ReviewFEMS yeast research2025
Fungal β-1,3-glucan synthase: a review of structure, mechanism, and regulation.
Review in FEMS yeast research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers, 1 of them a synthesis that pooled it.
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
7 citing papers in PubMed, 1 synthesis or guideline pooled it.
- A bibliometric and visual analysis of research on echinocandin treatment for urinary tract infections based on VOSviewer and CiteSpace.Frontiers in cellular and infection microbiology · 2026Pooled it
- Genome assembly and comparative genomic analysis of the extracellular polysaccharide-overproducing strain Schizophyllum commune SC-N.World journal of microbiology & biotechnology · 2026Article
- Article
- Green spectrofluorimetric determination of Ibrexafungerp using NBD-Cl derivatization.Scientific reports · 2026Article
- Minimal Computational Framework for Systematic Identification of Antimicrobial Targets.bioRxiv : the preprint server for biology · 2026Article
- Article
- Dynamics of 1,3-β-D-Glucan in Invasive Candidiasis: A Narrative Review of Microbiological Aspects and Diagnostic Implications.Antibodies (Basel, Switzerland) · 2026Review
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.
Funding
Abstract
Fungal β-1,3-glucan synthase (Fks) plays a central role in synthesizing β-1,3-glucan, the main structural polysaccharide of fungal cell walls, and serves as a key target for antifungal drugs, such as echinocandins and ibrexafungerp. Recent cryo-electron microscopy (cryo-EM) studies have revealed the architecture of the Fks1 and Fks1-Rho1 complex and provided new insights into its catalytic and regulatory mechanisms. This review summarizes current understanding of Fks, including its domain organization, transmembrane topology, conformational dynamics, and evolutionary comparison with structurally resolved glycosyltransferases (GTs), including bacterial cellulose synthase (BcsA), plant cellulose synthase (CesA), and other eukaryotic GTs. Through comparison of publicly available cryo-EM structures of Fks in both the apo-state and Rho1-bound state, a working mechanism of the activated Fks has been discussed. In addition, we present a potential gating model of β-glucan translocation and drug-inhibition by integrating literature with structure-based analyses. This review provides a structure-based functional model of fungal β-1,3-glucan synthase and the putative binding mechanism of its inhibitor, aiming to support future antifungal drug discovery.
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.