ライフサイエンスコーパス: phosphotyrosine residue

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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 CS1, via its Src homology 2 domain, binds to phosphotyrosine residues in its targets, reducing the am

17 drolyse a generic phosphatase substrate, and phosphotyrosine residues in synthetic peptides.

18 The STAT proteins bind to phosphotyrosine residues in the cytoplasmic domain of th

19 ggest that SHIP and CIS interact with distal phosphotyrosine residues in the G-CSFR to negatively reg

20 interactions among three negatively charged phosphotyrosine residues in the receptor C terminus may

21 ounding, the MBP kinase is phosphorylated on phosphotyrosine residues, indicating a relationship to t

22 ides in a similar mode, with the tyrosine or phosphotyrosine residue inserted into the phosphotyrosin

23 cellular signaling, and dephosphorylation of phosphotyrosine residues is crucial for termination of s

24 e carboxy-terminal location of the candidate phosphotyrosine residues is more reminiscent of the Kapo

25 ibers were distinct from diffuse staining of phosphotyrosine residues observed in asbestos-exposed cu

26 s insulin signaling by dephosphorylating the phosphotyrosine residues of the insulin receptor kinase

27 g insulin signaling by dephosphorylating the phosphotyrosine residues of the insulin receptor.

28 Thus, two phosphotyrosine residues of TLR3 activate two distinct p

29 We find that phosphotyrosine residues on ErbB1 have half-lives of a f

30 SH2 domain of STAT6 to block recruitment to phosphotyrosine residues on IL-4 or IL-13 receptors and

31 interaction between the STATc SH2 domain and phosphotyrosine residues on Pyk2 that are generated by a

32 protein-protein interactions by recognizing phosphotyrosine residues on target proteins.

33 It dephosphorylates phosphotyrosine residues on the four different 32P-tyros

34 ys a strong preference for dephosphorylating phosphotyrosine residues over phosphothreonine residues.

35 kinases by hydrolyzing phosphothreonine and phosphotyrosine residues present in the substrates.

36 of neighboring negatively charged N-terminal phosphotyrosine residues, promoting swelling of caveolae

37 A synthetic phosphotyrosine residue (pY) peptide derived from the er

38 This motif contains two phosphotyrosine residues separated by one residue (seque

39 nism have been elusive because c-Abl lacks a phosphotyrosine residue that triggers the assembly of th

40 ipates in the activation of Fyn by providing phosphotyrosine residues that bind the SH2 domain of Fyn

41 Inhibition of ACE by TFII-I requires phosphotyrosine residues that engage the SH2 (Src-homolo

42 By interacting with specific phosphotyrosine residues, they provide regulatable prote

43 d a ShcA mutant (R175Q) that no longer binds phosphotyrosine residues via its PTB domain.

44 In addition, the phosphotyrosine residue was replaced with a difluorophos

45 ABE-II requires the presence of at least one phosphotyrosine residue with Y(P)422 being the more impo

46 etermine that interaction of the homeodomain phosphotyrosine residues with an adjacent domain in the

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