ライフサイエンスコーパス: prothrombin

1 gle-1 to kringle-2 in the coagulation factor prothrombin.

2 eletion in the kringle 1 domain of zebrafish prothrombin.

3 activation and conformational plasticity of prothrombin.

4 ic or pharmacologic reduction of circulating prothrombin.

5 domain determine the functional behavior of prothrombin.

6 m a staphylothrombin complex upon binding to prothrombin.

7 ciate with, and non-proteolytically activate prothrombin.

8 [TF]-FVII) coagulation pathways, as well as prothrombin.

9 n of prothrombinase on two cleavage sites in prothrombin.

10 of an index case with factor V Leiden or the prothrombin 20210A gene variant, the presence of these a

11 The factors studied were prothrombin, activated factor VII, factor IX, factor X,

12 s N-terminal half, inhibited myosin-enhanced prothrombin activation (50% inhibition at 1.2 mum).

13 apedesis/adhesion, Fc macrophage activation, prothrombin activation and hepatic stellate cell activat

14 propiece plays essential roles in regulating prothrombin activation and proteinase function.

15 In FXa-catalyzed prothrombin activation assays, both FV and FV(DeltaIIa)

16 avy chain strongly inhibited myosin-enhanced prothrombin activation by factors Xa and Va (50% inhibit

17 The rate of prothrombin activation by vWbp(1-263) is controlled by a

18 Prothrombin activation can proceed through the intermedi

19 A molecular mechanism of prothrombin activation emerges from the structure.

20 Changes in plasma levels of thrombin, prothrombin activation fragment 1+2 (F1+2), TAT (thrombi

21 ributions that these 2 intermediates make to prothrombin activation in tissue factor (Tf)-activated b

22 critical length of 15 residues, the rate of prothrombin activation increases (10-fold) in the absenc

23 ssembled on synthetic phospholipid vesicles, prothrombin activation proceeds with an initial cleavage

24 ariants of meizothrombin, an intermediate of prothrombin activation that contains the propiece covale

25 ed blood, producing a membrane that supports prothrombin activation through the meizothrombin pathway

26 When prothrombin activation was monitored at a typical venous

27 e role of this flexibility in the context of prothrombin activation was tested with several deletions

28 These findings support a molecular model of prothrombin activation where Lnk2 presents the sites of

29 6-837) did not inhibit phospholipid-enhanced prothrombin activation, indicating its specificity for i

30 ermediates from the two possible pathways of prothrombin activation.

31 pathophysiologic conditions characterized by prothrombin activation.

32 echanistic basis for its accumulation during prothrombin activation.

33 es were contributing to approximately 35% of prothrombin activation.

34 id not inhibit phospholipid vesicle-enhanced prothrombin activation.

35 inhibitor of prothrombinase-bound FXa during prothrombin activation.

36 osin's neck region inhibits myosin-dependent prothrombin activation.

37 fect of adding a CD14 inhibitor to attenuate prothrombin activation.

38 lation by protein protease inhibitors during prothrombin activation.

39 agulation factors Xa and Va and accelerating prothrombin activation.

40 screened for inhibition of myosin-supported prothrombin activation.

41 ctor V-like, homologous subunit (Pt-FV) of a prothrombin activator from Pseudonaja textilis venom is

42 Rather, the bacteria-derived prothrombin activator vWbp was identified as the source

43 in-ICU death was positively associated with prothrombin activity less than 70% and negatively associ

44 oratory features selected in the model were: prothrombin activity, urea, white blood cell, interleuki

45 platelet and fibrinogen levels and increased prothrombin and activated partial thromboplastin times a

46 G20210A prothrombin and factor V gene mutations were assessed in

47 Finally, we present steady-state models of prothrombin and factor X activation under flow showing t

48 When prothrombin and factor X are activated coincident with e

49 dary progressive MS had significantly higher prothrombin and factor X levels than healthy donors, whe

50 ), which, following an association with host prothrombin and fibrinogen, form fibrin clots and enable

51 nd factor XIII, whereas Coa co-purified with prothrombin and fibrinogen.

