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1 TAFI activation, like protein C activation, is augmented
2 TAFI also shares high homology in zinc binding and catal
3 TAFI deficiency did not improve survival rate compared w
4 TAFI is able to reconstitute an APC-dependent shortening
5 TAFI is structurally very similar to pancreatic procarbo
6 TAFI-deficient mice developed normally, reached adulthoo
7 TAFI-deficient mice did not suffer from excess bleeding
10 found to have decreased ability to activate TAFI yet retained normal protein C activation, whereas t
11 s study, we examined the effect of activated TAFI (TAFIa) in modulating the proinflammatory functions
12 e found to be potent inhibitors of activated TAFI and selective versus the related carboxypeptidases
15 body-engineered bispecific inhibitor against TAFI and PAI-1 (heterodimer diabody, Db-TCK26D6x33H1F7)
16 nistration of a bispecific inhibitor against TAFI and PAI-1 results in a prominent profibrinolytic ef
20 tituted purified system, which included both TAFI and either form of factor V purified from pooled pl
23 protein (TBP) and three associated factors (TAFIs), does not have any sequence-specific DNA binding
34 ancing protein C activation while inhibiting TAFI activation, thereby preventing the generation of th
35 thrombin activatable fibrinolysis inhibitor (TAFI) and fibrinogen were significantly more pronounced
36 thrombin-activatable fibrinolysis inhibitor (TAFI) and plasminogen activator inhibitor-1 (PAI-1) are
37 thrombin-activatable fibrinolysis inhibitor (TAFI) and thereby helps coordinate coagulation, anticoag
38 f thrombin activable fibrinolysis inhibitor (TAFI) in plasma, secondary-extended thrombin generation
39 Thrombin-activable fibrinolysis inhibitor (TAFI) is a recently described plasma zymogen that can be
40 Thrombin-activable fibrinolysis inhibitor (TAFI) is a zymogen that inhibits the amplification of pl
41 e thrombin-activable fibrinolysis inhibitor (TAFI) is activated by thrombin/thrombomodulin on the end
42 Thrombin-activatable fibrinolysis inhibitor (TAFI) is an important regulator of fibrinolysis, and inh
43 Thrombin-activatable fibrinolysis inhibitor (TAFI) is the precursor of an exopeptidase that is identi
45 thrombin-activatable fibrinolysis inhibitor (TAFI), we generated homozygous TAFI-deficient mice by ta
58 ed thrombin generation and the activation of TAFI were essentially unopposed by 5A-APC due to its low
63 human plasma (NHP), plasma immunodepleted of TAFI (TdP), and TdP reconstituted with purified TAFI.
65 NAc-Hep prevented PF4-mediated inhibition of TAFI activation and the antifibrinolytic functions of TA
68 e determination of the activatable levels of TAFI in human and other animal plasma in the presence of
69 esidues around the substrate binding site of TAFI resulted in altered C-terminal substrate specificit
71 (EGF)-like domains 1 and 2 had no effect on TAFI or protein C activation, whereas deletions includin
72 To block the inhibitory effects of PF4 on TAFI activation, heparin derivatives were tested for the
73 of both soluble and cellular forms of TM on TAFI activation-dependent suppression of fibrinolysis we
74 nfluences lysis time, inhibitors of TAFIa or TAFI activation may prove to be important adjuvants for
75 229K, was able to activate endogenous plasma TAFI in mice, and E229K thrombin infusion effectively bl
76 hrombomodulin EGF-like domain 3 was present, TAFI competitively inhibited protein C activation cataly
77 nimal profibrinolytic activity and preserved TAFI-mediated anti-inflammatory carboxypeptidase activit
81 on also revealed that the binding to the TBP-TAFI complex SL1 is not sufficient to activate transcrip
83 the TBP-TAFII complexes, TFIID, and the TBP-TAFI complex, SL1, and in both cases these interactions
85 lin-induced writhing response, implying that TAFI does not play a major role in bradykinin catabolism
89 emained to be determined the extent to which TAFI is involved in the profibrinolytic effect of APC in
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