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1 11.2 +/- 3.2 nM vs K(d) 8.63 +/- 1.06 nM for factor XIa).
2 ully human monoclonal antibody that inhibits factor XIa.
3 n(-1) with factor XIIa and 2 nm.min(-1) with factor XIa.
4 ctor XIIa, and 1.3-14 (mean = 8) min(-1) for factor XIa.
5 nvolves the actions of factor Xa with PZ and factor XIa.
6 nt, reversible, and competitive inhibitor of factor XIa.
7 ctivation by Factor VIIa-tissue factor or by Factor XIa.
8 r IX is present on the third apple domain of factor XIa.
9 s present on the noncatalytic heavy chain of factor XIa.
10 alth Organization international standard for factor XIa.
11 factors, such as antithrombin, thrombin, and factor XIa.
12 hion, but also directly inhibits coagulation factor XIa.
13 inding site is located in the light chain of factor XIa.
14 ytic domain near the heparin binding site of factor XIa.
15  in recognition of factor IX by the protease factor XIa.
16 ge of a tripeptidic chromogenic substrate by factor XIa.
17 udy the mechanism of factor IX activation by factor XIa.
18 ely 10-fold lower than their affinity toward factor XIa.
19 -Ile(370) bonds by thrombin, factor XIIa, or factor XIa.
20 caused by a specific defect in activation by factor XIa.
21 tivated to factor IXabeta by factor VIIa and factor XIa.
22                      Factor VIIa (10 nM) and factor XIa (1 nM) are not observed to activate factor VI
23 f kallikrein-C1 inhibitor complexes, without Factor XIa activation and coagulation (see the related a
24  Consistent with this premise, inhibition of factor XIa activation of factor IX by aprotinin (Ki 0.89
25          It has been postulated that the two factor XIa active sites cleave both factor IX peptide bo
26 ight kininogen may play a role in regulating factor XIa activity.
27                                              Factor XIa also cleaves factor IX preferentially after A
28 -binding site within the catalytic domain of factor XIa also displaced [125I]factor XIa from the surf
29 ep, M(r) approximately 12000) inhibited both factor XIa amidolytic activity and factor IX activation
30                                              Factor XIa and 1/2-FXIa activate the substrate factor IX
31                       The rate constants for factor XIa and catalytic domain inhibition by recombinan
32 et al have established, in human blood, that factor XIa and polyphosphate make significant contributi
33 iciently long to provide a template to which factor XIa and protease nexin-2 molecules can bind simul
34 vation by alpha-thrombin, beta-thrombin, and factor XIa and that these reactions are supported by pol
35  II are localized to the catalytic domain of factor XIa and the Kunitz domain of protease nexin II.
36 tes ZPI to inhibit free factor Xa as well as factor XIa and therefore may play a physiologically and
37 y domain, and it inhibits plasma kallikrein, factor XIa, and plasmin.
38 that factor IX binds to free and S2366-bound factor XIa at exosites.
39 ytic domain loop were used as competitors in factor XIa binding and inhibition studies.
40  on activated platelets, suggesting that the factor XIa binding site for platelets is not located in
41 ese results provide compelling evidence that factor XIa binding to the polyanions, dextran sulfate an
42                    The data demonstrate that factor XIa binds with comparable affinity to factors IX
43 ivated normally by its physiologic activator factor XIa, but its phospholipid-dependent activation by
44                                Inhibition of factor XIa by protease nexin II (K(i) approximately 450
45 association rate constants for inhibition of factor XIa by protease nexin II [(3.35 +/- 0.35) x 10(6)
46 xamined binding of factors IX and IXabeta to factor XIa by surface plasmon resonance.
47 ne proteases, including cationic trypsin and factor XIa, by 2 orders of magnitude.
