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1 aflet of apoptotic cell membranes, and CD14 (LPS-binding protein).
2 ein and accessory proteins, such as CD14 and LPS binding protein.
3 s inhibited by anti-CD14 mAb and enhanced by LPS binding protein.
4 des directly inhibited the binding of LPS to LPS-binding protein.
5 anced by the addition of soluble CD14 and/or LPS-binding protein.
6 ses to LPS, and not to PGN, were enhanced by LPS-binding protein.
7 dependent and was not augmented by exogenous LPS-binding protein.
8 4-70Z/3 cells by H. pylori LPS also requires LPS-binding protein.
9 quires the presence of plasma containing the LPS-binding protein.
10 he 20S proteasome complex were identified as LPS-binding proteins.
11 opology of the "active-site" beta-strands of LPS-binding proteins.
13 nitially bound by transfer proteins, notably LPS binding protein and phospholipid transfer protein, a
14 by competing with E. coli LPS for binding to LPS-binding protein and by directly competing with E. co
15 man SR-BI orthologue, was determined to be a LPS-binding protein and endocytic receptor mediating the
16 and LPS-triggered responses were enhanced by LPS-binding protein and inhibited by an anti-CD14 monocl
18 suring circulating lipopolysaccharide (LPS), LPS-binding protein and soluble CD14 at baseline and whe
19 These data indicate that MD-2 is a genuine LPS-binding protein and strongly suggest that MD-2 could
20 cells to LPS require a plasma protein called LPS-binding protein and the glycosylphosphatidylinositol
21 The structure reveals homology to eukaryotic LPS-binding proteins and allowed for the prediction of a
22 homologous to the LPS binding region of the LPS binding protein, and we demonstrated that two basic
23 no acid conservation, structural analysis of LPS-binding proteins, and MD simulations further confirm
24 d formed monomeric complexes with MD-2 in an LPS-binding protein- and CD14-dependent manner with simi
25 by 12.4% (range: 6.7%-17.5%, P < 0.001), and LPS-binding protein by 20.7% (range: 14.1%-26.4%, P < 0.
26 /CD18-transfected CHO-K1, thus implying that LPS-binding protein can also transfer LPS to CD11/CD18.
27 100A8; the acute-phase protein SAA3; and the LPS binding protein CD14 were confirmed by Northern blot
28 rotein and protein-protein interactions with LPS-binding protein, CD14, myeloid differentiation prote
29 assay, suggest that recombinant factor C, an LPS binding protein, competitively inhibits high-density
32 induction of APP, including serum amyloid A, LPS-binding protein, fibrinogen, or ceruloplasmin; in co
33 es demonstrated that these surface expressed LPS-binding proteins had characteristics that were quali
34 lease from the cells, high concentrations of LPS-binding protein have a modest effect, and phospholip
35 easing protein (BPI) and lipopolysaccharide (LPS)-binding protein, have been considered to be members
38 This study addresses the role of CD14 and LPS-binding protein in the cellular response to H. pylor
39 This cross-linker was used to identify the LPS-binding proteins in membranes of the murine-macropha
42 s of microbial translocation, as measured by LPS-binding protein, in PTM correlated with the rate of
43 receptor molecules in HCEP, that one of the LPS binding proteins is galectin-3, and that the outer c
44 that TECs express CD14, a well-characterized LPS-binding protein known to mediate many LPS responses.
52 d plasma levels of lipopolysaccharide (LPS), LPS binding protein (LBP), soluble CD14 (sCD14), and int
53 ir blood drawn to assess endotoxemia markers LPS binding protein (LBP), soluble CD14 (sCD14), and the
62 de (LPS) (P = .0002), sCD14 (P = .0191), and LPS-binding protein (LBP) (P < .0001) were significantly
63 o closely related endogenous serum proteins, LPS-binding protein (LBP) and bactericidal/permeability-
64 We have investigated the effects of human LPS-binding protein (LBP) and human bactericidal/permeab
65 in, we found that two human plasma proteins, LPS-binding protein (LBP) and phospholipid transfer prot
66 between 2 plasma biomarkers of LPS exposures-LPS-binding protein (LBP) and soluble cluster of differe
67 popolysaccharide (LPS)-interactive proteins, LPS-binding protein (LBP) and the bacteridical/permeabil
72 sm(s) remains to be fully defined, the human LPS-binding protein (LBP) is known to regulate responses
74 lycosylphosphatidylinositol-anchored form of LPS-binding protein (LBP), a component of serum that bin
76 onses to LPS are markedly potentiated by the LPS-binding protein (LBP), a lipid-transfer protein that
77 cytokines as well as components of the LPS, LPS-binding protein (LBP), and CD14 system in bronchoalv
78 plex consisting of lipopolysaccharide (LPS), LPS-binding protein (LBP), and the cell surface antigen
79 and correlate with C-reactive protein (CRP), LPS-binding protein (LBP), and the NIH stroke scale (NIH
80 , TLR4, and MD-2, which, in conjunction with LPS-binding protein (LBP), bind LPS to the virus and aug
81 ormation of the LPS receptor complex by LPS, LPS-binding protein (LBP), CD14, and toll-like receptor
82 by two closely related LPS-binding proteins, LPS-binding protein (LBP), which potentiates LPS' inflam
90 PS)) can be regulated by two closely related LPS-binding proteins, LPS-binding protein (LBP), which p
91 that TLR2 associates with the high-affinity LPS binding protein membrane CD14 to serve as an LPS rec
92 n a CD14-dependent manner, and soluble CD14, LPS binding protein, or their combination potentiated bo
94 contrast, the addition of recombinant human LPS-binding protein (rLBP) had opposing effects on the L
95 els of circulating lipopolysaccharide (LPS), LPS-binding protein, soluble CD14, and fucose-binding le
96 n-induced cytokine production was maximal at LPS-binding protein:soluble CD14 ratios <1, typically ob
97 dividuals with subclinical infection; higher LPS-binding protein:soluble CD14 ratios were inhibitory.
98 ons, in a defined medium containing purified LPS-binding protein, the LPS-deacylating activity of MNC
99 form complexes with a serum protein known as LPS-binding protein; the LPS in this complex is subseque
100 we show that LPS in the presence of serum or LPS binding protein triggers formation of CD14-CR3 compl
104 increasing protein (BPI) are closely related LPS-binding proteins whose binding to LPS has markedly d
105 iginally identified as a lipopolysaccharide (LPS) binding protein with gram-negative bactericidal act