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.

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

Analyzing how mutations affect the main protease of SARS-CoV-2 may help researchers develop drugs that are effective against current and future variants of the virus.

Intramembrane proteases identify target proteins in a different way from other proteases.

The N-terminal domains enable Lon protease to discriminate and capture selected protein species for degradation by exposed hydrophobic patches and flexible linkages to the hexameric core complex.

Comprehensive mutational scanning of the SARS-CoV-2 protease, M^pro, provides functional and structural information to aid in the design of more effective inhibitors against the protease with reduced potential of evolving viral resistance.

Biochemical studies in combination with computational modeling and molecular dynamics simulations reveal that the lipid bilayer promotes intramembrane proteolysis by stabilizing the enzyme-substrate complex and the protease active site.

The conserved AMP-activated protein kinase inhibits mitochondrial import of misfolded proteins and helps preserve mitochondrial and cellular fitness under proteotoxic stress.

Proteases from diverse viruses, the first described pathogen-encoded activators of human NLRP1, cleave NLRP1 at a sequence that mimics the viral polyprotein, resulting in inflammasome activation and pro-inflammatory cytokine release.

Fixed, intact animals of C. elegans can be physically expanded with high isotropy, to enable super-resolved imaging of general proteins and nucleic acids throughout the organism, on conventional microscopes.