ライフサイエンスコーパス: tyrosine sulfate

1 This activation of the Dopa/tyrosine-sulfating activity of M-form PST by Mn(2+) via

2 itical in the Mn(2+) stimulation of the Dopa/tyrosine-sulfating activity of SULT1A3.

3 he remarkable Mn(2+) stimulation of the Dopa/tyrosine-sulfating activity of the human monoamine (M)-f

4 s a unique 3,4-dihydroxyphenylalanine (Dopa)/tyrosine-sulfating activity that is stereospecific for t

5 quired for the stereospecificity of its Dopa/tyrosine-sulfating activity, whereas variable Region I o

6 tly use CCR5 mutants severely damaged in the tyrosine-sulfated amino terminus or extracellular loop 2

7 PSGL-1 requires both tyrosine sulfate and O-linked glycans to bind P-selectin

8 ind P-selectin, PSGL-1 must be modified with tyrosine sulfate and sialylated, fucosylated, core-2 O-g

9 Comparison of 2909 to PG16 (which is tyrosine sulfated and the only other member of the class

10 id analysis confirmed that both proteins are tyrosine-sulfated and both proteins are expressed at com

11 h through the characterization of the doubly tyrosine-sulfated anti-gp120 antibody, 412d.

12 cture of the CCR5 N terminus and that of the tyrosine-sulfated antibody 412d in complex with gp120 an

13 Its N terminus is tyrosine-sulfated, as are many antibodies that react wit

14 The resulting protein contains tyrosine sulfate at any location specified by a TAG codo

15 human antibodies directed against gp120 are tyrosine sulfated at their antigen binding sites.

16 erminate HIV-1 entry by adding or removing a tyrosine-sulfated CCR5 peptide from the culture medium.

17 A tyrosine-sulfated CCR5-mimetic peptide, CCR5mim1, inhibi

18 ncluding CCR5(Delta18) lacking the important tyrosine sulfate-containing amino terminus.

19 8), a low-affinity mutant lacking the normal tyrosine sulfate-containing amino-terminal region of the

20 interactions between gp120's V3 loop and the tyrosine sulfate-containing CCR5 amino terminus, thereby

21 ed as a growth factor and as an influence on tyrosine sulfate content of thyroglobulin.

22 Fibromodulin and its tyrosine sulfate domain remained bound on the formed fib

23 The tyrosine-sulfated domain and the leucine-rich repeat dom

24 An acidic, tyrosine-rich, and tyrosine-sulfated domain of the CCR5 amino terminus play

25 full-length fibromodulin and its N-terminal tyrosine-sulfated domain purified from tissue, as well a

26 slational sulfation, while retaining the two tyrosine sulfates essential for function, yielding novel

27 Three new tyrosine-sulfated hemostatic proteins-protein S, prekall

28 Our data now demonstrate that tyrosine sulfate in other extracellular domains can func

29 These data demonstrate a functional role for tyrosine sulfate in the CXC-chemokine receptor family an

30 r, we demonstrate that RNase 9 and Mfge8 are tyrosine-sulfated in wild type and Tpst1(-/-), but not i

31 udies have suggested that PSGL-1 needs to be tyrosine-sulfated, in addition to glycosylated with sLe(

32 en fibril formation, we investigated whether tyrosine sulfate is involved in fibromodulin interaction

33 don corresponding to the desired location of tyrosine sulfate is TAG.

34 hemokine-binding assay demonstrated that the tyrosine sulfate moieties were critical for vGPCR associ

35 n adhesion-blocking mAb directed against the tyrosine sulfate motif of PSGL-1, abolished monocyte-adh

36 s process, the interaction of gp120 with the tyrosine-sulfated N-terminus of CCR5 is critical; howeve

37 n this issue of Cell, Choe et al. identified tyrosine-sulfated, neutralizing antibodies against HIV-1

38 Here we demonstrate that a tyrosine-sulfated peptide based on the N terminus of CCR

39 able binding of S22 peptide, a 22-amino acid tyrosine-sulfated peptide corresponding to the CCR5 N-te

40 e tyrosine-sulfated region) when the soluble tyrosine-sulfated peptide is present, we show that HIV-1

41 of CCR5 to serve as an HIV-1 coreceptor, and tyrosine-sulfated peptides based on this region physical

42 Here we show that the same tyrosine-sulfated peptides, but not their unsulfated ana

43 nd their ligands, O-linked carbohydrates and tyrosine sulfates play major roles in promoting the inte

44 rst example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, t

45 Although dozens of tyrosine-sulfated proteins are known, many more are like

46 e the utility of PSG2 in the purification of tyrosine-sulfated proteins from crude tissue samples.

47 Among the several candidate tyrosine-sulfated proteins identified, RNase 9 and Mfge8

48 We show that it can detect tyrosine-sulfated proteins in complex biological samples

49 r the heterologous expression of selectively tyrosine-sulfated proteins in Escherichia coli through t

50 d be widely applicable for identification of tyrosine-sulfated proteins in other systems and organism

51 We therefore sought to identify tyrosine-sulfated proteins in the male genital tract usi

52 pecific approach will allow investigation of tyrosine-sulfated proteins of other biochemical/physiolo

53 of new tools for the detection and study of tyrosine-sulfated proteins.

54 ite model of ligand association in which the tyrosine-sulfated region of the C5aR mediates the initia

55 These observations show that a tyrosine-sulfated region of the CCR5 amino terminus can

56 inst GP Ibalpha, including one directed at a tyrosine-sulfated region of the polypeptide.

57 of 18 N-terminal amino acids, including the tyrosine-sulfated region) when the soluble tyrosine-sulf

58 The conformations of tyrosine-sulfated regions of CCR5 (alpha-helix) and 412d

59 roperly positioned core-2 O-glycan and three tyrosine sulfate residues.

60 However, beads coated with a tyrosine-sulfated, sLe(x)-modified, PSGL-1-Fc chimera su

61 The tyrosine-sulfated, thrombin exosite-binding hirudin pept

62 PSGL-1 also requires tyrosine sulfate to bind P-selectin but not E-selectin.

63 sialylated, fucosylated O-linked glycans and tyrosine sulfate to bind P-selectin.

64 s(x) (sLe(X)), as well as a cluster of three tyrosine sulfate (tyr-SO(3)) groups near the N-terminus

65 GSP-6 contains three tyrosine sulfate (TyrSO(3)) residues and a monosialylate

66 us of PSGL-1, which contains three clustered tyrosine sulfates (TyrSO3-) adjacent to a Thr residue wi

67 the tyrosine subunit, and replacement of the tyrosine sulfate with other potential phosphate mimics.

68 ock and replacement of hydrolytically labile tyrosine sulfates with isosteric sulfonate analogues.