ArticleJournal of the American Chemical Society2015
Chemoenzymatic Assembly of Bacterial Glycoconjugates for Site-Specific Orthogonal Labeling.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Engineered bacteria and bacteria-derived nanomaterials for cancer therapy: Mechanisms, designs and advances.Bioactive materials · 2026Review
- Detergent exchange from lipid nanoparticles into detergent micelles unlocks a tool for biochemical and kinetic characterization of membrane proteins.bioRxiv : the preprint server for biology · 2025Article
- Selective Exoenzymatic Labeling of Lipooligosaccharides of Neisseria gonorrhoeae with α2,6-Sialoside Analogues.Chembiochem : a European journal of chemical biology · 2022Article
- Sweet impersonators: Molecular mimicry of host glycans by bacteria.Glycobiology · 2022Review
- Recent Chemical and Chemoenzymatic Strategies to Complex-TypeFrontiers in chemistry · 2022Review
- Chemical Reporters for Exploring Microbiology and Microbiota Mechanisms.Chembiochem : a European journal of chemical biology · 2020Review
- Chemoenzymatic Methods for the Synthesis of Glycoproteins.Chemical reviews · 2018Review
- Chemoenzymatic Synthesis and Applications of Prokaryote-Specific UDP-Sugars.Methods in enzymology · 2017Article
- Design and Synthesis of Nanofibers of Self-assembledTetrahedron · 2016Article
- Probing Polytopic Membrane Protein-Substrate Interactions by Luminescence Resonance Energy Transfer.Journal of the American Chemical Society · 2016Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The cell surfaces of bacteria are replete with diverse glycoconjugates that play pivotal roles in determining how bacteria interact with the environment and the hosts that they colonize. Studies to advance our understanding of these interactions rely on the availability of chemically defined glycoconjugates that can be selectively modified under orthogonal reaction conditions to serve as discrete ligands to probe biological interactions, in displayed arrays and as imaging agents. Herein, enzymes in the N-linked protein glycosylation (Pgl) pathway of Campylobacter jejuni are evaluated for their tolerance for azide-modified UDP-sugar substrates, including derivatives of 2,4-diacetamidobacillosamine and N-acetylgalactosamine. In vitro analyses reveal that chemoenzymatic approaches are useful for the preparation of undecaprenol diphosphate-linked glycans and glycopeptides with site-specific introduction of azide functionality for orthogonal labeling at three specific sites in the heptasaccharide glycan. The uniquely modified glycoconjugates represent valuable tools for investigating the roles of C. jejuni cell surface glycoconjugates in host pathogen interactions.
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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 OpenQuestion graph.