ArticleCell surface (Amsterdam, Netherlands)2018
The role of the jaw subdomain of peptidoglycan glycosyltransferases for lipid II polymerization.
Article in Cell surface (Amsterdam, Netherlands), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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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Who cites it
4 citing papers in PubMed, 11 citations in OpenAlex.
- Carbamate-Bearing Carbohydrates: Natural Occurrence, Pharmacological Relevance, and Chemical Synthesis.ACS omega · 2026Review
- Discovery of a Novel Benzothiophene Inhibitor of Penicillin-Binding Protein 2 with Potent Gram-Positive Activity.Antibiotics (Basel, Switzerland) · 2026Article
- Structural diversity, bioactivity, and biosynthesis of phosphoglycolipid family antibiotics: Recent advances.BBA advances · 2022Article
- CryoEM structure of the antibacterial target PBP1b at 3.3 Å resolution.Nature communications · 2021Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Bacterial peptidoglycan glycosyltransferases (PGT) catalyse the essential polymerization of lipid II into linear glycan chains required for peptidoglycan biosynthesis. The PGT domain is composed of a large head subdomain and a smaller jaw subdomain and can be potently inhibited by the antibiotic moenomycin A (MoeA). We present an X-ray structure of the MoeA-bound
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