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1 bility due to the release of bradykinin from high molecular weight kininogen.
2 r, and prevented cleavage and consumption of high-molecular-weight kininogen.
3 eration of plasma kallikrein and cleavage of high-molecular-weight kininogen.
4 ofactor activity was ascribed to domain 5 of high-molecular-weight kininogen.
5 ain plasma protein evolutionarily related to high-molecular-weight kininogen.
6 radykinin release resulting from cleavage of high-molecular-weight kininogen.
7 th dextran sulfate in the presence of either high molecular weight kininogen (45 nm) and ZnCl(2) (25
8 at prothrombin (1 microm) is able to replace high molecular weight kininogen (45 nm) as a cofactor fo
9  the HK31-mer (8 microm) are able to replace high molecular weight kininogen (45 nm) or prothrombin (
10                           In the presence of high molecular weight kininogen (45 nm), Zn(2+) and Ca(2
11 tofibrils bind to coagulation factor XII and high molecular weight kininogen and accelerate the activ
12 bserve reduced plasma prekallikrein, cleaved high molecular weight kininogen and elevated plasma brad
13 sed on the Apple 3 domain in the presence of high molecular weight kininogen and Zn2+ or prothrombin
14  C1 inhibitor deficiency reduced cleavage of high-molecular-weight kininogen and attacks of angioedem
15 ane rafts required prothrombin (and Ca2+) or high molecular weight kininogen (and Zn2+), which are re
16 ere endostatin, heat shock proteins, cleaved high molecular weight kininogen, and adipokines.
17 d by measurement of plasma levels of cleaved high-molecular-weight kininogen, and efficacy was assess
18 omain of factor XI at or near the site where high molecular weight kininogen binds.
19           In microtiter plates, biotinylated high molecular weight kininogen (biotin-HK) or biotin-FX
20  Inherited deficiency in factor XI or XII or high-molecular-weight kininogen, but not plasma kallikre
21 ne monoclonal antibody to the light chain of high molecular weight kininogen, C11C1, to inhibit tumor
22 bradykinin and that a monoclonal antibody to high-molecular weight kininogen, C11C1, blocked its bind
23                                              High-molecular-weight kininogen can be hydrolysed by pla
24             Plasma concentrations of cleaved high-molecular-weight kininogen (cHK), vascular endothel
25                                              High-molecular-weight kininogen cleavage protection at t
26 ecombinant FXII-W268R spontaneously triggers high-molecular-weight kininogen cleavage.
27                       When the prekallikrein-high molecular weight kininogen complex is bound to endo
28                                  With higher high molecular weight kininogen concentrations (360 nm),
29 ere significantly reduced in APAP-challenged high-molecular-weight kininogen-deficient (HK-/-) mice.
30                               Prekallikrein, high-molecular weight kininogen, factor XI, and factor X
31 flammatory bradykinin peptide and additional high molecular weight kininogen fragments containing the
32    In contrast, only FOG induced cleavage of high molecular weight kininogen, generating the proinfla
33                             A titration with high molecular weight kininogen had no effect on FXIa bi
34                          The cleaved form of high-molecular-weight kininogen has recently been demons
35 idoma producing a monoclonal antibody to the high molecular weight kininogen heavy chain or to an unr
36  and reversibly to HUVECs in the presence of high molecular weight kininogen (HK) (apparent Kd of 23
37                                              High molecular weight kininogen (HK) also stimulates the
38 finity (KD </= 0.8 nM) binding site for both high molecular weight kininogen (HK) and factor XII (FXI
39                                              High molecular weight kininogen (HK) and factor XII are
40                                              High molecular weight kininogen (HK) and its cleaved for
41      Previously we defined binding sites for high molecular weight kininogen (HK) and thrombin in the
42 (1.3 x 10(10) sites/well, K(D) = 12 nm) when high molecular weight kininogen (HK) and zinc are presen
43                                              High molecular weight kininogen (HK) and Zn2+ ions exert
44                    We have demonstrated that high molecular weight kininogen (HK) binds specifically
45 m 8 to 16 amino acids and derived from human high molecular weight kininogen (HK) domain 5 were inser
46 S565-K595) in domain 6 of the light chain of high molecular weight kininogen (HK) has previously been
47     Previously we defined a binding site for high molecular weight kininogen (HK) in the A1 domain of
48                  We have previously reported high molecular weight kininogen (HK) inhibition of throm
49                    The nonenzymatic cofactor high molecular weight kininogen (HK) is a precursor of b
50                                              High molecular weight kininogen (HK) is an endogenous pr
51                        Factor XII (FXII) and high molecular weight kininogen (HK) mutually block each
52 endent and not shared by either single-chain high molecular weight kininogen (HK) or low molecular we
53 nin system; thus we explored whether MPO and high molecular weight kininogen (HK) reside on CK1 toget
54 d levels of plasma kallikrein, which cleaves high molecular weight kininogen (HK) to release bradykin
55       Previous studies on the interaction of high molecular weight kininogen (HK) with endothelial ce
56  prekallikrein activation is the cleavage of high molecular weight kininogen (HK) with liberation of
57                        Proteolysis of plasma high molecular weight kininogen (HK) yielding bradykinin
58 a kallikrein, in the presence and absence of high molecular weight kininogen (HK), an important cofac
59 trate and capillary immunoassays to quantify high molecular weight kininogen (HK), plasma prekallikre
60 irculates as a complex with the glycoprotein high molecular weight kininogen (HK).