52 ctor-binding protein (vWbp) to activate host prothrombin and form fibrin cables, thereby promoting th

53 cretes coagulase (Coa), which activates host prothrombin and generates fibrin fibrils that protect th

54 In the blood, the zymogens prothrombin and prethrombin-2 require the prothrombinase

55 ause both metrics are strongly determined by prothrombin and prothrombin levels are considerably lowe

56 e substrate binding channel on fVa, to which prothrombin and the intermediate meizothrombin bind in 2

57 The three-dimensional architecture of prothrombin and the molecular basis of its activation re

58 d factor XIII, but not fibronectin, required prothrombin and triggered the non-proteolytic activation

59 family with a bleeding diathesis, prolonged prothrombin, and activated partial thromboplastin times,

60 tures composed only of factor Xa, factor Va, prothrombin, and calcium ions, myosin greatly enhanced p

61 ding factors IXa (FIXa), FXa/FX, FVa, FVIII, prothrombin, and PS-sensitive marker Annexin V were dist

62 with and activate the host hemostatic factor prothrombin, and the bacterial surface display of agglut

63 m through tumor cell-derived TF, circulating prothrombin, and tumor cell-derived PAR-1 and further in

64 report the first x-ray crystal structure of prothrombin as a Gla-domainless construct carrying an Al

65 o thrombin exosite II and has no affinity to prothrombin at all.

66 Burial of Arg-320 prevents prothrombin autoactivation and directs prothrombinase to

67 Prothrombin autoactivation induced by histone H4 emerges

68 Whether prothrombin autoactivation occurs in the wild-type under

69 ostatic activity in neonates is due to lower prothrombin availability.

70 overned by a differential ability to support prothrombin binding and the variable accumulation of int

71 hat antibodies directed against the variable prothrombin binding portion of coagulases confer type-sp

72 ative selection, the coding sequence for the prothrombin-binding D1-D2 domain is highly variable and

73 in the rate of thrombin formation for desGla prothrombin but with a major effect on the pathway for s

74 ade where cofactor Va enhances activation of prothrombin by factor Xa by compressing Lnk2 and morphin

75 The present study evaluates activation of prothrombin by full-length vWbp(1-474) through activity

76 framework for the mechanism of activation of prothrombin by prothrombinase.

77 Perturbation of prothrombin by selective removal of its constituent Gla

78 Although the activation of prothrombin by surface-localized prothrombinase is clear

79 alpha-thrombin in vivo is the activation of prothrombin by the prothrombinase complex assembled on e

80 ains in the pathophysiological activation of prothrombin by vWbp, and may reveal a function for autoc

81 ere we report how key structural features of prothrombin can be monitored by limited proteolysis with

82 ogenous fII gene, resulting in expression of prothrombin carrying 3 amino acid substitutions (R157A,

83 the NH(2)-terminal residues of vWbp into the prothrombin catalytic domain.

84 was required for a significantly attenuated prothrombin cleavage (72%, p < 0.05).

85 nt is evident as a switch in the pathway for prothrombin cleavage and the intermediate produced but w

86 Among the two conformations of prothrombin, collapsed and fully extended, histone H4 bi

87 nical trial to compare nonactivated 4-factor prothrombin complex concentrate (4F-PCC) with plasma for

88 pared the efficacy and safety of four-factor prothrombin complex concentrate (4F-PCC) with that of pl

89 measures and biomarkers by using a 4-factor prothrombin complex concentrate (4F-PCC).

90 efficacy of fresh frozen plasma (FFP) versus prothrombin complex concentrate (PCC) in patients with V

91 actice include fresh frozen plasma (FFP) and prothrombin complex concentrate (PCC).

