ArticleNature communications2024
Multimodal binding and inhibition of bacterial ribosomes by the antimicrobial peptides Api137 and Api88.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed.
- Flipping antimicrobial peptides in the exit tunnel of the bacterial ribosome.Nature communications · 2026Article
- A multi-stage computational pipeline andRSC advances · 2026Article
- Harnessing meat byproducts for health: bioactive peptides to modulate gut microbiota and promote sustainability.Food chemistry: X · 2026Review
- Antimicrobial peptides in the era of resistance: integrating AI-driven design, host-microbe interactions, and nanotechnological delivery.Frontiers in microbiology · 2026Review
- Molecular Epidemiology and Multilevel Drug Resistance Mechanisms ofInfection and drug resistance · 2026Review
- Exploiting peptide chirality and transport to dissect the complex mechanism of action of host peptides on bacteria.PLoS genetics · 2025Article
- Exploiting Peptide Chirality and Transport to Dissect the Complex Mechanism of Action of Host Peptides on Bacteria.bioRxiv : the preprint server for biology · 2025Article
- Substitution of Proline Residues by 4-Fluoro-l-Proline Affects the Mechanism of the Proline-Rich Antimicrobial Peptide Api137.Antibiotics (Basel, Switzerland) · 2025Article
- The structure of the Vibrio natriegens 70S ribosome in complex with the proline-rich antimicrobial peptide Bac5(1-17).Nucleic acids research · 2025Article
- The proline-rich antimicrobial peptide Api137 disrupts large ribosomal subunit assembly and induces misfolding.Nature communications · 2025Article
- Proline-Rich Antimicrobial Peptides from Invertebrates.Molecules (Basel, Switzerland) · 2024Review
- Activity, structure, and diversity of Type II proline-rich antimicrobial peptides from insects.EMBO reports · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
Abstract
Proline-rich antimicrobial peptides (PrAMPs) inhibit bacterial protein biosynthesis by binding to the polypeptide exit tunnel (PET) near the peptidyl transferase center. Api137, an optimized derivative of honeybee PrAMP apidaecin, inhibits protein expression by trapping release factors (RFs), which interact with stop codons on ribosomes to terminate translation. This study uses cryo-EM, functional assays and molecular dynamic (MD) simulations to show that Api137 additionally occupies a second binding site near the exit of the PET and can repress translation independently of RF-trapping. Api88, a C-terminally amidated (-CONH
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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.