Identification of Nucleophilic Probes for Protease-Mediated Transpeptidation

A Small Periplasmic Protein with a Hydrophobic C-Terminal Residue Enhances DegP Proteolysis as a Suicide Activator

Tripodal Lipoprotein Variants with C-Terminal Hydrophobic Residues Allosterically Modulate Activity of the DegP Protease

Enzymatic Cross-Linking of Side Chains Generates a Modified Peptide with Four Hairpin-like Bicyclic Repeats

A Conserved Activation Cluster Is Required for Allosteric Communication in HtrA-Family Proteases

Distinct regulatory mechanisms balance DegP proteolysis to maintain cellular fitness during heat stress

Cage assembly of DegP protease is not required for substrate-dependent regulation of proteolytic activity or high-temperature cell survival

Covalent Linkage of Distinct Substrate Degrons Controls Assembly and Disassembly of DegP Proteolytic Cages

Reconstitution of Outer Membrane Protein Assembly from Purified Components