92 therapies that promote formation of fibrin (prothrombin complex concentrate [PCC], activated PCC [aP

93 BEST PRACTICE ADVICE 7: The 4-factor prothrombin complex concentrate contains both pro- and a

94 ecombinant activated factor VII or activated prothrombin complex concentrate did not alter the delaye

95 rventional treatment was needed in 37.8% and prothrombin complex concentrate in 9.1%.

96 circumstances, avoiding the use of plasma or prothrombin complex concentrate in the nonemergent rever

97 rgent reversal with frozen plasma versus the prothrombin complex concentrate Octaplex.

98 ntial hematoma expansion (43% [12 of 28] for prothrombin complex concentrate vs 29% [5 of 17] for no

99 ng administration of hemostatic factors (eg, prothrombin complex concentrate), were left to the discr

100 ntial ability of a low dose of the activated prothrombin complex concentrate, FEIBA, to reestablish h

101 complex concentrate vs 29% [5 of 17] for no prothrombin complex concentrate, P = .53), or on the occ

102 agents with a fast onset of action, such as prothrombin complex concentrate, recombinant factor VIIa

103 pplied to guide the dosing of fibrinogen and prothrombin complex concentrate, which are selectively u

104 all, 57% (35 of 61) of the patients received prothrombin complex concentrate, with no statistically s

105 rfarin anticoagulation with frozen plasma or prothrombin complex concentrate.

106 Prothrombin complex concentrates (PCC) are fractionated

107 romboembolic events in patients treated with prothrombin complex concentrates (PCCs) for the manageme

108 Multiple guidelines suggest using prothrombin complex concentrates (PCCs) in these patient

109 Nonspecific hemostatic agents such as prothrombin complex concentrates and recombinant factor

110 Recombinant factor VIIa and activated prothrombin complex concentrates are similarly effective

111 tients with FII or FV deficiencies, for whom prothrombin complex concentrates or fresh frozen plasma

112 of coagulation factors (fresh frozen plasma, prothrombin complex concentrates or recombinant activate

113 r hemostasis with antifibrinolytic agents or prothrombin complex concentrates, which are widely avail

114 eal a function for autocatalysis of the vWbp.prothrombin complexes during initiation of blood coagula

115 rol, n = 1), bolus administration of a human prothrombin concentrate complex (hPCC; 2.5 mL/kg, n = 2)

116 Prothrombin concentrate may be considered in life-threat

117 Mice with a genetic deficit in prothrombin confirmed the specificity of the thrombin pr

118 normal clotting times, but markedly reduced prothrombin consumption.

119 re used to directly test the hypothesis that prothrombin contributes to tumor development in colitis-

120 as strongly inferred by the observation that prothrombin deficiency dramatically reduced the formatio

121 were compared by equilibrium binding to the prothrombin derivatives prethrombin 1, prethrombin 2, th

122 Active site labeling of all prothrombin derivatives with D-Phe-Pro-Arg-chloromethyl

123 The results suggest a role for prothrombin domains in the pathophysiological activation

124 findings confirm the molecular plasticity of prothrombin emerged from recent structural studies and s

125 Human prothrombin engineered with the equivalent mutation exhi

126 Prothrombin exists in equilibrium between two alternativ

127 re obtained with pharmacologic inhibition of prothrombin expression or inhibition of thrombin proteol

128 Reduced prothrombin expression was associated with lower mitotic

129 No significant increase in prothrombin F1 + 2 was noted during NMP.

130 To explore the hypothesis that reduced prothrombin (factor II [FII]) levels in SCD will limit v

131 The deficiency of fibrinogen, prothrombin, factor V (FV), FVII, FVIII, FIX, FX, FXI, a

132 irect comparison of the binding constants of prothrombin, factor X, activated factor VII, and activat

133 Prothrombin features a conformation 80 A long, with frag

134 vWbp bound to prothrombin, fibrinogen, fibronectin, and factor XIII, w

135 ligonucleotide (ASO-CON) or ASO specific for prothrombin (FII) (ASO-FII) to yield mFFP or ASO-CON mFF

136 Prothrombin (FII) is activated to alpha-thrombin (IIa) b

137 mbin is produced from the C-terminal half of prothrombin following its proteolytic activation.

