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1 d phosphorylated Thr-871 and Ser-1120 in the ErbB3 receptor.
2 these cells to the bone marrow requires the ErbB3 receptor.
3 activation of the PI3-kinase pathway by the ErbB3 receptor.
4 neuregulin-1beta (NRG1beta) binding to ErbB2/ErbB3 receptors.
6 ress, enhancing cell invasion, by activating ERBB3 receptor and its downstream targets PYK2 and SRC t
8 uronan to facilitate signaling through ErbB2/ErbB3 receptors and then is terminated by an increase in
9 ErbB2 heterodimerizes with and activates the ErbB3 receptor, and the two receptors synergize in promo
10 of EGF by up-regulating EGFR, c-ErbB2 and c-ErbB3 receptors, and by enhancing EGF-stimulated tyrosin
11 , are phenocopied by loss of oligodendrocyte ErbB3 receptors, and social isolation leads to reduced e
16 tein identified by its interactions with the ErbB3 receptor, down-regulates expression of AR and AR-r
18 induces the relocalization of the ErbB2 and ErbB3 receptors from intracellular compartments to the p
19 cted with adenoviral particles containing an ErbB3 receptor gene or a vehicle beta-galactosidase gene
21 his work, we altered the levels of ErbB2 and ErbB3 receptors, individually and in combination, by usi
22 ity, heregulin-beta (HRGbeta) binding to the erbB3 receptor initiated rapid and potent induction of b
23 nds the soluble extracellular domains of the ERBB3 receptor into a targeted and highly specific cross
25 th ATFs, the effects of changes in ErbB2 and ErbB3 receptor levels were evaluated by using cell proli
28 turally occurring secreted form of the human ErbB3 receptor, p85-soluble ErbB3 (sErbB3), is a potent
30 howed a specific interaction of Shc with the ErbB3 receptor protein and demonstrated the importance o
32 and L3.6pl cells, which highly expressed the ErbB3 receptor, significant reduction in cell viability,
33 he tyrosine phosphorylation of the ErbB2 and ErbB3 receptors to similar extents, but only NRG1beta po
35 iology, we are studying the specific role of ErbB3 receptor tyrosine kinase (RTK) since it is the rec
39 ved NRG1 activation of cancer cell ERBB2 and ERBB3 receptor tyrosine kinases as a mechanism by which
40 the insulin-like growth factor-I (IGF-I) and ErbB3 receptor tyrosine kinases, and prolonged the assoc
41 D44 constitutively associated with erbB2 and erbB3, receptor tyrosine kinases that heterodimerize and
42 ee receptors were expressed, though only the erbB3 receptor was phosphorylated, suggesting that overe
43 ulate the trafficking or localization of the ErbB3 receptor, we have identified a tripartite or RBCC