ライフサイエンスコーパス: Tyr residue

1 d by a loss in the packing constrains of the Tyr residue.

2 terion in vertebrate opsins is occupied by a Tyr residue.

3 moiety forms hydrophobic interactions with a Tyr residue.

4 observed at the site adjacent to a conserved Tyr residue.

5 inal binding domains and is coordinated by a Tyr residue.

6 g region 1 (LCDR1) that removes the critical Tyr residue.

7 nsphosphorylation engaged Ser but not Thr or Tyr residues.

8 s indicates the presence of oxidized Met and Tyr residues.

9 domain III protein revealed emissions due to Tyr residues.

10 ation in vivo requires mutation of all three Tyr residues.

11 d substrate phosphorylation on Ser, Thr, and Tyr residues.

12 Ser and Thr residues in addition to His and Tyr residues.

13 ng by reversible phosphorylation of specific Tyr residues.

14 Src as a common substrate, but on different Tyr residues.

15 ysteine (C15) to peroxidation requires three Tyr residues.

16 ation requires interactions with the opposed Tyr residues.

17 ompounds effectively acetylate Cys, Lys, and Tyr residues.

18 lates only one or a few proteins on specific Tyr residues.

19 with Asp residues 272, 274, 277 and sulfated Tyr residues 278 and 279 in GP Ibalpha.

20 Both cytokines cause phosphorylation of Tyr residue 701 and Ser residue 727 of STAT1, as shown b

21 lls to OnM is mediated in trans and involves Tyr residue 759 in gp130 but is not mediated by either S

22 p130 mutant receptor, in which intracellular Tyr residue 759 of gp130 is replaced by a Phe residue, m

23 al because mutation of invariant cytoplasmic Tyr residues abrogates ectodomain shedding, but not beca

24 The side chains of the penultimate Tyr residues (alpha140 and beta145) occupy the pockets m

25 emonstrate that phosphorylation of these two Tyr residues also play important roles in mediating the

26 is also accompanied by the hydration of the Tyr residue and approximately 4 Phe residues.

27 , and the side chains of both the N-terminal Tyr residue and its immediate neighbor bind within the Q

28 interactions have been observed between this Tyr residue and peptide substrates in the crystal struct

29 tic cage, being sandwiched between a Trp and Tyr residue and with the methyl group pointed toward ano

30 ed by Phe substitution of the conserved tail Tyr residue and with wild-type Hck following co-expressi

31 t the distance and degree of contact between Tyr residues and Kme3 plays an important role in tuning

32 hosphorylation of an artificial substrate on Tyr residues and not on Ser or Thr residues.

33 s, which autophosphorylates on Ser, Thr, and Tyr residues and phosphorylates Ser and Thr residues on

34 Mutation of the Tyr residues and the position of two GSH molecules confi

35 n bond network includes a strictly conserved Tyr residue, and previously we explored the role of this

36 nt tau proteins pseudophosphorylated at each Tyr residue are fully competent to stabilize MTs.

37 These Tyr residues are also the target of the cognate CpsB pho

38 In Glg1p, two Tyr residues are implicated, Tyr232 and Tyr600, mutation

39 ed data indicate that while many Ser/Thr and Tyr residues are indeed phosphorylated in vivo, striking

40 The critical stacking Tyr residues are L32, L49, H100, and H100A, while His L9

41 Although solvent-exposed His and Tyr residues are more reactive with SO(4)(-*) than with

42 The effects of mutating the two Tyr residues are quite different: Y240F has higher than

43 Using an add-back approach in which specific Tyr residues are reinserted into c-Fms inactivated by th

44 Tyrosine (Tyr) residues are critical for ONOO(-)-mediated oligomer

45 and the hydroxyl group of the m-tyrosine (m-Tyr) residue as key contributors to compound potency.

