Soluble Phospholipids Enhance Factor Xa-Catalyzed Prothrombin Activation in Solution†
about
Modulation of prothrombinase assembly and activity by phosphatidylethanolamineTrio engagement via plasma membrane phospholipids and the myristoyl moiety governs HIV-1 matrix binding to bilayersAcylcarnitines are anticoagulants that inhibit factor Xa and are reduced in venous thrombosis, based on metabolomics data.Functional and structural characterization of factor Xa dimer in solution.Ca2+ switches the effect of PS-containing membranes on Factor Xa from activating to inhibiting: implications for initiation of blood coagulationPhosphatidylserine and FVa regulate FXa structure.Soluble phosphatidylserine binds to two sites on human factor IXa in a Ca2+ dependent fashion to specifically regulate structure and activityLyso-Sulfatide Binds Factor Xa and Inhibits Thrombin Generation by the Prothrombinase Complex.Conservative mutations in the C2 domains of factor VIII and factor V alter phospholipid binding and cofactor activity.Phosphatidylserine-induced factor Xa dimerization and binding to factor Va are competing processes in solution.A phosphatidylserine binding site in factor Va C1 domain regulates both assembly and activity of the prothrombinase complex.Phosphatidylserine Stimulates Ceramide 1-Phosphate (C1P) Intermembrane Transfer by C1P Transfer Proteins.Effects of water soluble phosphotidylserine on bovine factor Xa: functional and structural changes plus dimerization.Association free energy of dipalmitoylphosphatidylserines in a mixed dipalmitoylphosphatidylcholine membrane.Localization of phosphatidylserine binding sites to structural domains of factor Xa.Soluble phosphatidylserine triggers assembly in solution of a prothrombin-activating complex in the absence of a membrane surface.Glucosylceramide, a neutral glycosphingolipid anticoagulant cofactor, enhances the interaction of human- and bovine-activated protein C with negatively charged phospholipid vesicles.Sphingolipids as bioactive regulators of thrombin generation.Prothrombin amino terminal region helps protect coagulation factor Va from proteolytic inactivation by activated protein C.Characterization of a factor Xa binding site on factor Va near the Arg-506 activated protein C cleavage site.Minor Plasma Lipids Modulate Clotting Factor Activities and May Affect Thrombosis Risk.Commentary: Lipids and Liposomes can do More Than Carry Drugs: Phosphatidylserine as a Regulator of Blood Coagulation
P2860
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P2860
Soluble Phospholipids Enhance Factor Xa-Catalyzed Prothrombin Activation in Solution†
description
im Juni 1996 veröffentlicher wissenschaftlicher Artikel
@de
scientific article published on 01 June 1996
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в січні 1996
@uk
name
Soluble Phospholipids Enhance Factor Xa-Catalyzed Prothrombin Activation in Solution†
@en
Soluble Phospholipids Enhance Factor Xa-Catalyzed Prothrombin Activation in Solution†
@nl
type
label
Soluble Phospholipids Enhance Factor Xa-Catalyzed Prothrombin Activation in Solution†
@en
Soluble Phospholipids Enhance Factor Xa-Catalyzed Prothrombin Activation in Solution†
@nl
prefLabel
Soluble Phospholipids Enhance Factor Xa-Catalyzed Prothrombin Activation in Solution†
@en
Soluble Phospholipids Enhance Factor Xa-Catalyzed Prothrombin Activation in Solution†
@nl
P2093
P356
P1433
P1476
Soluble phospholipids enhance factor Xa-catalyzed prothrombin activation in solution
@en
P2093
P304
P356
10.1021/BI952063D
P407
P577
1996-06-01T00:00:00Z