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 …

Here we perform phage-assisted continuous evolution (PACE) of TEV protease, which
canonically cleaves ENLYFQS, to cleave a very different target sequence, HPLVGHM, that is …

Catalytically inactive enzymes (also known as pseudoproteases, protease homologues or
paralogues, non-peptidase homologues, non-enzymes and pseudoenzymes) have …

The predominant view in structure-based drug design is that small-molecule ligands, once
bound to their target structures, display a well-defined binding mode. However, structural …

Solvation and hydrophobicity play a key role in a variety of biological mechanisms. In
substrate binding, but also in structure-based drug design, the thermodynamic properties of …

Matrix metalloproteinases play an important role in extracellular matrix remodeling.
Excessive activity of these enzymes can be induced by UV light and leads to skin damage, a …

The importance of 3D protein structure in proteolytic processing is well known. However,
despite the plethora of existing methods for predicting proteolytic sites, only a few of them …

One peptidase can usually be distinguished from another biochemically by its action on
proteins, peptides and synthetic substrates. Since 1996, the MEROPS database …

We present protease specificity profiling based on quantitative proteomics in combination
with proteome-derived peptide libraries. Peptide libraries are generated by endoproteolytic …

MEROPS is a database of proteolytic enzymes as well as their inhibitors and substrates.
Proteolytic enzymes and protein inhibitors are organized into protein domain families. In …