ライフサイエンスコーパス: tyrosine residue

1 regulated by the phosphorylation of a single tyrosine residue.

2 involving this carboxylate and the following tyrosine residue.

3 itates metal coordination by a non-canonical tyrosine residue.

4 is a covalent linkage of TOP1 with DNA via a tyrosine residue.

5 preference for 2'-deoxyribosyl groups have a tyrosine residue.

6 e ATP-binding template is blocked by a bulky tyrosine residue.

7 no nucleophilic involvement of the enzymatic tyrosine residue.

8 ent N-Calpha bond cleavage N-terminal to the tyrosine residue.

9 R3/PYL8, which are characterized by a unique tyrosine residue.

10 mo phosphorylation on a conserved C-terminal tyrosine residue.

11 ia an NPP7-specific aromatic box composed of tyrosine residues.

12 Gads, and PLCgamma1 through its four distal tyrosine residues.

13 pon ligand binding by phosphorylation on its tyrosine residues.

14 dditional posttranslational modifications at tyrosine residues.

15 ng reversible phosphorylation of proteins on tyrosine residues.

16 osphorylation of the PDGFbetaR at particular tyrosine residues.

17 cross-linking of chorion proteins via their tyrosine residues.

18 ion, which is inhibited by mutation of three tyrosine residues.

19 depends upon phosphorylation of its multiple tyrosine residues.

20 patially arranged redox-active tryptophan or tyrosine residues.

21 sformations arising from oxidative stress of tyrosine residues.

22 via reduced phosphorylation of specific EGFr tyrosine residues.

23 ate, and hydrogen bonding to two active site tyrosine residues.

24 ing, suggesting a differential role of these tyrosine residues.

25 ion; specifically through phosphorylation of tyrosine residues.

26 tor dimerization and transphosphorylation on tyrosine residues.

27 n conjugation of PDI possibly at active site tyrosine residues.

28 scribe a voltage sensor that is comprised of tyrosine residues.

29 s as well as chromatin modifiers at critical tyrosine residues.

30 hlorination of tryptophan and bromination of tyrosine residues.

31 e of the Jak2(FF/FF) mouse line reveals that tyrosine residues 1007/1008 are absolutely essential for

32 imulation Bak undergoes dephosphorylation at tyrosine residue 108 (Y108), a critical event that is ne

33 targeted mutation of phosphorylated nephrin tyrosine residues 1176 and 1193 abrogated the actions of

34 fically regulates p130Cas phosphorylation at tyrosine residue 128 (Y128) in colorectal cancer (CRC) c

35 e progression by phosphorylation of Cdc28 at tyrosine residue 19.

36 y epidermal growth factor receptor (EGFR) at tyrosine residues 3, 7, and 198.

37 re, activated Fyn phosphorylated PKCdelta at tyrosine residue 311, contributing to an inflammogen-ind

38 T is a direct substrate of PTK6 and that AKT tyrosine residues 315 and 326 are phosphorylated by PTK6

39 bited ZAP-70 variant in which two regulatory tyrosine residues (315 and 319) in the SH2-kinase linker

40 There are three tyrosine residues (32, 91, and 96) clustered in the dime

41 s activated PTK6, which is phosphorylated on tyrosine residue 342, is localized at the membrane.

42 enous anesthesia, we have used mice in which tyrosine residues 365/7 within the gamma2 subunit are mu

43 L fusion kinase phosphorylate human RAD51 on tyrosine residues 54 and 315.

44 We have identified the tyrosine residues 572, 591, and 919 of FLT3 as phosphory

45 n kinase (FAK) and phosphorylation of FAK at tyrosine residues 576/577 and 925 were required for Lyn-

46 o-incubated with the IGF-1R kinase indicated tyrosine residues 60, 133, and 250 in PCNA as IGF-1R tar

47 ition blocked VE-cadherin phosphorylation at tyrosine residue 685 and the concomitant formation of bu

48 FRvIII induces phosphorylation of Dock180 at tyrosine residue 722 (Dock180(Y722)) and stimulates Rac1

49 imerization that releases the autoinhibitory tyrosine residue, a mechanism conserved in unrelated kin

50 , we find that both antibodies present a key tyrosine residue, albeit on different chains, that inser

51 Basic amino acids and tyrosine residues along this entry channel are predicted

52 ncing phosphorylation of specific C-terminal tyrosine residues and activation of downstream signaling

53 -stimulated phosphorylation of specific EGFr tyrosine residues and activation of ERK but not Akt-1.

