ArticleThe Journal of organic chemistry2013
Synthesis of lipid-linked arabinofuranose donors for glycosyltransferases.
Article in The Journal of organic chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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.
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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
5 citing papers in PubMed.
- Chemical Reporters for Bacterial Glycans: Development and Applications.Chemical reviews · 2022Review
- Biosynthetic Glycan Labeling.Journal of the American Chemical Society · 2021Article
- Bacterial Cell Wall Modification with a Glycolipid Substrate.Journal of the American Chemical Society · 2019Article
- Magnesium pyrophosphates in enzyme mimics of nucleotide synthases and kinases and in their prebiotic chemistry.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Isoprenoid phosphonophosphates as glycosyltransferase acceptor substrates.Journal of the American Chemical Society · 2014Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Mycobacteria and corynebacteria use decaprenylphosphoryl-β-D-arabinofuranose (DPA) as a critical cell wall building block. Arabinofuranosyltransferases that process this substrate to mediate cell wall assembly have served as drug targets, but little is known about the substrate specificity of any of these enzymes. To probe substrate recognition of DPA, we developed a general and efficient synthetic route to β-D-arabinofuranosyl phosphodiesters. In this approach, the key glycosyl phosphodiester bond-forming reaction proceeds with high β-selectivity. In addition to its stereoselectivity, our route provides the means to readily access a variety of different lipid analogues, including aliphatic and polyprenyl substrates.
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Registered trials
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