48                   In contrast, activation by factor XIa.Ca2+ led to proteolysis at Arg318-Ser319[150-
49                                          The factor XIa catalytic domain contains a cysteine-constrai
50   Synthesized peptides representative of the factor XIa catalytic domain loop were used as competitor
51                   S2366 cleavage by isolated factor XIa catalytic domain was competitively inhibited
52 X alpha accumulated during activation by the factor XIa catalytic domain, demonstrating the importanc
53  a high-affinity heparin-binding site in the factor XIa catalytic domain.
54                             We conclude that factor XIa-catalyzed activation of factor IX proceeds vi
55 n be explained by one of two mechanisms: (1) factor XIa-catalyzed activation proceeds via a singly-cl
56                   In contrast, inhibition of factor XIa cleavage of S2366 by factor IX (Ki 224 +/- 32
57                                              Factor XIa cleavage of the tripeptide substrate S2366 wa
58                              We compared the factor XIa cleavage rates of free factor IX alpha and fa
59 ), prothrombinase (factor Va/factor Xa), and factor XIa complexes on PS-exposed activated platelets.
60 XIa (Ki approximately 1.4 nM) and a chimeric factor XIa containing the Apple 3 domain of prekallikrei
61 hibition of the isolated catalytic domain of factor XIa demonstrates a similar potentiation by hepari
62                                              Factor XIa devoid of the A3 domain displayed a major def
63  during coagulation, and that each half of a factor XIa dimer behaves as an independent enzyme with r
64 in analyses, suggest that the active site of factor XIa does not contribute significantly to the affi
65 mogen) platelet binding site and exposes the factor XIa (enzyme) platelet binding site within the cat
66 primary constituents of the contact pathway: factor XIa, factor XIIa, and plasma kallikrein, in the p
67 e affinity of leupeptin and aprotinin to the factor XIa-factor IX complex only approximately 10-fold
68 Ki approximately 2.7 nM) competed with [125I]factor XIa for binding sites on activated platelets, sug
69 , (538)H, and (539)K binds and competes with factor XIa for heparin-binding in a manner nearly identi
70 ic domain of factor XIa also displaced [125I]factor XIa from the surface of activated platelets (Ki a
71 n the intrinsic pathway of blood coagulation factor XIa (FXIa) activates factor IX (FIX) by cleaving
72       During blood coagulation, the protease factor XIa (fXIa) activates factor IX (fIX).
73 ymogen factor XI (FXI) and its protease form factor XIa (FXIa) as drug targets for treating and preve
74 s, there is intense interest in pursuing fXI/factor XIa (fXIa) as targets for achieving antithromboti
75            Heparin accelerates inhibition of factor XIa (fXIa) by the serpins antithrombin (AT) and C
76                                              Factor XIa (FXIa) cleaved chem163S, generating a novel c
77                      Factor XIIa (FXIIa) and factor XIa (FXIa) contribute to thrombosis in animal mod
78 e autolysis loop of the coagulation protease factor XIa (fXIa) for inhibition by serpins.
79 Antithrombotic agents that are inhibitors of factor XIa (FXIa) have the potential to demonstrate robu
80 Leverkusen, Germany), an oral small molecule factor XIa (FXIa) inhibitor, might prevent thrombosis wi
81 l, oral small molecule activated coagulation factor XIa (FXIa) inhibitor, might reduce thrombosis wit
82                                              Factor XIa (FXIa) inhibitors are promising novel anticoa
83                                         Oral factor XIa (FXIa) inhibitors may provide a promising new
84                                              Factor XIa (FXIa) is a blood coagulation enzyme that is
85                                Inhibition of factor XIa (FXIa) is a novel paradigm for developing ant
86                                              Factor XIa (FXIa) is a serine protease important for ini
87                                              Factor XIa (FXIa) is an enzyme in the coagulation cascad
88                                              Factor XIa (fXIa) is being recognized as a prime target
89 IX (FIX) to an exosite on the heavy chain of factor XIa (FXIa) is essential for the optimal activatio
90            To select residues in coagulation factor XIa (FXIa) potentially important for substrate an
91                            Human coagulation factor XIa (FXIa), a serine protease activated by site-s
92                    Moreover, the activity of factor XIa (FXIa), but not FXIIa, was higher in APP-KO m
93  related proteases (such as Factor Xa (FXa), Factor XIa (FXIa), urokinase-type plasminogen activator
94 lycan-binding proteins (GBPs), such as human factor XIa (FXIa), we screened a library of 26 synthetic
95 posits, is a potent inhibitor of coagulation factor XIa (FXIa).
