ArticleProceedings of the National Academy of Sciences of the United States of America2011
Structural basis for the broad specificity to host-cell ligands by the pathogenic fungus Candida albicans.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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.
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
57 citing papers in PubMed, 81 citations in OpenAlex.
- Candicidal Effect of a Nanoemulsion Based on the Essential Oil of the Medicinal PlantPharmaceuticals (Basel, Switzerland) · 2026Article
- mGem: Fungal adhesins inmBio · 2026Article
- Structural and Functional Insights into Viral and Fungal Proteins Involved in Chronic Inflammation and Their Biologic Treatments.Pharmaceutics · 2025Review
- Review
- Development of Miniprotein-Type Inhibitors of Biofilm Formation inJournal of microbiology and biotechnology · 2025Article
- Anticandidal activity ofFrontiers in pharmacology · 2025Article
- Sticking to the Subject: Multifunctionality in Microbial Adhesins.Journal of fungi (Basel, Switzerland) · 2023Review
- The catheterized bladder environment promotes Efg1- and Als1-dependentScience advances · 2023Article
- Calcineurin Inhibitors Synergize with Manogepix to Kill Diverse Human Fungal Pathogens.Journal of fungi (Basel, Switzerland) · 2022Article
- Candida albicans evades NK cell elimination via binding of Agglutinin-Like Sequence proteins to the checkpoint receptor TIGIT.Nature communications · 2022Article
- Cell-Cell Mating Interactions: Overview and Potential of Single-Cell Force Spectroscopy.International journal of molecular sciences · 2022Review
- Assessing Als3 Peptide-Binding Cavity and Amyloid-Forming Region Contributions toFrontiers in cellular and infection microbiology · 2022Article
- 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
- Development and validation of monoclonal antibodies specific for Candida albicans Als2, Als9-1, and Als9-2.PloS one · 2022Article
- Article
- Parasexuality ofFrontiers in cellular and infection microbiology · 2021Review
- Using Genomics to Shape the Definition of the Agglutinin-Like Sequence (Frontiers in cellular and infection microbiology · 2021Article
- Scalar nanostructure of theCell surface (Amsterdam, Netherlands) · 2020Article
- Motifs and interface amino acid-mediated regulation of amyloid biogenesis in microbes to humans: potential targets for intervention.Biophysical reviews · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Candida albicans is the most prevalent fungal pathogen in humans and a major source of life-threatening nosocomial infections. The Als (agglutinin-like sequence) glycoproteins are an important virulence factor for this fungus and have been associated with binding of host-cell surface proteins and small peptides of random sequence, the formation of biofilms and amyloid fibers. High-resolution structures of N-terminal Als adhesins (NT-Als; up to 314 amino acids) show that ligand recognition relies on a motif capable of binding flexible C termini of peptides in extended conformation. Central to this mechanism is an invariant lysine that recognizes the C-terminal carboxylate of ligands at the end of a deep-binding cavity. In addition to several protein-peptide interactions, a network of water molecules runs parallel to one side of the ligand and contributes to the recognition of diverse peptide sequences. These data establish NT-Als adhesins as a separate family of peptide-binding proteins and an unexpected adhesion system for primary, widespread protein-protein interactions at the Candida/host-cell interface.
Indexed as
Identifiers
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.