Proteinase Specificity and Functional Diversity in Point Mutants of Plasminogen Activator Inhibitor 1
Open Access
- 1 May 1997
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (19) , 12662-12666
- https://doi.org/10.1074/jbc.272.19.12662
Abstract
No abstract availableKeywords
This publication has 47 references indexed in Scilit:
- Pathophysiology of fibrinolysisJournal of Internal Medicine, 1994
- Interconversions between active, inert and substrate forms of denatured/refolded type-1 plasminogen activator inhibitorBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1993
- A substrate-like form of plasminogen-activator-inhibitor type 1. Conversions between different forms by sodium dodecyl sulphateEuropean Journal of Biochemistry, 1992
- The latent tendencies of PAI-1Trends in Biochemical Sciences, 1992
- Purification of active human plasminogen activator inhibitor 1 from Escherichia coliEuropean Journal of Biochemistry, 1989
- Implications of the three-dimensional structure of .alpha.1-antitrypsin for structure and function of serpinsBiochemistry, 1989
- Purification and characterization of natural and recombinant human plasminogen activator inhibitor‐1 (PAI‐1)European Journal of Biochemistry, 1988
- Plasminogen activator inhibitor type‐1 : reactive center and amino‐terminal heterogeneity determined by protein and cDNA sequencingFEBS Letters, 1986
- cDNA cloning of human plasminogen activator-inhibitor from endothelial cells.Journal of Clinical Investigation, 1986
- Cloning and sequence of a cDNA coding for the human beta-migrating endothelial-cell-type plasminogen activator inhibitor.Proceedings of the National Academy of Sciences, 1986