The Regulation of Factor IXa by Supersulfated Low Molecular Weight Heparin
Author:
Affiliation:
1. Department of Medicine/Hematology-Oncology, University of Wisconsin—Madison, Madison, Wisconsin 53706, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi100906q
Reference40 articles.
1. Inhibition by heparin of the human blood coagulation intrinsic pathway factor X activator.
2. Heparin Inhibits the Intrinsic Tenase Complex by Interacting with an Exosite on Factor IXa
3. The Factor IXa Heparin-Binding Exosite Is a Cofactor Interactive Site: Mechanism for Antithrombin-Independent Inhibition of Intrinsic Tenase by Heparin
4. Depolymerized holothurian glycosaminoglycan and heparin inhibit the intrinsic tenase complex by a common antithrombin-independent mechanism
5. Hypersulfated Low Molecular Weight Heparin with Reduced Affinity for Antithrombin Acts as an Anticoagulant by Inhibiting Intrinsic Tenase and Prothrombinase
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1. A novel factor IXa–specific enzyme-linked immunosorbent assay detects factor IXa in human plasma;Research and Practice in Thrombosis and Haemostasis;2024-01
2. A candidate activation pathway for coagulation factor VII;Biochemical Journal;2019-10-11
3. Sodium‐site in serine protease domain of human coagulation factor IX a: evidence from the crystal structure and molecular dynamics simulations study;Journal of Thrombosis and Haemostasis;2019-03-06
4. Selective disruption of heparin and antithrombin-mediated regulation of human factor IX;Journal of Thrombosis and Haemostasis;2015-05-10
5. Low molecular weight heparin inhibits plasma thrombin generation via direct targeting of factor IXa: contribution of the serpin-independent mechanism;Journal of Thrombosis and Haemostasis;2012-10
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