54 s hydroxyl-bearing serine, threonine, and/or tyrosine residues and myristic acid; this type of esteri

55 nal covalent oxidative modifications on four tyrosine residues and one tryptophan residue of hemopexi

56 ester bonds between the DNA 3'-phosphate and tyrosine residues and plays a major role in the repair o

57 domain (GPIbalpha-N) fully sulfated on three tyrosine residues and solved the structure of its comple

58 C headgroups via cation-pi interactions with tyrosine residues and suggest that cation-pi interaction

59 calisation was observed between RNS-modified tyrosine residues and the chemokine CCL2 in diseased kid

60 ght on the distinct nature of these modified tyrosine residues, and provides a physical-chemical foun

61 nt mutagenesis of the PTB domain and the CH1 tyrosine residues, and successive substitution of these

62 avin adenine dinucleotide from a neighboring tyrosine residue are used as a sensitive probe of the fu

63 One limitation occurs when multiple tyrosine residues are in close proximity, in which case

64 reast tumors in vivo, whereas all three ShcA tyrosine residues are required for efficient breast canc

65 Tyrosine residues are sensitive to oxidation and can be

66 tracytoplasmic domain, there are 2 conserved tyrosine residues arranged in a noncanonical immunorecep

67 e revealed that IL-10Rbeta uses a network of tyrosine residues as hydrophobic anchor points to engage

68 y required for binding to the phosphorylated tyrosine residue at codon 774 of c-Cbl, but is also esse

69 robe, Abeta(1-16)(Y10W), by substituting the tyrosine residue at position 10 in the hydrophilic domai

70 The tyrosine residue at position 169 is strictly conserved a

71 Within the beta2-alpha2 loop, a tyrosine residue at position 169 is strictly conserved a

72 based activation motif (ITAM) phosphorylated tyrosine residue at position 204 in the tail of the immu

73 The tyrosine residue at position 76, which is conserved in >

74 al analysis leads to identification of a key tyrosine residue at the calponin homology (CH) domain of

75 he -7 to -4 binding sites and suggest that a tyrosine residue at the tunnel entrance of HirCel7A may

76 we identified two possible phospho-accepting tyrosine residues at positions 22 and 131.

77 ructural linker with adjacent tryptophan and tyrosine residues at positions 833 and 945 (Trp(833) and

78 importance because it binds to the critical tyrosine residues at the C terminus of PSTPIP2, which is

79 imerizes, followed by autophosphorylation of tyrosine residues at the intracellular domain.

80 transfected with a mutant caspase-8 in which tyrosine residues at Tyr397 or Tyr465 are replaced by no

81 Mutation of the latter tyrosine residues blunted the NF-kappaB activity of wild

82 linked via the oxidative quinone ring of the tyrosine residue by aryl-alkylamine addition or aryloxy

83 1, however, phosphorylation of a neighboring tyrosine residue by Src family kinases disrupts COP1 bin

84 stable isotope labeling method that targets tyrosine residues by coupling with light cysteine (d(0))

85 tion of PAK1 required the phosphorylation of tyrosine residues by Etk/Bmx and protein kinase A (PKA)

86 Tyrosine residues can act as redox cofactors that provid

87 We show here that UL37 tyrosine residues conserved among all alphaherpesviruses

88 , also affecting exon 14, that substituted a tyrosine residue critical for MET receptor turnover and,

89 idues in Src homology 2 (SH2) domain and one tyrosine residue each in calponin homology 1 (CH1) domai

90 of CD300a depends on the phosphorylation of tyrosine residues embedded in ITIMs of the cytoplasmic t

91 ition, signaling downstream of specific ShcA tyrosine residues facilitates the survival, vascularizat

92 mon pathway to sulfate CCR5 on extracellular tyrosine residues, facilitating CCR5 recognition by the

93 onstrates the importance of domain interface tyrosine residues for interaction of small molecules wit

94 nant negative GAB1 mutants lacking canonical tyrosine residues for SHP2 and PI3K interactions or lent

95 oplasmic tail of LAT, including the critical tyrosine residues for signal propagation.

