The balanced utilization of energy sources, namely carbohydrates and fats, by mitochondria, is critically important for the long-term maintenance of both skeletal muscle and heart health.

Inhibiting PRMT1 enzymatic activity promotes megakaryocyte terminal differentiation via RBM15-mediated RNA metabolism, which is dysregulated in hematological malignancies.

The SARS-CoV-2 main protease specifically cleaves a conserved sequence in the human tRNA modifying enzyme TRMT1, resulting in reduced tRNA binding and the complete loss of TRMT1-mediated tRNA methyltransferase activity.

The stem cells of the postnatal muscle allow postnatal muscle growth and repair and withdraw from the cell cycle when the tyrosine phosphatase Ptpn11 (Shp2) is inhibited or mutated in mice.

SARS-CoV-2 infection reduces the intracellular levels of a human tRNA modification enzyme and alters host tRNA modification profiles.

Mg²⁺-dependent JAK1-mediated phosphorylation sensitizes TRPV2 activity and thermo-threshold, which is counterbalanced by PTPN1-mediated dephosphorylation, highlighting a role of phosphorylation homeostasis in setting the basal activity of TRPV2.

Genome-wide transcriptional profiling and genetic analyses reveal conserved mechanisms underlying the generation of neocortical basal radial glia and cerebellar Bergmann glia.

The PRMT1 protein mediates arginine methylation of KCNQ2 channels to control neuronal excitability.

The MIR domain of protein-O-mannosyltransferases participates in glycosylation by binding mannosylated peptides and regulates enzyme processivity.

Biochemical, transcriptomic, and proteomic analyses reveal that protein arginine methyltransferases post-transcriptionally regulate intron detention—introns that persist in nuclear polyadenylated RNA—through methylation of RNA splicing and processing factors.