138 thrombin generation in vivo), tissue factor, prothrombin fragment 1 + 2 (F1+2), and normalized APC se

139 rin on population pharmacokinetics, D-dimer, prothrombin fragment 1 + 2 (PF1+2), and clinical outcome

140 e- and concentration-dependent generation of prothrombin fragment 1+2 (PTF1.2), tissue factor (TF) mR

141 F1+2 (prothrombin fragment 1+2) and TAT (thrombin-antithrombin

142 and future VTE have been found for d-dimer, prothrombin fragment 1+2, and soluble P-selectin and als

143 extracorporeal membrane oxygenation therapy, prothrombin fragment 1.2 (F1.2) (1.36-2.4 microM), throm

144 steadily increased with increasing baseline prothrombin fragment 1.2 and thrombin-antithrombin compl

145 lower or negligible with increasing baseline prothrombin fragment 1.2 and thrombin-antithrombin compl

146 re greater in subgroups with higher baseline prothrombin fragment 1.2 or thrombin-antithrombin comple

147 ligand), coagulation activation/inhibition (prothrombin fragment 1.2, thrombin/antithrombin complex,

148 Concentration of prothrombin fragment F1 + 2 (marker of coagulation activ

149 Levels of prothrombin fragment F1 + 2 (P = 0.031) and D-dimers (P

150 The PAI-1/tPA complexes, D-dimers, and prothrombin fragment F1 + 2 were measured in plasma samp

151 , as reflected by lower plasma levels of the prothrombin fragment F1+2 (mean peak levels 57.9% [p<0.0

152 or necrosis factor receptor-1), coagulation (prothrombin fragment F1+2 and d-dimer), and endothelial

153 d-dimer, prothrombin fragment F1.2 and TATc concentrations were l

154 transient increases in levels of d-dimer and prothrombin fragments 1 and 2 were observed, which resol

155 Omission of prothrombin from 4F-VKDP significantly reduced its abili

156 ortant new details on the molecular basis of prothrombin function.

157 f human vitamin K-dependent proteins (VKDP) (prothrombin, FVII, FIX, or FX), or purified single human

158 lasma was associated with the recruitment of prothrombin, FXIII, and fibronectin as well as the forma

159 bophilic defects, including factor V Leiden, prothrombin G20210A defect, and deficiencies of the natu

160 the established factor V Leiden p.R506Q and prothrombin G20210A mutations.

161 homozygous FVL; 0.6% (0.4%) for heterozygous prothrombin G20210A; 8.2% (5.5%) for compound heterozygo

162 5.5%) for compound heterozygotes for FVL and prothrombin G20210A; 9.0% (6.1%) for antithrombin defici

163 The coagulation factor prothrombin has a complex spatial organization of its mo

164 te deficiency of the central clotting enzyme prothrombin has never been observed in humans and is inc

165 Prothrombin has three linkers connecting the N-terminal

166 profound contribution of membrane binding by prothrombin in determining the rate at which it is conve

167 posing a modest 50% reduction in circulating prothrombin in fII+/- mice, a level that carries no sign

168 cologic reduction of the coagulation zymogen prothrombin in mice.

169 details on the conformational plasticity of prothrombin in solution and the drastic structural diffe

170 er to access the conformational landscape of prothrombin in solution and uncover structural features

171 rements detect two distinct conformations of prothrombin in solution, in a 3:2 ratio, with the distan

172 tivated partial thromboplastin time (but not prothrombin index) differed significantly between cirrho

173 Platelets, fibrinogen, prothrombin index, activated partial thromboplastin time

174 based on platelets, fibrinogen, d-dimer, and prothrombin index.

