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1                Cleavage at Arg320 of ProT or prethrombin 1 (Pre 1) activates the catalytic site and t
2 distinguished exosite I environments on Pro, prethrombin 1 (Pre 1), and prethrombin 2 (Pre 2) but bou
3                                          FPR-prethrombin 1 (Pre 1), fragment 1 (F1), fragment 1.2 (F1
4 fragment 1 and generates the zymogen analog, prethrombin 1 (Pre 1).
5 active products of factor Xa-catalyzed human prethrombin 1 activation in the absence of the protein c
6  present, these differences in protein C and prethrombin 1 activation rates were decreased to about 2
7                        Loss of fragment 1 in prethrombin 1 enhanced affinity for both vWbp(1-263) and
8 ntrinsic property of factor Xa activation of prethrombin 1 that is modulated by factor Va.
9 brium binding to the prothrombin derivatives prethrombin 1, prethrombin 2, thrombin, meizothrombin, a
10 et mutants of des-(1-45)-factor Xa activated prethrombin 1.8-11-fold slower than wild-type enzyme.
11 activation of the charge reversal mutants of prethrombin-1 (in particular K36E, R67E, and K70E) were
12 n this study, we prepared several mutants of prethrombin-1 (prothrombin lacking Gla and Kringle-1 dom
13 y, the activation of proexosite-1 mutants of prethrombin-1 by the partially purified venom was studie
14                                              Prethrombin-1 differs from prothrombin for the absence o
15               The X-ray crystal structure of prethrombin-1 solved at 2.2-A resolution shows an overal
16 minutes), 1.7 +/- 0.5 nM for FPB release and prethrombin 2 (2.8 +/- 0.8 minutes), 7.0 +/- 2.2 nM for
17 he membrane binding domain is also lost when prethrombin 2 (P2) and F12 are produced following initia
18 ironments on Pro, prethrombin 1 (Pre 1), and prethrombin 2 (Pre 2) but bound with the same affinities
19                                              Prethrombin 2 (Pre 2), formed by factor Xa cleavage of P
20 om meizothrombin toward formation of the FPR-prethrombin 2 (Pre 2).F1.2 inhibitory intermediate.
21 g271 produces the inactive zymogen form, the prethrombin 2 (Pre 2).fragment 1.2 complex, which is cle
22 ombin, was a linear competitive inhibitor of prethrombin 2 activation without significantly inhibitin
23 24 mumol/L) is consumed yielding 400 nmol/ L prethrombin 2 and 360 nmol/l thrombin (B-chain) products
24                                              Prethrombin 2 and alpha-thrombin compete for binding to
25 be accounted for by a kinetic model in which prethrombin 2 and alphaBFX-2b bind in a mutually exclusi
26  R271 and R320, generating the intermediates prethrombin 2 and meizothrombin, respectively.
27  interacts with the 148 loop of thrombin and prethrombin 2 and the south rim of the catalytic site, w
28                                 We have used prethrombin 2 as a substrate analog for the first cleava
29                        By kinetic studies of prethrombin 2 cleavage by prothrombinase in the presence
30                              The kcat/Km for prethrombin 2 cleavage by prothrombinase was essentially
31 city measurements indicated that the rate of prethrombin 2 cleavage by the factor Xa-PCPS binary comp
32       We show that competitive inhibition of prethrombin 2 cleavage can be accomplished by interferin
33                              The kinetics of prethrombin 2 cleavage was studied to delineate macromol
34 n following initial cleavage at Arg(271) and prethrombin 2 formation (pre2 pathway).
35 bound to thrombin and its inactive precursor prethrombin 2 has indicated that SC activates ProT by in
36  binding inhibitor of the cleavage of either prethrombin 2 or meizothrombin des-fragment 1 by prothro
37 ge of phospholipid-bound prothrombin via the prethrombin 2 pathway, catalyzes the initial activation
38 e intermediates, meizothrombin (MzII(a)) and prethrombin 2 plus fragment 1.2 (Pre2 & F1.2).
39 rombin 2, prethrombin 2 plus fragment 2, and prethrombin 2 plus fragment 1.2 as substrates.
40 constants were obtained using prethrombin 2, prethrombin 2 plus fragment 2, and prethrombin 2 plus fr
41 s essentially identical to that obtained for prethrombin 2 saturated with fragment 2.