61 essed on their membranes and is able to bind high molecular weight kininogen (HK).
62 plasma prekallikrein (PK) within domain 6 of high molecular weight kininogen (HK).
63 ater than dextran sulfate in the presence of high molecular weight kininogen (HK, 45 nM), ZnCl2 (25 m
64 and leads to kallikrein-mediated cleavage of high molecular-weight kininogen (HK) and release of proi
65 expresses an active site when it is bound to high-molecular-weight kininogen (HK) and can digest HK t
66  serine protease known to induce cleavage of high-molecular-weight kininogen (HK) at sites of inflamm
67 y PRCP and the role of C1INH to regulate it, high-molecular-weight kininogen (HK) cleavage, and brady
68 lar artery thrombosis was recognized to have high-molecular-weight kininogen (HK) deficiency.
69                                              High-molecular-weight kininogen (HK) is an abundant plas
70                                              High-molecular-weight kininogen (HK) plays an important
71 ingle-chain precursor form, PK-R371A cleaves high-molecular-weight kininogen (HK) to release bradykin
72                                  Cleavage of high-molecular-weight kininogen (HK), a marker for activ
73 tor XII (FXII), FXI, prekallikrein (PK), and high-molecular-weight kininogen (HK), and has received i
74 diverse proteins, including the known ligand high-molecular-weight kininogen (HK), as well as the ext
75 electively knock down factor (f)XII, fXI, or high-molecular-weight kininogen (HK), key components of
76                           Kallikrein cleaves high-molecular-weight kininogen (HK), releasing the vaso
77 inogen activator receptor (uPAR), and gC1qR, high-molecular-weight kininogen (HK)-binding proteins on
78 e release of the nanopeptide bradykinin from high-molecular-weight kininogen (HK).
79 XII (FXII), prekallikrein (PK), and cofactor high-molecular-weight kininogen (HK).
80 nant PRCP (rPRCP) activates PK when bound to high-molecular-weight kininogen (HK).
81      A region of 31 amino acids derived from high molecular weight kininogen (HK31-mer) can also bind
82                                      Cleaved high molecular weight kininogen (HKa) has been shown to
83 ously reported that the binding of two-chain high molecular weight kininogen (HKa) to endothelial cel
84     One example of such a protein is cleaved high molecular weight kininogen (HKa).
85 vious studies have demonstrated that cleaved high-molecular-weight kininogen (HKa) induces endothelia
86  plasma kallikrein to bradykinin and cleaved high-molecular-weight kininogen (HKa).
87 tide bradykinin (BK), leaving behind cleaved high-molecular-weight kininogen (HKa).
88 was also seen against aerosol challenge with high-molecular-weight kininogen (HMWK), a substrate of T
89 prekallikrein (PK) activity, factor XII, and high-molecular weight kininogen in the plasma of 636 typ
90 dose of 300 mg or 400 mg reduced cleavage of high-molecular-weight kininogen in plasma from patients
91 of the precursor proteins prekalli-krein and high-molecular-weight kininogen indicated activation of
92 (FXII) and XI (FXI), prekallikrein (PK), and high molecular weight kininogen interact with anionic su
93                                      Cleaved high molecular weight kininogen is antiangiogenic.
94                     We have shown that human high molecular weight kininogen is proangiogenic due to
95                                              High molecular weight kininogen is the precursor for two
96                             We reported that high-molecular weight kininogen is proangiogenic by rele
97                                 HKa (cleaved high molecular weight kininogen) is an endogenous inhibi
98                                              High-molecular-weight kininogen (KNG) is a central const
99 at measures PK activation only when bound to high molecular weight kininogen linked to microtiter pla
100  molecular weight kininogen, suggesting that high molecular weight kininogen may play a role in regul
101         When prekallikrein (PK) assembles on high molecular weight kininogen on HUVEC, PK is activate
102     Recent studies indicate that assembly of high molecular weight kininogen on its multiprotein rece
103 inhibition of factor XII, plasma kallikrein, high-molecular-weight kininogen, or the bradykinin B2 re
104 ted the consumption of the contact proteins, high molecular weight kininogen (P<0.03), and factor XI
105                Furthermore, peptide RPPGF or high-molecular-weight kininogen prevented alpha-thrombin
106 (t(1/2) approximately 12.5 days) and blocked high molecular weight kininogen proteolysis in activated
107  protease nexin-2 was partially abrogated by high molecular weight kininogen, suggesting that high mo
108 antibody C11C1 efficiently blocks binding of high molecular weight kininogen to endothelial cells in
109 ma kallikrein (pKal) proteolytically cleaves high molecular weight kininogen to generate the potent v
110 nd tissue kallikreins, proteases that cleave high molecular weight kininogen to produce bradykinin.
111 sma kallikrein (PKa) activity, which cleaves high-molecular-weight kininogen to generate the proinfla
112               Plasma kallikrein (PK) cleaves high-molecular-weight kininogen to release bradykinin (B
113 tivation of prekallikrein, which cleaves HK (high-molecular-weight kininogen) to liberate bradykinin.
114  whereas levels of factors VIII, IX, XI, and high molecular weight kininogen were elevated.

 
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