175 ransferase and alanine aminotransferase, and prothrombin international normalized ratio; LR, 0.09; 95

176 y factor Xa by compressing Lnk2 and morphing prothrombin into a conformation similar to the structure

177 Taken together, these data establish that prothrombin is a powerful modifier of SCD-induced end-or

178 of cofactor Va and offers insights into how prothrombin is activated at the molecular level.

179 n important physiological role for Lnk2 when prothrombin is anchored to the membrane.

180 The zymogen prothrombin is composed of fragment 1 containing a Gla d

181 Prothrombin is conformationally activated by von Willebr

182 That prothrombin is linked to early events in CAC was strongl

183 The zymogen prothrombin is proteolytically converted by factor Xa to

184 Prothrombin is the dominant procoagulant component of PC

185 Two new crystal structures of prothrombin lacking 22 (ProTDelta146-167) or 14 (ProTDel

186 rethrombin-2 into the conventional assay for prothrombin level in human plasma, employing ecarin and

187 s are strongly determined by prothrombin and prothrombin levels are considerably lower in neonates we

188 olitis showed that mice carrying half-normal prothrombin levels were comparable to control mice in mu

189 risk of clotting based on their circulating prothrombin levels, and to guide the development of futu

190 lood clot severity may depend on circulating prothrombin levels.

191 mains in protein C as opposed to kringles in prothrombin likely accounts for the different conformati

192 , hepatic encephalopathy, variceal bleeding, prothrombin <45%, serum bilirubin >45 mumol/L, albumin <

193 rovide insight into the role of kringle 1 in prothrombin maturation and activity.

194 ts for kringle-1 relative to the rest of the prothrombin molecule.

195 otease thrombin, which is unable to activate prothrombin or prethrombin-2.

196 Prothrombin, or coagulation factor II, is a multidomain

197 -levels of intraclot thrombin suggest robust prothrombin penetration into clots.

198 ctive vitamin K-dependent MGP (dp-ucMGP) and prothrombin (PIVKA-II) were measured, inversely related

199 w the complex assembles and its mechanism of prothrombin processing are of central importance to huma

200 Notecarin D (NotD) is a prothrombin (ProT) activator in the venom of the tiger s

201 hylocoagulase (SC), thereby activating human prothrombin (ProT) and evading immune clearance.

202 e factor Xa (FXa)-mediated conversion of the prothrombin (ProT) zymogen to active alpha-thrombin (alp

203 ceptor (MCSFR), paraoxonase 1 (normalized to prothrombin protein), and leukocyte cell-derived chemota

204 gam et al report that long-term reduction of prothrombin (PT) expression results in diminished vascul

205 (Gla) domain, a calcium-binding module, and prothrombin (PT) was the most abundant.

206 atives with factor V Leiden (FVL) or G20210A prothrombin (PT20210A) gene polymorphisms may differ acc

207 .8% vs 20% vs 20.9%; p = 0.003) and the mean prothrombin ratio (86.3 vs 61.6 vs 67.1; p = 0.003).

208 strengthened the initial binding of vWbp to prothrombin, resulting in higher activity and an approxi

209 and endothelial cells on fully carboxylated prothrombin reveals new mechanistic insights into functi

210 PCC or four factor- (4F-) VKDP or prothrombin significantly reduced bleeding from TT or LL

211 cular species such as the thrombin precursor prothrombin, thrombin in complex with some of its natura

212 rum albumin level, 2.58 g/dL), coagulopathy (prothrombin time > 20 s compared with that of a normal c

213 fined according to the "50-50 criteria" (ie, prothrombin time <50% and serum bilirubin >50 micromol/L

214 /= 127 g/L; odds ratio, 0.99; p < 0.01), and prothrombin time (</= 58%; odds ratio, 0.98; p < 0.05) w

215 irect bilirubin (0.13 versus 0.1, P = 0.01), prothrombin time (14.4 versus 12.4, P = 0.002), and AST-

216 nd 2.3 [0.8-8.7] microg/mL, p = .05), longer prothrombin time (19.3 [15.4-25.9] vs. 15.3 [14.8-17.1],

