Role of the Acidic Hirudin-like COOH-Terminal Amino Acid Region of Factor Va Heavy Chain in the Enhanced Function of Prothrombinase
Author:
Affiliation:
1. Department of Chemistry, Cleveland State University, Cleveland, Ohio 44115, and Department of Molecular Cardiology, The Lerner Research Institute, The Cleveland Clinic, Cleveland, Ohio 44195
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi800593k
Reference50 articles.
1. The Regulation of Clotting Factors
2. Role of Proexosite I in Factor Va-dependent Substrate Interactions of Prothrombin Activation
3. Proexosite-1 on Prothrombin Is a Factor Va-dependent Recognition Site for the Prothrombinase Complex
4. The Activation of Prothrombin
5. A Plausible Mechanism for Prothrombin Activation by Factor Xa, Factor Va, Phospholipid, and Calcium Ions
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1. Blood coagulation factor Va's key interactive residues and regions for prothrombinase assembly and prothrombin binding;Journal of Thrombosis and Haemostasis;2019-06-17
2. Identification and characterization of a factor Va-binding site on human prothrombin fragment 2;Scientific Reports;2019-02-21
3. Spellbinding Effects of the Acidic COOH-Terminus of Factor Va Heavy Chain on Prothrombinase Activity and Function;ACS Omega;2017-09-06
4. The Dual Regulatory Role of Amino Acids Leu480 and Gln481 of Prothrombin;Journal of Biological Chemistry;2016-01
5. Amino Acid Region 1000–1008 of Factor V Is a Dynamic Regulator for the Emergence of Procoagulant Activity;Journal of Biological Chemistry;2013-12
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