Results 71 to 80 of about 13,209 (106)
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Blood, 2005
Abstract Previous studies by us have shown that blood coagulation factor IXa is relatively resistant to inhibition by the Kunitz-type inhibitor bovine pancreatic trypsin inhibitor (BPTI; aprotinin), but that this resistance can be partially alleviated by the presence of low molecular weight heparin.
Armen Nalian +2 more
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Abstract Previous studies by us have shown that blood coagulation factor IXa is relatively resistant to inhibition by the Kunitz-type inhibitor bovine pancreatic trypsin inhibitor (BPTI; aprotinin), but that this resistance can be partially alleviated by the presence of low molecular weight heparin.
Armen Nalian +2 more
openaire +2 more sources
Biochemistry, 1999
Factor IXa binding to the activated platelet surface is required for efficient catalysis of factor X activation. Platelets possess a specific binding site for factor IXa, occupancy of which has been correlated with rates of factor X activation. However, the specific regions of the factor IXa molecule that are critical to this interaction have not yet ...
Peter N. Walsh +2 more
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Factor IXa binding to the activated platelet surface is required for efficient catalysis of factor X activation. Platelets possess a specific binding site for factor IXa, occupancy of which has been correlated with rates of factor X activation. However, the specific regions of the factor IXa molecule that are critical to this interaction have not yet ...
Peter N. Walsh +2 more
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The Structure of Synthetic Oligosaccharides in Relation to Factor IXa Inhibition
Thrombosis and Haemostasis, 2002SummaryWe investigated the effect of various oligosaccharides (OS) on the inhibition of factor IXa by antithrombin (AT) in a purified system. The OS comprised the AT-binding pentasaccharide sequence prolonged by saccharide chains with various lengths and charges. We show that factor IXa inhibition depended on the molecular weight of the OS.
Petitou Maurice +6 more
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Inhibition of bovine factor IXa and factor Xa.beta. by antithrombin III
Biochemistry, 1976Factor IXa and factor Xabeta are serine proteases which participate in the middle phase of blood coagulation. These two enzymes are inhibited by antithrombin III by the formation of an enzyme-inhibitor complex containing 1 mol of enzyme and 1 mol of antithrombin III.
Kazuo Fujikawa +3 more
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Phosphatidylserine Regulation of Coagulation Proteins Factor IXa and Factor VIIIa
The Journal of Membrane Biology, 2022Blood coagulation is an intricate process, and it requires precise control of the activities of pro- and anticoagulant factors and sensitive signaling systems to monitor and respond to blood vessel insults. These requirements are fulfilled by phosphatidylserine, a relatively miniscule-sized lipid molecule amid the myriad of large coagulation proteins ...
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Molecular models of the procoagulant Factor VIIIa–Factor IXa complex
Journal of Thrombosis and Haemostasis, 2005Formation of the intrinsic tenase complex is an essential event in the procoagulant reactions that lead to clot formation. The tenase complex is formed when the activated serine protease, Factor IXa (FIXa), and its cofactor Factor VIIIa (FVIIIa) assemble on a phospholipid surface to proteolytically convert the zymogen Factor X (FX) into its active form
Ludovic Autin +5 more
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Factor IXa as a target for anticoagulation in thrombotic disorders and conditions
Drug Discovery Today, 2014From acute coronary syndrome (ACS) to the prevention of cardioembolic events in patients with atrial fibrillation and thrombosis of mechanical heart valves, there is a quest to develop a new generation of anticoagulants. Perhaps the 'holy grail' of antithrombotic therapy is not only a drug that will prevent coagulation without promoting bleeding but ...
Richard C. Becker, Dia Smiley
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The influence of sodium ion binding on factor IXa activity
Thrombosis and Haemostasis, 2006SummarySodium plays an important role in modulating both the amidolytic and proteolytic activities of thrombin. By contrast, while the optimal amidolytic activity of factor Xa requires Na+, the proteolytic activity of factor Xa in the prothrombinase complex is minimally affected by the monovalent cation.
Alireza R. Rezaie, Kota N. Gopalakrishna
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Blood
Background: The goal of achieving therapeutically relevant levels of FIX activity in hemophilia B (HB) has been enhanced with the use of the hyperactive factor IX variant R338L (FIX-Padua). FIX-Padua has between 4 to 9-fold higher specific activity than wild-type (wt-) FIX, although the exact mechanism of enhanced ...
Lei Ke +2 more
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Background: The goal of achieving therapeutically relevant levels of FIX activity in hemophilia B (HB) has been enhanced with the use of the hyperactive factor IX variant R338L (FIX-Padua). FIX-Padua has between 4 to 9-fold higher specific activity than wild-type (wt-) FIX, although the exact mechanism of enhanced ...
Lei Ke +2 more
openaire +1 more source
RNA aptamers as reversible antagonists of coagulation factor IXa
Nature, 2002Many therapeutic agents are associated with adverse effects in patients. Anticoagulants can engender acute complications such as significant bleeding that increases patient morbidity and mortality. Antidote control provides the safest means to regulate drug action.
Juliana M. Layzer +6 more
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