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1 4 of 5 patients reacted with sulfatide-bound beta2-glycoprotein I.
2 is reduction is dependent on the presence of beta2-glycoprotein I.
3 with anionic phospholipids in the absence of beta2-glycoprotein I.
4 attern with preferential reactivity to mouse beta2-glycoprotein I.
6 up 1 patients who were positive for IgA anti-beta2-glycoprotein I (aB2GP1) and B2A-CIC (n=125); group
7 ne origin, which are known to bind to plasma beta2-glycoprotein I (aka apolipoprotein H), correlates
11 holipid antibodies, bound to sulfatide-bound beta2-glycoprotein I and previous absorption on cardioli
12 lly: 3 in serum (anticardiolipin antibodies, beta2-glycoprotein I, and anti-phosphatidyl-serine) and
13 ents and procoagulation factors such as anti-beta2-glycoprotein I (anti-beta2GPI) or anticardiolipin
14 , anticardiolipin antibodies (aCL), and anti-beta2-glycoprotein I antibodies (anti-beta2GPI) were als
16 hase I trial of a tolerogen directed at anti-beta2-glycoprotein I antibodies demonstrated a decrease
17 , or positivity for anticardiolipin- or anti-beta2-glycoprotein I antibodies were not associated with
18 al anticardiolipin antibodies (aCL) (as anti-beta2-glycoprotein I antibodies) by semiquantitative 32P
20 investigated the role of the serum protein, beta2-glycoprotein I as an initiating Ag for Ab recognit
21 circulating immune complexes of IgA bound to beta2-glycoprotein I (B2A-CIC) has been associated with
22 anionic phospholipid and the plasma protein beta2-glycoprotein I (beta 2GPI) or the protein beta 2GP
23 I as an initiating Ag for Ab recognition and beta2-glycoprotein I (beta2-GPI) peptides as a therapeut
26 ibodies are directed against prothrombin and beta2-glycoprotein I beta2GPI), a phospholipid-binding p
27 n of the phospholipid binding plasma protein beta2 glycoprotein I (beta2GPI) for antibody binding and
28 antiphospholipid antibodies (aPL) binding to beta2 glycoprotein I (beta2GPI) induce endothelial cell-
29 PLAs associated with these events react with beta2 glycoprotein I (beta2GPI), and endothelial cell re
36 Most pathogenic APLAs are directed against beta2-glycoprotein I (beta2GPI), a plasma phospholipid b
40 recognize a conformational epitope shared by beta2-glycoprotein I (beta2GPI; the major autoantigen fo
41 nclude discovery of the crystal structure of beta2-glycoprotein I, (beta2GPI), genetic studies of bet
44 reased the immunoreactivity toward sulfatide-beta2-glycoprotein I complex by >50% in 12 of 14 patient
46 riodontal disease status for serum levels of beta2-glycoprotein I-dependent anti-cardiolipin autoanti
48 periodontitis have elevated serum levels of beta2-glycoprotein-I-dependent anti-cardiolipin (anti-CL
52 entration of 5 microg/mL, maximal binding of beta2-glycoprotein I is observed at a coating density of
53 icroM, but if the reactants are reversed and beta2-glycoprotein I is on the solid-phase support, then
54 mice of anti-phospholipid Abs reacting with beta2-glycoprotein I may contribute to the pathogenesis
55 Ib or anionic phospholipid-binding proteins (beta2-glycoprotein I or annexin V) had no effect in thes
57 sulfatide coating density of 1 microg/well, beta2-glycoprotein I reaches half-maximal binding at 2.5
59 indicated that binding of the serum protein, beta2-glycoprotein I, to the endothelium initiates a cas
60 erived from the binding domain (domain V) of beta2-glycoprotein I would attenuate ischemia/reperfusio
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