Role of the Residues of the 39-Loop in Determining the Substrate and Inhibitor Specificity of Factor IXa
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference46 articles.
1. COFACTOR PROTEINS IN THE ASSEMBLY AND EXPRESSION OF BLOOD CLOTTING ENZYME COMPLEXES
2. The coagulation cascade: initiation, maintenance, and regulation
3. Structure, function, and molecular defects of factor IX
4. The molecular basis of blood coagulation
5. Factor VIII-Factor IX Interactions: Molecular Sites Involved in Enzyme-Cofactor Complex Assembly
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1. The Interaction of Factor Xa and IXa with Non-Activated Antithrombin in Michaelis Complex: Insights from Enhanced-Sampling Molecular Dynamics Simulations;Biomolecules;2023-05-06
2. Characterization of Protein Z-Dependent Protease Inhibitor/Antithrombin Chimeras Provides Insight into the Serpin Specificity of Coagulation Proteases;ACS Omega;2017-07-07
3. Pharmacology of Heparin and Related Drugs;Pharmacological Reviews;2015-12-15
4. Understanding the specificity of serpin–protease complexes through interface analysis;Journal of Biomolecular Structure and Dynamics;2014-09-09
5. Residues of the 39-Loop Restrict the Plasma Inhibitor Specificity of Factor IXa;Journal of Biological Chemistry;2013-05
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