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1 at the productive recognition of factor X by Xase arises from a multistep reaction requiring an initi
2 activation of factor X by an enzyme complex (Xase) composed of the trypsin-like serine proteinase, fa
3 s in the presence of calcium ions (extrinsic Xase complex).
4 cognition of human factor X by the extrinsic Xase complex is not achieved through specific interactio
5 te recognition and cleavage by the extrinsic Xase complex is unclear.
6 tely activated to factor Xa by the extrinsic Xase complex or by a purified activator from Russell's v
7 (fX) by factor VIIa (fVIIa) in the extrinsic Xase pathway.
8 gulation without input from extrinsic factor Xase activity.
9  showed >9-fold increases in K(d) for factor Xase assembly, implicating these residues in stabilizing
10 ts Ki for inhibition of the intrinsic factor Xase (105 microM).
11                         The intrinsic factor Xase complex (FXase) is comprised of a serine protease,
12 in potent inhibition of the intrinsic factor Xase complex.
13 or at two levels within the intrinsic factor Xase complex.
14 3) in normal hemostasis the intrinsic factor Xase function contributes to the durability of the resup
15 resupply; 2) impairments in intrinsic factor Xase function, i.e. hemophilias A and B, result in an im
16 nhibition of factor VIIIa-factor IXa (factor Xase) enzyme complex.
17 ed by the activity of a reconstituted factor Xase system.
18         The first assay reconstituted factor Xase using varying concentrations of A2 mutant and fixed
19 lso enhanced activity of fVIII in the factor Xase complex by two- to fourfold.
20       The catalytic activities of the factor Xase complex composed of the hemophilia A-associated FVI
21 s as a cofactor for factor IXa in the factor Xase complex.
22 participation in the formation of the factor Xase complex.
23 is necessary for full activity of the factor Xase complex.
24 hibitor of the prothrombinase and the factor Xase complexes regardless of the degree of membrane curv
25 s to the K(m) for factor X binding to factor Xase, and this parameter is critical for activity assess
26 p critical to interaction with factor IXa in Xase.
27 its ability to function within the intrinsic Xase complex to activate X may play a significant role i
28 pid, fVIIIa incorporation into the intrinsic Xase complex, thrombin generation in plasma, and fVIII u
29 eptor tissue factor (TF) or by the intrinsic Xase complex, which consists of active factors VIII (VII
30 I or IX, the two components of the intrinsic Xase complex.
31 tive site but does not alter the affinity of Xase for factor X.
32 sis for the protein substrate specificity of Xase using TF reconstituted into vesicles of phosphatidy
33  2 major complexes of the intrinsic pathway, Xase and prothrombinase, leading to a 20- and 10-fold in
34 C6 phosphatidylcholine, also accelerated the Xase complex, indicating that kcat enhancement has less
35        An alternative approach to bypass the Xase complex is to inhibit endogenous anticoagulant acti
36 ity of interaction between components of the Xase complex, activated factors VIII and IX.
37 occupation of the active site of VIIa within Xase by a reversible inhibitor or an alternate peptidyl
38 ractions with the active site of VIIa within Xase.

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