ArticleThe Journal of biological chemistry2018
Structure-guided engineering of the substrate specificity of a fungal β-glucuronidase toward triterpenoid saponins.
Article in The Journal of biological chemistry, 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.
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
8 citing papers in PubMed, 32 citations in OpenAlex.
- Differential Biotransformation of Glycyrrhizin by Licorice-Derived Endophytic Fungi and Accumulation-Promoting Effects of Fungal Inoculation.International journal of molecular sciences · 2026Article
- Investigating the Metabolism of Estrogens inNutrients · 2024Article
- Qualitative metabolomics-based characterization of a phenolic UDP-xylosyltransferase with a broad substrate spectrum fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
- O-glycosyltransferases fromSynthetic and systems biotechnology · 2021Article
- Construction of a CaHPOFrontiers of chemical science and engineering · 2019Article
- Tailoring Proteins to Re-Evolve Nature: A Short Review.Molecular biotechnology · 2018Review
- β-Glucuronidases of opportunistic bacteria are the major contributors to xenobiotic-induced toxicity in the gut.Scientific reports · 2018Article
- A Novel β-Glucuronidase from Talaromyces pinophilus Li-93 Precisely Hydrolyzes Glycyrrhizin into Glycyrrhetinic Acid 3-Applied and environmental microbiology · 2018Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycoside hydrolases (GHs) have attracted special attention in research aimed at modifying natural products by partial removal of sugar moieties to manipulate their solubility and efficacy. However, these modifications are challenging to control because the low substrate specificity of most GHs often generates undesired by-products. We previously identified a GH2-type fungal β-glucuronidase from
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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.