The interaction of prothrombin with phospholipid membranes is independent of either kringle domain
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference44 articles.
1. A simple method for the preparation of homogeneous phospholipid vesicles
2. A metal ion-binding site in the kringle region of bovine prothrombin fragment 1.
3. Metal ion induced conformational transitions of prothrombin and prothrombin fragment 1
4. Metal and phospholipid binding properties of partially carboxylated human prothrombin variants.
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1. How the Linker Connecting the Two Kringles Influences Activation and Conformational Plasticity of Prothrombin;Journal of Biological Chemistry;2016-03
2. Crystal Structure of Prothrombin Reveals Conformational Flexibility and Mechanism of Activation;Journal of Biological Chemistry;2013-08
3. Association of pharmacokinetic (CYP2C9) and pharmacodynamic (factors II, VII, IX, and X; proteins S and C; and γ-glutamyl carboxylase) gene variants with warfarin sensitivity;Blood;2004-04-01
4. The ω-Loop Region of the Human Prothrombin γ-Carboxyglutamic Acid Domain Penetrates Anionic Phospholipid Membranes;Journal of Biological Chemistry;2001-06
5. The Gla Domain of Human Prothrombin Has a Binding Site for Factor Va;Journal of Biological Chemistry;2000-12
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