Journal: Future Drug Discovery

Article Title: Overcoming nonstructural protein 15-nidoviral uridylate-specific endoribonuclease (nsp15/NendoU) activity of SARS-CoV-2

doi: 10.4155/fdd-2020-0012

Figure Lengend Snippet: PDB ID: 6VWW Global Symmetry top view: arrows indicate the proposed RNA substrate mimetics as ligands and competitive inhibitors of the nsp15 monomers. Crystal structure adapted from Kim et al. .

Article Snippet: Here, we describe a novel hypothetical approach: combining available broad-spectrum antiviral agents such as nucleoside analogs with potential inhibitors of NendoU, for example nsp15 RNA substrate mimetics.

Techniques:

Journal: Communications Chemistry

Article Title: A microscale thermophoresis-based enzymatic RNA methyltransferase assay enables the discovery of DNMT2 inhibitors

doi: 10.1038/s42004-025-01439-9

Figure Lengend Snippet: A , B MST traces of the METTL3/14 enzyme reaction incubated with variable concentrations of SAM yielded significant thermophoresis shifts and enabled the determination of the Michaelis-Menten constant K M . C Inhibitor characterization of STM2457: MST-derived dose-response curves. D , E MST traces and substrate conversion plots (F norm vs time) revealing initial S. aureus TrmD kinetics. F Inhibitor characterization of 5-phenylthieno[2,3- d ]pyrimidin-4(1 H )-one: MST-derived dose-response curves. All inhibitor characterizations were performed in triplicates (mean ± SD, n = 3).

Article Snippet: RNA substrates for TrmD (synthetic tRNA Leu : 5′-GCGAAGGUGGCGGAAUUGGUAGACGCGCUAGCUUCAGG UGUUAGUGUCCUUACGGACGUGGGGGUUCAAGUCCCCCCCCUCGCACCA-3′) and METTL3/14 (5′-AACUUAAUGUUGCAUUGGACUUGAGUUA-3′) were obtained commercially (GenScript).

Techniques: Incubation, Derivative Assay

Journal: Future Drug Discovery

Article Title: Overcoming nonstructural protein 15-nidoviral uridylate-specific endoribonuclease (nsp15/NendoU) activity of SARS-CoV-2

doi: 10.4155/fdd-2020-0012

Figure Lengend Snippet: PDB ID: 6VWW Global Symmetry top view: arrows indicate the proposed RNA substrate mimetics as ligands and competitive inhibitors of the nsp15 monomers. Crystal structure adapted from Kim et al. .

Article Snippet: This raises the possibility of a novel approach where RNA substrate mimetics of nsp15 can be deployed as endonuclease inhibitors.

Techniques: