ArticleChemical communications (Cambridge, England)2015
Active site-directed proteomic probes for adenylation domains in nonribosomal peptide synthetases.
Article in Chemical communications (Cambridge, England), 2015. 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.
- Native mass spectrometry reveals DltA catalysis, DltC loading, and inhibition in the d-alanylation pathway.RSC advances · 2026Article
- Inhibition of Surfactin Biosynthesis in Bacillus Subtilis Using Cell-Permeable Adenylation Domain Inhibitors.Chembiochem : a European journal of chemical biology · 2025Article
- Functional Diversity and Engineering of the Adenylation Domains in Nonribosomal Peptide Synthetases.Marine drugs · 2024Review
- Development of a chemical scaffold for inhibiting nonribosomal peptide synthetases in live bacterial cells.Beilstein journal of organic chemistry · 2024Article
- Chemoproteomic Approaches for Unraveling Prokaryotic Biology.Israel journal of chemistry · 2023Article
- Exploring a chemical scaffold for rapid and selective photoaffinity labelling of non-ribosomal peptide synthetases in living bacterial cells.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023Article
- Activity-based protein profiling of a surfactin-producing nonribosomal peptide synthetase inSTAR protocols · 2022Article
- Developing crosslinkers specific for epimerization domain in NRPS initiation modules to evaluate mechanism.RSC chemical biology · 2022Article
- Refining and expanding nonribosomal peptide synthetase function and mechanism.Journal of industrial microbiology & biotechnology · 2019Review
- Trapping interactions between catalytic domains and carrier proteins of modular biosynthetic enzymes with chemical probes.Natural product reports · 2018Review
- Mining for Microbial Gems: Integrating Proteomics in the Postgenomic Natural Product Discovery Pipeline.Proteomics · 2018Review
- Novel approaches in function-driven single-cell genomics.FEMS microbiology reviews · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
We describe a general strategy for selective chemical labeling of individual adenylation (A) domains in nonribosomal peptide synthetases (NRPSs) using active site-directed proteomic probes coupled to the 5'-O-N-(aminoacyl)sulfamoyladenosine (AMS) scaffold with a clickable benzophenone functionality. These proteomic tools can greatly facilitate the molecular identification, functional characterization, and profiling of virtually any kind of A domains of NRPS enzymes in complex biological systems.
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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.