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Serine proteases
Open accessAbstract
Over one third of all known proteolytic enzymes are serine proteases. Among these, the trypsins underwent the most predominant genetic expansion yielding the enzymes responsible for digestion, blood coagulation, fibrinolysis, development, fertilization, apoptosis, and immunity. The success of this expansion resides in a highly efficient fold that couples catalysis and regulatory interactions. Added complexity comes from the recent observation of a significant conformational plasticity of the trypsin fold. A new paradigm emerges where two forms of the protease, E* and E, are in allosteric equilibrium and determine biological activity and specificity. © 2009 IUBMB IUBMB Life 61(5): 510–515, 2009
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Cited by
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Mahadevi, A. S., & Sastry, G. N. (2016) · Chemical Reviews · doi:10.1021/cr500344e · Cited by 933
Lawrence, M. G., Lai, J., & Clements, J. A. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0034 · Cited by 265
Cathepsins: Proteases that are vital for survival but can also be fatal
Patel, S., Homaei, A., El-Seedi, H. R., & Akhtar, N. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.05.148 · Cited by 224
The emerging roles of bacterial proteases in intestinal diseases
Caminero, A., Guzman, M., Libertucci, J., & Lomax, A. E. (2023) · Gut Microbes · doi:10.1080/19490976.2023.2181922 · Cited by 92
Synergistic strategies of predominant toxins in snake venoms
Xiong, S., & Huang, C. (2018) · Toxicology Letters · doi:10.1016/j.toxlet.2018.02.004 · Cited by 78
Metadata
- Authors
- Di Cera, E.
- Venue
- IUBMB Life
- Publisher
- Wiley
- Published
- 2009-01-29
- Volume
- 61
- Issue
- 5
- Pages
- 510-515
- ISSN
- 1521-6543 (ISSN-L)
- 1521-6551
- OpenAlex
- W3187441563
- Cited by
- 378
- References
- 0
- FWCI
- 4.18
- Type
- journal article
- Language
- en
- Open access
- green
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