Remodelling of the tumour microenvironment by the kallikrein-related peptidases
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Earth and Planetary Sciences,General Environmental Science
Link
https://www.nature.com/articles/s41568-021-00436-z.pdf
Reference231 articles.
1. Kalinska, M., Meyer-Hoffert, U., Kantyka, T. & Potempa, J. Kallikreins — the melting pot of activity and function. Biochimie 122, 270–282 (2016).
2. Skala, W. et al. Structure–function analyses of human kallikrein-related peptidase 2 establish the 99-loop as master regulator of activity. J. Biol. Chem. 289, 34267–34283 (2014).
3. Guo, S. et al. A single glycan at the 99-loop of human kallikrein-related peptidase 2 regulates activation and enzymatic activity. J. Biol. Chem. 291, 593–604 (2016). This reference highlights the structural loops and the significance of glycosylation for KLK enzymatic function.
4. Koumandou, V. L. & Scorilas, A. Evolution of the plasma and tissue kallikreins, and their alternative splicing isoforms. PLoS ONE 8, e68074 (2013).
5. Filippou, P. S. et al. Expression profile of human tissue kallikrein 15 provides preliminary insights into its roles in the prostate and testis. Clin. Biochem. 59, 78–85 (2018).
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