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Coronaviral RNA-methyltransferases: function, structure and inhibition
Nucleic Acids Research 50 (2): 635–650 (2022)
Coronaviral methyltransferases (MTases), nsp10/16 and nsp14, catalyze the last two steps of viral RNA-cap creation that takes place in cytoplasm. This cap is essential for the stability of viral RNA and, most importantly, for the evasion of innate immune system. Non-capped RNA is recognized by innate immunity which leads to its degradation and the activation of antiviral immunity. As a result, both coronaviral MTases are in the center of scientific scrutiny. Recently, X-ray and cryo-EM structures of both enzymes were solved even in complex with other parts of the viral replication complex. High-throughput screening as well as structure-guided inhibitor design have led to the discovery of their potent inhibitors. Here, we critically summarize the tremendous advancement of the coronaviral MTase field since the beginning of COVID pandemic.
Nonaqueous capillary electrophoresis and quantum chemical calculations applied to investigation of acid–base and electromigration properties of azahelicenes
Electrophoresis 2022: Early View
TRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A1
Heliyon 7 (12): e08490 (2021)
The Ad-MD method to calculate NMR shift including effects due to conformational dynamics: The 31P NMR shift in DNA
Journal of Computational Chemistry 43 (2): 132-143 (2022)