ArticleActa crystallographica. Section F, Structural biology communications2018
Structural studies of a glycoside hydrolase family 3 β-glucosidase from the model fungus Neurospora crassa.
Article in Acta crystallographica. Section F, Structural biology communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Xylose and ethanol stimulate a thermostable β-glucosidase from Humicola brevis var. thermoidea.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026Article
- Expression and Characterization of a Rice β-Xylosidase with Xylooligosaccharide Hydrolysis and Transglycosylation Activities.Journal of agricultural and food chemistry · 2025Article
- Deciphering domain structures of Aspergillus and Streptomyces GH3-β-Glucosidases: a screening system for enzyme engineering and biotechnological applications.BMC research notes · 2024Article
- A Multiomics Perspective on Plant Cell Wall-Degrading Enzyme Production: Insights from the Unexploited FungusJournal of fungi (Basel, Switzerland) · 2024Article
- Unveiling a classical mutant in the context of the GH3 β-glucosidase family in Neurospora crassa.AMB Express · 2024Article
- Genomic evidence for the first symbiotic Deferribacterota, a novel gut symbiont from the deep-sea hydrothermal vent shrimpFrontiers in microbiology · 2023Article
- Improving the Substrate Affinity and Catalytic Efficiency of β-Glucosidase Bgl3A fromBiomolecules · 2021Article
- Crystal Structure of a GH3 β-Glucosidase from the Thermophilic FungusInternational journal of molecular sciences · 2019Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glycoside hydrolase family 3 (GH3) β-glucosidases are a structurally diverse family of enzymes. Cel3A from Neurospora crassa (NcCel3A) belongs to a subfamily of key enzymes that are crucial for industrial biomass degradation. β-Glucosidases hydrolyse the β-1,4 bond at the nonreducing end of cellodextrins. The hydrolysis of cellobiose is of special importance as its accumulation inhibits other cellulases acting on crystalline cellulose. Here, the crystal structure of the biologically relevant dimeric form of NcCel3A is reported. The structure has been refined to 2.25 Å resolution, with an R
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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.