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1 type I (IL-1RI) and IL-1R accessory protein (IL-1RAcP).
2 designated IL-1 receptor accessory protein (IL-1RAcP).
3 6R.IL-36alpha binary complex, which recruits IL-1RAcP.
4 ary complex with IL-36R, which then recruits IL-1RAcP.
5 signaling by a decrease of interaction with IL-1RAcP.
6 raction of IL-1Rrp2 ECD with the co-receptor IL-1RAcP.
7 ated co-immunoprecipitation of IL-1Rrp2 with IL-1RAcP.
8 ceptor family members IL-1Rrp2 (IL-1RL2) and IL-1RAcP.
9 uction can be inhibited by dominant-negative IL-1RAcP.
10 -1F8, and IL-1F9 signal through IL-1Rrp2 and IL-1RAcP.
11 s dependent on the expression of IL-1RI, not IL-1RAcP.
12 e was no change in the surface expression of IL-1RAcP.
13 ide 4 recognized intact IL-1RAcP and soluble IL-1RAcP.
14 tion of a complex containing both IL-1RI and IL-1RAcP.
15 to this complex through its association with IL-1RAcP.
16 cromolar affinity but do not detectably bind IL-1RAcP.
17 form a complex with IL-1R accessory protein (IL-1RAcP), a signaling receptor subunit that is also a m
19 rface plasmon resonance (SPR), we found that IL-1RAcP also does not bind IL-36R when no agonist is pr
23 pression of IL-1 receptor accessory protein (IL-1RAcp) and IL-1 type I receptor (IL-1RI), but not IL-
25 and transfection of cytoplasmically deleted IL-1RAcP both blocked activation of the pathway leading
27 The implications of this shared usage of IL-1RAcP by IL-1(alpha and beta) and IL-33 are discussed
28 upt the interaction of MyD88 with the IL-1RI/IL-1RAcP complex, we analyzed the involvement of MyD88 i
31 the IL-1RI/IL-1 receptor accessory protein (IL-1RAcP) complex through homomeric Toll/IL-1 receptor (
32 ot measure the binding affinity of IL-36R to IL-1RAcP directly, so we engineered a fragment crystalli
34 xpression of ectodomain (ECD) of Il-1Rrp2 or IL-1RAcP exhibited dominant-negative effect on IL-36R si
35 R1) and the IL-1 receptor accessory protein (IL-1RAcP) form a functional IL-1 receptor complex that i
36 mRNA arises from alternative splicing of the IL-1RAcP gene (shown here to encompass 12 exons spanning
37 tallizable-linked construct to induce IL-36R.IL-1RAcP heterodimerization and predicted the binding af
39 e previously reported a novel isoform of the IL-1RAcP, IL-1RAcPb, found exclusively in CNS neurons.
44 nvolved in complex formation with IL-1RI, 3) IL-1RAcP is not regulated as is IL-1RI in the same cells
46 ine family, IL-1 receptor accessory protein (IL-1RAcP) is the co-receptor for eight receptor-cytokine
49 2, 3, and 4 recognized surface expression of IL-1RAcP on the Th2 D10S cells by FACS and inhibited IL-
54 33Ralpha (ST2L)/IL-1alpha accessory protein (IL-1RAcP) receptor that coordinates activation of ERK an
55 that IL-36Ra binds to IL-1Rrp2 and prevents IL-1RAcP recruitment and the formation of a functional s
56 Two alternatively spliced isoforms, soluble IL-1RAcP (sIL-1RAcP) and sIL-1RAcP-beta, which lack tran
57 Proportional expression of the different IL-1RAcP splice variants may be an important determinant
58 at the main pathway to the IL-36R.IL-36alpha.IL-1RAcP ternary complex is through the IL-36R.IL-36alph
59 ophilic peptide regions of the extracellular IL-1RAcP that may be available for complex formation (pe
60 and engaged identical molecular surfaces of IL-1RAcP, these cytokines had starkly different strategi
61 o IL-1RI to properly present the cytokine to IL-1RAcP, whereas IL-33 binds to ST2 in order to conform
62 the heterodimerization of IL-1 receptor and IL-1RAcP, whereas the intracellular TIR domain inhibits
63 rmalities that are dependent on IL-1Rrp2 and IL-1RAcP, which are two members of the IL-1R family.
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