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1                                              PCPS markedly accelerated the initial rate of prethrombi
2 avage of the factor Va heavy chain (with APC-PCPS) at Arg505, Arg662 and Arg306 results in a drastic
3 e truly immunogenic antigens are produced by PCPS, therefore providing a marginal contribution to the
4 that, albeit with different timing, both FXa/PCPS and E coli infusion led to robust thrombin and plas
5  a strong burst of thrombin and plasmin, FXa/PCPS infusion did not produce measurable levels of compl
6 es a maximum value of 18 pM/s at 5-20 microM PCPS; further increases in the levels of PCPS decrease t
7 .1 nM), 0.76 pM/s, is achieved at 200 microM PCPS.
8 ts the collective contribution from multiple PCPS and linear products.
9 of prethrombin-2 by E2-fXa in the absence of PCPS, they are ineffective competitors in the presence o
10 holipid vesicles followed by the addition of PCPS vesicles and activated protein C (APC).
11 ndependent estimation of the contribution of PCPS to the immunopeptidome, we first reviewed methodolo
12 roM PCPS; further increases in the levels of PCPS decrease the activation rate of factor VII.
13 for factor VII activation in the presence of PCPS at optimal concentrations vary from 1.2 microM for
14              Factor VIIIa in the presence of PCPS has no effect on factor VII activation by factor IX
15 ssay (with or without APC) with platelets or PCPS vesicles added to induce clot formation indicated t
16 phosphatidylserine, 75% phosphatidylcholine, PCPS) were evaluated using sedimentation velocity/equili
17 e of phosphatidylcholine-phosphatidylserine (PCPS) vesicles or purified human plasma lipoproteins.
18 (FXa/phosphatidylcholine-phosphatidylserine [PCPS]) vs LD100 Escherichia coli We found that, albeit w
19 y 0.05 nM factor Xa is anionic phospholipid (PCPS) dependent and achieves a maximum value of 18 pM/s
20       Proteasome-catalyzed peptide splicing (PCPS) of cancer-driving antigens could generate attracti
21 about proteasome-catalyzed peptide splicing (PCPS), the emerging rules governing this process, and th
22 rough proteasome-catalyzed peptide splicing (PCPS).
23  from proteasome-catalyzed peptide splicing (PCPS).
24 -, or 100,000-fold for TF(S), TF(PC), and TF(PCPS).
25 osphatidylcholine and phosphatidylserine (TF(PCPS)).
26 idylcholine:phosphatidylserine membranes (TF/PCPS) or PC membranes (TF/PC).
27 mation using increasing concentrations of TF/PCPS or TF/PC in the presence of TFPI yielded families o
28  was colinear with EGFRvIII, indicating that PCPS fragments may be a component of MHC class I recogni
29 t being colinear with EGFRvIII, two of three PCPS products tested were capable of increasing survival
30 esence and absence of phospholipid vesicles (PCPS vesicles).
31 on that available algorithms or the in vitro PCPS reaction reliably simulate in vivo splicing and arg
32 ed neo-splicetopes was generated by in vitro PCPS.
33                                    Nine were PCPS products and only one peptide was colinear with EGF
34 results suggest that interaction of fVa with PCPS improves the affinity of the activation complex for
35 he interaction of the Gla domain of fXa with PCPS also induces conformational changes in the protease
36 e of prethrombin 2 cleavage by the factor Xa-PCPS binary complex was increased by a factor of approxi
37 ) value (15.2 s-1) is observed for factor Xa-PCPS.
38 rating concentrations of factor Va to the Xa-PCPS binary complex led to increases in catalytic effici