ライフサイエンスコーパス: arginyl

1 thyronine, dabsyl-L-valine, and N-benzoyl-L-arginyl-4-amino-benzoic acid to generate a series of 13

2 that the RGD in the pro-toxin was changed to arginyl-alanyl-aspartic or to arginyl-glycyl-glutamic, w

3 t H-R-1-[4aS, 8aS]perhydroisoquinolyl-prolyl-arginyl aldehyde (D-Piq-Pro-Arg-H; 32).

4 s composed of N,N-distearyl-N-methyl-N-2-(N'-arginyl) aminoethyl ammonium chloride (DSAA), a guanidin

5 c lipid, i.e. N,N-distearyl-N-methyl-N-2-(N'-arginyl) aminoethyl ammonium chloride, which can induce

6 sh that there is an absolute requirement for arginyl, as none of the [R46X]V1aR mutant constructs sup

7 nity as SI, indicating the importance of the arginyl cation.

8 CK) and, to a lesser extent, H-D-Tyr-L-Pro-L-arginyl chloromethyl ketone (YPRCK) and was relatively i

9 ve-site labeling with dansyl-glutamyl-glycyl-arginyl chloromethyl ketone or immunoblot analysis showe

10 bitors hirudin and D-phenylalanyl-L-prolyl-L-arginyl chloromethyl ketone, indicating that the effect

11 tes are similar to the D-phenylalanyl-prolyl-arginyl chloromethylketone structure.

12 a lysyl hydroxylase rather than an N-methyl arginyl-demethylase.

13 peptide substrates for attachment of various arginyl dipeptides.

14 ngiform taste papillae (HBO) cells with five arginyl dipeptides: Ala-Arg (AR), Arg-Ala (RA), Arg-Pro

15 Arg-Glu (RE), and Glu-Arg (ER); and two non-arginyl dipeptides: Asp-Asp (DD) and Glu-Asp (ED).

16 yield fluorescein-D-phenylalanyl-L-prolyl-L-arginyl-fVIIa (Fl-FPR-fVIIa).

17 ucted to examine the effect of the dipeptide arginyl-glutamine (Arg-Gln) on vascular endothelial cell

18 taminases significantly increases their RGD (arginyl-glycyl-aspartate)-dependent interaction with end

19 ds 140 to 142 of the pre-pro-protein form an arginyl-glycyl-aspartic (RGD) sequence, a motif involved

20 Arginyl-glycyl-aspartic acid (RGD), a cell adhesion trip

21 tein (eADF4(C16)) tagged with the tripeptide arginyl-glycyl-aspartic acid cell adhesion motif RGD, wh

22 where E[c(RGDfk)](2) = glutamic acid-[cyclo(arginyl-glycyl-aspartic acid-D-phenylalanine-lysine)], b

23 sion of H10 cells to vitronectin and (glycyl-arginyl-glycyl-aspartyl-serine)4 and significant inhibit

24 r rates to the polymeric RGD peptide (glycyl-arginyl-glycyl-aspartyl-serine)4 than to monomeric RGD p

25 was changed to arginyl-alanyl-aspartic or to arginyl-glycyl-glutamic, were expressed in Escherichia c

26 ned from the fungus, but the control peptide arginyl-glycyl-glutamyl-serine provided no protection.

27 e spastic cerebral arteries via binding to L-arginyl-glycyl-L-aspartate-dependent integrin receptors

28 MT activity includes recognition of specific arginyl groups within targeted proteins and the generati

29 biological processes by methylating specific arginyl groups within targeted proteins.

30 It has recently been reported that an arginyl in the distal N-terminus of the V1aR is critical

31 Our findings explain why arginyl is conserved at this locus throughout the evolut

32 A tris(carbobenzyloxy)arginyl(k)norleucine pseudopeptide was synthesized and c

33 otrypsin substrate 3-carbomethoxypropionyl-L-arginyl-L-prolyl-L-tyrosine-p-nitroanili ne- HCl (S-2586

34 expression and/or protein citrullination and arginyl methylation in human and mouse optic nerve and i

35 ullination in POAG optic nerve and decreased arginyl methylation.

36 By contrast, we did not observe N-methyl arginyl N-demethylation with purified JMJD6.

37 The P1 arginyl of antipain also binds at this site, but the pos

38 omogenic substrate L-pyroglutamyl-L-prolyl-L-arginyl-p-nitroaniline (S-2366) and on the activation of

39 examine inhibitors that target the substrate arginyl peptide, SAM, or both binding sites, and the typ

40 polar granules made of cyanophycin [multi-L-arginyl-poly (L-aspartic acid)], which is synthesized by

41 s the wild-type three glutaminyl (Q) and one arginyl (R) residues for optimal fusion.

