Discovery and characterisation of an antibody that selectively modulates the inhibitory activity of plasminogen activator inhibitor-1
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-019-38842-x.pdf
Reference59 articles.
1. Pannekoek, H. et al. Endothelial plasminogen activator inhibitor (PAI): a new member of the Serpin gene family. The EMBO journal 5, 2539–2544 (1986).
2. Dupont, D. M. et al. Biochemical properties of plasminogen activator inhibitor-1. Frontiers in bioscience (Landmark edition) 14, 1337–1361 (2009).
3. Gils, A. & Declerck, P. J. The structural basis for the pathophysiological relevance of PAI-I in cardiovascular diseases and the development of potential PAI-I inhibitors. Thrombosis and haemostasis 91, 425–437, https://doi.org/10.1160/TH03-12-0764 (2004).
4. Kruithof, E. K., Tran-Thang, C. & Bachmann, F. The fast-acting inhibitor of tissue-type plasminogen activator in plasma is also the primary plasma inhibitor of urokinase. Thrombosis and haemostasis 55, 65–69 (1986).
5. Stefansson, S. & Lawrence, D. A. The serpin PAI-1 inhibits cell migration by blocking integrin alpha V beta 3 binding to vitronectin. Nature 383, 441–443, https://doi.org/10.1038/383441a0 (1996).
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