Cancer progression with uncontrolled tumor growth, local invasion, and metastasis depends
largely on the proteolytic activity of numerous matrix metalloproteinases (MMPs), which …

Matrix metalloproteinases (MMPs) are zinc‐dependent endopeptidases that were first
discovered as proteases, which target and cleave extracellular proteins. During the past 20 …

Heparanase is the only mammalian enzyme that cleaves heparan sulphate, an important
component of the extracellular matrix. This leads to the remodelling of the extracellular …

Inflammatory conditions in selected organs increase the risk of cancer. An inflammatory
component is present also in the microenvironment of tumors that are not epidemiologically …

Matrix metalloproteases (MMPs) comprise a family of enzymes that cleave protein substrates
based on a conserved mechanism involving activation of an active site-bound water …

Adaption of a single protein to perform multiple independent functions facilitates functional
plasticity of the proteome allowing a limited number of protein-coding genes to perform a …

Matrix metalloproteinases (MMPs), originally discovered to function in the breakdown of
extracellular matrix proteins, have gained the status of regulatory proteases in signaling …

Proteomics encompasses powerful techniques termed 'degradomics' for unbiased high-
throughput protease substrate discovery screens that have been applied to an important …

Matrix metalloproteinases (MMPs) are critical enzymes involved in a variety of cellular
processes. MMPs are well known for their ability to degrade the extracellular matrix (ECM) …

Proteolytic processing is an irreversible posttranslational modification affecting a large
portion of the proteome. Protease-cleaved mediators frequently exhibit altered activity, and …