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1 ion in a crystallized form of calcium-bovine prothrombin fragment 1.
2 to 0.30 ng/mL); -0.02 [corrected] nmol/L for prothrombin fragment 1 + 2 (95% CI, -0.03 to 0.01 nmol/L
3 f thrombin: thrombin-antithrombin III (TAT), prothrombin fragment 1 + 2 (F1 + 2), and fibrinopeptide
4 thrombin generation in vivo), tissue factor, prothrombin fragment 1 + 2 (F1+2), and normalized APC se
5 rin on population pharmacokinetics, D-dimer, prothrombin fragment 1 + 2 (PF1+2), and clinical outcome
6                                              Prothrombin fragment 1 + 2 levels also decreased in volu
7 e plasminogen activator antigen, factor VII, prothrombin fragment 1 + 2, urinary fibrinopeptide A, C-
8 ian levels of thrombin-antithrombin complex, prothrombin fragments 1 + 2, and von Willebrand factor a
9 e- and concentration-dependent generation of prothrombin fragment 1+2 (PTF1.2), tissue factor (TF) mR
10                         Thrombin generation (prothrombin fragment 1+2 [F1+2] and thrombin-antithrombi
11 tly increased baseline circulating levels of prothrombin fragment 1+2 and thrombin-antithrombin compl
12                                        F1+2 (prothrombin fragment 1+2) and TAT (thrombin-antithrombin
13  and future VTE have been found for d-dimer, prothrombin fragment 1+2, and soluble P-selectin and als
14  activity and antigen, activated factor XII, prothrombin fragment 1+2, fibrinopeptide A, and fibrinog
15   We analysed concentrations of prothrombin, prothrombin fragment 1+2, thrombin-antithrombin complex,
16 antly higher median plasma concentrations of prothrombin fragment 1+2, tissue plasminogen activator (
17        The primary end points were change in prothrombin fragments 1+2 (F1+2), and anti-factor Xa act
18  terminal complement complex sC5b9 3.6-fold, prothrombin fragments 1+2 (PTF1+2) 25-fold, tissue facto
19 artial thromboplastin and prothrombin times, prothrombin fragments 1+2, fibrinogen, thrombomodulin, p
20  and amyloid-P) and coagulation (D-dimer and prothrombin-fragment 1+2) markers were determined.
21 ecrosis factor-alpha, von Willebrand factor, prothrombin fragment 1-2, D-dimer, and plasmin antiplasm
22 extracorporeal membrane oxygenation therapy, prothrombin fragment 1.2 (F1.2) (1.36-2.4 microM), throm
23 ntithrombin III (TAT) complex formation, and prothrombin fragment 1.2 (F1.2) were measured via commer
24                           We measured plasma prothrombin fragment 1.2 (PF1.2) and p-selectin, fibrino
25  reversed by prothrombin (1-3 microM) and by prothrombin fragment 1.2 (PF1.2), but not by prothrombin
26 ty; thrombin-antithrombin complexes; and the prothrombin fragment 1.2 (PF1.2), which is produced by t
27  steadily increased with increasing baseline prothrombin fragment 1.2 and thrombin-antithrombin compl
28 lower or negligible with increasing baseline prothrombin fragment 1.2 and thrombin-antithrombin compl
29           Tifacogin significantly attenuated prothrombin fragment 1.2 and thrombin:antithrombin compl
30                                              Prothrombin fragment 1.2 increased by 28% (p < 0.02), in
31 re greater in subgroups with higher baseline prothrombin fragment 1.2 or thrombin-antithrombin comple
32                         Thrombin generation (prothrombin fragment 1.2) was evident within 1 h of UFH
33 n generation (thrombin antithrombin complex, prothrombin fragment 1.2), inflammation (C-reactive prot
34  ligand), coagulation activation/inhibition (prothrombin fragment 1.2, thrombin/antithrombin complex,
35 7.6 ng/ml to 33.2 +/- 17.4 ng/ml, p = 0.003; prothrombin fragment 1.2: 95.6 +/- 45.6 micromol/l to 24
36 either treatment changed fibrinopeptide A or prothrombin fragment 1 and 2.
37  significantly greater reduction in D-dimer, prothrombin fragments 1 and 2 (F1 + 2), endogenous throm
38 transient increases in levels of d-dimer and prothrombin fragments 1 and 2 were observed, which resol
39 positions in the crystal structure of bovine prothrombin fragment 1 bound with calcium ions (bf1/Ca).
40                                              Prothrombin fragment 1 is believed to disrupt this react
41  we have evaluated three mechanisms by which prothrombin fragment 1 may inhibit factor X activation.
42                           We have found that prothrombin fragment 1 not only is able to displace fact
43 prothrombin fragment 1.2 (PF1.2), but not by prothrombin fragment 1 (PF1).
44 investigate the binding of the Gla domain of prothrombin fragment 1 (PT1) to anionic lipids in the pr
45                   Factor X, prothrombin, and prothrombin fragment 1 (residues 1-155) were equipotent
46 lapped precisely with the behavior of bovine prothrombin fragment 1 (residues 1-156).
47 The three-dimensional structure of strontium-prothrombin fragment 1 shows that these positions are cl
48 f Mg(2+) to FVIIa, Gla-domainless FVIIa, and prothrombin fragment 1 supports the crystal data.