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1 DRH3 regions are typically long, acidic, and tyrosine sulfated.
4 he remarkable Mn(2+) stimulation of the Dopa/tyrosine-sulfating activity of the human monoamine (M)-f
5 s a unique 3,4-dihydroxyphenylalanine (Dopa)/tyrosine-sulfating activity that is stereospecific for t
6 quired for the stereospecificity of its Dopa/tyrosine-sulfating activity, whereas variable Region I o
7 coreceptor (CCR5) recognition through CCR5's tyrosine-sulfated amino (N) terminus, release of the gp4
8 tly use CCR5 mutants severely damaged in the tyrosine-sulfated amino terminus or extracellular loop 2
10 ind P-selectin, PSGL-1 must be modified with tyrosine sulfate and sialylated, fucosylated, core-2 O-g
12 ) recognition domain consisting of clustered tyrosine sulfates and a Core 2 O-glycan terminated with
13 id analysis confirmed that both proteins are tyrosine-sulfated and both proteins are expressed at com
15 cture of the CCR5 N terminus and that of the tyrosine-sulfated antibody 412d in complex with gp120 an
19 21 amino acid CIF peptide ligands, which are tyrosine sulfated by the tyrosylprotein sulfotransferase
20 erminate HIV-1 entry by adding or removing a tyrosine-sulfated CCR5 peptide from the culture medium.
23 8), a low-affinity mutant lacking the normal tyrosine sulfate-containing amino-terminal region of the
24 interactions between gp120's V3 loop and the tyrosine sulfate-containing CCR5 amino terminus, thereby
26 equires both the cellular receptor CD4 and a tyrosine-sulfated coreceptor to infect its target cells.
27 nd 3.5 angstrom cryo-EM structures of E51, a tyrosine-sulfated coreceptor-mimicking antibody, complex
31 full-length fibromodulin and its N-terminal tyrosine-sulfated domain purified from tissue, as well a
33 ng phenylalanine sulfonate, a bioisostere of tyrosine sulfate, enabling orthogonal protection strateg
34 slational sulfation, while retaining the two tyrosine sulfates essential for function, yielding novel
37 These data demonstrate a functional role for tyrosine sulfate in the CXC-chemokine receptor family an
38 r, we demonstrate that RNase 9 and Mfge8 are tyrosine-sulfated in wild type and Tpst1(-/-), but not i
39 udies have suggested that PSGL-1 needs to be tyrosine-sulfated, in addition to glycosylated with sLe(
40 asymmetric Env interact with E51, revealing tyrosine-sulfated interactions with gp120 mimicking CCR5
41 en fibril formation, we investigated whether tyrosine sulfate is involved in fibromodulin interaction
44 hemokine-binding assay demonstrated that the tyrosine sulfate moieties were critical for vGPCR associ
45 n adhesion-blocking mAb directed against the tyrosine sulfate motif of PSGL-1, abolished monocyte-adh
46 s process, the interaction of gp120 with the tyrosine-sulfated N-terminus of CCR5 is critical; howeve
47 n this issue of Cell, Choe et al. identified tyrosine-sulfated, neutralizing antibodies against HIV-1
49 able binding of S22 peptide, a 22-amino acid tyrosine-sulfated peptide corresponding to the CCR5 N-te
50 e tyrosine-sulfated region) when the soluble tyrosine-sulfated peptide is present, we show that HIV-1
51 of CCR5 to serve as an HIV-1 coreceptor, and tyrosine-sulfated peptides based on this region physical
53 nd their ligands, O-linked carbohydrates and tyrosine sulfates play major roles in promoting the inte
54 rst example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, t
56 e the utility of PSG2 in the purification of tyrosine-sulfated proteins from crude tissue samples.
59 r the heterologous expression of selectively tyrosine-sulfated proteins in Escherichia coli through t
60 d be widely applicable for identification of tyrosine-sulfated proteins in other systems and organism
62 pecific approach will allow investigation of tyrosine-sulfated proteins of other biochemical/physiolo
64 ite model of ligand association in which the tyrosine-sulfated region of the C5aR mediates the initia
67 of 18 N-terminal amino acids, including the tyrosine-sulfated region) when the soluble tyrosine-sulf
70 ssified and understudied group of eukaryotic tyrosine sulfated ribosomally synthesized, posttranslati
76 s(x) (sLe(X)), as well as a cluster of three tyrosine sulfate (tyr-SO(3)) groups near the N-terminus
78 us of PSGL-1, which contains three clustered tyrosine sulfates (TyrSO3-) adjacent to a Thr residue wi
80 the tyrosine subunit, and replacement of the tyrosine sulfate with other potential phosphate mimics.
81 ock and replacement of hydrolytically labile tyrosine sulfates with isosteric sulfonate analogues.