ライフサイエンスコーパス: Tyr residue

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

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

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

4 phosphorylated on at least one Ser, Thr, or Tyr residue.

5 moiety forms hydrophobic interactions with a Tyr residue.

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

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

8 g the signals of interest from other Trp and Tyr residues.

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

10 nsphosphorylation engaged Ser but not Thr or Tyr residues.

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

12 domain III protein revealed emissions due to Tyr residues.

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

14 aryl coupling reaction between two flanking Tyr residues.

15 ntify modified precursors containing His and Tyr residues.

16 2 induces phosphorylation of the receptor on Tyr residues.

17 ost commonly to the heme iron by His, Cys or Tyr residues.

18 tion of proteins, primarily on Ser, Thr, and Tyr residues.

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

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

21 ng by reversible phosphorylation of specific Tyr residues.

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

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

24 ation requires interactions with the opposed Tyr residues.

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

26 site of O-arylation at a proximal tyrosine (Tyr) residue.

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

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

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

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

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

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

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

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

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

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

37 her via a unique double cross-link between a Tyr residue and the catalytic heme moiety of an adjacent

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

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

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

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

42 ase undergoes autophosphorylation on Thr and Tyr residues and phosphorylates a classical eukaryotic p

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

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

45 rophile-based fragment screening for His/Lys/Tyr residues and to characterize the resulting hits.

46 , whereas bacterial stand-alone LanCs have a Tyr residue, and LanM enzymes that have LanC-like domain

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

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

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

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

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

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

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

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

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

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

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

58 the inclusion of the side chains of Leu and Tyr residues, as well as an extensive network of hydroge

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

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

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

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

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

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

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

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

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

68 s involving sidechains of Gln, Asn, Ser, and Tyr residues, both along and transverse to the fibril gr

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

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

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

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

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

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

75 In single-subunit RNAPs, a conserved Tyr residue discriminates against 2'dNTPs, whereas selec

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

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

78 Phosphorylation of proteins on tyrosine (Tyr) residues evolved in metazoan organisms as a mechani

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

80 o a charged (Asp or Arg) or bulky (Pro, Trp, Tyr) residue, F3 secretion was also compromised, indicat

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

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

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

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

85 residues in CtSal, different from the paired Tyr residues found in TcLtp2.

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

87 Protein and phosphorylated Ser, Thr, and Tyr residues from left ventricular tissue were quantifie

88 rategy with fluorosulfates targeting His/Lys/Tyr residues has yet to be reported.

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

90 re achieved in the O-arylation at a proximal Tyr residue in a number of cases, including a peptide-sm

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

92 A catalyzes auto-acetylation of an invariant Tyr residue in its conserved C-terminal hexapeptide moti

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

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

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

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

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

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

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

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

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

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

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

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

105 re DEPC labeling reactivity of Ser, Thr, and Tyr residues in intact proteins with peptide fragments f

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

131 enhanced reactivity of certain Ser, Thr, and Tyr residues occurs due to higher local concentrations o

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

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

134 OGT catalyzes the transfer of O-GlcNAc onto Tyr residues of peptides and OGA catalyzes its removal.

135 r work reveals widespread O-GlcNAcylation on Tyr residues of proteins and that Tyr O-GlcNAcylation is

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

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

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

139 , O-GlcNAcylation was found on 121 tyrosine (Tyr) residues of 93 proteins.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

159 how this element contains a highly conserved Tyr residue that can be phosphorylated and that negative

160 cetyl group from acetyl-CoA on the catalytic Tyr residue that is located on an extracytoplasmic loop

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

162 on path and induced rotation of an invariant Tyr residue that tightens the intracellular gate.

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

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

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

166 catalyse the phosphorylation of thousands of Tyr residues throughout the proteome(1-3).

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

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

169 oselectively with the phenolic side chain of Tyr residues to form stable C-N1-linked cyclic peptides.

170 queous conditions with internal and terminal Tyr residues to furnish Tyr-linked cyclic peptides.

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

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

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

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

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

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

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

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

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

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

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

182 rmation of a radical on a strictly conserved Tyr residue (Tyr34) that is key for the activation of O(

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

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

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

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

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

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

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

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

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

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

193 ant was further modified by replacing the P1 Tyr residue with para-substituted Phe derivatives, gener

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

195 3 are 69 % identical and each contains eight Tyr residues with seven at equivalent structural positio

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

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

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

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

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

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