96  a potent inhibitor of the blood coagulation Factor XIa (FXIa).
97 d competitive inhibitor of blood coagulation factor XIa (FXIa).
98 anoside (SPGG) as an allosteric inhibitor of factor XIa (FXIa).
99 e replaced it with Ala or Val in coagulation factor XIa (FXIa).
100 ctivators, plasma kallikrein and coagulation factor XIa (FXIa).
101                         It seems likely that factor XIa-generated intermediates observed under some r
102                           The termination of factor XIa generation by added hirudin in the factor XI
103 -2366) and on the activation of factor IX by factor XIa have been investigated.
104 vation suggests that binding of factor IX to factor XIa heavy chain affects the interactions of leupe
105 factor IX binds initially to exosites on the factor XIa heavy chain, followed by interaction at the a
106  domain, demonstrating the importance of the factor XIa heavy chain.
107 sion of a potent inhibitor of Factor IXa and Factor XIa (ie, protease nexin-2/ amyloid beta-protein p
108 d <1% of the coagulant activity of wild type factor XIa in a plasma coagulation assay, whereas the ch
109 tein Z-dependent protease inhibitor inhibits factor XIa in a protein Z-independent fashion.
110 with a K(d) = 86 +/- 15 nM and competes with factor XIa in binding to heparin, K(i) = 241 +/- 37 nM.
111 llikrein, activated forms of factor XII, and factor XIa in plasma.
112         Besides factor Xa, ZPI also inhibits factor XIa in the absence of PZ, phospholipids, and Ca(+
113 e demonstrated roles for the factor XIIa and factor XIa in thrombosis.
114 est that the major interactions required for factor XIa inhibition by protease nexin II are localized
115 ions with 32-64 saccharide units potentiated factor XIa inhibition by protease nexin-2 in a size- and
116                                 No effect on factor XIa inhibition by protease nexin-2 was observed w
117              Heparin-mediated enhancement of factor XIa inhibition by protease nexin-2 was partially
118  phenotype than PZ deficiency, implying that factor XIa inhibition by ZPI is physiologically relevant
119 and the extent (99% vs 93% at 30 minutes) of factor XIa inhibition by ZPI.
120                     Colchicine treatment and factor XIa inhibition constitute 2 novel pharmacologic a
121                              The efficacy of factor XIa inhibition for thromboprophylaxis is unknown.
122                                              Factor XIa inhibition with milvexian, added to dual anti
123                                Postoperative factor XIa inhibition with oral milvexian in patients un
124                          Asundexian, a novel factor XIa inhibitor, was compared with apixaban in pati
125 he efficacy and safety of milvexian, an oral factor XIa inhibitor.
126                                              Factor XIa inhibitors for the prevention and treatment o
127                   Over the past two decades, Factor XIa inhibitors have emerged as an exciting new cl
128      The zymogen, factor XI, and the enzyme, factor XIa, interact specifically with functional recept
129                                              Factor XIa is a serine protease which participates in bo
130                                              Factor XIa is inhibited by a recombinant Kunitz domain w
131             The isolated catalytic domain of factor XIa is inhibited by protease nexin II with an inh
132                   In contrast, activation by factor XIa is not phospholipid-dependent, raising questi
133                      Factor IX activation by factor XIa is thought to proceed through the singly-clea
134                                  Addition of factor XIa, IXa, VIIIa, or Va failed to correct the PTT
135 oop or a C-terminal heparin-binding region), factors XIa, IXa, Xa, and thrombin; group B (binding by
136 to factor XIa (K(i) 34 nm) and activation by factor XIa (K(i) 33 nm).
