ArticleNature chemical biology2020
Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family.
Article in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 18 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
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Who cites it
18 citing papers in PubMed, 51 citations in OpenAlex.
- Conformational gating mechanism for processive catalysis of β(1,3)-glucans.Nature communications · 2026Article
- Characterization and expression ofMycoscience · 2026Article
- A novel acidic laminarinase derived from Jermuk hot spring metagenome.Applied microbiology and biotechnology · 2025Article
- Gene Expression by a Model Fungus in the Ascomycota Provides Insight Into the Decay of Fungal Necromass.Environmental microbiology · 2024Article
- Molecular insights into the hydrolysis and transglycosylation of a deep-seaApplied and environmental microbiology · 2024Article
- Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks.BMC genomics · 2024Article
- Review
- Structural insights into curdlan degradation via a glycoside hydrolase containing a disruptive carbohydrate-binding module.Biotechnology for biofuels and bioproducts · 2024Article
- Metagenomic insights into the dynamic degradation of brown algal polysaccharides by kelp-associated microbiota.Applied and environmental microbiology · 2024Article
- Biochemical characterization of Fsa16295Glu fromFrontiers in microbiology · 2024Article
- An objective criterion to evaluate sequence-similarity networks helps in dividing the protein family sequence space.PLoS computational biology · 2023Article
- Expanding the viewpoint: Leveraging sequence information in enzymology.Current opinion in chemical biology · 2023Review
- Review
- Structural basis for glucosylsucrose synthesis by a member of the α-1,2-glucosyltransferase family.Acta biochimica et biophysica Sinica · 2022Article
- Gut microbiome of the largest living rodent harbors unprecedented enzymatic systems to degrade plant polysaccharides.Nature communications · 2022Article
- Recent advances in enzymatic synthesis of β-glucan and cellulose.Carbohydrate research · 2021Review
- Fungal Biofilms as a Valuable Target for the Discovery of Natural Products That Cope with the Resistance of Medically Important Fungi-Latest Findings.Antibiotics (Basel, Switzerland) · 2021Review
- Discovery of new enzymatic functions and metabolic pathways using genomic enzymology web tools.Current opinion in biotechnology · 2021Review
Corrections and comments
- Commented on by
- Erratum issued
Authors and funding
19 authors at 3 institutions in 2 countries.
Funding
Abstract
The fundamental and assorted roles of β-1,3-glucans in nature are underpinned on diverse chemistry and molecular structures, demanding sophisticated and intricate enzymatic systems for their processing. In this work, the selectivity and modes of action of a glycoside hydrolase family active on β-1,3-glucans were systematically investigated combining sequence similarity network, phylogeny, X-ray crystallography, enzyme kinetics, mutagenesis and molecular dynamics. This family exhibits a minimalist and versatile (α/β)-barrel scaffold, which can harbor distinguishing exo or endo modes of action, including an ancillary-binding site for the anchoring of triple-helical β-1,3-glucans. The substrate binding occurs via a hydrophobic knuckle complementary to the canonical curved conformation of β-1,3-glucans or through a substrate conformational change imposed by the active-site topology of some fungal enzymes. Together, these findings expand our understanding of the enzymatic arsenal of bacteria and fungi for the breakdown and modification of β-1,3-glucans, which can be exploited for biotechnological applications.
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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.