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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
13 molecules containing one of three different IL-3 receptor agonists linked with a common G-CSF recept
15 s due at least in part to down-regulation of IL-3 receptor alpha (IL-3Ralpha) surface expression in t
17 e found that in primary patient samples, the IL-3 receptor alpha chain CD123 was highly expressed on
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
24 imeric proteins that are both interleukin-3 (IL-3) receptor and granulocyte colony-stimulating factor
26 factor receptor beta common (IL-3Rbetac) and IL-3 receptor beta (IL-3Rbeta) chains in murine embryoni
28 sine phosphorylation; phosphorylation of the IL-3 receptor beta subunit and the Shc protein were both
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
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
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-
48 involvement with FSCCL cells that expressed IL-3 receptors had temporary growth arrest of the circul
50 y permuted G-CSF (cpG-CSF) sequences with an IL-3 receptor (IL-3R) agonist moiety attached at locatio
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,
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