42 g residues 1-325 (SC-(1-325)) bound to human prethrombin 2 showed previously that SC inserts its Ile(
43 and have also relied on the known ability of prethrombin 2 to interact tightly but reversibly with fr
44                      Both alpha-thrombin and prethrombin 2 were cleaved with chymotrypsin at Trp148 a
45 Val(2) N terminus into the Ile(16) pocket of prethrombin 2, inducing a functional active site in the
46 ive site-independent binding of prothrombin, prethrombin 2, meizothrombin des fragment 1 and thrombin
47  state kinetic constants were obtained using prethrombin 2, prethrombin 2 plus fragment 2, and prethr
48 o the prothrombin derivatives prethrombin 1, prethrombin 2, thrombin, meizothrombin, and meizothrombi
49                      Binding was inferred by prethrombin 2-dependent perturbations in the fluorescenc
50 ile hydrolysis of Arg(273)-Thr(274) produces prethrombin 2-fragment 1.2 (Pre2-F1.2).
51 l substrates does not alter the affinity for prethrombin 2.
52 nesis of the authentic P(1)-P(3) sequence in prethrombin 2/fragment 1.2 yielded substrate variants th
53 ase takes place without preference along the prethrombin-2 (cleavage at Arg(271) first) or meizothrom
54  pathways generating either the intermediate prethrombin-2 (following initial cleavage at R271) or me
55 t Arg-271, generating the inactive precursor prethrombin-2 (Pre2), which is further attacked at Arg-3
56 CPS markedly accelerated the initial rate of prethrombin-2 activation by E2-fXa, with the cofactor ex
57 nition by thrombin and its zymogen precursor prethrombin-2 and have direct relevance to other members
58 nt from that of its direct zymogen precursor prethrombin-2 and more similar to that of its fully acti
59                   Crystal structures of both prethrombin-2 and thrombin are available and show almost
60  to glucokinase, thrombin, and its precursor prethrombin-2 are used as relevant examples.
61  protease thrombin and its zymogen precursor prethrombin-2 as relevant models we resolve the relative
62 inhibitors of the fVa-mediated activation of prethrombin-2 by E2-fXa in the absence of PCPS, they are
63                     Since neither E2-fXa nor prethrombin-2 can interact with membranes, these results
64                              Prothrombin and prethrombin-2 gave nearly identical results while meizot
65                       The thrombin precursor prethrombin-2 has R15 at the site of activation in ionic
66  of E* and E forms observed for thrombin and prethrombin-2 indicates that zymogen activation is linke
67 -320, leading to thrombin generation via the prethrombin-2 intermediate.
68                    Addition of mutated mouse prethrombin-2 into the conventional assay for prothrombi
69                            In this scenario, prethrombin-2 is more dynamic and exists predominantly i
70               We hypothesize that use of the prethrombin-2 pathway serves to optimize the procoagulan
71 d initiates activation along the alternative prethrombin-2 pathway.
72   In the blood, the zymogens prothrombin and prethrombin-2 require the prothrombinase complex to be c
73 e pairs of chymotrypsinogen, trypsinogen and prethrombin-2 showed a similar distribution of the flexi
74      Comparison with thrombin shows that the prethrombin-2 to thrombin conversion enhances ligand bin
75 to proceed through the inactive intermediate prethrombin-2 via an initial cleavage at Arg-271 followe
76 mediated catalytic activity of E2-fXa toward prethrombin-2 was analyzed in both the absence and prese
77 duced recombinant mutants of human and mouse prethrombin-2 which are able to convert themselves autoc
78  mutant was expressed in Escherichia coli as prethrombin-2(148) using a T7 expression system previous
79            After refolding and purification, prethrombin-2(148) was activated to thrombin(148) with E
80 a and both kringle domains of the substrate (prethrombin-2) had been deleted.
81 rombin with the same regions of prothrombin, prethrombin-2, and meizothrombin.
82 chitecture of the free forms of thrombin and prethrombin-2, consistent with an E*-E equilibrium and p
83 t Arg271 generates the inactive intermediate prethrombin-2, initial cleavage at Arg320 generates the
84  the inactive zymogen precursor of thrombin, prethrombin-2, resolves all rate constants for a binding
85                               In the case of prethrombin-2, the equilibrium is shifted strongly (10:1
86 her potential intermediate, meizothrombin or prethrombin-2, was observed in the effluent.
87 gh prothrombin is much larger than thrombin, prethrombin-2, which contains all of the same amino acid
88 n was initially cleaved at Arg271 generating prethrombin-2, with alpha-thrombin formation quickly aft
89 , which is unable to activate prothrombin or prethrombin-2.
90 d through the intermediates meizothrombin or prethrombin-2.
91 the same positions as E14e, D14l, and E18 in prethrombin-2.
92  pathway of activation from meizothrombin to prethrombin-2.
93 teases: chymotrypsinogen, proproteinase, and prethrombin-2.
94 on system previously described for wild-type prethrombin-2.
95                 Both AN78 and AN129 bound to prethrombin I (the fragment lacking the Gla domain and t
96 lel pathways: (1) the inactive intermediate, prethrombin; or (2) the proteolytically active intermedi