SV-IV Peptide1-16 reduces coagulant power in normal Factor V and Factor V Leiden.

A peptide derivative (1-70 fragment) of protein SV-IV accelerates human blood coagulation in vitro by selective inhibition of the heparin-induced antithrombin III activation process.

Effects of second and third generation oral contraceptives and their respective progestagens on the coagulation system in the absence or presence of the factor V Leiden mutation.

Coagulation assay with improved specificity to factor V mutants insensitive to activated protein C.

Evaluation of a highly specific functional test for the detection of factor V Leiden.

The clinical application of a new specific functional assay to detect the factor V(Leiden) mutation associated with activated protein C resistance.

Factor V and thrombotic disease: description of a janus-faced protein.

The procoagulant effects of factor V Leiden may be balanced against decreased levels of factor V and do not reflect in vivo thrombin formation in newborns.

Interactions and inhibition of blood coagulation factor Va involving residues 311-325 of activated protein C.

Rat protein SV-IV (seminal vesicle protein No. 4) accelerates human blood coagulation in vitro by selective inhibition of antithrombin III.

Activation of protein C in vivo.

Protein C inhibitor acts as a procoagulant by inhibiting the thrombomodulin-induced activation of protein C in human plasma.

A novel exosite in the light chain of human activated protein C essential for interaction with blood coagulation factor Va.

Role of thrombin compared with factor Xa in the procoagulant activity of whole blood clots.

The predictability of factor V Leiden (FV:Q(506)) gene mutation via clotting-based diagnosis of activated protein C resistance.

The effect of activated protein C on fibrinolysis in cell-free plasma can be attributed specifically to attenuation of prothrombin activation.

Platelet-derived microvesicles and activated platelets express factor Xa activity.

Use of annexin-V to demonstrate the role of phosphatidylserine exposure in the maintenance of haemostatic balance by endothelial cells.

Inhibition of antithrombin by protein SV-IV normalizes the coagulation of hemophilic blood.

Anticoagulant and antithrombotic properties of a gamma-carboxyglutamic acid-rich peptide derived from the light chain of blood coagulation factor X.