ArticleCell chemical biology2016
Systematic Survey of Serine Hydrolase Activity in Mycobacterium tuberculosis Defines Changes Associated with Persistence.
Article in Cell chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 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
42 citing papers in PubMed, 86 citations in OpenAlex.
- Proteomic characterization ofmSystems · 2025Article
- Advancing Gut Microbiome Research: The Shift from Metagenomics to Multi-Omics and Future Perspectives.Journal of microbiology and biotechnology · 2025Review
- Activity-Based Protein Profiling of Serine Hydrolases in Bacteria: Methods and Protocols.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Identifying Inhibitor Targets in Mycobacteria by Activity-Based Probe Profiling.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Shifting Mycobacterial Serine Hydrolase Activity Visualized Using Multi-Layer In-Gel Activity Assays.Molecules (Basel, Switzerland) · 2024Article
- Chemical Probes Review: Choosing the Right Path Towards Pharmacological Targets in Drug Discovery, Challenges and Future Perspectives.Combinatorial chemistry & high throughput screening · 2024Review
- Activity-based protein profiling of serine hydrolases and penicillin-binding proteins inFEMS microbes · 2024Article
- Roles of Lipolytic enzymes inFrontiers in microbiology · 2024Review
- Development of Oxadiazolone Activity-Based Probes Targeting FphE for Specific Detection ofbioRxiv : the preprint server for biology · 2023Article
- Chemoproteomic identification of a DPP4 homolog in Bacteroides thetaiotaomicron.Nature chemical biology · 2023Article
- Target Identification in Anti-Tuberculosis Drug Discovery.International journal of molecular sciences · 2023Review
- Chemical approaches to unraveling the biology of mycobacteria.Cell chemical biology · 2023Review
- Sequence and Structural Motifs Controlling the Broad Substrate Specificity of the Mycobacterial Hormone-Sensitive Lipase LipN.ACS omega · 2023Article
- Chemoproteomic Approaches for Unraveling Prokaryotic Biology.Israel journal of chemistry · 2023Article
- Activity-based annotation: the emergence of systems biochemistry.Trends in biochemical sciences · 2022Review
- Review
- Identification of covalent inhibitors that disrupt M. tuberculosis growth by targeting multiple serine hydrolases involved in lipid metabolism.Cell chemical biology · 2022Article
- Identification of cell wall synthesis inhibitors active against Mycobacterium tuberculosis by competitive activity-based protein profiling.Cell chemical biology · 2022Article
- Feasibility of novel approaches to detect viableFrontiers in medicine · 2022Review
- Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The transition from replication to non-replication underlies much of Mycobacterium tuberculosis (Mtb) pathogenesis, as non- or slowly replicating Mtb are responsible for persistence and poor treatment outcomes. Therapeutic targeting of non-replicating populations is a priority for tuberculosis treatment, but few drug targets in non-replicating Mtb are currently known. Here, we directly measured the activity of the highly diverse and druggable serine hydrolases (SHs) during active replication and non-replication using activity-based proteomics. We predict SH activity for 78 proteins, including 27 proteins with unknown function, and identify 37 SHs that remain active in the absence of replication, providing a set of candidate persistence targets. Non-replication was associated with major shifts in SH activity. These activity changes were largely independent of SH abundance, indicating extensive post-translational regulation of SHs. By probing a large cross-section of druggable Mtb enzyme space during replication and non-replication, we identify new SHs and suggest new persistence targets.
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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.