ArticleBioorganic & medicinal chemistry2021
Next generation Glucose-1-phosphate thymidylyltransferase (RmlA) inhibitors: An extended SAR study to direct future design.
Article in Bioorganic & medicinal chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 14 citations in OpenAlex.
- Development of a spectrophotometric assay for high-throughput screening and mechanistic characterization of glucose-1-phosphate thymidylyltransferase inhibitors.RSC chemical biology · 2026Article
- Dysregulation of a nucleotidyltransferase induces division and surface glycan defects inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Olive Leaf Protein Hydrolysate as a Novel Source of Antimicrobial Peptides: Peptidomic Characterization and In Silico Evaluation.Molecules (Basel, Switzerland) · 2025Article
- Resistance phenotypes and genomic features ofFrontiers in cellular and infection microbiology · 2025Article
- Identifying potential novel widespread determinants of bacterial pathogenicity using phylogenetic-based orthology analysis.Frontiers in microbiology · 2025Article
- A putative glucose-1-phosphate thymidylyltransferase is required for virulence, membrane-associated mechanisms, and tolerance to external stresses inFrontiers in plant science · 2025Article
- Article
- Protein Structure Inspired Drug Discovery.bioRxiv : the preprint server for biology · 2024Article
- Feedback Inhibition of Bacterial Nucleotidyltransferases by Rare Nucleotide l-Sugars Restricts Substrate Promiscuity.Journal of the American Chemical Society · 2023Article
- Expanding the Substrate Scope of a Bacterial Nucleotidyltransferase via Allosteric Mutations.ACS infectious diseases · 2022Article
- Rhamnose-Containing Compounds: Biosynthesis and Applications.Molecules (Basel, Switzerland) · 2022Review
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
The monosaccharide l-Rhamnose is an important component of bacterial cell walls. The first step in the l-rhamnose biosynthetic pathway is catalysed by glucose-1-phosphate thymidylyltransferase (RmlA), which condenses glucose-1-phosphate (Glu-1-P) with deoxythymidine triphosphate (dTTP) to yield dTDP-d-glucose. In addition to the active site where catalysis of this reaction occurs, RmlA has an allosteric site that is important for its function. Building on previous reports, SAR studies have explored further the allosteric site, leading to the identification of very potent P. aeruginosa RmlA inhibitors. Modification at the C6-NH
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What OpenQuestion holds
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.