96 g haem, although they are missing a critical tyrosine residue found in the ligand-binding pocket of o

97 Finally, we show that the highly conserved tyrosine residue found in the vSAg TGXY motif is require

98 a T cell receptor stimulation time course on tyrosine residues found on upstream signaling proteins (

99 tyr at potentials high enough to oxidize the tyrosine residues have allowed the electrooxidation of N

100 ation, and nitrosylation of thiol groups and tyrosine residues, have received comparatively little at

101 Specifically, phenylalanine, tryptophan and tyrosine residues highly populate the paratope of the an

102 the importance of a catalytic glutamate vs. tyrosine residue in determining the outcome of the reduc

103 sensing agonists involves a highly conserved tyrosine residue in helix VI.

104 vator of transcription 3 (STAT3) on a single tyrosine residue in response to growth factors, cytokine

105 C-IIA) as being phosphorylated in a specific tyrosine residue in response to L. monocytogenes infecti

106 omain of PLCgamma and a conserved N-terminal tyrosine residue in Spry1 and Spry2.

107 onstrate that mutation of a single conserved tyrosine residue in the ankyrin-binding motif of both Ca

108 that altering the backbone conformation of a tyrosine residue in the arginine loop can induce the A-f

109 luorosulfate probe 1 reacts with a conserved tyrosine residue in the ligand-binding site of a subset

110 production by pDC is dependent on an intact tyrosine residue in the Ly49Q cytoplasmic ITIM.

111 for anti-HCV activity, whereas the conserved tyrosine residue in the N-terminal domain of IFITM2 and

112 of the fragments within the vicinity of each tyrosine residue in the protein enables quantitative eva

113 Introduction of a key tyrosine residue in the sGC heme binding domain beta1(1-

114 ies, DrrA-mediated AMPylation of a conserved tyrosine residue in the switch II region of Rab1 was det

115 or interaction with alpha2, with a conserved tyrosine residue in the tail (Tyr(356) in Escherichia co

116 how TPSTs catalyze the sulfation of multiple tyrosine residues in a substrate protein remain unresolv

117 Mutational analysis indicates that the tyrosine residues in both inhibitory motifs of FCRL2 are

118 n the N-terminal of SOCS36E blocks access to tyrosine residues in Dome.

119 Systematic mutation of tyrosine residues in Gly/Ser-Tyr-Gly/Ser motifs of the I

120 NO derived from iNOS mediates nitration of tyrosine residues in IRF5 protein, leading to the suppre

121 on-independent mechanisms that require the 3 tyrosine residues in its cytoplasmic domain and involves

122 lementary to MptpA, phosphorylates these two tyrosine residues in MptpA.

123 anine substitution of serine, threonine, and tyrosine residues in ORF2 increased the steady-state pro

124 es) can introduce azide functional groups at tyrosine residues in peptide substrates.

125 on, the alkoxylation is highly selective for tyrosine residues in peptides and proteins, yet remarkab

126 opy for the identification of phosphorylated tyrosine residues in peptides.

127 Iodination of tyrosine residues in proteins has many uses in chemistry

128 Stable oxidation products of tyrosine residues in proteins may reflect the oxidative

129 PTPs) are enzymes that remove phosphate from tyrosine residues in proteins.

130 29 cells led to the local phosphorylation of tyrosine residues in protrusions, a signaling event that

131 We observe three classes of tyrosine residues in PYP that exhibit very different pK(

132 the role of nitration at single or multiple tyrosine residues in regulating alpha-syn structure, mem

133 that PKCdelta is phosphorylated on specific tyrosine residues in response to apoptotic agents.

