ArticleJournal of natural medicines2026
Selective α-glucosidase inhibitory activity of (+)-eupenoxide and 3-ketone derivatives produced by the endophytic fungus of Aspergillus sp.
Article in Journal of natural medicines, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed.
- Morpho-molecular approach reveals a myco-endophyte, Aspergillus novoparasiticus CBS126849 (MTCC-13997) from the roots of Capparis decidua with therapeutic and enzymatic potential.Archives of microbiology · 2026Article
- Diversity, bioactivities, and metabolomics of culturable endophytic fungi from the medicinal plantFrontiers in microbiology · 2026Article
- Selective α-glucosidase inhibitory activity of (+)-eupenoxide and 3-ketone derivatives produced by the endophytic fungus of Aspergillus sp.Journal of natural medicines · 2026Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
α-Glucosidase and α-amylase are two important glycosidases involved in carbohydrate metabolism. Inhibitors of these enzymes are considered crucial therapeutic agents for carbohydrate absorption disorders such as diabetes and obesity. However, the inhibition of salivary amylase can result in undigested starch reaching the stomach, causing indigestion and potentially leading to gastric and duodenal ulcers as well as gastritis. Selective inhibitors that possess α-glucosidase inhibitory activity without affecting α-amylase are needed to address this issue. It has been revealed that (+)-eupenoxide and its 3-ketone derivative, produced by the endophytic fungus of Aspergillus sp. C-1-1 strain associated with Catharanthus roseus, selectively inhibits α-glucosidase. Additionally, from the α-glucosidase inhibitory activity of related compounds, we have successfully deduced the chemical structure feature necessary for α-glucosidase inhibition.
Indexed as
Identifiers
41099792What 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.