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1 tion of the gene KLKB1, which encodes plasma prekallikrein.
2 cells possess the ability to activate plasma prekallikrein.
3 so corrected by reconstitution with purified prekallikrein.
4 with the identity of the Fletcher factor and prekallikrein.
5  contact phase proteins, factor XII, HK, and prekallikrein.
6                    In contrast, we show that prekallikrein, a FXI homolog, did not bind to SkM, refle
7  intrachain disulfide bond with Cys326 as in prekallikrein, a plasma protein that exists as a monomer
8             Replacing the A3 domain with the prekallikrein A3 domain increases K(m) for fIX cleavage
9 a template for a series of proteins in which prekallikrein A3 sequence was replaced with factor XI se
10 cells, factor XII activation is secondary to prekallikrein activation and amplifies it.
11 temic amyloidosis allow for plasma FXIIa and prekallikrein activation and increased formation of kall
12                                  Controlling prekallikrein activation by C1 inhibitor (C1Inh) represe
13               The fCS polysaccharides showed prekallikrein activation comparable with dextran sulfate
14 s the protein responsible for zinc-dependent prekallikrein activation in the presence of HK.
15          The immediate consequence of plasma prekallikrein activation is the cleavage of high molecul
16        Peptides GPV15 and PGG15 also blocked prekallikrein activation on endothelial cells.
17 at blocked HK binding to uPAR also inhibited prekallikrein activation on HUVEC.
18 iated HK is proteolyzed during the course of prekallikrein activation, releasing kallikrein from the
19 ial cells could augment release of Hsp90 and prekallikrein activation.
20 unregulated kallikrein activity or increased prekallikrein activation.
21 ogen on its multiprotein receptor allows for prekallikrein activation.
22 cal vein endothelial cell (HUVEC)-associated prekallikrein activator (PKA).
23                     Homology scanning, using prekallikrein amino acid substitutions within the synthe
24 ne mapping of the heparin-binding site using prekallikrein analogue amino acid substitutions of the s
25 lement 1 inhibitor, neutralizing antibody to prekallikrein and bradykinin receptor antagonism.
26 of a surface, FXII-R353A and FXII-T activate prekallikrein and cleave the tripeptide S-2302, demonstr
27                                  Mean plasma prekallikrein and D-dimer concentrations decreased, and
28  proteins are normal except for an increased prekallikrein and decreased factor XI.
29  activity and HK cleavage and reduced plasma prekallikrein and Factor XII activation in plasma.
30 high molecular weight kininogen (HK), plasma prekallikrein and Factor XII cleavage.
31 ide YHK9 also inhibits FXIIa's activation of prekallikrein and FXI on HUVECs.
32 cher factor-deficient plasma is deficient in prekallikrein and therefore generates no bradykinin upon
33  of the contact proteases factor XII (FXII), prekallikrein, and factor XI (FXI) can trigger coagulati
34 urfaces requiring interaction of factor XII, prekallikrein, and high M(r) kininogen (HK).
35 sine-sulfated hemostatic proteins-protein S, prekallikrein, and plasminogen-were identified.
36 a variety of known substrates such as plasma prekallikrein, bradykinin, angiotensins II and III, and
37  suggest that free HK, or HK in complex with prekallikrein but not in complex with factor XI, interac
38 -MVs directly activated factor XII (FXII) or prekallikrein, but not FXI or FIX.
39       Furthermore, we observe reduced plasma prekallikrein, cleaved high molecular weight kininogen a
40 lial cells possessed the ability to catalyze prekallikrein conversion to kallikrein, and activation d
41  system" factors (factor XI, factor XII, and prekallikrein) could not be identified.
42                       Neither FXII, FXI, nor prekallikrein deficiency mitigated coagulation activatio
43   Interestingly, RBC-MVs generated FIXa in a prekallikrein-dependent manner.
44                          However, homologous prekallikrein-derived peptides (encompassing Pro(45)-Gly
45             We have previously reported that prekallikrein expresses an active site when it is bound
46 isense oligonucleotide, specifically reduces prekallikrein expression.
47 presence of a physiological concentration of prekallikrein, factor XI abrogates HK binding to HUVEC i
48 ule with the A3 domain replaced with A3 from prekallikrein (FXI/PKA3) activated factor IX with a K(m)
49                         We observed that the prekallikrein gene (Klkb1) is expressed highly in the ma
50 l, whereas the recombinant Apple 3 domain of prekallikrein had little effect.
51                                              Prekallikrein, high-molecular weight kininogen, factor X
52                                     When the prekallikrein-high molecular weight kininogen complex is
53 nt HK cleavage either by prekallikrein or by prekallikrein-HK autoactivation to generate kallikrein.
