ArticleMethods in molecular biology (Clifton, N.J.)2019
Characterization of Arabinosyl Transfer Reactions in the Biosynthesis of Mycobacterial Cell Envelope (Lipo)Polysaccharides.
Article in Methods in molecular biology (Clifton, N.J.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
4 citing papers in PubMed, 3 citations in OpenAlex.
- Microbial Natural Products Targeting theMicroorganisms · 2026Review
- Acylation of glycerolipids in mycobacteria.Nature communications · 2023Article
- Use of Synthetic Glycolipids to Probe the Number and Position of Arabinan Chains on Mycobacterial Arabinogalactan.ACS chemical biology · 2021Article
- Lipoarabinomannan as a Point-of-Care Assay for Diagnosis of Tuberculosis: How Far Are We to Use It?Frontiers in microbiology · 2021Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
D-Arabinofuranose is a major glycosyl constituent of mycobacteria found in two essential cell envelope heteropolysaccharides, arabinogalactan and lipoarabinomannan. Seven different arabinosyltransferases at least are required to synthesize the arabinan domain of these two major glycans. Because of their interest from the perspective of drug development, these enzymes have been the object of intense investigations. In this chapter, we describe the protocols used to perform nonradioactive arabinosyltransferase assays with synthetic acceptor and donor substrates and characterize the enzymatic products of the reactions by mass spectrometry.
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