134 NO mediates nitration of tyrosine residues in RORgammat, leading to the suppressi

135 However, the role of these tyrosine residues in signaling and transformation mediat

136 f Shc where Jak3 directly phosphorylated two tyrosine residues in Src homology 2 (SH2) domain and one

137 s known to be governed by phosphorylation of tyrosine residues in the activation loop of the kinase d

138 orylation of critical serine, threonine, and tyrosine residues in the C terminus of this protein.

139 Although potential CD1d-binding tyrosine residues in the CDR2beta region are conserved b

140 f the AP-2 clathrin adaptor complex and ITIM tyrosine residues in the cytoplasmic domain of 3DL1.

141 that harbored different combinations of key tyrosine residues in the cytoplasmic tail, Tyr-173, Tyr-

142 les induces the phosphorylation of conserved tyrosine residues in the cytoplasmic tails of tetherin d

143 ril formation in vitro and in vivo Some nine tyrosine residues in the fibromodulin N-terminal domain

144 ted in rapid autophosphorylation of selected tyrosine residues in the kinase domain of wild-type but

145 Thus, the two tyrosine residues in the Kv11.1 S4S5 linker play critica

146 y, we investigated the role of these phospho-tyrosine residues in the platelet functional responses a

147 bserved enhanced phosphorylation of FCRL4 on tyrosine residues in the presence of the HCK p59 or FGR.

148 t aspartate, cysteine, serine, threonine, or tyrosine residues in the rgfC mutant.

149 ivation was related to nitration of specific tyrosine residues in the three subunits.

150 y of PG9 and RSH is the presence of sulfated tyrosine residues in their antigen-binding regions.

151 re commonly post-translationally sulfated on tyrosine residues in their N-terminal regions, the initi

152 ions about the impact of mutating the distal tyrosine residues in this hydrogen bonding network on th

153 ngly, VEGF-Ax induces phosphorylation of key tyrosine residues in VEGFR-2.

154 usly shown that cortactin phosphorylation at tyrosine residues, in particular tyrosine 421, promotes

155 that phosphorylation at distinct serine and tyrosine residues inhibits PDHA1 through distinct mechan

156 gs suggest that phosphorylation at different tyrosine residues inhibits PDP1 through independent mech

157 Mutation of these tyrosine residues inhibits the promoter DNA-binding acti

158 roduced for incorporating the fluorosulfated tyrosine residue into peptides of interest.

159 The variant that altered a key tyrosine residue involved in FAD binding prevented recon

160 irected mutagenesis of RCAR1 showed that its tyrosine residue is critical for AHG1 interaction and re

161 We further demonstrate that the tyrosine residue is phosphorylated by Src family kinases

162 that is present in methanofuran cofactors, a tyrosine residue is present in methylofuran, which was f

163 nilines to o-aminophenol groups derived from tyrosine residues is also described.

164 Direct polymer conjugation at peptide tyrosine residues is described.

165 ted that the presence of at least one of the tyrosine residues is essential for efficient catalysis b

166 In the absence of this tyrosine residue, levels of DM remained unchanged irresp

167 O and M into clusters based on a cysteine or tyrosine residue located at position 181 of RT and linke

168 Results demonstrated that a tyrosine residue located on a catalytic loop proximal to

169 bstrate interaction is mediated by conserved tyrosine residues located in flexible loops in nucleotid

170 ases (SFKs) and that this occurs on multiple tyrosine residues located within its negative regulatory

171 only AL-09 favors dimer conformations where tyrosine residues mediate crucial interactions for amylo

172 is the first kinase to phosphorylate the key tyrosine residue needed to maintain BAK in an inactive c

173 these predictions for a lysine residue and a tyrosine residue of the C-terminal extension that penetr

174 and efficient phosphorylation of C-terminal tyrosine residues of alpha-syn remain to be identified.

175 l that MPO chlorinates and nitrates specific tyrosine residues of apoA-I, the major HDL protein.

