ArticleJournal of bacteriology2001
Interaction of alpha-agglutinin and a-agglutinin, Saccharomyces cerevisiae sexual cell adhesion molecules.
Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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.
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Who cites it
28 citing papers in PubMed, 54 citations in OpenAlex.
- Regulation of the Cell Wall Integrity pathway at the contact site between mating partners in yeast.The Journal of cell biology · 2026Article
- Dual spatio-functional control of a fission yeast-based bioprocessor upon chemical induction.RSC chemical biology · 2026Article
- Oral Immunization with Yeast-Surface Display of SARS-CoV-2 Antigens inInfectious disease reports · 2025Article
- Conserved signaling modules regulate filamentous growth in fungi: a model for eukaryotic cell differentiation.Genetics · 2024Review
- Creeping yeast: a simple, cheap and robust protocol for the identification of mating type in Saccharomyces cerevisiae.FEMS yeast research · 2022Article
- Cell-Cell Mating Interactions: Overview and Potential of Single-Cell Force Spectroscopy.International journal of molecular sciences · 2022Review
- Single-cell fluidic force microscopy reveals stress-dependent molecular interactions in yeast mating.Communications biology · 2021Article
- Using Genomics to Shape the Definition of the Agglutinin-Like Sequence (Frontiers in cellular and infection microbiology · 2021Article
- Amyloid-Like β-Aggregates as Force-Sensitive Switches in Fungal Biofilms and Infections.Microbiology and molecular biology reviews : MMBR · 2018Review
- High-throughput characterization of protein-protein interactions by reprogramming yeast mating.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Gamete signalling underlies the evolution of mating types and their number.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016Article
- Sensory input attenuation allows predictive sexual response in yeast.Nature communications · 2016Article
- Differences in environmental stress response among yeasts is consistent with species-specific lifestyles.Molecular biology of the cell · 2016Article
- Candida albicans Agglutinin-Like Sequence (Als) Family Vignettes: A Review of Als Protein Structure and Function.Frontiers in microbiology · 2016Review
- Article
- Between Amyloids and Aggregation Lies a Connection with Strength and Adhesion.New journal of science · 2014Article
- Regulation of cell wall biogenesis in Saccharomyces cerevisiae: the cell wall integrity signaling pathway.Genetics · 2011Review
- Accelerated and adaptive evolution of yeast sexual adhesins.Molecular biology and evolution · 2011Article
- Unfolding individual als5p adhesion proteins on live cells.ACS nano · 2009Article
- Growth temperature exerts differential physiological and transcriptional responses in laboratory and wine strains of Saccharomyces cerevisiae.Applied and environmental microbiology · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
alpha-Agglutinin and a-agglutinin are complementary cell adhesion glycoproteins active during mating in the yeast Saccharomyces cerevisiae. They bind with high affinity and high specificity: cells of opposite mating types are irreversibly bound by a few pairs of agglutinins. Equilibrium and surface plasmon resonance kinetic analyses showed that the purified binding region of alpha-agglutinin interacted similarly with purified a-agglutinin and with a-agglutinin expressed on cell surfaces. At 20 degrees C, the K(D) for the interaction was 2 x 10(-9) to 5 x 10(-9) M. This high affinity was a result of a very low dissociation rate ( approximately 2.6 x 10(-4) s(-1)) coupled with a low association rate (= 5 x 10(4) M(-1) s(-1)). Circular-dichroism spectroscopy showed that binding of the proteins was accompanied by measurable changes in secondary structure. Furthermore, when binding was assessed at 10 degrees C, the association kinetics were sigmoidal, with a very low initial rate. An induced-fit model of binding with substantial apposition of hydrophobic surfaces on the two ligands can explain the observed affinity, kinetics, and specificity and the conformational effects of the binding reaction.
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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.