Results 251 to 260 of about 24,619 (304)
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Selective epitaxy of GaAs, AlxGa1−xAs, and InxGa1−xAs
Journal of Crystal Growth, 1991Abstract Many device structures benefit from the ability to selectively deposit epitaxial materials. Through the use of a masking material, such as Si3N4 or SiO2, on the substrate surface, patterns generated through standard lithographic procedures can be used to define regions for selective deposition. Highly selective growth can be achieved through
T.F. Kuech +8 more
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Perspectives on Factor Xa Inhibition
Current Medicinal Chemistry, 2001Blood coagulation involves a complex cascade of enzymatic reactions, ultimately generating fibrin, the basis of all blood clots. This cascade is comprised of two arms, the intrinsic and extrinsic pathways which converge at factor Xa to form the common pathway.
R, Rai +3 more
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Anti-factor Xa (Anti-Xa) Assay
2013The anti-factor Xa (anti-Xa) assay is a functional assay that facilitates the measurement of antithrombin (AT)-catalyzed inhibition of factor Xa by unfractionated heparin (UFH) and direct inhibition of factor Xa by low-molecular-weight heparin (LMWH) (Kitchen, Br J Haematol 111:397-406, 2000; Walenga et al., Semin Thromb Hemost 11:17-25, 1985; Levine ...
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IBM Systems Journal, 1989
The VM/XA System Product manages the vast amounts of real and expanded storage available on the new Enterprise Systems Architecture/370™ processors for both guest use and support of internal operating system functions. The management algorithms are examined, and the rationale for their selection is presented.
Geoff O. Blandy, S. Richard Newson
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The VM/XA System Product manages the vast amounts of real and expanded storage available on the new Enterprise Systems Architecture/370™ processors for both guest use and support of internal operating system functions. The management algorithms are examined, and the rationale for their selection is presented.
Geoff O. Blandy, S. Richard Newson
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Anthranilamide inhibitors of factor Xa
Bioorganic & Medicinal Chemistry Letters, 2007SAR about the B-ring of a series of N(2)-aroyl anthranilamide factor Xa (fXa) inhibitors is described. B-ring o-aminoalkylether and B-ring p-amine probes of the S1' and S4 sites, respectively, afforded picomolar fXa inhibitors that performed well in in vitro anticoagulation assays.
David, Mendel +20 more
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Protamine sulfate stimulates degradation of factor Xa and the factor Xa–antithrombin complex
Blood Coagulation & Fibrinolysis, 2011The effect of protamine sulfate on factor Xa (FXa) and the factor Xa-antithrombin complex was studied via SDS-PAGE and Western blot analysis. Human factor Xa [(FXaα) ∼52 kDa, FXaβ ∼47 kDa] and human antithrombin (AT ∼55 kDa) form a primary (1°) complex at 109 and 104 kDa, a secondary (2°) complex at 99 and 95 kDa, and a tertiary (3°) complex at 66 and ...
Martin H, Coggin +4 more
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Antidote for Factor Xa Anticoagulants
New England Journal of Medicine, 2015Oral anticoagulant options have exploded. Dabigatran, a direct thrombin inhibitor, was approved for use in the United States in 2010 for the prevention of stroke in patients with atrial fibrillation; this was rapidly followed by approval of the direct factor Xa inhibitors rivaroxaban, apixaban, and edoxaban within 5 years. The drive for the development
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The FASEB Journal, 1995
Cellular inflammatory responses and early mechanisms of vascular injury are invariably associated with activation of blood coagulation and deposition of insoluble fibrin. This process occurs on vascular cell surfaces through the ability of the coagulation protease factor Xa to generate thrombin.
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Cellular inflammatory responses and early mechanisms of vascular injury are invariably associated with activation of blood coagulation and deposition of insoluble fibrin. This process occurs on vascular cell surfaces through the ability of the coagulation protease factor Xa to generate thrombin.
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1992
The assembly and function of the prothrombinase complex on the bovine and human platelet membrane is mediated through binding interactions in which factor Va bound to the platelet surface forms at least part of the "receptor" for factor Xa in a 1:1 stoichiometric complex. A model depicting these binding interactions is shown in Fig. 12.
P B, Tracy, M E, Nesheim, K G, Mann
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The assembly and function of the prothrombinase complex on the bovine and human platelet membrane is mediated through binding interactions in which factor Va bound to the platelet surface forms at least part of the "receptor" for factor Xa in a 1:1 stoichiometric complex. A model depicting these binding interactions is shown in Fig. 12.
P B, Tracy, M E, Nesheim, K G, Mann
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