By targeting invasive organisms, antibiotics insert themselves into the ancient struggle of the
host-pathogen evolutionary arms race. As pathogens evolve tactics for evading antibiotics …

Extracellular matrix (ECM) proteins confer biomechanical properties, maintain cell
phenotype and mediate tissue repair (via release of sequestered cytokines and proteases) …

Molecular de-extinction could offer avenues for drug discovery by reintroducing bioactive
molecules that are no longer encoded by extant organisms. To prospect for antimicrobial …

Regulation of proteolysis plays a critical role in a myriad of important cellular processes. The
key to better understanding the mechanisms that control this process is to identify the …

The ability to catalytically cleave protein substrates after synthesis is fundamental for all
forms of life. Accordingly, site-specific proteolysis is one of the most important post …

Motivation Proteases are enzymes that cleave target substrate proteins by catalyzing the
hydrolysis of peptide bonds between specific amino acids. While the functional proteolysis …

Proteases are enzymes that specifically cleave the peptide backbone of their target proteins.
As an important type of irreversible post-translational modification, protein cleavage …

Proteases are enzymes that cleave and hydrolyse the peptide bonds between two specific
amino acid residues of target substrate proteins. Protease-controlled proteolysis plays a key …

The roles of proteolytic cleavage have been intensively investigated and discussed during
the past two decades. This irreversible chemical process has been frequently reported to …

Site-specific proteolysis by the enzymatic cleavage of small linear sequence motifs is a key
posttranslational modification involved in physiology and disease. The ability to robustly and …