Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Andrew J. Gale"'
Publikováno v:
The FASEB Journal. 27:2918-2925
Protein S (PS) is a multifunctional plasma protein of the hemostatic and inflammatory pathways, although mechanisms for its regulation are poorly understood. Since certain plasma proteins are regulated through extracellular phosphorylation, we invest
Publikováno v:
Thrombosis and Haemostasis. 109:229-237
SummaryAnticoagulant plasma protein S (PS) is essential for maintaining haemostatic balance. About 2.5% of PS is stored in platelets and released upon platelet stimulation. So far, little is known about the functionality and importance of platelet (p
Publikováno v:
PROTEOMICS. 11:2377-2388
Proteases are critical in many physiological processes and the human genome encodes for 566 predicted proteolytic enzymes. Therefore, there is great interest in identifying and characterizing physiologic protease-substrate relationships. The coagulat
Autor:
Andrew J. Gale
Publikováno v:
Toxicologic Pathology. 39:273-280
The goal of this review is to briefly summarize the two primary pathways of hemostasis, primary hemostasis and secondary hemostasis, as well as to summarize anticoagulant mechanisms and fibrinolysis. In addition, this review will discuss pathologies
Publikováno v:
Protein Science. 11:2091-2101
Procoagulant factor Va (FVa) is inactivated via limited proteolysis at three Arg residues in the A2 domain by the anticoagulant serine protease, activated protein C (APC). Cleavage by APC at Arg306 in FVa causes dissociation of the A2 domain from the
Publikováno v:
Thrombosis and Haemostasis. 101:55-61
SummaryThe hypothesis that prothrombin (FII) protects coagulation factor Va (FVa) from proteolytic inactivation by activated protein C (APC) was tested using purified proteins. FII dose-dependently protected FVa from APC proteolysis under conditions
Publikováno v:
Journal of Biological Chemistry. 282:21848-21855
Prothrombin is proteolytically activated by the prothrombinase complex comprising the serine protease Factor (F) Xa complexed with its cofactor, FVa. Based on inhibition of the prothrombinase complex by synthetic peptides, FVa residues 493-506 were p
Autor:
Andrew J. Gale, John H. Griffin
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 54:433-441
Activation of the anticoagulant human plasma serine protease zymogen, protein C, by a complex of thrombin and the membrane protein, thrombomodulin, generates activated protein C, a physiologic anti-thrombotic, anti-inflammatory and anti-apoptotic age
Publikováno v:
Journal of Biological Chemistry. 277:28836-28840
The anticoagulant human plasma serine protease, activated protein C (APC), inhibits blood coagulation by specific inactivation of the coagulation cofactors factor Va (FVa) and factor VIIIa. Site-directed mutagenesis of residues in three surface loops
Publikováno v:
Blood. 96:585-593
The anticoagulant human plasma serine protease, activated protein C (APC), inactivates blood coagulation factors Va (FVa) and VIIIa. The so-called autolysis loop of APC (residues 301-316, equivalent to chymotrypsin [CHT] residues 142-153) has been hy