137 s a potent inhibitor of factor IX binding to factor XIa (K(i) 34 nm) and activation by factor XIa (K(
138 metry of 1.9 +/- 0.4 mol of factor IX/mol of factor XIa (Kd = 70 +/- 40 nm).
139 an plasma kallikrein (Ki = 0.3 nM) and human factor XIa (Ki = 6 nM).
140                                         Both factor XIa (Ki approximately 1.4 nM) and a chimeric fact
141 ithout free intermediate generation, whereby factor XIa makes both proteolytic cleavages in a single
142                                   A chimeric factor XIa molecule with the A3 domain replaced with A3
143  one inhibited active site, or a recombinant factor XIa monomer.
144 astin time (aPTT) assay and was activated by factor XIa more slowly than wild-type factor IX (FIXwt).
145 alenesulfonyl)glutamylglycylarginyl- (DEGR-) factor XIa observed when the fluorophore was in complex
146 , including glycoprotein VI on platelets and factor XIa of the coagulation system.
147 gher than the Km for activation by wild type factor XIa or the other factor XI/PK chimeras (0.11-0.37
148 During hemostasis, factor IX is activated by factors XIa or VIIa, by cleavage of the peptide bonds af
149 ces for factor XI activation by factor XIIa, factor XIa, or thrombin.
150                         Activated factor XI (factor XIa) participates in blood coagulation by activat
151        The Km for activation of factor IX by factor XIa/PKA3 (12.7 microM) is more than 30-fold highe
152 factor pathway inhibitor-2 (TFPI-2) inhibits factor XIa, plasma kallikrein, and factor VIIa/tissue fa
153 ed with KD1-WT, the KD1-L17R did not inhibit factor XIa, plasma kallikrein, or factor VIIa/tissue fac
154                      These data suggest that factor XIa plays a significant role in venous thrombosis
155              This is due primarily to murine factor XIa preferentially cleaving a site on zymogen fac
156 vation in plasma, conversion of factor XI to factor XIa proceeds through an intermediate with one act
157  by providing a template for the assembly of factor XIa-protease nexin-2 complexes, and only heparin
158 vage of factor IX by four single active site factor XIa proteases.
159 nvolved in factor IX activation, recombinant factor XIa proteins containing alanine substitutions for
160             Activated coagulation factor XI (factor XIa) proteolytically cleaves its substrate, facto
161 luorescence titration of active site-labeled factor XIa revealed a binding stoichiometry of 1.9 +/- 0
162 d to identify the molecular subdomain within factor XIa that binds to activated platelets.
163 ition accompanies conversion of factor XI to factor XIa that conceals the Apple 3 domain factor XI (z
164  effect, suggesting that the binding site in factor XIa that interacts with the platelet surface resi
165 le370-Val607) inhibited the binding of [125I]factor XIa to the platelets (Ki approximately 3.5 nM), w
166 erations of ZPI reactions with factor Xa and factor XIa to yield second order rate constants approach
167  contribute significantly to the affinity of factor XIa toward factor IX.
168 ed, irrespective of whether tissue factor or factor XIa was used as an initiator.
169 e development during factor IX activation by factor XIa when using a low substrate to enzyme ratio (4
170 potent inhibitors of factor IX activation by factor XIa, whereas antibodies against the A2 (1A6) and
171               Recombinant factor IX bound to factor XIa with a K(d) of 107 nm, whereas factor IX with
172 s the ability of protease nexin-2 to inhibit factor XIa with a parabolic concentration dependence, pr
173 Kunitz-type domain, is a potent inhibitor of factor XIa with an inhibition constant of 250-400 pM.
174        Plasma factors IX and IXabeta bind to factor XIa with K(d) values of 120 +/- 11 nm and 110 +/-
175 ediate formation was detected with 1/2-FXIa, factor XIa with one inhibited active site, or a recombin
176 is the zymogen of a dimeric plasma protease, factor XIa, with two active sites.
177 ts inhibitory interaction with factor Xa and factor XIa, ZPI is proteolytically cleaved with the rele

 
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