A novel factor IXa-specific enzyme-linked immunosorbent assay detects factor IXa in human plasma. [PDF]
Factor (F)IXa activity has been detected in human plasma and may impact thrombotic risk. Current FIXa activity assays are complex and cumbersome.To develop a reproducible enzyme-linked immunosorbent assay (ELISA) using a novel monoclonal antibody that detects total FIXa in human plasma.A monoclonal antibody was raised against the new N-terminus exposed
Misenheimer TM +4 more
europepmc +5 more sources
Molecular Dynamics Simulation Study of the Selective Inhibition of Coagulation Factor IXa over Factor Xa [PDF]
Thromboembolic disorders, arising from abnormal coagulation, pose a significant risk to human life in the modern world. The FDA has recently approved several anticoagulant drugs targeting factor Xa (FXa) to manage these disorders.
Hyun Jung Yoon +2 more
doaj +3 more sources
A Structure Based Study of Selective Inhibition of Factor IXa over Factor Xa [PDF]
Blood coagulation is an essential physiological process for hemostasis; however, abnormal coagulation can lead to various potentially fatal disorders, generally known as thromboembolic disorders, which are a major cause of mortality in the modern world ...
Sibsankar Kundu, Sangwook Wu
doaj +3 more sources
Aptamer-based factor IXa inhibition preserves hemostasis and prevents thrombosis in a piglet model of ECMO [PDF]
Extracorporeal membrane oxygenation (ECMO) requires anticoagulation to prevent clotting when the patient’s blood contacts the circuit. Unfractionated heparin (UFH) usually prevents clotting but can cause life-threatening bleeding.
Christopher R. Reed +10 more
doaj +3 more sources
Factor VIIIa A2 subunit shows a high affinity interaction with factor IXa: contribution of A2 subunit residues 707-714 to the interaction with factor IXa. [PDF]
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
Griffiths AE, Rydkin I, Fay PJ.
europepmc +4 more sources
Analysis of factor XIa, factor IXa and tissue factor activity in burn patients. [PDF]
An elevated procoagulant activity observed in trauma patients is, in part, related to tissue factor (TF) located on blood cells and microparticles. However, analysis of trauma patient plasma indicates that there are other contributor(s) to the procoagulant activity.
Shupp JW +5 more
europepmc +5 more sources
Circulating contact-pathway-activating microparticles together with factors IXa and XIa induce spontaneous clotting in plasma of hematology and cardiologic patients. [PDF]
BACKGROUND AND OBJECTIVE: Using an in vitro experimental model of immobilized tissue factor-initiated clot growth in platelet-free plasma (thrombodynamics), we observed formation of activator-independent isolated spontaneous clots (SC) throughout the ...
Elena Lipets +8 more
doaj +3 more sources
Activation of factor VIII by factor IXa [PDF]
Abstract Thrombin causes an increase in factor VIII coagulant (VIII:C) activity, which is followed by a decay of VIII:C activity to below baseline levels. It has been suggested that a similar interaction of trace amounts of thrombin and factor VIII is a necessary prerequisite before factor VIII can participate in the coagulation cascade.
ME Rick
openalex +4 more sources
Soluble phosphatidylserine binds to two sites on human factor IXa in a Ca2+ dependent fashion to specifically regulate structure and activity. [PDF]
Clinical studies have demonstrated a correlation between elevated levels of FIX and the risk of coronary heart disease, while reduced plasma FIX causes hemophilia B.
Rinku Majumder +7 more
doaj +2 more sources
Localization of the Heparin Binding Exosite of Factor IXa [PDF]
Factor IXa (FIXa) is known to have a binding site for heparin that has not been mapped by a mutagenesis study. By homology modeling based on structural data, we identified eight basic residues in the catalytic domain of FIXa that can potentially bind to heparin.
Likui Yang +2 more
openalex +4 more sources