46 Against this backdrop, we mutated the Tyr residue at the -4th position of EF III to the Phe re

47 phasize the importance to gp120 binding of a Tyr residue at the apex of the H2 loop that forms a seco

48 Serpin-1H, -1K, and -1Z, all with a Tyr residue at the P1 position, inhibited chymotrypsin a

49 arboxyl-terminal Gly-Arg-X-Arg-Phe-amide and Tyr residues at positions 10 and 17 from the carboxyl te

50 Furthermore, the Y(8a) mode of the other two Tyr residues at positions 16 and 72 that are remote from

51 ectra were consistent with an additional two Tyr residues being exposed to the solvent in PITP(1-259)

52 te Zn present) were preformed to titrate all Tyr residues between pH 5.4-11.0.

53 atic interactions as well as surface-exposed Tyr residues bind WaaG to the membrane.

54 of an 18-amino acid domain surrounding this Tyr residue both diminished cleavage of membrane PAM by

55 mic tail of FcmuR contains conserved Ser and Tyr residues, but none of the Tyr residues match the imm

56 regulated by phosphorylation on both Thr and Tyr residues by a dual-specificity MAPK kinase (MAPKK).

57 )S(5)P(6)S(7) repeats, in which Ser, Thr and Tyr residues can all be phosphorylated.

58 he594) was identified that, with the Trp and Tyr residues, completed a ring or "basket" of aromatic a

59 Although dual phosphorylation of Thr and Tyr residues confers full activation of ERK, in vitro st

60 it requires the cytoplasmic tail but not the Tyr residue critical for lysosomal sorting of CD1d.

61 ndicates that the G and H helices around the Tyr residues do not melt.

62 tion, as pseudophosphorylation at these same Tyr residues does not inhibit tau assembly.

63 and the use of an IRS-1 variant lacking all Tyr residues except those which activate PI3K.

64 oligomerization, as tau proteins lacking all Tyr residues fail to generate oligomers upon ONOO- treat

65 than 6 billion peptides oriented by a common Tyr residue for their ability to bind to ZAP-70, we dete

66 east Glg proteins appear to require multiple Tyr residues for functionality.

67 since IRS-1 variants lacking the SH2-binding Tyr residues for these proteins are fully active.

68 riodic lattice sites, sandwiched between two Tyr residues from adjacent tetramers.

69 e synthases, that contains invariant Asp and Tyr residues implicated in catalysis.

70 and Cs+ indicated a very low exposure of the Tyr residue in both native and intermediate conformation

71 s perform this role: in GABA(A) receptors, a Tyr residue in loop A forms a cation-pi interaction with

72 o the identification of a key determinant; a Tyr residue in position 5 increases potency for NR2D, wh

73 The presence of a Tyr residue in the active site of DMSOR and BSOR that is

74 itution in the active site of the protein: a Tyr residue in the active sites of SCO 1441 and SCO 2687

75 diated phosphorylation of a highly conserved Tyr residue in the P + 1 loop of protein kinase D2 (PKD2

76 mma binding region or mutation of a critical Tyr residue in the region did not prevent the interferen

77 We also found that a conserved Tyr residue in the same motif not only affects sensitivi

78 The Tyr residue in VPg that is nucleotidylated by the viral

79 The presence of conserved His and Tyr residues in all of the homologs characterized to dat

80 dation, because mutagenesis of Met, His, and Tyr residues in alpha-syn did not abrogate this inhibiti

81 ys that promote the chlorination of specific Tyr residues in apoA-I are controversial, and the mechan

82 The Tyr residues in both motifs can be phosphorylated, and i

83 Replacement of 74% (+/- 10%) of the Tyr residues in PvuII endonuclease by 3-fluorotyrosine p

84 re conservative variants in which individual Tyr residues in the active site are replaced by 3-chloro

85 rane folding topology indicated that several Tyr residues in the bilayer region of the three transmem

86 insulin receptor (IR), which phosphorylates Tyr residues in the insulin receptor substrate-signaling

