Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.2217/epi-2020-0203 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
AANAT kinetics of CoASH-targeted electrophiles of tryptamine and related analogs.
Bioorg Med Chem Lett
November 2024
Department of Chemistry, University of Nebraska at Kearney, Kearney, NE 69949, USA. Electronic address:
Arylalkylamine N-acetyltransferase (AANAT) catalyzes the rate-limiting step in melatonin synthesis and is a potential target for disorders involving melatonin overproduction, such as seasonal affective disorder. Previously described AANAT inhibitor bromoacetyltryptamine (BAT) and benzothiophenes analogs were reported to react with CoASH to form potent bisubstrate inhibitors through AANAT's alkyltransferase function, which is secondary to its role as an acetyltransferase. We replaced the bromoacetyl group in BAT with various Michael acceptors to mitigate possible off-target activity of its bromoacetyl group.
View Article and Find Full Text PDFBisubstrate inhibitors of 6-hydroxymethyl-7,8-dihydroptein pyrophosphokinase: Toward cell permeability.
Bioorg Med Chem Lett
November 2024
Center for Structural Biology, National Cancer Institute, Frederick, MD 21702, USA.
6-Hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) is a key enzyme in the folate biosynthesis pathway. It catalyzes the pyrophosphoryl transfer from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP). HPPK is essential for microorganisms but is absent in mammals.
View Article and Find Full Text PDFHigh Content Screening Assay of Inhibitors of the Legionella Pneumophila Histone Methyltransferase RomA in Infected Cells.
Chembiochem
December 2024
Epigenetic Chemical Biology, Department of Structural Biology and Chemistry, Institut Pasteur, Université Paris Cité, CNRS UMR n°3523 Chem4Life, F-75015, Paris, France.
Article Synopsis
- - Resistance to antimicrobial agents poses a significant global health threat, prompting the need for new treatment strategies targeting pathogens’ ability to manipulate host defenses, especially through epigenetic modification.
- - Legionella pneumophila, a Gram-negative intracellular bacterium, releases a specific methyltransferase named RomA that alters host epigenetic regulation by methylating H3 K14, helping the pathogen evade immune responses.
- - To inhibit RomA's activity, researchers developed a high-content imaging assay to screen chemical compounds targeting methyltransferases, successfully identifying potential inhibitors from an initial library of 477 compounds.
Structure, Function, and Activity of Small Molecule and Peptide Inhibitors of Protein Arginine Methyltransferase 1.
J Med Chem
September 2024
Pharmaceutical analysis Laboratory, College of Pharmacy, University of Manitoba, 750 McDermot Avenue West, Winnipeg, Manitoba R3E 0T5, Canada.
Protein arginine -methyltransferases (PRMT) are a family of -adenosyl-l-methionine (SAM)-dependent enzymes that transfer methyl-groups to the ω-N of arginyl residues in proteins. PRMTs are involved in regulating gene expression, RNA splicing, and other activities. PRMT1 is responsible for most cellular arginine methylation, and its dysregulation is involved in many cancers.
View Article and Find Full Text PDFDiscovery of Heparin Mimetic, Potent, and Selective Inhibitors of Human Clotting Factor XIIIa.
ACS Omega
July 2024
Division of Basic Pharmaceutical Sciences, College of Pharmacy, Xavier University of Louisiana, New Orleans, Louisiana 70125, United States.
Factor XIIIa (FXIIIa) is a cysteine transglutaminase that catalyzes the last step in the coagulation process. An anion-binding site inhibition of FXIIIa is a paradigm-shifting strategy that may offer key advantages of controlled inhibition. Such an approach is likely to lead to novel FXIIIa inhibitors that do not carry bleeding risks.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!