ArticleActa pharmaceutica Sinica. B2024
Molecular characterization and structure basis of a malonyltransferase with both substrate promiscuity and catalytic regiospecificity from
Article in Acta pharmaceutica Sinica. B, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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
6 citing papers in PubMed.
- Advances in the heterologous biosynthesis of QS saponins: a review.Microbial cell factories · 2026Review
- Biosynthesis of cinchona alkaloids.Nature · 2026Article
- Promiscuous Transferases Malonylate Furaneol Glucoside inJournal of agricultural and food chemistry · 2026Article
- Inheritance and enzymatic basis of anthocyanin malonylation in Fragaria × ananassa.The Plant journal : for cell and molecular biology · 2025Article
- Computer-Aided Drug Design in Research on Chinese Materia Medica: Methods, Applications, Advantages, and Challenges.Pharmaceutics · 2025Review
- Complete pathway elucidation of echinacoside in Cistanche tubulosa and de novo biosynthesis of phenylethanoid glycosides.Nature communications · 2025Article
Corrections and comments
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymatic malonylation of natural glycosides provides a promising alternative method for drug-like malonylated glycosides supply. However, the catalytic potential and structural basis of plant malonyltransferase are far from being fully elucidated. This work identified a new malonyltransferase CtMaT1 from
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Registered trials
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