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1 nsible for the enhanced activation of FII by prothrombinase.
2 ry for efficient catalysis of prothrombin by prothrombinase.
3 ential role in its proteolytic activation by prothrombinase.
4 le for the enhanced procoagulant function of prothrombinase.
5 bin kinetics was determined predominantly by prothrombinase.
6 es the sequential cleavage of prothrombin by prothrombinase.
7 nt docking of Arg(271) at the active site of prothrombinase.
8 ding a recognition site for factor Va within prothrombinase.
9 a detectable way to the enhanced function of prothrombinase.
10 pending on the incorporation of factor Va in prothrombinase.
11 r Va molecule with the various components of prothrombinase.
12 he mechanism of activation of prothrombin by prothrombinase.
13 ffectively unaltered following assembly into prothrombinase.
14 cturally conserved residues in factor Xa and prothrombinase.
15 ane-bound procoagulant complexes, tenase and prothrombinase.
16 or V derivatives to assemble and function in prothrombinase.
17 one of two conformations to a single form of prothrombinase.
18 on of substrate derivatives and product with prothrombinase.
19 serine and inhibit the enzymatic activity of prothrombinase.
20 e of Oregon Green(488) at the active site of prothrombinase.
21 both possible intermediates, or product with prothrombinase.
22 s to bind in a mutually exclusive fashion to prothrombinase.
23 e with the incorporation of prothrombin into prothrombinase.
24 contribution of factor Va to the activity of prothrombinase.
25 nor does it fully explain the specificity of prothrombinase.
26 tor Xa or factor Xa saturably assembled into prothrombinase.
27 iants that could be converted to thrombin by prothrombinase.
28 eceding the scissile bond to the function of prothrombinase.
29 te-mediated protein substrate recognition by prothrombinase.
30 ulation zymogen not known to be activated by prothrombinase.
31 haBFX-2b bind in a mutually exclusive way to prothrombinase.
32 (AP4') was found to be a potent inhibitor of prothrombinase.
33 dent recognition of the protein substrate by prothrombinase.
34 oes not interfere with the assembly of human prothrombinase.
35 on of physiologically relevant inhibition of prothrombinase.
36 Va and/or prothrombin recognition by FXa in prothrombinase.
37 ability to accelerate thrombin production by prothrombinase.
38 rate at which it is converted to thrombin by prothrombinase.
39 on of the rate of cleavage of prothrombin by prothrombinase.
40 FII) is activated to alpha-thrombin (IIa) by prothrombinase.
41 for the strong procoagulant nature of venom prothrombinase.
42 s between the proteinase and cofactor within prothrombinase.
43 te of cleavage of prothrombin at Arg(271) by prothrombinase.
44 335) is required for the optimal activity of prothrombinase.
45 n the timely formation of alpha-thrombin via prothrombinase, a Ca(2+)-dependent complex of factors Va
46 ade, prothrombin is converted to thrombin by prothrombinase, a complex consisting of serine protease
48 se findings suggest that platelet-associated prothrombinase activates prothrombin via an efficient co
49 ested that although the peptide inhibits the prothrombinase activation of the wild type zymogen with
51 sistent with its activity, Alboserpin blocks prothrombinase activity and increases both prothrombin t
54 re deficient in IQGAP1 demonstrate increased prothrombinase activity compared with wild-type litterma
56 centration of 20 microM but had no effect on prothrombinase activity in the presence of excess factor
59 tant factor Va are required for half-maximal prothrombinase activity on membranes containing 25% PS.
