ArticleEukaryotic cell2012
Topological and mutational analysis of Saccharomyces cerevisiae Fks1.
Article in Eukaryotic cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 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
39 citing papers in PubMed, 69 citations in OpenAlex.
- Article
- Role of Pbr1, a putative oxidoreductase, in the ER quality control and folding of yeast Fks1 glucan synthase.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Micafungin exposure drives multidrug resistance inbioRxiv : the preprint server for biology · 2026Article
- Article
- Mutational landscape and molecular bases of echinocandin resistance in Saccharomyces cerevisiae.Genetics · 2026Article
- Deciphering the multidrug resistance paradigm inAntimicrobial agents and chemotherapy · 2026Review
- Molecular landscape of the fungal plasma membrane and implications for antifungal action.Nature communications · 2025Article
- Translation Inhibition by Rocaglamide A Enhances Susceptibility of Yeasts to Caspofungin.bioRxiv : the preprint server for biology · 2025Article
- A Candidozyma (Candida) auris-Optimized Episomal Plasmid-Induced Cas9-Editing System Reveals the Direct Impact of the S639F-Encoding FKS1 Mutation.The Journal of infectious diseases · 2025Article
- Cryo-EM structure of the β-1,3-glucan synthase FKS1-Rho1 complex.Nature communications · 2025Article
- Fission yeast Bgs1 glucan synthase participates in the control of growth polarity and membrane traffic.iScience · 2024Article
- Globospiramine Exhibits Inhibitory and Fungicidal Effects againstBiomolecules · 2024Article
- Structure of a fungal 1,3-β-glucan synthase.Science advances · 2023Article
- Novel Non-Hot Spot Modification in Fks1 of Candida auris Confers Echinocandin Resistance.Antimicrobial agents and chemotherapy · 2023Article
- Article
- Analysis of the Localization ofInternational journal of molecular sciences · 2023Article
- Heterologous Expression of Candida Antifungal Target Genes in the Model Organism Saccharomyces cerevisiae.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Benzylic Dehydroxylation of Echinocandin Antifungal Drugs Restores Efficacy against Resistance Conferred by Mutated Glucan Synthase.Journal of the American Chemical Society · 2022Article
- Echinocandin Drugs Induce Differential Effects in Cytokinesis Progression and Cell Integrity.Pharmaceuticals (Basel, Switzerland) · 2021Article
- DoJournal of fungi (Basel, Switzerland) · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Fks1, with orthologs in nearly all fungi as well as plants and many protists, plays a central role in fungal cell wall formation as the putative catalytic component of β-1,3-glucan synthase. It is also the target for an important new antifungal group, the echinocandins, as evidenced by the localization of resistance-conferring mutations to Fks1 hot spots 1, 2, and 3 (residues 635 to 649, 1354 to 1361, and 690 to 700, respectively). Since Fks1 is an integral membrane protein and echinocandins are cyclic peptides with lipid tails, Fks1 topology is key to understanding its function and interaction with echinocandins. We used hemagglutinin (HA)-Suc2-His4C fusions to C-terminally truncated Saccharomyces cerevisiae Fks1 to experimentally define its topology and site-directed mutagenesis to test function of selected residues. Of the 15 to 18 transmembrane helices predicted in silico for Fks1 from evolutionarily diverse fungi, 13 were experimentally confirmed. The N terminus (residues 1 to 445) is cytosolic and the C terminus (residues 1823 to 1876) external; both are essential to Fks1 function. The cytosolic central domain (residues 715 to 1294) includes newly recognized homology to glycosyltransferases, and residues potentially involved in substrate UDP-glucose binding and catalysis are essential. All three hot spots are external, with hot spot 1 adjacent to and hot spot 3 largely embedded within the outer leaflet of the membrane. This topology suggests a model in which echinocandins interact through their lipid tails with hot spot 3 and through their cyclic peptides with hot spots 1 and 2.
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.