Results 61 to 70 of about 13,209 (106)
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Inactivation of factor VIII by factor IXa
Biochemistry, 1992Factor VIII (FVIII) is the nonproteolytic cofactor for FIXa in the tenase complex of blood coagulation. FVIII is proteolytically activated by thrombin and FXa in vitro to form a heterotrimer with full procoagulant activity. Activated protein C inactivates thrombin-activated FVIII through cleavage adjacent to position Arg 336 in the cofactor.
Donogh P. O'Brien+3 more
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SAR and factor IXa crystal structure of a dual inhibitor of factors IXa and Xa
Bioorganic & Medicinal Chemistry Letters, 2004Modifications to the P4 moiety and pyrazole C3 substituent of factor Xa inhibitor SN-429 provided several new compounds, which are 5-10nM inhibitors of factor IXa. An X-ray crystal structure of one example complexed to factor IXa shows that these compounds adopt a similar binding mode to that previously observed with pyrazole inhibitors in the factor ...
Jianmin Wang+12 more
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The Activation of Bovine Factor X by Factors IXa and VIII. [PDF]
The esterase activity of bovine factor xa on the synthetic substrate α-N-benzoyl-L-arginineethyl ester can be used to follow the activation of factor X by the intrinsic pathway of coagulation. Bovine factor IXa activates factor X in a reaction having an absolute requirement for calcium ions, but little affected by phospholipid.
G.G. Neal, S.I. Chavin
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The Regulation of Factor IXa by Phosphatidylserine.
Blood, 2004Abstract A number of clinical studies have demonstrated correlation between elevated levels of factor IX and the risk of coronary heart disease. Studies by different groups have shown that blocking procoagulant activity of factor IXa could reduce the risk of thrombosis.
Rinku Majumder+3 more
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Thrombosis and Haemostasis, 2019
AbstractA nonasaccharide (FG9) derived from natural fucosylated glycosaminoglycan (FG) is identified as a selective intrinsic factor Xase complex (FIXa-FVIIIa-Ca2+-phospholipid, FXase) inhibitor that possesses potential inhibition of venous thrombus in rats and shows negligible bleeding risk. The mechanism and molecular target of the nonasaccharide for
Na Gao+7 more
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AbstractA nonasaccharide (FG9) derived from natural fucosylated glycosaminoglycan (FG) is identified as a selective intrinsic factor Xase complex (FIXa-FVIIIa-Ca2+-phospholipid, FXase) inhibitor that possesses potential inhibition of venous thrombus in rats and shows negligible bleeding risk. The mechanism and molecular target of the nonasaccharide for
Na Gao+7 more
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Purification and Properties of Human Factor IXa
Thrombosis and Haemostasis, 1976SummaryHuman factor IXa was purified 5,000-fold from serum by ion exchange chromatography. The preparation was free from other clotting factors. Both pH sensitivity and heat stability of purified factor IXa appeared to be different from those of factor IX in the plasma. The molecular weight of human factor IXa is 80,000 as estimated from gel-filtration
Susan Elödi, Katalin Varadi
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Discovery of hydroxy pyrimidine Factor IXa inhibitors
Bioorganic & Medicinal Chemistry Letters, 2020The synthesis and structure activity relationship development of a pyrimidine series of heterocyclic Factor IXa inhibitors is described. Increased selectivity over Factor Xa inhibition was achieved through SAR expansion of the P1 element. Select compounds were evaluated in vivo to assess their plasma levels in rat.
Charles L. Jayne+17 more
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[6] Human factor IX and factor IXa
1993Publisher Summary This chapter provides methods for factor IX and factor IXa isolation from human plasma and recombinant cultures and discusses the preparation of [ 3 H]sialyl and of 125 I-labeled tyrosyl factor IX and their use in investigations of the structure-function relationships in the protein.
S P Bajaj, J J Birktoft
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Structure–Function Relationships in Factor IX and Factor IXa
Trends in Cardiovascular Medicine, 2003Factor IX (FIX) consists of an N-terminal gamma-carboxyglutamic acid (Gla) domain followed by two epidermal growth factor (EGF)-like domains, and the C-terminal serine protease domain. During physiologic coagulation, one of the activators of FIX is the FVIIa/tissue factor (TF) complex.
Amy E. Schmidt, S. Paul Bajaj
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The acceleration by polylysine of the activation of factor X by factor IXa
Thrombosis Research, 1982The present study reports that polylysine can function as a cofactor in the conversion of factor X to factor Xa by factor IXa. In the presence of polylysine, factor X is converted to factor Xa by factor IXa as demonstrated by both clotting and amidolytic assays.
Harold R. Roberts, Roger L. Lundblad
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