ReviewJournal of molecular biology2020
Structures of Bacterial MraY and Human GPT Provide Insights into Rational Antibiotic Design.
Review in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 28 citations in OpenAlex.
- Structures of Bacterial and Human Phosphoglycosyltransferases Bound to a Common Inhibitor Inform Selective Therapeutics.ACS chemical biology · 2026Article
- Structures of bacterial and human phosphoglycosyltransferases bound to a common inhibitor inform selective therapeutics.bioRxiv : the preprint server for biology · 2025Article
- Design, synthesis and optimization of TarO inhibitors as multifunctional antibiotics against Methicillin-resistant Staphylococcus aureus.npj antimicrobials and resistance · 2025Article
- Identifying Opportunity Targets in Gram-Negative Pathogens for Infectious Disease Mitigation.ACS central science · 2025Review
- Computational prediction of CNP0387675 as a non-nucleoside inhibitor of MraY, from natural product-based multi-template screening againstFrontiers in microbiology · 2025Article
- Development of a natural product optimization strategy for inhibitors against MraY, a promising antibacterial target.Nature communications · 2024Article
- The tunicamycin derivative TunR2 exhibits potent antibiotic properties with low toxicity in an in vivo Mycobacterium marinum-zebrafish TB infection model.The Journal of antibiotics · 2024Article
- Structure-Based Insight on the Mechanism of N-Glycosylation Inhibition by Tunicamycin.Molecules and cells · 2023Review
- The challenges and opportunities of developing small molecule inhibitors of MraY.Annual reports in medicinal chemistry · 2023Article
- Structure and Mechanism of the Lipid Flippase MurJ.Annual review of biochemistry · 2022Review
- Peptidoglycan biosynthesis is driven by lipid transfer along enzyme-substrate affinity gradients.Nature communications · 2022Article
- Identification and characterization of enzymes involved in the biosynthesis of pyrimidine nucleoside antibiotics.Natural product reports · 2021Review
- Synthesis and evaluation of cyclopentane-based muraymycin analogs targeting MraY.European journal of medicinal chemistry · 2021Article
- β-Lactams against the Fortress of the Gram-PositiveChemical reviews · 2021Review
- Cell Surface Biosynthesis and Remodeling Pathways in Mycobacteria Reveal New Drug Targets.Frontiers in cellular and infection microbiology · 2020Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The widespread emergence of antibiotic resistance in pathogens necessitates the development of antibacterial agents inhibiting underexplored targets in bacterial metabolism. One such target is phospho-MurNAc-pentapeptide translocase (MraY), an essential integral membrane enzyme that catalyzes the first committed step of peptidoglycan biosynthesis. MraY has long been considered a promising candidate for antibiotic development in part because it is the target of five classes of naturally occurring nucleoside inhibitors with potent in vivo and in vitro antibacterial activity. Although these inhibitors each have a nucleoside moiety, they vary dramatically in their core structures, and they have different activity properties. Until recently, the structural basis of MraY inhibition was poorly understood. Several recent structures of MraY and its human paralog, GlcNAc-1-P-transferase, have provided insights into MraY inhibition that are consistent with known inhibitor activity data and can inform rational drug design for this important antibiotic target.
Indexed as
Identifiers
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.