Results 201 to 210 of about 12,711,395 (233)

Purification and Properties of Human Factor IXa

Thrombosis and Haemostasis, 1976
SummaryHuman 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
K, Váradi, S, Elödi
openaire   +2 more sources

Structure–Function Relationships in Factor IX and Factor IXa

Trends in Cardiovascular Medicine, 2003
Factor 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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Zymogen Factor IX Potentiates Factor IXa-Catalyzed Factor X Activation

Biochemistry, 2000
Intrinsic factor X activation is accelerated >10(7)-fold by assembly of the entire complex on the activated platelet surface. We have now observed that increasing the concentration of zymogen factor IX to physiologic levels ( approximately 100 nM) potentiates factor IXa-catalyzed activation of factor X on both activated platelets and on negatively ...
F S, London, P N, Walsh
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SAR and Factor IXa Crystal Structure of a Dual Inhibitor of Factors IXa and Xa.

ChemInform, 2005
AbstractFor Abstract see ChemInform Abstract in Full Text.
Joanne M. Smallheer, et al. et al.
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Molecular models of the procoagulant Factor VIIIa–Factor IXa complex

Journal of Thrombosis and Haemostasis, 2005
Formation 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
L, Autin, M A, Miteva, W H, Lee, K, Mertens, K-P, Radtke, B O, Villoutreix   +5 more
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Insight into Factor IXa Selectivity and Reactivity Using Kunitz-Type Inhibitors: Importance of Factor IXa Residue K98.

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.
Pierre F. Neuenschwander, Stephen R. Williamson, Armen Nalian   +2 more
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Discovery of novel hydroxy pyrazole based factor IXa inhibitor

Bioorganic & Medicinal Chemistry Letters, 2006
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Dange, Vijaykumar, Paul A, Sprengeler, Michael, Shaghafi, Jeffrey R, Spencer, Brad A, Katz, Christine, Yu, Roopa, Rai, Wendy B, Young, Brian, Schultz, James, Janc   +9 more
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CRYSTAL STRUCTURE OF HUMAN COAGULATION FACTOR IXa

, 2019
Essentials Consensus sequence and biochemical data suggest a Na+ -site in the factor (F) IXa protease domain. X-ray structure of the FIXa EGF2/protease domain at 1.37 A reveals a Na+ -site not observed earlier. Molecular dynamics simulations data support
Kanagasabai Vadivel, Herman Schreuder, A. Liesum, Amy E. Schmidt, G. Goldsmith, S. P. Bajaj   +5 more
semanticscholar   +1 more source

Antidote‐Controlled Antithrombotic Therapy Targeting Factor IXa and Von Willebrand Factor

Annals of the New York Academy of Sciences, 2009
Thrombotic disorders and their common clinical phenotypes of acute myocardial infarction, ischemic stroke, and venous thromboembolism are the proximate cause of substantial morbidity, mortality, and health care expenditures worldwide. Accordingly, therapies designed to attenuate thrombus initiation and propagation, reflecting integrated platelet ...
Richard C, Becker, Sabah, Oney, Kristian C D, Becker, Bruce, Sullenger   +3 more
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Contribution of Factor VIII A3 Domain Residues 1793-1795 to a Factor IXa-Interactive Site

Blood, 2018
Factor (F) VIII functions as a cofactor in the tenase complex responsible for phospholipid surface-dependent conversion of FX to FXa by FIXa. FIXa binding sites were identified on A2, A3, and C2 domains of FVIII. Some earlier studies confirmed the FIXa-
M. Takeyama, K. Nogami, Kana Sasai, M. Shima   +3 more
semanticscholar   +1 more source