ArticleBioorganic chemistry2026
New Insights of Muraymycin A1 and Its Analogs as DPAGT1 Inhibitors.
Article in Bioorganic chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Structures of Bacterial and Human Phosphoglycosyltransferases Bound to a Common Inhibitor Inform Selective Therapeutics.ACS chemical biology · 2026Article
- DPAGT1-Perspective as an Anticancer Drug Target.Molecules (Basel, Switzerland) · 2025Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Muraymycin A1 (MA1, 1), a complex nucleoside antibiotic, is a potent inhibitor of DPAGT1 (dolichylphosphate N-acetylglucosamine phosphotransferase 1), yet its relationship to cytotoxicity has remained unclear. Through a total synthetic route, we generated sufficient quantities of MA1 and key analogs to define the structural features required for selective DPAGT1 inhibition. Synthetic MA1 proved to be a stronger DPAGT1 inhibitor than tunicamycin V (TM-V), a broadly cytotoxic phosphotransferase inhibitor, but uniquely displayed slow antiproliferative activity against breast cancer cells including triple-negative subtypes, while sparing normal cells. The MA1 analogs MA1-NH₂ (3) and MA1-NH₂-Guanidyl (4), readily accessed from a common intermediate, matched MA1 in both enzyme inhibition and selective cytotoxicity. These studies delineate the minimum structural requirements of MA1 necessary for DPAGT1 inhibitory activity. Together, these compounds constitute highly selective biochemical tools for probing N-glycosylation in solid cancers and provide a foundation for developing more targeted anticancer strategies.
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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 Socratic graph.