ArticleEuropean journal of medicinal chemistry2020
Development of small-molecule inhibitors of fatty acyl-AMP and fatty acyl-CoA ligases in Mycobacterium tuberculosis.
Article in European journal of medicinal chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
17 citing papers in PubMed, 28 citations in OpenAlex.
- Type 1 diabetes alters early macrophage-iScience · 2026Article
- Diversity of FAAL enzymes and prediction of their substrate specificity using FAALPred.Protein science : a publication of the Protein Society · 2026Article
- The AcasR-FadD9 regulatory axis modulates iron homeostasis and susceptibility to the anti-mycobacterial compound ACA.Frontiers in tuberculosis · 2026Article
- Essential redundancies fuel Mycobacterium tuberculosis adaptation to the host.PLoS pathogens · 2025Review
- The Mechanism of the Rappe Rearrangement─A Stereochemical Investigation Using Density Functional Theory.The Journal of organic chemistry · 2025Article
- Biosynthesis of isonitrile lipopeptides.Current opinion in chemical biology · 2024Review
- Article
- New Flexible Analogues of 8-Aza-7-deazapurine Nucleosides as Potential Antibacterial Agents.International journal of molecular sciences · 2023Article
- Structural basis for the development of potential inhibitors targeting FadD23 from Mycobacterium tuberculosis.Acta crystallographica. Section F, Structural biology communications · 2023Article
- Mycobacterium tuberculosis Requires the Outer Membrane Lipid Phthiocerol Dimycocerosate for Starvation-Induced Antibiotic Tolerance.mSystems · 2023Article
- The Key Roles ofFrontiers in microbiology · 2023Article
- A d-Phenylalanine-Benzoxazole Derivative Reveals the Role of the Essential Enzyme Rv3603c in the Pantothenate Biosynthetic Pathway ofACS infectious diseases · 2022Article
- The missing enzymatic link in syntrophic methane formation from fatty acids.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Metabolic Versatility ofMetabolites · 2021Review
- Lipid Droplets, the Central Hub Integrating Cell Metabolism and the Immune System.Frontiers in physiology · 2021Review
- Synthesis of an acyl-acyl carrier protein synthetase inhibitor to study fatty acid recycling.Scientific reports · 2020Article
- Cell Surface Biosynthesis and Remodeling Pathways in Mycobacteria Reveal New Drug Targets.Frontiers in cellular and infection microbiology · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Lipid metabolism in Mycobacterium tuberculosis (Mtb) relies on 34 fatty acid adenylating enzymes (FadDs) that can be grouped into two classes: fatty acyl-CoA ligases (FACLs) involved in lipid and cholesterol catabolism and long chain fatty acyl-AMP ligases (FAALs) involved in biosynthesis of the numerous essential and virulence-conferring lipids found in Mtb. The precise biochemical roles of many FACLs remain poorly characterized while the functionally non-redundant FAALs are much better understood. Here we describe the systematic investigation of 5'-O-[N-(alkanoyl)sulfamoyl]adenosine (alkanoyl adenosine monosulfamate, alkanoyl-AMS) analogs as potential multitarget FadD inhibitors for their antitubercular activity and biochemical selectivity towards representative FAAL and FACL enzymes. We identified several potent compounds including 12-azidododecanoyl-AMS 28, 11-phenoxyundecanoyl-AMS 32, and nonyloxyacetyl-AMS 36 with minimum inhibitory concentrations (MICs) against M. tuberculosis ranging from 0.098 to 3.13 μM. Compound 32 was notable for its impressive biochemical selectivity against FAAL28 (apparent K
Indexed as
Identifiers
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.