Kringle-2 domain of the tissue-type plasminogen activator. 1H-NMR assignments and secondary structure
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1991.tb15894.x/fullpdf
Reference34 articles.
1. Proton NMR structural characterization of a recombinant kringle 2 domain from human tissue-type plasminogen activator
2. Differences in the binding to fibrin of native plasminogen and plasminogen modified by proteolytic degradation influence of ω-aminocarboxylic acids
3. Adsorption to fibrin of native fragments of known primary structure from human plasminogen
4. On the interaction of the finger and the kringle-2 domain of tissue-type plasminogen activator with fibrin. Inhibition of kringle-2 binding to fibrin by epsilon-amino caproic acid.
5. Autonomous functions of structural domains on human tissue-type plasminogen activator.
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1. Miguel Llinás and the Structure of the Kringle Fold;The Protein Journal;2021-03-31
2. Inhibition of Pathological Retinal Neovascularization by a Small Peptide Derived from Human Tissue-Type Plasminogen Kringle 2;Frontiers in Pharmacology;2020-01-28
3. Selective Stabilization and Destabilization of Protein Domains in Tissue-Type Plasminogen Activator Using Formulation Excipients;Molecular Pharmaceutics;2018-12-19
4. What the structure of angiostatin may tell us about its mechanism of action;Journal of Thrombosis and Haemostasis;2004-01
5. The Col-1 Module of Human Matrix Metalloproteinase-2 (MMP-2): Structural/Functional Relatedness between Gelatin-Binding Fibronectin Type II Modules and Lysine-Binding Kringle Domains;Biological Chemistry;2002-01-23
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