ArticleEukaryotic cell2010
Yeast cell adhesion molecules have functional amyloid-forming sequences.
Article in Eukaryotic cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.
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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.
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Who cites it
83 citing papers in PubMed, 157 citations in OpenAlex.
- An edge β-strand mutation turns ubiquitin into a pore-forming amyloid.Protein science : a publication of the Protein Society · 2026Article
- The prion-like characteristic of ORF3 contributes to virion release and pathogenesis of hepatitis E virus.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Functional Amyloids in Adhesion of Non-Pathogens (Basel, Switzerland) · 2025Article
- Review
- Article
- Secreted Aspartic Proteinases: Key Factors inInternational journal of molecular sciences · 2024Review
- Use of the Fluorescent Dye Thioflavin T to Track Amyloid Structures in the Pathogenic YeastBio-protocol · 2024Article
- Strain and temperature dependent aggregation ofCell surface (Amsterdam, Netherlands) · 2023Article
- Amyloids and prions in the light of evolution.Current genetics · 2023Review
- Article
- 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
- Article
- Structure and Conservation of Amyloid Spines From theFrontiers in molecular biosciences · 2022Article
- Development and Use of a Monoclonal Antibody Specific for theFrontiers in cellular and infection microbiology · 2022Article
- FLO11, a Developmental Gene Conferring Impressive Adaptive Plasticity to the YeastPathogens (Basel, Switzerland) · 2021Review
- The Flo Adhesin Family.Pathogens (Basel, Switzerland) · 2021Review
- Protein Aggregation and Disaggregation in Cells and Development.Journal of molecular biology · 2021Review
- Article
- A New Function for Amyloid-Like Interactions: Cross-Beta Aggregates of Adhesins form Cell-to-Cell Bonds.Pathogens (Basel, Switzerland) · 2021Review
23 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
16 authors at 7 institutions in 2 countries.
Funding
Abstract
The occurrence of highly conserved amyloid-forming sequences in Candida albicans Als proteins (H. N. Otoo et al., Eukaryot. Cell 7:776-782, 2008) led us to search for similar sequences in other adhesins from C. albicans and Saccharomyces cerevisiae. The beta-aggregation predictor TANGO found highly beta-aggregation-prone sequences in almost all yeast adhesins. These sequences had an unusual amino acid composition: 77% of their residues were beta-branched aliphatic amino acids Ile, Thr, and Val, which is more than 4-fold greater than their prevalence in the S. cerevisiae proteome. High beta-aggregation potential peptides from S. cerevisiae Flo1p and C. albicans Eap1p rapidly formed insoluble amyloids, as determined by Congo red absorbance, thioflavin T fluorescence, and fiber morphology. As examples of the amyloid-forming ability of the native proteins, soluble glycosylphosphatidylinositol (GPI)-less fragments of C. albicans Als5p and S. cerevisiae Muc1p also formed amyloids within a few days under native conditions at nM concentrations. There was also evidence of amyloid formation in vivo: the surfaces of cells expressing wall-bound Als1p, Als5p, Muc1p, or Flo1p were birefringent and bound the fluorescent amyloid-reporting dye thioflavin T. Both of these properties increased upon aggregation of the cells. In addition, amyloid binding dyes strongly inhibited aggregation and flocculation. The results imply that amyloid formation is an intrinsic property of yeast cell adhesion proteins from many gene families and that amyloid formation is an important component of cellular aggregation mediated by these proteins.
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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.