The Preferred Pathway of Glycosaminoglycan-accelerated Inactivation of Thrombin by Heparin Cofactor II
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference72 articles.
1. A player of many parts: The spotlight falls on thrombin's structure
2. The refined 1.9-Å X-ray crystal structure of d-Phe-Pro-Arg chloromethylketone-inhibited humanα-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships
3. Inactivation of Thrombin by Antithrombin Is Accompanied by Inactivation of Regulatory Exosite I
4. Transient kinetics of heparin-catalyzed protease inactivation by antithrombin III. Linkage of protease-inhibitor-heparin interactions in the reaction with thrombin.
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1. The Glycosaminoglycan Side Chains and Modular Core Proteins of Heparan Sulphate Proteoglycans and the Varied Ways They Provide Tissue Protection by Regulating Physiological Processes and Cellular Behaviour;International Journal of Molecular Sciences;2023-09-14
2. Mannose 2, 3, 4, 5, 6-O-pentasulfate (MPS): a partial activator of human heparin cofactor II with anticoagulation potential;Journal of Biomolecular Structure and Dynamics;2022-03-28
3. SARS-CoV-2 spike protein causes blood coagulation and thrombosis by competitive binding to heparan sulfate;International Journal of Biological Macromolecules;2021-12
4. Therapeutic SERPINs: Improving on Nature;Frontiers in Cardiovascular Medicine;2021-03-31
5. Identification and characterization of a novel isoform of heparin cofactorIIin human liver;IUBMB Life;2020-08-22
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