217 ody mass index (HR 1.40; 95% CI: 1.01-1.95), prothrombin time (HR 0.79; 95% CI: 0.70-0.90), serum alb

218 We analyzed altered prothrombin time (measured as international normalized r

219 0.0001), alkaline phosphatase (P = 0.0009), prothrombin time (P = 0.0005), and maximal vital capacit

220 h baseline esophageal varices (P = 0.01) and prothrombin time (P = 0.002), but not with disease progr

221 Coagulation studies revealed prothrombin time (PT) 13.5 seconds, internationalized no

222 The low hemolysis of 2.39% with short prothrombin time (PT) and activated partial thromboplast

223 Increases in prothrombin time (PT) and international normalised ratio

224 Prothrombin time (PT) and the associated international n

225 vated partial thromboplastin time (aPTT) and prothrombin time (PT) are clinical tests commonly used t

226 vated partial thromboplastin time (APTT) and prothrombin time (PT) are less sensitive and may be norm

227 neral overview of the plasmatic coagulation, prothrombin time (PT) tests are frequently combined with

228 ortable testing of blood coagulation time or prothrombin time (PT).

229 e (MA), LY30] with their corresponding CCTs [prothrombin time (PT)/activated partial thromboplastin t

230 thod affected only by factors II and X (Fiix-prothrombin time [Fiix-PT]) compared with standard PT-IN

231 Knockout FVII mice demonstrated a delayed prothrombin time and decreased plasma FVII expression.

232 varices demonstrated a significantly longer prothrombin time and lower platelet count, there was no

233 d patients had more severe injury, prolonged prothrombin time and partial thromboplastin time (PTT),

234 er 90%, whereas fVII knockdown prolonged the prothrombin time and reduced fVII activity to a similar

235 inverse correlation with platelet count and prothrombin time but not with serum albumin level.

236 r months to years, to maintain a near-normal prothrombin time can reverse the coagulopathy associated

237 ed activated partial thromboplastin time and prothrombin time clotting times to baseline at 60 mins.

238 f seven serine proteases, and FVII-deficient prothrombin time EC2x = 1.2 muM.

239 markers for liver function are bilirubin and prothrombin time expressed as International Normalized R

240 s thrombin potential and partial reversal of prothrombin time following 50 IU/kg.

241 el greater than or equal to 250 mumol/L, and prothrombin time greater than or equal to 30 seconds was

242 ma activated partial thromboplastin time and prothrombin time increased over 10-fold during the bleed

243 owed that patient age older than 65 years, a prothrombin time international normalized ratio greater

244 rinogen, activated partial prothrombin time, prothrombin time international normalized ratio, D-dimer

245 e influence of several anticoagulants on the prothrombin time limits its diagnostic value.

246 rtate aminotransferase, cholinesterases, and prothrombin time not differed in 2 groups.

247 hromboplastin time of 49.2 seconds, a normal prothrombin time of 12.4 seconds, and a platelet count o

248 lation panel was unremarkable and included a prothrombin time of 15.4 seconds, an international norma

249 national normalized ratio of more than 11, a prothrombin time of more than 120 seconds, and an activa

250 times are best suited for dabigatran and the prothrombin time or the anti-FXa for rivaroxaban.

251 emia, renal insufficiency, hyponatremia, and prothrombin time prolongation (all P < 0.001).

252 Baseline prothrombin time was 28+/-0.8 secs (n=8) and followed a

253 Mean prothrombin time was shorter in arterial strokes (P < .0

254 Effects on prothrombin time were partially reversed at 50 IU/kg.

255 clotting test with the quick clotting time (prothrombin time), it was possible to diagnose factor VI

256 thological grades, total bilirubin, albumin, prothrombin time, alpha-fetoprotein, and tumor number, w

257 orts, activated partial thromboplastin time, prothrombin time, and deep vein thrombosis.

