ArticleNature communications2019
Chemical logic of MraY inhibition by antibacterial nucleoside natural products.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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.
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Who cites it
35 citing papers in PubMed.
- Structures of Bacterial and Human Phosphoglycosyltransferases Bound to a Common Inhibitor Inform Selective Therapeutics.ACS chemical biology · 2026Article
- A metal-aware library-expansion and virtual-screening workflow forFrontiers in microbiology · 2026Article
- 1,2,4-Triazole-Based First-in-Class Non-Nucleoside Inhibitors of the Bacterial Enzyme MraY.ACS bio & med chem Au · 2025Article
- Structures of bacterial and human phosphoglycosyltransferases bound to a common inhibitor inform selective therapeutics.bioRxiv : the preprint server for biology · 2025Article
- The TetR-like regulator Sco4385 and Crp-like regulator Sco3571 modulate heterologous production of antibiotics inApplied and environmental microbiology · 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
- Tunicamycins from Marine-DerivedMarine drugs · 2024Article
- Development of a natural product optimization strategy for inhibitors against MraY, a promising antibacterial target.Nature communications · 2024Article
- The MraY Inhibitor Muraymycin D2 and Its Derivatives Induce Enlarged Cells in Obligate IntracellularAntibiotics (Basel, Switzerland) · 2024Article
- The fall of the mycobacterial cell wall: interrogating peptidoglycan synthesis for novel anti-TB agents.PeerJ · 2024Review
- Unrealized targets in the discovery of antibiotics for Gram-negative bacterial infections.Nature reviews. Drug discovery · 2023Review
- Chemical genetic approaches for the discovery of bacterial cell wall inhibitors.RSC medicinal chemistry · 2023Review
- Nucleoside Analogs: A Review of Its Source and Separation Processes.Molecules (Basel, Switzerland) · 2023Review
- The mechanism of the phage-encoded protein antibiotic from ΦX174.Science (New York, N.Y.) · 2023Article
- Structure-Based Insight on the Mechanism of N-Glycosylation Inhibition by Tunicamycin.Molecules and cells · 2023Review
- Synthesis of an Antimicrobial Enterobactin-Muraymycin Conjugate for Improved Activity Against Gram-Negative Bacteria.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Expanding structural diversity of 5'-aminouridine moiety of sansanmycin via mutational biosynthesis.Frontiers in bioengineering and biotechnology · 2023Article
- The challenges and opportunities of developing small molecule inhibitors of MraY.Annual reports in medicinal chemistry · 2023Article
- Synthesis of macrocyclic nucleoside antibacterials and their interactions with MraY.Nature communications · 2022Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Novel antibacterial agents are needed to address the emergence of global antibiotic resistance. MraY is a promising candidate for antibiotic development because it is the target of five classes of naturally occurring nucleoside inhibitors with potent antibacterial activity. Although these natural products share a common uridine moiety, their core structures vary substantially and they exhibit different activity profiles. An incomplete understanding of the structural and mechanistic basis of MraY inhibition has hindered the translation of these compounds to the clinic. Here we present crystal structures of MraY in complex with representative members of the liposidomycin/caprazamycin, capuramycin, and mureidomycin classes of nucleoside inhibitors. Our structures reveal cryptic druggable hot spots in the shallow inhibitor binding site of MraY that were not previously appreciated. Structural analyses of nucleoside inhibitor binding provide insights into the chemical logic of MraY inhibition, which can guide novel approaches to MraY-targeted antibiotic design.
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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.