61 of factor Va (P15H) had no effect on either prothrombinase activity or the ability of the cofactor t
65 252C) potently inhibited plasma clotting and prothrombinase activity with 50% inhibition between 41 a
67 -704), were found to be potent inhibitors of prothrombinase activity with IC(50) values of approximat
68 I, induces platelet aggregation and platelet prothrombinase activity, and binds uniquely to GPVI in l
70 otently inhibited plasma clotting assays and prothrombinase activity, with 50% inhibition of 12 and 1
79 n of prothrombin to thrombin is catalyzed by prothrombinase, an enzyme complex composed of the serine
80 ity binding and function of factor Xa within prothrombinase and 2) a binding site for prothrombin is
81 exosite-dependent tethering of substrate to prothrombinase and a relaxation in the constrained prese
82 Va heavy chain to factor Xa activity within prothrombinase and demonstrate that amino acid region 65
84 f factor Xa (FXa) with factor Va (FVa) forms prothrombinase and drives thrombin formation essential f
85 hat is modulated following its assembly into prothrombinase and in turn determines the binding specif
86 al cells can support formation of tenase and prothrombinase and may be a source of activated tissue f
87 Therefore, extended interactions between prothrombinase and substrate regions removed from the cl
88 s a prototypic exosite-directed inhibitor of prothrombinase and suggest that the occlusion of a surfa
89 actadherin was an efficient inhibitor of the prothrombinase and the factor Xase complexes regardless
90 ns and interactions with other components of prothrombinase, and (d) to use the model in order to und
91 x activates ProT with K(m)((app)) similar to prothrombinase, and approximately 85-fold weaker without
92 en activation when both extrinsic tenase and prothrombinase are assembled on an appropriate membrane.
93 es (exosites) rather than the active site of prothrombinase are the principal determinants of binding
95 croparticles were isolated and quantified by prothrombinase assay at admission, day 3, and day 7.
96 ibited a near normal affinity for fVa in the prothrombinase assay, but a markedly lower affinity for
97 atelet factor 3 availability assay and, in a prothrombinase assay, generated only background levels o
100 tent correlated positively with PS-direct in prothrombinase assays and clotting assays, but APC-cofac
103 on when Gla-domainless factor Xa was used in prothrombinase assays, whereas sphingosine inhibited act
104 I does not inhibit prothrombin activation by prothrombinase assembled on a two-dimensional lipid bila
105 Extension of these findings to the action of prothrombinase assembled on platelets and endothelial ce
107 a potent inhibitor of thrombin generation by prothrombinase assembled with C6PS, while TFPI-160 and K
108 ant molecules were impaired and the k cat of prothrombinase assembled with factor Va (KF) and factor
112 n approximately 39% increase in k cat, while prothrombinase assembled with factor Va(4A) exhibited an
113 y employing purified reagents, we found that prothrombinase assembled with factor Va(Delta680-709) di
114 tivation compared to the value obtained with prothrombinase assembled with factor Va(Wt), while proth
120 ombinase assembled with factor Va(Wt), while prothrombinase assembled with saturating concentrations
122 of plasma-derived prothrombin at Arg320 than prothrombinase assembled with saturating concentrations
123 for the overall activation of prothrombin by prothrombinase assembled with saturating concentrations
125 phoresis analyzing prothrombin activation by prothrombinase assembled with the mutant molecules revea
126 prothrombin at both Arg(320) and Arg(271) by prothrombinase assembled with the mutant molecules, resu
128 via a concerted mechanism through a study of prothrombinase assembly and function on collagen-adhered
130 ssays, representing inhibition of productive prothrombinase assembly and possible disruption of FXa i
132 f phospholipid-associated factor Xa prior to prothrombinase assembly and/or by slowing formation of t
142 al for coordinated prothrombin activation by prothrombinase because it regulates meizothrombin cleava
143 These data suggest that the peptides inhibit prothrombinase because they interfere with the incorpora
144 the affinity of the wild type substrate for prothrombinase but did not engage the active site of the
145 n (DYDYQ) inhibits prothrombin activation by prothrombinase by inhibiting meizothrombin generation.
146 Similar analyses of the inhibition of human prothrombinase by PD0313052 also identified a slow-onset
149 e individual cleavage reactions catalyzed by prothrombinase by using a series of recombinant derivati
150 us, the observed pathway of bond cleavage by prothrombinase can be explained by the kinetic constants
151 er, mutation of Arg(320) to Gln reveals that prothrombinase can cleave prothrombin following Arg side
154 n activated platelets with factor Va to form prothrombinase completely restores biologic activity.
