The role of phospholipids and factor Va in the prothrombinase complex
about
Platelet lipidomics: modern day perspective on lipid discovery and characterization in plateletsCrystal Structure of Prothrombin Reveals Conformational Flexibility and Mechanism of ActivationThe linker connecting the two kringles plays a key role in prothrombin activationCdc50p, a protein required for polarized growth, associates with the Drs2p P-type ATPase implicated in phospholipid translocation in Saccharomyces cerevisiae.Drs2p-related P-type ATPases Dnf1p and Dnf2p are required for phospholipid translocation across the yeast plasma membrane and serve a role in endocytosis.Insights into the complex association of bovine factor Va with acidic-lipid-containing synthetic membranes.Active site-labeled prothrombin inhibits prothrombinase in vitro and thrombosis in vivo.Surface-mediated control of blood coagulation: the role of binding site densities and platelet depositionCellular procoagulant activity dictates clot structure and stability as a function of distance from the cell surface.Ca2+ switches the effect of PS-containing membranes on Factor Xa from activating to inhibiting: implications for initiation of blood coagulationCrystallization and preliminary X-ray crystallographic analysis of blood coagulation factor V-activating proteinase (RVV-V) from Russell's viper venomSystems biology of coagulation initiation: kinetics of thrombin generation in resting and activated human blood.Comparative response of platelet fV and plasma fV to activated protein C and relevance to a model of acute traumatic coagulopathy.Peptides derived from MARCKS block coagulation complex assembly on phosphatidylserine.Differentiation-dependent expression of phosphatidylserine in mammalian plasma membranes: quantitative assessment of outer-leaflet lipid by prothrombinase complex formation.Activated factor V is a cofactor for the activation of factor XI by thrombin in plasma.Fourier transform infrared spectroscopic study of Ca2+ and membrane-induced secondary structural changes in bovine prothrombin and prothrombin fragment 1.Modeling of human factor Va inactivation by activated protein C.Phosphatidylserine and FVa regulate FXa structure.A high-yield co-expression system for the purification of an intact Drs2p-Cdc50p lipid flippase complex, critically dependent on and stabilized by phosphatidylinositol-4-phosphate.Dilutional control of prothrombin activation at physiologically relevant shear ratesA coagulation pathway on bovine aortic segments leading to generation of Factor Xa and thrombin.Prothrombin structure: unanticipated features and opportunities.Why Ser and not Thr brokers catalysis in the trypsin foldProtection of factor Xa from neutralization by the heparin-antithrombin complex.Isolation of functional human coagulation factor V by using a hybridoma antibodyNotecarin D binds human factor V and factor Va with high affinity in the absence of membranes.Membrane-dependent coagulation reaction is independent of the concentration of phospholipid-bound substrate: fluid phase factor X regulates the extrinsic system2013 scientific sessions Sol Sherry distinguished lecture in thrombosis: polyphosphate: a novel modulator of hemostasis and thrombosis.Lyso-Sulfatide Binds Factor Xa and Inhibits Thrombin Generation by the Prothrombinase Complex.MASP-1 Induced Clotting--The First Model of Prothrombin Activation by MASP-1.Membrane binding events in the initiation and propagation phases of tissue factor-initiated zymogen activation under flow.Kinetic dissection of the pre-existing conformational equilibrium in the trypsin fold.Conservative mutations in the C2 domains of factor VIII and factor V alter phospholipid binding and cofactor activity.Plasma membrane translocation of fluorescent-labeled phosphatidylethanolamine is controlled by transcription regulators, PDR1 and PDR3Binding sites for blood coagulation factor Xa and protein S involving residues 493-506 in factor Va.Simulated Thrombin Generation in the Presence of Surface-Bound Heparin and Circulating Tissue FactorThe role of thrombin exosites I and II in the activation of human coagulation factor V.Factor Va alters the conformation of the Na+-binding loop of factor Xa in the prothrombinase complexHow the Linker Connecting the Two Kringles Influences Activation and Conformational Plasticity of Prothrombin
P2860
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P2860
The role of phospholipids and factor Va in the prothrombinase complex
description
1980 nî lūn-bûn
@nan
1980 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1980 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1980年の論文
@ja
1980年論文
@yue
1980年論文
@zh-hant
1980年論文
@zh-hk
1980年論文
@zh-mo
1980年論文
@zh-tw
1980年论文
@wuu
name
The role of phospholipids and factor Va in the prothrombinase complex
@ast
The role of phospholipids and factor Va in the prothrombinase complex
@en
The role of phospholipids and factor Va in the prothrombinase complex
@nl
type
label
The role of phospholipids and factor Va in the prothrombinase complex
@ast
The role of phospholipids and factor Va in the prothrombinase complex
@en
The role of phospholipids and factor Va in the prothrombinase complex
@nl
prefLabel
The role of phospholipids and factor Va in the prothrombinase complex
@ast
The role of phospholipids and factor Va in the prothrombinase complex
@en
The role of phospholipids and factor Va in the prothrombinase complex
@nl
P2093
P1476
The role of phospholipids and factor Va in the prothrombinase complex
@en
P2093
Govers-Riemslag JW
P304
P407
P577
1980-01-01T00:00:00Z