"Coenzyme A Ligases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.
|Coenzyme A Ligases
- Coenzyme A Ligases
- Ligases, Coenzyme A
- Coenzyme A Synthetases
- Synthetases, Coenzyme A
- Acid-Thiol Ligases
- Acid Thiol Ligases
- Ligases, Acid-Thiol
- Co A Ligases
- Ligases, Co A
- Acyl Coenzyme A Synthetases
- Acyl CoA Synthetases
- CoA Synthetases, Acyl
- Synthetases, Acyl CoA
Below are MeSH descriptors whose meaning is more general than "Coenzyme A Ligases".
Below are MeSH descriptors whose meaning is more specific than "Coenzyme A Ligases".
This graph shows the total number of publications written about "Coenzyme A Ligases" by people in this website by year, and whether "Coenzyme A Ligases" was a major or minor topic of these publications.
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Below are the most recent publications written about "Coenzyme A Ligases" by people in Profiles.
Creatine-mediated crosstalk between adipocytes and cancer cells regulates obesity-driven breast cancer. Cell Metab. 2021 03 02; 33(3):499-512.e6.
Development of small-molecule inhibitors of fatty acyl-AMP and fatty acyl-CoA ligases in Mycobacterium tuberculosis. Eur J Med Chem. 2020 Sep 01; 201:112408.
ACSF3 and Mal(onate)-Adapted Mitochondria. Cell Chem Biol. 2017 Jun 22; 24(6):649-650.
ACSL6 is associated with the number of cigarettes smoked and its expression is altered by chronic nicotine exposure. PLoS One. 2011; 6(12):e28790.
Root system architecture in Arabidopsis grown in culture is regulated by sucrose uptake in the aerial tissues. Plant Cell. 2008 Oct; 20(10):2643-60.
Aryl acid adenylating enzymes involved in siderophore biosynthesis: fluorescence polarization assay, ligand specificity, and discovery of non-nucleoside inhibitors via high-throughput screening. Biochemistry. 2008 Nov 11; 47(45):11735-49.
Developmental regulation of the catalytic subunit of the apolipoprotein B mRNA editing enzyme (APOBEC-1) in human small intestine. J Lipid Res. 1995 Aug; 36(8):1664-75.