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1 ctly inhibits thrombin generated by FXa/FVa (prothrombinase complex).
2 neously decreased thrombin generation by the prothrombinase complex.
3 ted Factor V is an essential cofactor in the prothrombinase complex.
4 catalytic efficiency of factor Xa within the prothrombinase complex.
5 telet membranes regulate the activity of the prothrombinase complex.
6 sequential cleavages at R271 and R320 by the prothrombinase complex.
7 ed as an extended FXa binding surface in the prothrombinase complex.
8 ependent prothrombin recognition site in the prothrombinase complex.
9 rsor prothrombin by factor Xa as part of the prothrombinase complex.
10 oth FIXa in the FXase complex and FXa in the prothrombinase complex.
11 ely 3-fold lower catalytic efficiency in the prothrombinase complex.
12 le in FXa recognition of the cofactor in the prothrombinase complex.
13 phatidylserine (PS) regulate activity of the prothrombinase complex.
14 or Va and the Gla domain of factor Xa in the prothrombinase complex.
15 iate interactions between fVa and fII in the prothrombinase complex.
16 ndent recognition sites for factor Xa in the prothrombinase complex.
17 iate interactions between fXa and fII in the prothrombinase complex.
18 ction as zymogens for both factor Xa and the prothrombinase complex.
19 assembly and/or by slowing formation of the prothrombinase complex.
20 e protein substrate recognition by the human prothrombinase complex.
21 and phospholipid membranes, and inhibit the prothrombinase complex.
22 nt for interaction of the substrate with the prothrombinase complex.
23 Q333D fXa is fully functional as part of the prothrombinase complex.
24 ation response prior to the formation of the prothrombinase complex.
25 type enzymes are equivalent when part of the prothrombinase complex.
26 6 APC-cleavage site in the regulation of the prothrombinase complex.
27 ts, is the essential protein cofactor of the prothrombinase complex.
28 spholipid, factor Va, and prothrombin in the prothrombinase complex.
29 des a suitable surface for activation of the prothrombinase complex.
30 catalytic efficiency of factor Xa within the prothrombinase complex.
31 its interaction with the cofactor within the prothrombinase complex.
32 d EPR-1 mediates factor Xa assembly into the prothrombinase complex.
33 the activated platelet to form a functional prothrombinase complex.
34 common" pathway at the level of the FXa/FVa (prothrombinase) complex.
35 egulator of both the intrinsic FXase and the prothrombinase complexes.
36 estingly, ATS-119 inhibited factor Xa in the prothrombinase complex 2-6-fold more potently and 2-3-fo
40 (cleavage at Arg323-Ile324) catalyzed by the prothrombinase complex and have also relied on the known
41 e cleavage of prothrombin indicates both the prothrombinase complex and the formation of prothrombina
43 hrombin) for the intrinsic pathway FXase and prothrombinase complexes are bound to the phospholipid s
44 vivo is the activation of prothrombin by the prothrombinase complex assembled on either an activated
45 ad essentially no detectable activity in the prothrombinase complex assembled on synthetic phospholip
51 iding the necessary procoagulant surface for prothrombinase complex assembly and thrombin generation.
52 agulation protein and provides evidence that prothrombinase complex assembly on thrombin-activated pl
54 nes support formation of a 60-70% functional prothrombinase complex at saturating factor Va concentra
55 = approximately 40 nm) of a partially active prothrombinase complex between factor Xa and factor Va(2
59 und and Na(+)-free forms of factor Xa in the prothrombinase complex can efficiently activate prothrom
64 thrombin is proteolytically activated by the prothrombinase complex comprising the serine protease Fa
67 Factor Xa (FXa), the serine protease of the prothrombinase complex, contains a Tyr at this position.
69 a, either in free form or assembled into the prothrombinase complex during the process of prothrombin
70 antithrombin inhibition of factor Xa in the prothrombinase complex (factor Va, negatively charged me
71 tivation of prothrombin, as catalyzed by the prothrombinase complex (factor X(a), enzyme; factor V(a)
72 prothrombin recognition by factor Xa in the prothrombinase complex (factor Xa, factor Va, phosphatid
73 nt sPLA2, inhibited thrombin generation from prothrombinase complex (factors Xa, V, II, Ca2+, and pho
74 m spontaneous binding to fXa and unnecessary prothrombinase complex formation, which in turn results
76 The central findings are as follows: 1) the prothrombinase complex (fVa-fXa-Ca(2+)-membrane) accumul
77 nd prothrombin (fII) that may be involved in prothrombinase complex (fXa.factor Va.fII.phospholipids)
78 y sequences in prothrombin (fII) involved in prothrombinase complex (fXa.fVa.fII.phospholipids) assem
79 avage of prothrombin (ProT) at Arg320 by the prothrombinase complex generates proteolytically active,
81 t from its interaction with factor Va in the prothrombinase complex have been probed using a recombin
82 ts to determine the crystal structure of the prothrombinase complex have been thwarted by the depende
83 dent recognition site for prothrombin in the prothrombinase complex; however, Lys-96 is a recognition
85 d Partial Thromboplastin Time'' (aPTT) and ''Prothrombinase complex-induced Clotting Test'' (PiCT) ha
86 and that a cofactor function for fVa in the prothrombinase complex involves inducing a conformationa
87 enzyme activated factor X (FXa) to form the prothrombinase complex is a pivotal initial event in blo
89 ht heparins, indicates that factor Xa in the prothrombinase complex is protected from inhibition by a
90 undation for the establishment of a complete prothrombinase complex model, which might be successful
91 rsion of fII to alpha-thrombin (fIIa) by the prothrombinase complex occurs through 2 parallel pathway
92 Thrombin activation requires assembly of a prothrombinase complex of activated coagulation factors
94 pt that protein substrate recognition by the prothrombinase complex of coagulation is achieved by int
97 blocking phospholipid binding sites for the prothrombinase complex on the surfaces of vesicles and a
99 ally efficient production of thrombin by the prothrombinase complex relies on suitable positioning of
100 ide a surface for assembly of the tenase and prothrombinase complexes required for thrombin generatio
102 soluble PS to trigger formation of a soluble prothrombinase complex suggests that exposure of PS mole
103 sis, factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold in
104 e-exposed phosphatidylserine (PS) forms the "prothrombinase complex" that is essential for efficient
105 e site-blocked factor Xa to factor Va in the prothrombinase complex, the Kd for peptide-Va interactio
106 t into the architecture and mechanism of the prothrombinase complex-the molecular engine of blood coa
107 espect to their ability to assemble into the prothrombinase complex to activate prothrombin and inter
108 ns prothrombin and prethrombin-2 require the prothrombinase complex to be converted to the mature pro
109 lex and then to function as an enzyme in the prothrombinase complex to catalyze the conversion of pro
111 ant substrates; however, its activity in the prothrombinase complex toward most of mutants was severe
112 f prothrombin to thrombin is catalyzed by a "prothrombinase" complex, traditionally viewed as factor
114 of human prothrombin in interaction with the prothrombinase complex was studied using a peptide with
115 ts or endothelial cells, factor Xa forms the prothrombinase complex, which is responsible for the pro
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