176 We have identified the specific tyrosine residues of CitK that are phosphorylated and sh

177 Mutation analysis of known tyrosine residues of FGFR1 reveals that tyrosine 653/654

178 t of biological functions by phosphorylating tyrosine residues of intracellular proteins upon extrace

179 orylate extracellular serine, threonine, and tyrosine residues of numerous proteins have been identif

180 rc-dependent phosphorylation of two critical tyrosine residues of p130CAS, leading to the assembly of

181 oxyribozymes, DNA enzymes) can phosphorylate tyrosine residues of peptides.

182 serve as docking elements to dephosphorylate tyrosine residues of target proteins.

183 ates that the 3-fluorosialyl moiety modifies tyrosine residues of the sialidases.

184 Here, we show that nitration of a single tyrosine residue on a small proportion of 90-kDa heat-sh

185 unctional implications of previously unknown tyrosine residues on beta-catenin phosphorylated by Jak3

186 Upon stimulation, FGFR2 phosphorylates tyrosine residues on Grb2, promoting dissociation from t

187 in a ligand-dependent manner through unique tyrosine residues on IL-17RB.

188 ukocyte PECAM induces phosphorylation of two tyrosine residues on its cytoplasmic tail.

189 , was associated with several phosphorylated tyrosine residues on nephrin.

190 ulose surface, leading to alignment of three tyrosine residues on the binding face of the enzyme with

191 inase, which promotes the phosphorylation of tyrosine residues on the intracellular tail of LepRb.

192 aling events initiated by phosphorylation of tyrosine residues on the long form of the leptin recepto

193 gating the effects of oxidative nitration of tyrosine residues on the structure of aS and its interac

194 finding of BAK1 to be autophosphorylated at tyrosine residues, our results unveiled the tyrosine pho

195 es SHP-1 and causes dephosphorylation of SPL tyrosine residues, PGI2 and forskolin cause phosphorylat

196 th the proposal that conserved histidine and tyrosine residues play important catalytic roles.

197 e show M13 phage genetically engineered with tyrosine residues precisely fused to the major coat prot

198 here both the distal Cu and the redox-active tyrosine residue present in CcO are modelled.

199 P apparently clashes with a highly conserved tyrosine residue, preventing the formation of a correct

200 ce, whereas mimicking phosphorylation of the tyrosine residue promoted internalization and reduced ce

201 osition 33, but not in any of the other four tyrosine residues prone to nitration in Hsp90, was suffi

202 lalanines that can be selectively mutated to tyrosine residues, provides an ideal protein with which

203 Protein phosphorylation at distinct tyrosine residues (pY) is essential for fast, specific,

204 Although reversible phosphorylation on tyrosine residues regulates the activity of many eukaryo

205 rm crucial hydrogen bonds with glutamate and tyrosine residues, respectively.

206 ephrin or with a mutant Nephrin in which the tyrosine residues responsible for SH2 domain binding wer

207 abilizes the deprotonation of an active-site tyrosine residue, resulting in a very large isotope effe

208 atase (TCPTP) dephosphorylated TbetaRII tail tyrosine residues, resulting in inhibition of TbetaR-dep

209 T constructs with combinatorial mutations of tyrosine residues reveal a previously unidentified allos

210 caused a fairly indiscriminate nitration of tyrosine residues, reversible modifications of protein t

211 this was related to de-nitration of specific tyrosine residues, suggesting KGDHC may have a denitrase

212 ed by a cluster of four manganese ions and a tyrosine residue that comprise the redox-active componen

213 Y147del), a mutant with a deleted C-terminal tyrosine residue that fails to suppress ICD, cannot inte

214 may interact with Y529, a conserved R-helix tyrosine residue that forms part of the CLC ion conducti

215 We show that EgtB contains a conserved tyrosine residue that reacts via proton-coupled electron

216 ET9 or RET51 isoforms harboring mutations in tyrosine residues that act as docking sites for the adap

217 on of insulin receptor substrate 1 (IRS1) on tyrosine residues that activate PI3K.

218 controlled this process as well as the EGFR tyrosine residues that are involved.

