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1 ctly inhibits thrombin generated by FXa/FVa (prothrombinase complex).
2 oagulation by supporting the assembly of the prothrombinase complex.
3 catalytic efficiency of factor Xa within the prothrombinase complex.
4 its interaction with the cofactor within the prothrombinase complex.
5 d EPR-1 mediates factor Xa assembly into the prothrombinase complex.
6  the activated platelet to form a functional prothrombinase complex.
7 neously decreased thrombin generation by the prothrombinase complex.
8 ted Factor V is an essential cofactor in the prothrombinase complex.
9 catalytic efficiency of factor Xa within the prothrombinase complex.
10 ary steps in the assembly of the prothrombin-prothrombinase complex.
11 sights into the assembly and function of the prothrombinase complex.
12 telet membranes regulate the activity of the prothrombinase complex.
13 sequential cleavages at R271 and R320 by the prothrombinase complex.
14 ed as an extended FXa binding surface in the prothrombinase complex.
15 ependent prothrombin recognition site in the prothrombinase complex.
16 rsor prothrombin by factor Xa as part of the prothrombinase complex.
17 ne-like support for factors Xa and Va in the prothrombinase complex.
18 oth FIXa in the FXase complex and FXa in the prothrombinase complex.
19 ed factor V to bind Xa and assemble into the prothrombinase complex.
20 ely 3-fold lower catalytic efficiency in the prothrombinase complex.
21 le in FXa recognition of the cofactor in the prothrombinase complex.
22 phatidylserine (PS) regulate activity of the prothrombinase complex.
23 or Va and the Gla domain of factor Xa in the prothrombinase complex.
24 iate interactions between fVa and fII in the prothrombinase complex.
25 ndent recognition sites for factor Xa in the prothrombinase complex.
26 iate interactions between fXa and fII in the prothrombinase complex.
27 ction as zymogens for both factor Xa and the prothrombinase complex.
28  assembly and/or by slowing formation of the prothrombinase complex.
29 e protein substrate recognition by the human prothrombinase complex.
30  and phospholipid membranes, and inhibit the prothrombinase complex.
31 nt for interaction of the substrate with the prothrombinase complex.
32 Q333D fXa is fully functional as part of the prothrombinase complex.
33 ation response prior to the formation of the prothrombinase complex.
34 type enzymes are equivalent when part of the prothrombinase complex.
35 6 APC-cleavage site in the regulation of the prothrombinase complex.
36 ts, is the essential protein cofactor of the prothrombinase complex.
37 spholipid, factor Va, and prothrombin in the prothrombinase complex.
38 des a suitable surface for activation of the prothrombinase complex.
39 common" pathway at the level of the FXa/FVa (prothrombinase) complex.
40 egulator of both the intrinsic FXase and the prothrombinase complexes.
41 estingly, ATS-119 inhibited factor Xa in the prothrombinase complex 2-6-fold more potently and 2-3-fo
42                                   The formed prothrombinase complex activates factor VII at approxima
43         Thrombin generation assays measuring prothrombinase complex activity demonstrated 1.5-fold hi
44 th fXa, Ca2+, and phospholipids, defines the prothrombinase complex and activates prothrombin in the
45 ty lipoprotein (LDL) support assembly of the prothrombinase complex and generation of thrombin.
46 (cleavage at Arg323-Ile324) catalyzed by the prothrombinase complex and have also relied on the known
47 e cleavage of prothrombin indicates both the prothrombinase complex and the formation of prothrombina
48 ng tissue factor VIIa activity, Xa activity, prothrombinase complex, and thrombin generation.
49 hrombin) for the intrinsic pathway FXase and prothrombinase complexes are bound to the phospholipid s
50 vivo is the activation of prothrombin by the prothrombinase complex assembled on either an activated
51 ad essentially no detectable activity in the prothrombinase complex assembled on synthetic phospholip
52                                          The prothrombinase complex assembled on the surface of plate
53                                          The prothrombinase complex assembles through reversible inte
54                                          The prothrombinase complex assembles through reversible inte
55 man platelet membrane protein that regulates prothrombinase complex assembly and function.
56  323-331 and tested them for their effect on prothrombinase complex assembly and function.
57 iding the necessary procoagulant surface for prothrombinase complex assembly and thrombin generation.
58 agulation protein and provides evidence that prothrombinase complex assembly on thrombin-activated pl
59 PS, with binding to the C1 domain regulating prothrombinase complex assembly.
60 nes support formation of a 60-70% functional prothrombinase complex at saturating factor Va concentra
61 = approximately 40 nm) of a partially active prothrombinase complex between factor Xa and factor Va(2
62 ibody (moAb) annexin V protein reacting with prothrombinase complex binding sites.
63 on cascade and highlights parallels with the prothrombinase complex, but will also provide a novel ra
64                        The inhibition of the prothrombinase complex by R3A-TAP was characterized by s
65                   Based on inhibition of the prothrombinase complex by synthetic peptides, FVa residu
66 und and Na(+)-free forms of factor Xa in the prothrombinase complex can efficiently activate prothrom
67                                          The prothrombinase complex catalyzes the activation of proth
68  prothrombin is converted to thrombin by the prothrombinase complex composed of factor Xa, cofactor V
69                                          The prothrombinase complex, composed of factor Xa and factor
70                                          The prothrombinase complex, composed of the protease factor
71                                          The prothrombinase complex, composed of the proteinase, fact
72 thrombin is proteolytically activated by the prothrombinase complex comprising the serine protease Fa
73  cascade converge to a common step where the prothrombinase complex, comprising the enzyme factor Xa