155 antithrombin inhibition of factor Xa in the prothrombinase complex (factor Va, negatively charged me
156 tivation of prothrombin, as catalyzed by the prothrombinase complex (factor X(a), enzyme; factor V(a)
157 prothrombin recognition by factor Xa in the prothrombinase complex (factor Xa, factor Va, phosphatid
158 The central findings are as follows: 1) the prothrombinase complex (fVa-fXa-Ca(2+)-membrane) accumul
159 nd prothrombin (fII) that may be involved in prothrombinase complex (fXa.factor Va.fII.phospholipids)
160 y sequences in prothrombin (fII) involved in prothrombinase complex (fXa.fVa.fII.phospholipids) assem
162 vivo is the activation of prothrombin by the prothrombinase complex assembled on either an activated
165 iding the necessary procoagulant surface for prothrombinase complex assembly and thrombin generation.
167 nes support formation of a 60-70% functional prothrombinase complex at saturating factor Va concentra
168 = approximately 40 nm) of a partially active prothrombinase complex between factor Xa and factor Va(2
171 thrombin is proteolytically activated by the prothrombinase complex comprising the serine protease Fa
175 a, either in free form or assembled into the prothrombinase complex during the process of prothrombin
176 m spontaneous binding to fXa and unnecessary prothrombinase complex formation, which in turn results
177 avage of prothrombin (ProT) at Arg320 by the prothrombinase complex generates proteolytically active,
178 ts to determine the crystal structure of the prothrombinase complex have been thwarted by the depende
179 and that a cofactor function for fVa in the prothrombinase complex involves inducing a conformationa
180 enzyme activated factor X (FXa) to form the prothrombinase complex is a pivotal initial event in blo
182 ht heparins, indicates that factor Xa in the prothrombinase complex is protected from inhibition by a
183 undation for the establishment of a complete prothrombinase complex model, which might be successful
184 rsion of fII to alpha-thrombin (fIIa) by the prothrombinase complex occurs through 2 parallel pathway
185 pt that protein substrate recognition by the prothrombinase complex of coagulation is achieved by int
187 blocking phospholipid binding sites for the prothrombinase complex on the surfaces of vesicles and a
190 soluble PS to trigger formation of a soluble prothrombinase complex suggests that exposure of PS mole
191 sis, factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold in
192 espect to their ability to assemble into the prothrombinase complex to activate prothrombin and inter
193 ns prothrombin and prethrombin-2 require the prothrombinase complex to be converted to the mature pro
194 lex and then to function as an enzyme in the prothrombinase complex to catalyze the conversion of pro
195 ant substrates; however, its activity in the prothrombinase complex toward most of mutants was severe
196 e-exposed phosphatidylserine (PS) forms the "prothrombinase complex" that is essential for efficient
200 ts or endothelial cells, factor Xa forms the prothrombinase complex, which is responsible for the pro
201 d Partial Thromboplastin Time'' (aPTT) and ''Prothrombinase complex-induced Clotting Test'' (PiCT) ha
202 t into the architecture and mechanism of the prothrombinase complex-the molecular engine of blood coa
220 dent recognition site for prothrombin in the prothrombinase complex; however, Lys-96 is a recognition
223 f prothrombin to thrombin is catalyzed by a "prothrombinase" complex, traditionally viewed as factor
225 ide a surface for assembly of the tenase and prothrombinase complexes required for thrombin generatio
228 cket indicate that assembly of the mutant in prothrombinase corrected the impaired binding of these p
229 lpha produces isoform-specific inhibition of prothrombinase during the initiation of coagulation, an
230 r interactions that underlie the assembly of prothrombinase, efficient inhibition of enzyme complex a
232 Exosite-dependent binding of prothrombin to prothrombinase facilitates active site docking by Arg(32
233 intrinsic tenase (factor VIIIa/factor IXa), prothrombinase (factor Va/factor Xa), and factor XIa com
234 Because all three protein components of prothrombinase, factors (f) Xa and Va and prothrombin, b
235 irudin, or CD39, or lacking the gene for the prothrombinase, fibrinogen-like protein-2, is anticipate
237 milieu already containing factor Xa enables prothrombinase formation with consequent meizothrombin f
238 cells, whereas TFPIalpha dampens the initial prothrombinase formed on the activated platelet surface.