219 I1 compared to wild-type FLI1 and depends on tyrosine residues that are necessary for phase transitio

220 ction by acting as a molecular shield of key tyrosine residues that are targets for the tyrosine phos

221 te that ACK1 phosphorylates cortactin on key tyrosine residues that create docking sites for adaptor

222 binding appear to be conserved glutamine and tyrosine residues that form hydrogen bonds with the carb

223 sine kinases involves autophosphorylation of tyrosine residues that recruit Src-homology 2 (SH2)-doma

224 mic acid residue acts synergistically with a tyrosine residue to function in ADP-dependent subunit-su

225 ingle-nucleotide substitution that shifted a tyrosine residue to histidine near the active site of th

226 The ability to selectively mutate tyrosine residues to fluorotyrosines is limited, however

227 er (HAT) pathway with a pair of cysteine and tyrosine residues to regenerate SAM.

228 ch of which has a different position for the tyrosine residue, together with competing functionalitie

229 3'-phospho-adenosine-5'-phospho-sulfate onto tyrosine residues, TPST1 and TPST2, are anchored to the

230 ed activation of TRPV4, which requires a key tyrosine residue (TRPV4-Tyr-110).

231 phosphorylation status of two well conserved tyrosine residues, typically located in the D-loop, regu

232 Here, we report that phosphorylation of a tyrosine residue Tyr-301 also inhibits PDH alpha 1 (PDHA

233 hosphorylation of beta-catenin, primarily on tyrosine residues Tyr 654 and Tyr 670.

234 teracts with DEF6 and phosphorylates DEF6 at tyrosine residues Tyr(210) and Tyr(222).

235 esence of an arginine residue (Arg(105)) and tyrosine residue (Tyr(102)) in the acyl pocket of Sirt5.

236 results from insertion of a conserved CHMP5 tyrosine residue (Tyr(182)) at the core of LIP5NTD struc

237 single nitration site in Akt1 located at the tyrosine residue (Tyr(350)) located within the client-bi

238 Mutating a tyrosine residue (Tyr(4)(5)(8)) in the Kv1.2 C terminus

239 tes NMHC-IIA in a previously uncharacterized tyrosine residue (Tyr-158) located in its motor domain n

240 Crystal structures of GltPh revealed a tyrosine residue (Tyr-33) that we propose interacts with

241 We identified four tyrosine residues (Tyr-649, Tyr-671, Tyr-734, and Tyr-81

242 on the phosphorylation of a highly conserved tyrosine residue, Tyr 57, in histone H2A and is mediated

243 re we report that phosphorylation at another tyrosine residue, Tyr-94, inhibits PDP1 by reducing the

244 M2 has two closely spaced tyrosine residues, Tyr(120) and Tyr(129), which are phos

245 anization is governed, on one side, by three tyrosine residues, Tyr(194), Tyr(196), and Tyr(199), whi

246 he crystal structure of VAO reveals that two tyrosine residues, Tyr-108 and Tyr-503, are positioned t

247 ements show that mutation of two pore-lining tyrosine residues, Tyr-23 and Tyr-149 in sheep AQP0, to

248 to study radical formation in DHP when three tyrosine residues, Tyr-28, Tyr-34, and Tyr-38, were repl

249 sequence motif in EL5 containing a conserved tyrosine residue (Tyr293) whose aromatic side chain is e

250 lations of AtNIP7;1 suggest that a conserved tyrosine residue (Tyr81) located in transmembrane helix

251 g results in the unique conformations of two tyrosine residues, Tyr9(1.35) and Tyr271(7.36), which ar

252 rmed by covalent ortho-ortho coupling of two tyrosine residues under conditions of oxidative stress b

253 studies reveal that Dbl is phosphorylated on tyrosine residues upon stimulation by growth factors and

254 ning phosphocholinated serine, threonine, or tyrosine residues using preformed functional amino acid

255 in, where Jak3 directly phosphorylated three tyrosine residues, viz.