74                                          The prothrombinase complex consists of the protease factor X
75                             The fully formed prothrombinase complex containing this FVa mutant had fa
76  Factor Xa (FXa), the serine protease of the prothrombinase complex, contains a Tyr at this position.
77                                          The prothrombinase complex converts prothrombin to alpha-thr
78 a, either in free form or assembled into the prothrombinase complex during the process of prothrombin
79  antithrombin inhibition of factor Xa in the prothrombinase complex (factor Va, negatively charged me
80 tivation of prothrombin, as catalyzed by the prothrombinase complex (factor X(a), enzyme; factor V(a)
81  prothrombin recognition by factor Xa in the prothrombinase complex (factor Xa, factor Va, phosphatid
82 nt sPLA2, inhibited thrombin generation from prothrombinase complex (factors Xa, V, II, Ca2+, and pho
83 m spontaneous binding to fXa and unnecessary prothrombinase complex formation, which in turn results
84 n at concentrations consistent with complete prothrombinase complex formation.
85        Based on the crystal structure of the prothrombinase complex from the venom of the Australian
86  The central findings are as follows: 1) the prothrombinase complex (fVa-fXa-Ca(2+)-membrane) accumul
87 nd prothrombin (fII) that may be involved in prothrombinase complex (fXa.factor Va.fII.phospholipids)
88 y sequences in prothrombin (fII) involved in prothrombinase complex (fXa.fVa.fII.phospholipids) assem
89 avage of prothrombin (ProT) at Arg320 by the prothrombinase complex generates proteolytically active,
90 tic substrates, but the role of Na(+) in the prothrombinase complex has not been investigated.
91 t from its interaction with factor Va in the prothrombinase complex have been probed using a recombin
92 ts to determine the crystal structure of the prothrombinase complex have been thwarted by the depende
93 dent recognition site for prothrombin in the prothrombinase complex; however, Lys-96 is a recognition
94 d blocks the assembly and/or activity of the prothrombinase complex in the same way.
95 ufficient to produce the fully active human "prothrombinase" complex in solution.
96 letal muscle and cardiac myosins support the prothrombinase complex indirectly through contaminating
97 d Partial Thromboplastin Time'' (aPTT) and ''Prothrombinase complex-induced Clotting Test'' (PiCT) ha
98  and that a cofactor function for fVa in the prothrombinase complex involves inducing a conformationa
99  enzyme activated factor X (FXa) to form the prothrombinase complex is a pivotal initial event in blo
100                                          The prothrombinase complex is comprised of an enzyme, factor
101 hrombin to the protease meizothrombin by the prothrombinase complex is linked to a large conformation
102 ht heparins, indicates that factor Xa in the prothrombinase complex is protected from inhibition by a
103 ught holds that factor Xa (FXa) bound in the prothrombinase complex is resistant to regulation by pro
104 undation for the establishment of a complete prothrombinase complex model, which might be successful
105 rsion of fII to alpha-thrombin (fIIa) by the prothrombinase complex occurs through 2 parallel pathway
106   Thrombin activation requires assembly of a prothrombinase complex of activated coagulation factors
107 ic formation of thrombin is catalyzed by the prothrombinase complex of blood coagulation.
108 pt that protein substrate recognition by the prothrombinase complex of coagulation is achieved by int
109 ng platelet membranes to form the essential "prothrombinase" complex of blood coagulation.
110                                       In the prothrombinase complex on the platelet surface, FXa clea
111  blocking phospholipid binding sites for the prothrombinase complex on the surfaces of vesicles and a
112 but serves as a procoagulant cofactor in the prothrombinase complex once activated to FVa.
113       Pseutarin C is an intrinsically stable prothrombinase complex preassembled in the venom gland o
114                                          The prothrombinase complex processes prothrombin to thrombin
115 ally efficient production of thrombin by the prothrombinase complex relies on suitable positioning of
116 or Va (FVa) is the cofactor component of the prothrombinase complex required for rapid generation of
117 ated fV (fVa), an essential component of the prothrombinase complex required for the rapid activation
118 ide a surface for assembly of the tenase and prothrombinase complexes required for thrombin generatio
119           Further studies with the wild-type prothrombinase complex revealed that FXa binds to factor
120 soluble PS to trigger formation of a soluble prothrombinase complex suggests that exposure of PS mole
121 sis, factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold in
122 e-exposed phosphatidylserine (PS) forms the "prothrombinase complex" that is essential for efficient
123 e site-blocked factor Xa to factor Va in the prothrombinase complex, the Kd for peptide-Va interactio
124 t into the architecture and mechanism of the prothrombinase complex-the molecular engine of blood coa
125 espect to their ability to assemble into the prothrombinase complex to activate prothrombin and inter
126 ns prothrombin and prethrombin-2 require the prothrombinase complex to be converted to the mature pro
127 lex and then to function as an enzyme in the prothrombinase complex to catalyze the conversion of pro
128 s in prothrombin cleaved by Factor Xa in the prothrombinase complex to form thrombin.
129          Platelet PA promotes binding of the prothrombinase complex to the platelet membrane, greatly
130 ant substrates; however, its activity in the prothrombinase complex toward most of mutants was severe
131 f prothrombin to thrombin is catalyzed by a "prothrombinase" complex, traditionally viewed as factor
132                                  In ECs, the prothrombinase complex uses surface-attached FV and y-ca
133 tion assays using purified components of the prothrombinase complex was examined.
134 of human prothrombin in interaction with the prothrombinase complex was studied using a peptide with
135 ts or endothelial cells, factor Xa forms the prothrombinase complex, which is responsible for the pro
136 crom and inhibits thrombin generation by the prothrombinase complex with a K(i) of 0.8 microm.

 
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