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1 s may be mediated by direct interaction with IL-3 receptor.
2 e IL-6 receptor, gp130, or by co-transfected IL-3 receptor.
3 ability to activate Stat5 via the endogenous IL-3 receptor.
4 a protein represents the beta subunit of the IL-3 receptor.
5 -deficient cells selectively upregulated the IL-3 receptor.
6  myeloid progenitors expressed low levels of IL-3 receptor.
7 n is internalized by hematopoietic cells via IL-3 receptors.
8  by the beta c subunit of the interleukin-3 (IL-3) receptor.
9  results suggested that cytokine-independent IL-3 receptor activation could be a dominant signaling c
10 similar to control cells, demonstrating that IL-3 receptor activation is not essential for BCR-ABL-in
11 s potent than that of the individual cognate IL-3 receptor agonist.
12 iation rates than the corresponding specific IL-3 receptor agonists alone.
13  molecules containing one of three different IL-3 receptor agonists linked with a common G-CSF recept
14 otent than those of their individual cognate IL-3 receptor agonists.
15 s due at least in part to down-regulation of IL-3 receptor alpha (IL-3Ralpha) surface expression in t
16      NIH 3T3 cells transduced with the human IL-3 receptor alpha and beta chains were highly suscepti
17 e found that in primary patient samples, the IL-3 receptor alpha chain CD123 was highly expressed on
18  in hypophosphorylated Rb, but did not alter IL-3 Receptor alpha or beta subunit levels.
19 ests that the interface between IL-3 and the IL-3 receptor alpha subunit consists of a cluster of hyd
20 , we detected increased IL-1RI and decreased IL-3 receptor alpha-chain (CD123) and CCR3 expression on
21 aluated the expression of the interleukin 3 (IL-3) receptor alpha subunit (CD123), an established mar
22                    CD123, the interleukin-3 (IL-3) receptor alpha-chain, is highly expressed in vario
23                            We found that the IL-3 receptor-alpha (IL-3Ralpha) is a promising candidat
24 imeric proteins that are both interleukin-3 (IL-3) receptor and granulocyte colony-stimulating factor
25 ures that is inhibited by anti-IL-3 and anti-IL-3 receptor antibodies.
26 factor receptor beta common (IL-3Rbetac) and IL-3 receptor beta (IL-3Rbeta) chains in murine embryoni
27           CIS is known to associate with the IL-3 receptor beta chain and erythropoietin receptor and
28 sine phosphorylation; phosphorylation of the IL-3 receptor beta subunit and the Shc protein were both
29                            Although the IL-3/IL-3 receptor beta subunit interface cannot be uniquely
30 s to define the interaction between IL-3 and IL-3 receptor beta subunit.
31 of PI-3K, others, such as the interleukin-3 (IL-3) receptor beta common chain (betac) and the IL-2 re
32 ly through an additional beta subunit of the IL-3 receptor (beta IL3) that is present in the mouse.
33 ed to stable tyrosine phosphorylation of the IL-3 receptor, beta common (betac), and STAT5 following
34 erved that a constitutively activated mutant IL-3 receptor, beta(c)V449E, cooperated with PML-RARalph
35 eceptor agonist have been examined for their IL-3 receptor binding characteristics.
36 ferential modulation of affinity observed in IL-3 receptor binding may be a direct result of the magn
37 in was identified as the beta subunit of the IL-3 receptor by immunoblotting with an anti-beta antibo
38 hibited in the presence of neutralizing anti-IL-3 receptor (CD123) Abs.
39                      The beta subunit of the IL-3 receptor co-immunoprecipitated with hck in lysates
40                          A model of the IL-3.IL-3 receptor complex based on the human growth hormone
41  To unambiguously define the significance of IL-3 receptor-dependent signaling in BCR-ABL-induced leu
42 , whereas BCR-ABL+ NIH 3T3 cells lacking the IL-3 receptor do not utilize the Jak2 pathway, but still
43   Taken together, these results suggest that IL-3 receptors engage and activate both c-Raf and A-Raf
44  molecules to the heteromultimeric alphabeta IL-3 receptor expressed on TF-1 cells was either 3-, 10-
45 agar, whereas BCR-ABL+ NIH 3T3 cells lacking IL-3 receptor expression did not.
46                                              IL-3 receptor expression was dramatically up-regulated i
47                             The up-regulated IL-3 receptor expression was not affected by IL-3 or STA
48  involvement with FSCCL cells that expressed IL-3 receptors had temporary growth arrest of the circul
49 ignal transduction pathways activated by the IL-3 receptor, however, are not fully understood.
50 y permuted G-CSF (cpG-CSF) sequences with an IL-3 receptor (IL-3R) agonist moiety attached at locatio
51                                 Although the IL-3 receptor is expressed on the surfaces of follicular
52 dicate that Bcr-Abl oncoprotein requires the IL-3 receptor/Jak2/Stat5 pathways for oncogenic transfor
53 ) SC-55494 is a high-affinity interleukin-3 (IL-3) receptor ligand that stimulates greater in vitro m
54  has been suggested that p210Bcr/Abl and the IL-3 receptor may activate some common signal transducti
55  Signaling studies indicate that the BCR-ABL/IL-3 receptor+ NIH 3T3 cells utilize the Gab2/PI-3 kinas
56 nse to IL-3 through dephosphorylation of the IL-3 receptor, perhaps in an intracellular compartment,
57        Moreover, IFN-stimulated interleukin (IL)-3 receptor (R)alpha(+) blood precursor (pre-)DCs dis
58          Binding to the alpha-subunit of the IL-3 receptor revealed that the affinity of the MPO mole
59 nd activating factor for eosinophils and the IL-3 receptor shares with the IL-5 and GM-CSF receptors
60 portance of targeting ICAM-1 and GM-CSF/IL-5/IL-3 receptor systems as a therapeutic strategy to count
61 nk between the alpha4beta1 integrin and IL-3/IL-3-receptor that could affect the position of stem and
62 e three kinases with the beta subunit of the IL-3 receptor was further investigated using bacterial f
63 in circulating eosinophils and expression of IL-3 receptors, whereas airway eosinophilia and eosinoph
64 es signaling via the beta-common and/or beta-IL-3 receptors, with evidence of deregulated responses t
65  determined whether forced expression of the IL-3 receptor would allow oncogenic transformation of NI