256 ex on evolutionarily conserved threonine and tyrosine residues was recently identified and shown to b

257 nation position is restricted by a conserved tyrosine residue, whereas access to this same position s

258 mutant RPTPgammas retained a phosphorylated tyrosine residue, whereas similarly expressed wild type

259 s change is accompanied by a conversion of a tyrosine residue, which is identified as the formation o

260 holipase Cgamma2, a protein reported to bind tyrosine residues, which are absent in the cytoplasmic d

261 hat sequence specificity is conferred by two tyrosine residues, which insert into the minor groove of

262 Several tyrosine residues with elevated phosphorylation (i.e. Ty

263 Moreover, we have identified two tyrosine residues with opposing regulatory functions: on

264 oxynitrite-mediated nitration of a conserved tyrosine residue within B56delta (B56delta(Y289)).

265 A tyrosine residue within the cytoplasmic tail of Env was

266 o-step phosphorylation mechanism involving a tyrosine residue within the kinase inhibitory domain and

267 Itk catalyzes phosphorylation on tyrosine residues within a number of its natural substra

268 tory receptors, phosphorylation of cytosolic tyrosine residues within ITIMs results in recruitment of

269 ranslationally modified by sulfate groups at tyrosine residues within its N-terminal extracellular do

270 h c-Abl and underwent phosphorylation on two tyrosine residues within its regulatory activation funct

271 Previous studies have shown that several tyrosine residues within JAK2 are phosphorylated on grow

272 how that a triad of strongly hydrogen-bonded tyrosine residues within the active site of the enzyme k

273 te-directed mutagenesis showed that specific tyrosine residues within the ChtA CR domain were critica

274 aRII-induced signaling; however, there are 5 tyrosine residues within the cytoplasmic tail that could

275 o the extracellular domain of MPL and that 3 tyrosine residues within the intracellular domain of MPL

276 inker, and we show that two highly conserved tyrosine residues within the KCNH subfamily of channels

277 ted with actin, can be phosphorylated on two tyrosine residues within the switch regions, suggesting

278 Interestingly, three tyrosine residues within the T-bet DNA-binding domain ar

279 Lysine and tyrosine residues within this binding site interact with

280 showed that post-translational nitration of tyrosine residues within this protein is responsible for

281 ession and phosphorylation of critical c-Met tyrosine residues without activation of mitogen-activate

282 pletely abolishes the phosphorylation of all tyrosine residues, without measurable effects on recepto

283 The highly conserved tyrosine residue Y(7.53) undergoes transitions between t

284 HIPK2 by phosphorylating a highly conserved tyrosine residue Y-361 within the kinase domain.

285 GIRK phosphorylation at this amino terminal tyrosine residue (Y12) enhances channel deactivation.

286 We also identified a tyrosine residue (Y152) within the HPM motif of HIP1 tha

287 owever, in the pCU1 structure, the conserved tyrosine residues (Y18,19,26,27) that are required for D

288 elded from the substrate or the solvent by a tyrosine residue (Y224).

289 S. aureus AgrA identifies a highly conserved tyrosine residue, Y229, as a major amino acid determinan

290 Alanine mutation of a conserved H-I loop tyrosine residue, Y232, prevents regulation demonstratin

291 w that Swe1(Wee1) phosphorylates a conserved tyrosine residue (Y24 in yeast Hsp90 and Y38 in human Hs

292 is frequently phosphorylated at a conserved tyrosine residue, Y240, in GBM clinical samples.

293 re examined in a mutant of the key I4R motif tyrosine residue (Y325F) and different gammaC truncation

294 ere, we have shown that phosphorylation of a tyrosine residue (Y36) present in ERbeta, but not in ERa

295 which are contingent on phosphorylation of a tyrosine residue (Y380) found in the linker region betwe

296 III in domain IV of TetM, revealing that the tyrosine residues Y506 and Y507 are not responsible for

297 In addition, the NDV F CT has two conserved tyrosine residues (Y524 and Y527) and a dileucine motif

298 In OprP there are two tyrosine residues, Y62 and Y114, whereas the correspondi

299 Phosphorylation of a single tyrosine residue, Y836, is required for activation of EF

300 gB/gH-gL-induced cell-cell fusion in vitro, tyrosine residues Y881 and Y920 in the gBcyt were substi