258 , D-dimer, alpha-2-antiplasmin, antitrombin, prothrombin time, and platelet count) and the DIC score

259 EVTF activity, fibrinogen, activated partial prothrombin time, D-dimer, tissue plasminogen activator

260 A combination of prothrombin time, endothelium-derived CD105-microparticl

261 survival was independently predicted by PS, prothrombin time, extrahepatic tumor spread, macrovascul

262 Acetazolamide improved prothrombin time, factor X, and antithrombin.

263 had hepatic encephalopathy; median levels of prothrombin time, INR, and total bilirubin were, respect

264 gradation products, whereas abnormalities in prothrombin time, partial thromboplastin time, and plate

265 iabetes mellitus, relative lymphocyte count, prothrombin time, peripheral artery disease, and contral

266 EVTF activity, fibrinogen, activated partial prothrombin time, prothrombin time international normali

267 24.77 vs 73.17 + 53.71 IU/L; P = 0.04), and prothrombin time-international normalized ratio (1.16 +

268 Postoperative serum bilirubin and prothrombin time-international normalized ratio (PT-INR)

269 sferase; POD3 aspartate aminotransferase and prothrombin time-international normalized ratio; postope

270 m: age, Glasgow Coma Scale, base excess, and prothrombin time.

271 ha fetal protein cholesterol, triglycerides, prothrombin time.

272 or Xa inhibitor which has a strong impact on prothrombin time.

273 nogen at the time of surgery, with unchanged prothrombin time.

274 brain "thromboplastic" activity used in the prothrombin time.

275 irubin, albumin, creatinine, and hemoglobin; prothrombin time; and numbers of platelets and white cel

276 th a relatively modest 1.25-fold increase in prothrombin times, and in the absence of hemorrhagic com

277 g activated partial thromboplastin times and prothrombin times.

278 S), binds to discrete sites on FXa, FVa, and prothrombin to alter their conformations, to promote FXa

279 ar-mediated binding to VWF and activation of prothrombin to form S aureus-fibrin-platelet aggregates.

280 secreted coagulase that activates the host's prothrombin to generate fibrin.

281 gnificant flexibility in solution and enable prothrombin to sample alternative conformations.

282 ecent studies have documented the ability of prothrombin to spontaneously convert to the mature prote

283 tion cascade where conversion of the zymogen prothrombin to the protease meizothrombin by the prothro

284 sembled on the surface of platelets converts prothrombin to thrombin by cleaving at Arg-271 and Arg-3

285 (f)Xa and cofactor fVa, efficiently converts prothrombin to thrombin by specific sequential cleavage

286 ere, we report that binding of histone H4 to prothrombin under physiological conditions generates thr

287 uring prothrombinase-catalyzed activation of prothrombin under physiologically relevant conditions.

288 Prothrombin uses the intramolecular collapse of kringle-

289 Using desGla prothrombin variants in which the individual cleavage si

290 the action of prothrombinase on full-length prothrombin variants lacking gamma-carboxyglutamate modi

291 platelet-associated prothrombinase activates prothrombin via an efficient concerted mechanism in whic

292 d show little specificity of interaction for prothrombin vs. thrombin.

293 n exogenous ZPI-PZ complex was added whether prothrombin was activated directly by FXa or through ext

294 In addition to alpha-thrombin enrichment, prothrombin was also efficiently captured from plasma sa

295 In addition, FVII, FIX, FX, and prothrombin were detected by fluorescent microscopy in E

296 TF, FVII, FIX, FX, and prothrombin were detected in ECs, and TF, FVII, FIX, and

297 urther ~3-4-fold when plasma levels of S195A prothrombin were present (k(a) ((app)) 2 x 10(5) m(-1) s

298 y, gene-targeted mice carrying low levels of prothrombin were used to directly test the hypothesis th

299 Small angle x-ray scattering measurements of prothrombin wild type stabilized 70% in the closed confo

300 ons document direct binding of histone H4 to prothrombin with an affinity in the low nm range.