2020Review
- How Microbes Use Force To Control Adhesion.Journal of bacteriology · 2020Review
- Inhibitory effect of novel Eugenol Tosylate Congeners on pathogenicity of Candida albicans.BMC complementary medicine and therapies · 2020Article
- An Amyloid Core Sequence in the Major Candida albicans Adhesin Als1p Mediates Cell-Cell Adhesion.mBio · 2019Article
- Fluidic Force Microscopy Demonstrates That Homophilic Adhesion by Candida albicans Als Proteins Is Mediated by Amyloid Bonds between Cells.Nano letters · 2019Article
- Article
1 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Cell adhesion molecules in Saccharomyces cerevisiae and Candida albicans contain amyloid-forming sequences that are highly conserved. We have now used site-specific mutagenesis and specific peptide perturbants to explore amyloid-dependent activity in the Candida albicans adhesin Als5p. A V326N substitution in the amyloid-forming region conserved secondary structure and ligand binding, but abrogated formation of amyloid fibrils in soluble Als5p and reduced cell surface thioflavin T fluorescence. When displayed on the cell surface, Als5p with this substitution prevented formation of adhesion nanodomains and formation of large cellular aggregates and model biofilms. In addition, amyloid nanodomains were regulated by exogenous peptides. An amyloid-forming homologous peptide rescued aggregation and biofilm activity of Als5p(V326N) cells, and V326N substitution peptide inhibited aggregation and biofilm activity in Als5p(WT) cells. Therefore, specific site mutation, inhibition by anti-amyloid peturbants, and sequence-specificity of pro-amyloid and anti-amyloid peptides showed that amyloid formation is essential for nanodomain formation and activation.
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What OpenQuestion holds
Registered trials
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.