54             Zinc-dependent activation of the prekallikrein-HK complex also depended on addition of ei
55 lease of Hsp90 and augment activation of the prekallikrein-HK complex to generate kallikrein and brad
56                  Augmented activation of the prekallikrein-HK complex to generate kallikrein was seen
57  results indicate that C1-INH stabilizes the prekallikrein-HK complex to prevent HK cleavage either b
58                            Activation of the prekallikrein-HK complex was measured by using pro-phe-a
59      Addition of 0.1% factor XII relative to prekallikrein-HK leads to rapid formation of kallikrein;
60                          We demonstrate that prekallikrein-HK will activate to kallikrein in phosphat
61 that streptococcal supernatants can activate prekallikrein, in addition to causing plasminogen activa
62 nogen complex is bound to endothelial cells, prekallikrein is stoichiometrically converted to kallikr
63                          The plasma protease prekallikrein is structurally homologous to factor XI, b
64  factor XIa containing the Apple 3 domain of prekallikrein (Ki approximately 2.7 nM) competed with [1
65   In summary, RBC-MVs activate both FXII and prekallikrein, leading to FIX activation by 2 independen
66              Surprisingly, exposing VSMCs to prekallikrein leads to activation of the ERK1/2 mitogen-
67  precise mechanism for reduced thrombosis in prekallikrein null mice (Klkb1(-/-)) is unknown.
68 -HK complex to prevent HK cleavage either by prekallikrein or by prekallikrein-HK autoactivation to g
69 highly restricted in its ability to initiate prekallikrein or FXI activation.
70 ilar results were obtained in plasma lacking prekallikrein or FXII (the zymogens of PKa and FXIIa) an
71 tically active stimulus since neither C5 nor prekallikrein or inactivated kallikrein could enhance me
72  nM) but does not target either the zymogen (prekallikrein) or any other serine protease tested.
73 actors of the contact (factor XII [FXII] and prekallikrein) or intrinsic coagulation (FXI) pathway we
74                              We examined how prekallikrein (PK) activation on human microvascular end
75 nti-gC1qR blocked both biotin-HK binding and prekallikrein (PK) activation on HUVECs with an inhibito
76 vein endothelial cells (HUVECs), is a plasma prekallikrein (PK) activator.
77 We measured the circulating levels of plasma prekallikrein (PK) activity, factor XII, and high-molecu
78  cells (HUVECs) results in the activation of prekallikrein (PK) and its dependent pathways.
79                                         When prekallikrein (PK) assembles on high molecular weight ki
80                   The hypothesis that plasma prekallikrein (PK) is a risk factor for the development
81                                              Prekallikrein (PK) is the precursor of the trypsin-like
82 ations determined the relative preference of prekallikrein (PK) or factor XI/XIa (FXI/FXIa) binding t
83  to be responsible for the binding of plasma prekallikrein (PK) or kallikrein.
84    The plasma proteins factor XII (FXII) and prekallikrein (PK) undergo reciprocal activation to the
85 n to encompass the binding domain for plasma prekallikrein (PK) within domain 6 of high molecular wei
86 act system is composed of factor XII (FXII), prekallikrein (PK), and cofactor high-molecular-weight k
87 when plasma factors XII (FXII) and XI (FXI), prekallikrein (PK), and high molecular weight kininogen
88 tact system includes factor XII (FXII), FXI, prekallikrein (PK), and high-molecular-weight kininogen
89 a), generated by activation of its precursor prekallikrein (PK), plays a role in the contact activati
90                             Levels of plasma prekallikrein (PK), the precursor of KK, were markedly e
91  the functional role of HK in the absence of prekallikrein (PK), the proenzyme of plasma kallikrein,
92 ng the FXI A4 domain with the A4 domain from prekallikrein (PK).
93 omologous but functionally distinct protease prekallikrein (PK).
94 n system (KKS) consists of serine proteases, prekallikrein (pKal) and factor XII (FXII), and a cofact
95   We demonstrate that selective reduction of prekallikrein (PKK), another member of the contact syste
96 We investigated the effects of tPA on plasma prekallikrein (PPK) activation and the role of PKal on c
97               Selective inhibition of plasma prekallikrein production by antisense oligonucleotide tr
98                               The ability of prekallikrein to correct the coagulation, fibrinolytic,
99 eplaced with the corresponding A domain from prekallikrein to investigate SkM-mediated enhancement of
100 h factor XII and C1-INH led to conversion of prekallikrein to kallikrein and cleavage of HK, as was s
101 heat shock protein 90 leads to conversion of prekallikrein to kallikrein in a zinc-dependent reaction
102      Prolylcarboxypeptidase (PRCP) activates prekallikrein to plasma kallikrein, leading to bradykini
103              Corn trypsin inhibitor binds to prekallikrein to prevent rPRCP activation, but it does n
104 s, the plasma proteins factor XII (FXII) and prekallikrein undergo reciprocal proteolytic conversion
105 amino acid sequence of the Apple 3 domain of prekallikrein was replaced with that of factor XI was as
106 e was associated with reduced factor XII and prekallikrein, whereas levels of factors VIII, IX, XI, a
107 tes inflammation by reciprocal activation of prekallikrein, which cleaves HK (high-molecular-weight k
108 ability to serve as an acquired receptor for prekallikrein, which, after its activation, may directly

 
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