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1 -directed mutagenesis to define the specific phosphorylated tyrosine residues.
2 mino-terminal region of Cbl (Cbl-N) binds to phosphorylated tyrosine residues and has cell-transformi
3 l killer cells, and the functions of the two phosphorylated tyrosine residues are distinct and separa
4 hatase from its association with N-cadherin, phosphorylated tyrosine residues are retained on beta-ca
5 CTEN is not only required for binding to the phosphorylated tyrosine residue at codon 774 of c-Cbl, b
6 eptor tyrosine-based activation motif (ITAM) phosphorylated tyrosine residue at position 204 in the t
7                                              Phosphorylated tyrosine residues can serve as associatio
8                                              Phosphorylated tyrosine residues function as binding sit
9 interaction between the LNK SH2 domain and a phosphorylated tyrosine residue in KIAA0157 (Abraxas2),
10 s of v-Src bind to proline-rich motifs and a phosphorylated tyrosine residue in the C-terminal tail o
11 -Pyk2 association, and mutating specific Src-phosphorylated tyrosine residues in dynamin blunts the d
12 eriments revealed that Lnk directly binds to phosphorylated tyrosine residues in JAK2 following TPO s
13 d ion spectroscopy for the identification of phosphorylated tyrosine residues in peptides.
14 bers are activated by SCF and associate with phosphorylated tyrosine residues in the c-Kit juxtamembr
15 binding is dependent on interactions between phosphorylated tyrosine residues in zeta-chain activatio
16 ses that bind the cytoplasmic domain through phosphorylated tyrosine residues located within consensu
17                                              Phosphorylated tyrosine residues of growth factor recept
18                                              Phosphorylated tyrosine residues on beta-catenin are cor
19 nhibitors also result in the accumulation of phosphorylated tyrosine residues on beta-catenin, loss o
20 core protein, results in the accumulation of phosphorylated tyrosine residues on beta-catenin, uncoup
21 ze the number and relative levels of in vivo-phosphorylated tyrosine residues on endogenous p190 from
22  its SH2 domain, was associated with several phosphorylated tyrosine residues on nephrin.
23         During leptin signaling, each of the phosphorylated tyrosine residues on the long form of the
24 growth factor (PDGF) receptors, and multiple phosphorylated tyrosine residues on the PDGF receptor we
25  v/v) show five phosphorus sites assigned to phosphorylated tyrosine residues, phosphorylated serine
26 een Src-homology 2 domains (SH2) domains and phosphorylated tyrosine residues serves a critical role
27  require that the SH2 domain be able to bind phosphorylated tyrosine residues - thus Grb2 bound to Bt
28 s of Sos, is known to depend on a C-terminal phosphorylated tyrosine residue (Tyr798) in RPTPalpha an
29                        The function of these phosphorylated tyrosine residues was assessed by mutatio
30 93 cells, these mutant RPTPgammas retained a phosphorylated tyrosine residue, whereas similarly expre
31 ed fluorescence assay, we mapped the various phosphorylated tyrosine residues with the actin-nucleati
32               The current study identified a phosphorylated tyrosine residue within the C-terminal po
33           Grb2 binding is mediated through a phosphorylated tyrosine residue (Y177) located within a