87 the intrinsic proton affinity of one of the Tyr residues in the network, Tyr16, does not remain cons

88 tant matrilysin with substrates with Leu and Tyr residues in the P1' position confirm that the KM val

89 requires dual phosphorylation of the Thr and Tyr residues in the TXY motif of the activation loop by

90 FPheK reacted with adjacent Lys, Cys, and Tyr residues in thioredoxin in high yields.

91 Csk and Chk, are rare exceptions for lacking Tyr residues in this loop.

92 potential role of the two existing tyrosine (Tyr) residues in the intracellular regions and the carbo

93 e mediated by Src family kinases at multiple Tyr residues including Tyr(734).

94 UV absorption spectroscopy of the Phe and Tyr residues indicated that the native --> intermediate

95 bility of Me15 may increase its affinity for Tyr residues influencing steric drug interaction with th

96 f Rhodobacter sphaeroides DMSOR and insert a Tyr residue into the equivalent position in TMAOR.

97 baicalein was abolished by conversion of the Tyr residues into Phe, demonstrating that Tyr is involve

98 oups on the surface of the vesicles and that Tyr residue is embedded in the vesicles.

99 Hence, this Tyr residue is essential in controlling unproductive enc

100 In fact, nitration of only a single Tyr residue is often sufficient to induce profound chang

101 omolar affinity only when an aromatic Phe or Tyr residue is present at a specific location in the ext

102 served Ser and Tyr residues, but none of the Tyr residues match the immunoreceptor tyrosine-based act

103 ite beta-sheet face with two surface-exposed Tyr residues may be involved in protein contacts.

104 tion, indicating that p-Y1105 was the sole p-Tyr residue mediating binding to p120.

105 Cells expressing an Rpb1 derivative with all Tyr residues mutated to Phe (Rpb1-Y1F) were inviable.

106 l measurements show that the para-group of a Tyr residue near the ion conduction pathway has a critic

107 Pf Fd with Asp, Ser, Cys, Val, His, Asn, and Tyr residues occupying position 14, i.e., proximal to th

108 terial enzyme, here we show that a conserved Tyr residue of the cytochrome b subunit of cytochrome bc

109 In this study Tyr residues of both leucine enkephalin and salmon calci

110 peptides phosphorylated at all Ser, Thr, or Tyr residues of the human checkpoint 2 (Chk2) protein ki

111 asis of sequence comparison we mutated three Tyr residues of the putative P2Y1 binding pocket to Ala

112 but not the double, mutations of the Thr and Tyr residues of the TEY phosphorylation lip caused a ca.

113 ation and redirects nitration to alternative Tyr residues on COX-1, preserving catalytic activity.

114 This suggests that Tyr residues on the surface of the protein are oxidized

115 identified several differentially activated Tyr residues, one of which is not only more sensitive to

116 N-Methylation of either the N-terminal Tyr residue or of Cys(6) in the Tyr series resulted in a

117 Vpu may target either the BST-2 cytoplasmic Tyr residues or the NH(2) terminus itself for ubiquitina

118 ed to the O-phosphorylation of Ser, Thr, and Tyr residues, our understanding of histidine phosphoryla

119 o the conclusion that the side chain of this Tyr residue played a major role in recognition of the pr

120 To test the prediction that a Tyr residue predicts dipeptide ligase while an Phe resid

121 or O-O cleavage derive from the cross-linked Tyr residue present at the active site.

122 Furthermore, mutagenesis of the four Tyr residues present at positions 169 to 172 which are p

123 Phosphorylation on Tyr residues regulates the kinase activity of PrkD and P

124 The Ms Fer subunit lacks one of the three Tyr residues required for the rapid biomineralization of

125 this is due to the exclusive nitration of 2 Tyr residues (residues 106 and 114) at the glutathione d

126 promotes dephosphorylation of its regulatory Tyr residue, resulting in ERK inactivation.

