ArticleJournal of medicinal chemistry2011
Initial efforts toward the optimization of arylomycins for antibiotic activity.
Article in Journal of medicinal chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed, 50 citations in OpenAlex.
- Making Blank Faces Expressive: Chemical Approaches to the Modification of Chemically Inert Peptides.Journal of peptide science : an official publication of the European Peptide Society · 2026Review
- Fighting Antimicrobial Resistance: Innovative Drugs in Antibacterial Research.Angewandte Chemie (International ed. in English) · 2025Review
- A Review of Antibacterial Candidates with New Modes of Action.ACS infectious diseases · 2024Review
- Lipid Tales: Optimizing Arylomycin Membrane Anchors.ACS medicinal chemistry letters · 2023Article
- Stretching Peptides to Generate Small Molecule β-Strand Mimics.ACS central science · 2023Article
- Carrier Protein-Free Enzymatic Biaryl Coupling in Arylomycin A2 Assembly and Structure of the Cytochrome P450 AryC.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Emerging peptide antibiotics with therapeutic potential.Medicine in drug discovery · 2021Review
- Article
- Inhibition of Protein Secretion inAntimicrobial agents and chemotherapy · 2019Article
- Article
- Optimization of a β-Lactam Scaffold for Antibacterial Activity via the Inhibition of Bacterial Type I Signal Peptidase.ACS medicinal chemistry letters · 2018Article
- Scalable Access to Arylomycins via C-H Functionalization Logic.Journal of the American Chemical Society · 2018Article
- Bacterial proteases, untapped antimicrobial drug targets.The Journal of antibiotics · 2017Review
- Polishing the tarnished silver bullet: the quest for new antibiotics.Essays in biochemistry · 2017Review
- The inhibition of type I bacterial signal peptidase: Biological consequences and therapeutic potential.Bioorganic & medicinal chemistry letters · 2015Review
- Article
- Origins of Yersinia pestis sensitivity to the arylomycin antibiotics and the inhibition of type I signal peptidase.Antimicrobial agents and chemotherapy · 2015Article
- A putative cro-like repressor contributes to arylomycin resistance in Staphylococcus aureus.Antimicrobial agents and chemotherapy · 2015Article
- Efforts toward broadening the spectrum of arylomycin antibiotic activity.Bioorganic & medicinal chemistry letters · 2013Article
- Mechanism of action of the arylomycin antibiotics and effects of signal peptidase I inhibition.Antimicrobial agents and chemotherapy · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
While most clinically used antibiotics were derived from natural products, the isolation of new broad-spectrum natural products has become increasingly rare and narrow-spectrum agents are typically deemed unsuitable for development because of intrinsic limitations of their scaffold or target. However, it is possible that the spectrum of a natural product antibiotic might be limited by specific resistance mechanisms in some bacteria, such as target mutations, and the spectra of such "latent" antibiotics might be reoptimized by derivatization, just as has been done with clinically deployed antibiotics. We recently showed that the spectrum of the arylomycin natural product antibiotics, which act via the novel mechanism of inhibiting type I signal peptidase, is broader than previously believed and that resistance in several key human pathogens is due to the presence of a specific Pro residue in the target peptidase that disrupts interactions with the lipopeptide tail of the antibiotic. To begin to test whether this natural resistance might be overcome by derivatization, we synthesized analogues with altered lipopeptide tails and identified several with an increased spectrum of activity against S. aureus. The data support the hypothesis that the arylomycins are latent antibiotics, suggest that their spectrum may be optimized by derivatization, and identify a promising scaffold upon which future optimization efforts might focus.
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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.