HIV-1 infection activates the human CARD8 inflammasome via innate immune recognition of HIV-1 viral protease activity.

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.

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.

The modularity and unequivocal input/response of Notch signaling are harnessed to measure cell-surface shedding of diverse transmembrane receptors to identify new proteolytic switches and detect modulation of proteolysis by therapeutics.

Divergence in immunoproteasome substrate specificity and regulation from the constitutive proteasome impacts peptide cleavage quantity and the cellular capacity of the ubiquitin-proteasome system.

A novel mechanism of intramembrane protease regulation involves a protein blocking the active site of the enzyme.

Post-translational processing of the SKN-1A/Nrf1 transcription factor regulates proteasome expression.

The LOVdeg tag is a versatile tool for bacterial optogenetics, offering modular, blue light-inducible protein degradation for a range of synthetic biology and metabolic engineering applications.

Peptidase activity of DDI2 is required to activate Nrf1 in order to enable proteasome recovery in response to proteasome inhibition.