Results 231 to 240 of about 85,730 (276)
Synchrotron structural biology at SSRL, the beginning and beyond. [PDF]
J Synchrotron RadiatHodgson K.
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Spectroelectrochemical insight into copper cobalt catalysts for CO<sub>2</sub> and nitrite co-electroreduction to urea. [PDF]
Nat CommunRamadhany P +12 more
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In Situ Insights into Ni Phyllosilicate Evolution: Cationic Ni Species as Key to Enhanced Stability in Methane-Rich Dry Reforming. [PDF]
ACS CatalŚwirk Da Costa K +6 more
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Enhanced Proton Spillover at Pt-Cluster/NiO Interface Reduces the Acidic-Alkaline Hydrogen Evolution Activity Gap. [PDF]
Small SciKumar A, Lee J, Kim MG, Tüysüz H.
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Structural Rearrangements of a Cobalt-Free Lithium-Rich Layered Oxide Cathode during Formation. [PDF]
ACS Appl Energy MaterBusato M +7 more
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Hematology/Oncology Clinics of North America, 2010
Several new oral drugs that selectively and directly inhibit factor Xa seem promising alternatives to existing antithrombotic drugs. These drugs have a convenient route of administration, can be given in fixed doses, and do not require coagulation monitoring.
Romualdi E, AGENO, WALTER
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Several new oral drugs that selectively and directly inhibit factor Xa seem promising alternatives to existing antithrombotic drugs. These drugs have a convenient route of administration, can be given in fixed doses, and do not require coagulation monitoring.
Romualdi E, AGENO, WALTER
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Nature Structural Biology, 1998
X-ray absorption spectroscopy, which relies on synchrotron radiation, can accurately determine aspects of metalloprotein active site structure, can be applied to solution or crystalline samples and can be used independently or to supplement crystallographic information.
G N, George, B, Hedman, K O, Hodgson
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X-ray absorption spectroscopy, which relies on synchrotron radiation, can accurately determine aspects of metalloprotein active site structure, can be applied to solution or crystalline samples and can be used independently or to supplement crystallographic information.
G N, George, B, Hedman, K O, Hodgson
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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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2011
Blood coagulation mechanism consists of sequential reactions leading to the reaction where prothrombin is transformed into thrombin. Factor VIIa has culminant position in this mechanism, given its ability to activate both factor IX and X. It is well known today that in vivo coagulation is triggered after the release of tissue factor and the subsequent ...
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Blood coagulation mechanism consists of sequential reactions leading to the reaction where prothrombin is transformed into thrombin. Factor VIIa has culminant position in this mechanism, given its ability to activate both factor IX and X. It is well known today that in vivo coagulation is triggered after the release of tissue factor and the subsequent ...
openaire +1 more source