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コーパス検索結果 (１語後でソート)

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1 invading 5'-OH poised to attack the covalent phosphotyrosine residue.
2 , which recognizes phosphoserine rather than phosphotyrosine residues.
3 (BPS and Src homology domains) with receptor phosphotyrosine residues.
4 ssing Bcr-Abl under conditions that preserve phosphotyrosine residues also reduced Bcr's kinase activ
5 aptor protein, docking to others through its phosphotyrosine residues and protein-interacting domain.
6 inds of D-tetrapeptide containing one or two phosphotyrosine residues and with the N-terminal capped
7  consisting of an N-capped d-tetrapeptide, a phosphotyrosine residue, and a diester or a diamide grou
8 ve been shown in cell culture systems to use phosphotyrosine residues as docking sites for certain si
9 hrough binding of the Nck1 SH2 domain to the phosphotyrosine residue at position 602 (Y602) of the Ep
10 ommercial phosphopeptide containing a single phosphotyrosine residue but did not cleave phosphoserine
11 d changes that interfere with Shc binding to phosphotyrosine residues do not affect Numb activity in
12  dephosphorylation on the critical 1007-1008 phosphotyrosine residues, implying JAK2 inhibition and t
13 tions involve binding of the SH2 domain to a phosphotyrosine residue in the C-terminal tail and assoc
14 phorylating the phosphothreonine but not the phosphotyrosine residue in the phosphorylation lip.
15 phosphotyrosine binding domain that binds to phosphotyrosine residues in both human and Drosophila in
16 e substrates; however, the function of these phosphotyrosine residues in cancer cells is a subject of
17 CS1, via its Src homology 2 domain, binds to phosphotyrosine residues in its targets, reducing the am
18 drolyse a generic phosphatase substrate, and phosphotyrosine residues in synthetic peptides.
19                    The STAT proteins bind to phosphotyrosine residues in the cytoplasmic domain of th
20 ggest that SHIP and CIS interact with distal phosphotyrosine residues in the G-CSFR to negatively reg
21  interactions among three negatively charged phosphotyrosine residues in the receptor C terminus may
22 ounding, the MBP kinase is phosphorylated on phosphotyrosine residues, indicating a relationship to t
23 ides in a similar mode, with the tyrosine or phosphotyrosine residue inserted into the phosphotyrosin
24 cellular signaling, and dephosphorylation of phosphotyrosine residues is crucial for termination of s
25 e carboxy-terminal location of the candidate phosphotyrosine residues is more reminiscent of the Kapo
26 ibers were distinct from diffuse staining of phosphotyrosine residues observed in asbestos-exposed cu
27 s insulin signaling by dephosphorylating the phosphotyrosine residues of the insulin receptor kinase
28 g insulin signaling by dephosphorylating the phosphotyrosine residues of the insulin receptor.
29                                    Thus, two phosphotyrosine residues of TLR3 activate two distinct p
30                                 We find that phosphotyrosine residues on ErbB1 have half-lives of a f
31  SH2 domain of STAT6 to block recruitment to phosphotyrosine residues on IL-4 or IL-13 receptors and
32 interaction between the STATc SH2 domain and phosphotyrosine residues on Pyk2 that are generated by a
33  protein-protein interactions by recognizing phosphotyrosine residues on target proteins.
34                          It dephosphorylates phosphotyrosine residues on the four different 32P-tyros
35 ys a strong preference for dephosphorylating phosphotyrosine residues over phosphothreonine residues.
36  kinases by hydrolyzing phosphothreonine and phosphotyrosine residues present in the substrates.
37 of neighboring negatively charged N-terminal phosphotyrosine residues, promoting swelling of caveolae
38                                  A synthetic phosphotyrosine residue (pY) peptide derived from the er
39                      This motif contains two phosphotyrosine residues separated by one residue (seque
40 nism have been elusive because c-Abl lacks a phosphotyrosine residue that triggers the assembly of th
41 ipates in the activation of Fyn by providing phosphotyrosine residues that bind the SH2 domain of Fyn
42         Inhibition of ACE by TFII-I requires phosphotyrosine residues that engage the SH2 (Src-homolo
43                 By interacting with specific phosphotyrosine residues, they provide regulatable prote
44 d a ShcA mutant (R175Q) that no longer binds phosphotyrosine residues via its PTB domain.
45                             In addition, the phosphotyrosine residue was replaced with a difluorophos
46 nce are enriched on proteins with two nearby phosphotyrosine residues, which can be directly protecte
47 ABE-II requires the presence of at least one phosphotyrosine residue with Y(P)422 being the more impo
48 etermine that interaction of the homeodomain phosphotyrosine residues with an adjacent domain in the