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1 ), requires outside-in signaling through the fibrinogen receptor.
2 sess normal levels of the alpha(IIb)/beta(3) fibrinogen receptor.
3 pon active plasmin, yet independent of known fibrinogen receptors.
4 e C-regulated pathway leads to inhibition of fibrinogen receptor activation on platelets adherent to
5 Thromboxane A2 (TxA2) generation, as well as fibrinogen receptor activation, are normal in the absenc
9 ocyte chemoattractant protein-1, P-selectin, fibrinogen, receptor activator of nuclear factor-kappaB
10 nearly 250 analogues, which were assayed for fibrinogen receptor affinity and inhibition of platelet
11 n RGE-containing peptide and four nonpeptide fibrinogen receptor (alpha IIb beta 3) antagonists faile
17 oxide, fibrinogen binding, and activation of fibrinogen receptor alphaIIbbeta3, was observed in throm
19 uded that both outside-in signaling from the fibrinogen receptor and inside-out signaling from the P2
20 ot dependent on either the FcgammaRII or the fibrinogen receptor and that appears to play a role in p
21 re, occurs in 1% to 2% of patients given the fibrinogen receptor antagonist abciximab, a chimeric Fab
22 yl-beta-alanine, 6d (L-767,679), is a potent fibrinogen receptor antagonist able to inhibit the ADP-i
24 ation of this prodrug strategy to the chiral fibrinogen receptor antagonist L-734,217 resulted in a p
25 structure-activity surrounding the prototype fibrinogen receptor antagonist RWJ-50042 (racemate of 1)
26 ition of 2-MeSADP-induced TxA2 generation by fibrinogen receptor antagonist was not rescued by co-sti
29 tivation with aspirin had no effect, but the fibrinogen receptor antagonist, GR144053F, inhibited pla
33 exes and human platelets pretreated with the fibrinogen receptor antagonists eptifibatide or abcixima
34 y potent nonpeptide 3-oxo-1,4-benzodiazepine fibrinogen receptor antagonists from a constrained, RGD-
36 ent, selective, orally active, peptide-based fibrinogen receptor antagonists with a long duration of
38 ore spherical and extrude pseudopodia, their fibrinogen receptors are activated, causing them to aggr
39 e had nonsignificantly greater wound-induced fibrinogen receptor binding than the other subjects.
40 wn, except that alpha IIb beta 3, a platelet fibrinogen receptor, binds to the gamma C HHLGGAKQAGDV40
45 characterized by shape change, induction of fibrinogen receptor expression and release of granular c
46 t of Integrelin, which inhibits the platelet fibrinogen receptor glycoprotein (GP) IIb/IIIa, on the f
47 Variabilin was a potent antagonist of the fibrinogen receptor glycoprotein IIb-IIIa (GPIIb-IIIa; a
48 limited the ability to maintain the platelet fibrinogen receptor, glycoprotein alpha(IIb)/beta(3), in
49 , results from abnormalities in the platelet fibrinogen receptor, GP(IIb)-IIIa (integrin alpha(IIb)be
50 cy because of the lack or dysfunction of the fibrinogen receptor GPIIb/IIIa (integrin alphaIIbbeta3),
51 ough intravenously administered antiplatelet fibrinogen receptor (GPIIb/IIIa) antagonists have become
52 for GPIb differs from that reported for the fibrinogen receptor, GPIIb-IIIa, and could have profound
55 protein that binds to the alpha(IIb)beta(3) fibrinogen receptor, interacts exclusively with activate
58 alphaIIbbeta3 (or GPIIb/IIIa), the platelet fibrinogen receptor, is unknown but may involve the bind
59 conclude that collagen-induced activation of fibrinogen receptor on adherent platelets through GPVI s
61 clear whether collagen can directly activate fibrinogen receptors on the adherent platelets without a
63 elated, being inhibited by blocking platelet fibrinogen receptors or by preventing plasminogen bindin
64 ntegrin alpha v beta 3, a widely distributed fibrinogen receptor, recognizes the RGD572-574 motif in
66 in the beta subunit of the alpha(IIb)beta(3) fibrinogen receptor, suggesting a mechanism for facilita
68 ly activates the integrin alphaIIbbeta3 (the fibrinogen receptor), the PDI inhibitors were without ef
69 elet aggregation is mediated by the platelet fibrinogen receptor, the alpha IIb beta 3 integrin (glyc
70 ) is converted from an inactive to an active fibrinogen receptor, thereby mediating platelet aggregat
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