ArticleAngewandte Chemie (International ed. in English)2019
Fluorescent Triazole Urea Activity-Based Probes for the Single-Cell Phenotypic Characterization of Staphylococcus aureus.
Article in Angewandte Chemie (International ed. in English), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 46 citations in OpenAlex.
- Fluorogenic Coupled Assays Reveal Catalytic Properties, Inhibition Constants and Cellular Location of Mucin-Active Carbohydrate Sulfatases.Angewandte Chemie (International ed. in English) · 2026Article
- Unique structural and ligand-binding properties of theProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Targeting the Reactive Proteome: Recent Advances in Activity-Based Protein Profiling and Probe Design.Biomolecules · 2025Review
- Unique structural and ligand binding properties of thebioRxiv : the preprint server for biology · 2025Article
- Identification of covalent inhibitors of Staphylococcus aureus serine hydrolases important for virulence and biofilm formation.Nature communications · 2025Article
- Similar but Distinct-Biochemical Characterization of the Staphylococcus aureus Serine Hydrolases FphH and FphI.Proteins · 2025Article
- Activity-Based Protein Profiling of Serine Hydrolases in Bacteria: Methods and Protocols.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Single-cell phenotypic profiling and backtracing exposes and predicts clinically relevant subpopulations in isogenic Staphylococcus aureus communities.Communications biology · 2024Article
- Activity-based protein profiling of serine hydrolases and penicillin-binding proteins inFEMS microbes · 2024Article
- Development of Oxadiazolone Activity-Based Probes Targeting FphE for Specific Detection ofbioRxiv : the preprint server for biology · 2023Article
- Biochemical and Cellular Characterization of the Function of Fluorophosphonate-Binding Hydrolase H (FphH) inACS infectious diseases · 2023Article
- Activity-based protein profiling in microbes and the gut microbiome.Current opinion in chemical biology · 2023Review
- Activity-based probes in pathogenic bacteria: Investigating drug targets and molecule specificity.Current opinion in chemical biology · 2023Review
- Chemoproteomic Approaches for Unraveling Prokaryotic Biology.Israel journal of chemistry · 2023Article
- Chemical Proteomics Reveals Antibiotic Targets of Oxadiazolones in MRSA.Journal of the American Chemical Society · 2023Article
- Identification of cell wall synthesis inhibitors active against Mycobacterium tuberculosis by competitive activity-based protein profiling.Cell chemical biology · 2022Article
- Reactive chemistry for covalent probe and therapeutic development.Trends in pharmacological sciences · 2022Review
- Editorial: Serine protease inhibitors and their therapeutic applications.Frontiers in chemistry · 2022Article
- Novel Inhibitors and Activity-Based Probes Targeting Trypsin-Like Serine Proteases.Frontiers in chemistry · 2022Article
- Newly discoveredADMET & DMPK · 2022Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
Phenotypically distinct cellular (sub)populations are clinically relevant for the virulence and antibiotic resistance of a bacterial pathogen, but functionally different cells are usually indistinguishable from each other. Herein, we introduce fluorescent activity-based probes as chemical tools for the single-cell phenotypic characterization of enzyme activity levels in Staphylococcus aureus. We screened a 1,2,3-triazole urea library to identify selective inhibitors of fluorophosphonate-binding serine hydrolases and lipases in S. aureus and synthesized target-selective activity-based probes. Molecular imaging and activity-based protein profiling studies with these probes revealed a dynamic network within this enzyme family involving compensatory regulation of specific family members and exposed single-cell phenotypic heterogeneity. We propose the labeling of enzymatic activities by chemical probes as a generalizable method for the phenotyping of bacterial cells at the population and single-cell level.
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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.