Proteases and Their Inhibitors
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".
Deadline for manuscript submissions: 31 October 2026 | Viewed by 3028
Special Issue Editor
Interests: serine proteases and extracellular proteolysis; inhibitors of serine proteases (SERPINs); protein translocation across membranes; genetics of bacteria and phages
Special Issue Information
Dear Colleagues,
The control of protein homeostasis is essential in all aspects of life. Proteases are present both inside cells and in the extracellular space. The main families of proteases are serine proteases, thiol proteases, acid proteases, and metalloproteases. Serine proteases include digestive enzymes (trypsin, chymotrypsin, etc.) whose enzymatic mechanism is well understood, as well as enzymes of the coagulation and fibrinolytic cascades. More recently, the proteasome of eukaryotes has been shown to play a key role in the cytoplasm. Viral proteases are important targets in therapeutic approaches.
Protease inhibitors are usually classified as low- or high-molecular-weight molecules. Small inhibitors include many natural and synthetic molecules. They are essential tools both in a clinical context and in biochemical experiments. The most well-studied large inhibitors belong to the family of SERPINs (serine protease inhibitors, although several of them also inhibit thiol proteases). However, ovalbumin, a founding member of the SERPINs, is not a known protease inhibitor. Finally, alpha-2-macroglobulins are very large proteins that inhibit many proteases, regardless of their mechanism of action or substrate specificity.
Prof. Dr. Dominique Belin
Guest Editor
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Keywords
- protease
- serine proteases
- thiol proteases
- acid proteases
- metalloproteases
- protease inhibitor
- SERPINs
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