239 ntapeptide with this sequence inhibited both prothrombinase function with an IC(50) of 1.6 microm (wi
243 n, DYDYQ) inhibits prothrombin activation by prothrombinase in a competitive manner with respect to s
244 (2K2F) had impaired cofactor activity within prothrombinase in a system using purified reagents.
245 teolyzed prothrombin species by preassembled prothrombinase in phospholipid-coated glass capillaries
246 ation of the incorporation of factor Va into prothrombinase in vivo by using synthetic peptides that
250 s thrombin is known to bind to an exosite on prothrombinase, initial interactions at an exosite likel
251 ferred pathway for prothrombin activation by prothrombinase involves initial cleavage at Arg(320) to
253 tivation of prothrombin by surface-localized prothrombinase is clearly mediated by flow-induced dilut
256 Tris(+) and that the catalytic efficiency of prothrombinase is enhanced less than 1.5-fold by the spe
257 ontributes to enhanced catalytic efficacy of prothrombinase is not precisely known but is generally a
258 n of all three possible substrate species by prothrombinase is regulated by their ability to bind mem
260 ce this modified derivative was assembled in prothrombinase, it functioned in an equivalent manner to
262 complexes of the intrinsic pathway, Xase and prothrombinase, leading to a 20- and 10-fold increase in
263 r rate over preassembled platelet-associated prothrombinase neither potential intermediate, meizothro
265 e for cleavage, yet the sequential action of prothrombinase on Arg(320) followed by Arg(271) is impli
266 of the fVa-dependent site(s) for fXa within prothrombinase on FII, required for efficient initial cl
268 specificity as well as the ordered action of prothrombinase on its compound substrate is regulated by
269 hrombin is produced by the ordered action of prothrombinase on two cleavage sites in prothrombin.
270 te directed inhibitor of human factor Xa and prothrombinase, PD0313052, and identifies structurally c
272 ork tests whether or not platelet-associated prothrombinase proceeds via a concerted mechanism throug
274 actor Xa with factor Va on membranes to form prothrombinase profoundly increases the rate of the prot
275 rate of 83.9 +/- 3.8 nM/min by about 120 pM prothrombinase, reaching ultimate levels of 851 +/- 53 n
276 ipids, the exact role of the membrane in the prothrombinase reaction has not been fully understood.
277 n are part of a cooperative mechanism within prothrombinase regulating cleavage and activation of pro
278 on of the cofactor molecule, factor Va, into prothrombinase results in a five orders of magnitude inc
279 hus, alphaBFX-2b binding to factor Xa within prothrombinase selectively leads to the inhibition of pr
282 actor Xa is the serine protease component of prothrombinase, the enzymatic complex responsible for th
284 local electrostatic potential then redirects prothrombinase toward Arg-320, leading to thrombin gener
287 (S195A), the pathway of FPR-ProT cleavage by prothrombinase was redirected from meizothrombin toward
288 n with the factor Xa variants assembled into prothrombinase was unaltered, whereas the k(cat) was mod
290 meizothrombin des fragment 1 and thrombin to prothrombinase were comparable with their affinities inf
291 factor Va governing its incorporation within prothrombinase will provide the scaffold for the synthes
292 actor Va binding to any of the components of prothrombinase, will allow for control of the rate of th
293 at HC3 and HC4 are competitive inhibitors of prothrombinase with respect to prothrombin with K(i) val
294 d that AP4' is a noncompetitive inhibitor of prothrombinase with respect to prothrombin, with a K(i)
296 trate cleavage by human Xa incorporated into prothrombinase with saturating concentrations of membran
297 of plasma-derived prothrombin activation by prothrombinase, with increasing concentrations of peptid
298 fVa-dependent recognition exosite for fXa in prothrombinase within the amino acid sequence Ser(478)-V
299 7t) inhibits thrombin formation catalyzed by prothrombinase without obscuring the active site of Xa w
300 .93 +/- 0.3 nM/min catalyzed by about 1.3 pM prothrombinase yielding approximately 26 nM thrombin.
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