ArticleACS omega2019
Probing the Effect of Glucose on the Activity and Stability of β-Glucosidase: An All-Atom Molecular Dynamics Simulation Investigation.
Article in ACS omega, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed, 41 citations in OpenAlex.
- Characterization of a Novel GH3 β-Glucosidase with Alkali-Tolerant and Halophilic Properties from Pontixanthobacter luteolus SW-109.Applied biochemistry and biotechnology · 2026Article
- EPIC: A Machine-Learning Framework for Product-Dependent Behavior in β‑Glucosidases.ACS omega · 2026Article
- Temperature-Dependent Conformational Dynamics of Substrate Entrance Loops in β-Glucosidase: Insights from Molecular Dynamics Simulations.International journal of molecular sciences · 2026Article
- Article
- Computational Insights into Glucose Tolerance and Stimulation in a Family 1 β-glucosidase.Journal of chemical information and modeling · 2025Article
- Composition of Lignocellulose Hydrolysate in Different Biorefinery Strategies: Nutrients and Inhibitors.Molecules (Basel, Switzerland) · 2024Review
- A thermostable and inhibitor resistant β-glucosidase from Rasamsonia emersonii for efficient hydrolysis of lignocellulosics biomass.Bioprocess and biosystems engineering · 2024Article
- Enzyme characterization of lactic acid bacteria isolated from duck excreta.Veterinary world · 2024Article
- The Conformational Change of the L3 Loop Affects the Structural Changes in the Substrate Binding Pocket Entrance of β-Glucosidase.Molecules (Basel, Switzerland) · 2023Article
- Profiling of the β-glucosidases identified in the genome ofApplied and environmental microbiology · 2023Article
- A higher flexibility at the SARS-CoV-2 main protease active site compared to SARS-CoV and its potentialities for new inhibitor virtual screening targeting multi-conformers.Journal of biomolecular structure & dynamics · 2022Article
- VTR: A Web Tool for Identifying Analogous Contacts on Protein Structures and Their Complexes.Frontiers in bioinformatics · 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
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
β-Glucosidase (EC 3.2.1.21) plays an essential role in the removal of glycosyl residues from disaccharide cellobiose to produce glucose during the hydrolysis of lignocellulosic biomass. Although there exist a few β-glucosidase that are tolerant to large concentrations of glucose, these enzymes are typically prone to glucose inhibition. Understanding the basis of this inhibition is important for the production of cheaper biofuels from lignocellulose. In this study, all
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.