127 Energy transfer was detected between Tyr residue(s) and the bound NADPH, indicating that the

128 While replacement of the Tyr residues showed little, if any, effect on rates of t

129 ) was demonstrated by (i) the constraints on Tyr residues shown by the amplitude of near-UV circular

130 conserved Trp residues and one non-conserved Tyr residue, shown previously to be of functional import

131 ce of activity on the pKa of the substituted Tyr residues suggests that the KSI oxyanion hole does no

132 Mutation of a highly conserved Tyr residue that provides the bottom of the hydrophobic

133 ant alterations in the topography of Phe and Tyr residues that could be buried in the protein matrix.

134 ydroquinones and a hydrogen network of three Tyr residues that could provide the proton for reductive

135 To identify PTPase 1B tyrosine (Tyr) residues that are phosphorylated in response to ins

136 sist of five acidic residues and three sulfo-Tyr residues, thus representing a high density of negati

137 analysis revealed dominant contributions of Tyr residues to binding as well as striking molecular mi

138 ing mutagenesis of acidic residues to Ala or Tyr residues to Phe and expression and purification of t

139 t critical for signaling because mutation of Tyr residues to Phe did not prevent the biological respo

140 ion is due to the LiP-catalyzed oxidation of Tyr residues to Tyr radicals, followed by intermolecular

141 Mutation to Phe of all four cytoplasmic Tyr residues together (ALL F mutant) greatly reduced the

142 Mutation of this Tyr residue, together with mutation of Tyr166 within the

143 cation-pi (between PC choline headgroups and Tyr residues) transient interactions with phospholipids.

144 Phosphorylation was abolished by mutation of Tyr residues Tyr(69)/Tyr(74) within the tandem repeat se

145 Purified PALcc in which the only conserved Tyr residue (Tyr(654)) was mutated to Phe was secreted n

146 O complexed to Fab 40-50 shows a heavy chain Tyr residue (Tyr-H100) which is part of the cardiac glyc

147 minal tail of Syk, which has three conserved Tyr residues (Tyr-623, Tyr-624, and Tyr-625 of rat Syk).

148 ted ShuT mutants of the absolutely conserved Tyr residues, Tyr-94 (Y94A) and Tyr-228 (Y228F), which a

149 The C-terminal tail contains a Tyr residue, Tyr527.

150 Phosphorylation of Tyr residues (Tyrs 315 and 319) within the Interdomain B

151 An essential role for a Tyr residue was confirmed by elimination of PAL activity

152 th Arg55 of cyclophilin A (Cyp A), and the m-Tyr residue was displaced into solvent.

153 ce of a 12-amino acid motif starting at this Tyr residue was sufficient to confer responsiveness to P

154 synuclein in which one of the four intrinsic Tyr residues was replaced by Trp, and two others by Phe,

155 absence of all seven functionally important Tyr residues, we find that Tyr-559 is necessary but not

156 e competition demonstrated that both Pro and Tyr residues were required for specific interaction of I

157 horylates Src family kinases on a C-terminal Tyr residue, which down-regulates their activities.

158 lycan, but required only one of three nearby Tyr residues, which are sites for Tyr-SO(3) formation.

159 revealed no change in surface topography of Tyr residues with removal of Zn2+.

160 3 are 69 % identical and each contains eight Tyr residues with seven at equivalent structural positio

161 de that the universally conserved GAF domain Tyr residue, with which the bilin chromophore is intimat

162 hat tetranitromethane treatment modified the Tyr residue within the Ser95-Tyr96 dipeptide.

163 of this enhanced response as mutation of the Tyr residues within this region to Phe resulted in a rec

164 city kinases that phosphorylate the Thr- and Tyr-residues within the TXY motif of MAP-kinases of play

165 The initial phosphorylation site is a Tyr residue (Y14) present in the N-terminal A/B domain o

166 ity of the oxidized form of the redox-active Tyr residue, YD, in the D2 protein.