The DOI matches its Crossref record; 104 of the 104 references it cites were found in a registry or an index.
Unconventional serine proteases: Variations on the catalytic Ser/His/Asp triad configuration
Open accessAbstract
Serine proteases comprise nearly one‐third of all known proteases identified to date and play crucial roles in a wide variety of cellular as well as extracellular functions, including the process of blood clotting, protein digestion, cell signaling, inflammation, and protein processing. Their hallmark is that they contain the so‐called “classical” catalytic Ser/His/Asp triad. Although the classical serine proteases are the most widespread in nature, there exist a variety of “nonclassical” serine proteases where variations to the catalytic triad are observed. Such variations include the triads Ser/His/Glu, Ser/His/His, and Ser/Glu/Asp, and include the dyads Ser/Lys and Ser/His. Other variations are seen with certain serine and threonine peptidases of the Ntn hydrolase superfamily that carry out catalysis with a single active site residue. This work discusses the structure and function of these novel serine proteases and threonine proteases and how their catalytic machinery differs from the prototypic serine protease class.
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Cites
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Wieczorek, R., Adamala, K., Gasperi, T., Polticelli, F., & Stano, P. (2017) · Life · doi:10.3390/life7020019 · Cited by 53
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Li, W., Huang, B., Guo, M., Zeng, Z., Cai, T., Feng, L., Zhang, X., Guo, L., Jiang, X., Yin, Y., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115773 · Cited by 13
Dey, D., Nishijima, M., Tanaka, R., Kurisu, G., Tanaka, H., & Ito, H. (2022) · Protein Science · doi:10.1002/pro.4430 · Cited by 7
Metadata
- Authors
- Ekici, Ö. D., Paetzel, M., & Dalbey, R. E.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2008-12
- Volume
- 17
- Issue
- 12
- Pages
- 2023-2037
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- OpenAlex
- W2101973479
- Cited by
- 334
- References
- 104
- FWCI
- 3.13
- Type
- journal article
- Language
- en
- Open access
- bronze
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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