42 ciens ADP-glucose pyrophosphorylase with the arginyl reagent phenylglyoxal resulted in complete desen

43 ng residues surrounding the putative sessile arginyl residue and found stimulated platelets released

44 Alanine substitution of the single arginyl residue in CooA, the major pilin, had no effect

45 ge of pro-EGF first occurs at the C-terminal arginyl residue of the EGF domain, and that proteolysis

46 te the presence of several substrate-binding arginyl residues and the absence of a hydrophobic pocket

47 We show here that chemical modification of arginyl residues in CS1 pili abolishes CS1-mediated aggl

48 hat transfer methyl-groups to the omega-N of arginyl residues in proteins.

49 e, double, or triple alanyl substitutions at arginyl residues significantly decreased TonB activity.

50 hrough the replacement of one of the binding arginyl residues with several unnatural alkyl and aryl a

51 this study suggest differing roles for these arginyl residues.

52 34mM of the synthetic substrate N-benzoyl-dl-arginyl-rho-nitroanilide, whereas Vmax was 0.056+/-0.001

53 ve dramatically different placements for the arginyl side chain and carboxyl terminus.

54 ns, bacterial peptides with a central cyclic arginyl structure, as inhibitors of this activity.

55 hibition of CheZ activity as a result of the arginyl substitution at CheY position 59 are discussed.

56 vestigations of phenylalanyl, methionyl, and arginyl ternary complexes, and the development of a stra

57 tures a post-translational conjugation of an arginyl to a protein, making it extremely challenging to

58 -of-function mutant of rrt-1 that encodes an arginyl-transfer RNA (tRNA) synthetase, an enzyme essent

59 then undergoes efficient arginylation by an arginyl transferase (ATE1).

60 mutants; this constitutive response required arginyl transferase activity and RAP-type Group VII ethy

61 The arginyl-transferase ATE1 is a tRNA-dependent enzyme that

62 uces the proteasome-dependent degradation of arginyl-transferase in vivo, thus acting as both a "stoi

63 We report that arginyl-transferase of either the mouse or the yeast Sac

64 Furthermore, we show that hemin inhibits arginyl-transferase through a redox mechanism that invol

65 The conjugation of arginine, by arginyl-transferase, to N-terminal aspartate, glutamate

66 In eukaryotes, ATE1-encoded arginyl-transferases (R(D,E,C*)-transferases) conjugate

67 nd cysteine--are arginylated by ATE1-encoded arginyl-transferases.

68 sed with the E. coli dnaY gene, encoding the arginyl tRNA for the codons AGA and AGG.

69 ally discovered through its interaction with arginyl-tRNA protein transferase 1 (Ate1), a component o

70 We also show that cells lacking arginyl-tRNA protein transferase are less susceptible to

71 ercome apoptosis resistance in cells lacking arginyl-tRNA protein transferase that express R-CRT on t

72 mation decreased levels of nuclear-localized arginyl-tRNA synthetase (ArgRS).

73 There are two isoforms of cytoplasmic arginyl-tRNA synthetase (hcArgRS) in human cells.

74 amma-glutamylcyclotransferase 1 (Chac1), and arginyl-tRNA synthetase 1 (Rars).

75 oluble, and p.Arg403Trp disrupted QARS-RARS (arginyl-tRNA synthetase 1) interaction.

76 ein synthesis efficiency is not dependent on arginyl-tRNA synthetase and glutaminyl-tRNA synthetase i

77 this, we generated mammalian cells in which arginyl-tRNA synthetase and/or glutaminyl-tRNA synthetas

78 ion and two others when bound to the cognate arginyl-tRNA synthetase or to codons on the ribosome whe

79 ion was identified as the binding partner of arginyl-tRNA synthetase, a polypeptide of the multi-amin

80 RARS encodes the cytoplasmic arginyl-tRNA synthetase, an enzyme essential for RNA tra

81 atalyzed by a family of enzymes known as the arginyl-tRNA transferases (ATE1s), which are conserved a

82 they function through their conjugation, by arginyl-tRNA-protein transferase (R-transferase), to arg

83 post-translational modification catalyzed by arginyl-tRNA-protein transferase 1 (ATE1) in mammalian s

84 Arginyl-tRNA-protein transferase 1 (ATE1) is a master re

85 peared independent of the charging status of arginyl-tRNA.

86 rth intron of the AtATE1 gene, which encodes arginyl-tRNA:protein arginyltransferase (EC. 2.3.2.8, R-

87 y, a feature that contributes to maintaining arginyl-tRNAArg levels unaffected.

88 the Arg concentration increased; all of the arginyl-tRNAs examined appeared maximally charged at low

89 st target, because citrullination eliminates arginyl tryptic sites.

90 e is a tripeptide, L-tyrosinyl-L-isoleucyl-L-arginyl, which competitively inhibits the hydrolysis of