Structure and function of factor XI
Open Access
- 1 April 2010
- journal article
- review article
- Published by American Society of Hematology in Blood
- Vol. 115 (13), 2569-2577
- https://doi.org/10.1182/blood-2009-09-199182
Abstract
Factor XI (FXI) is the zymogen of an enzyme (FXIa) that contributes to hemostasis by activating factor IX. Although bleeding associated with FXI defiKeywords
This publication has 115 references indexed in Scilit:
- Identification of Coagulation Factor XI as a Ligand for Platelet Apolipoprotein E Receptor 2 (ApoER2)Arteriosclerosis, Thrombosis, and Vascular Biology, 2009
- Structural and functional features of factor XIJournal of Thrombosis and Haemostasis, 2009
- Characterization of a Heparin-Binding Site on the Catalytic Domain of Factor XIa: Mechanism of Heparin Acceleration of Factor XIa Inhibition by the Serpins Antithrombin and C1-InhibitorBiochemistry, 2009
- Evolution of the contact phase of vertebrate blood coagulationJournal of Thrombosis and Haemostasis, 2008
- Survival Advantage of Coagulation Factor XI–Deficient Mice during Peritoneal SepsisThe Journal of Infectious Diseases, 2008
- Factor XI Homodimer Structure Is Essential for Normal Proteolytic Activation by Factor XIIa, Thrombin, and Factor XIaPublished by Elsevier BV ,2008
- Characterization of Novel Forms of Coagulation Factor XIaPublished by Elsevier BV ,2008
- A Catalytic Domain Exosite (Cys527−Cys542) in Factor XIa Mediates Binding to a Site on Activated PlateletsBiochemistry, 2007
- Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activationProceedings of the National Academy of Sciences of the United States of America, 2007
- Dimer Dissociation and Unfolding Mechanism of Coagulation Factor XI Apple 4 Domain: Spectroscopic and Mutational AnalysisJournal of Molecular Biology, 2007