ライフサイエンスコーパス: phosphotyrosine binding

1 dependent of the well established SH2 domain/phosphotyrosine binding.

2 yrosine kinase activity, as assessed by anti-phosphotyrosine binding.

3 Thus, Dp110 integrates inputs from its phosphotyrosine-binding adaptor and Ras to achieve maxim

4 To determine the roles of the phosphotyrosine binding adaptors in Th2 differentiation,

5 ck, suggesting that EPEC exploits additional phosphotyrosine-binding adaptors capable of initiating a

6 tions with PKC-theta occurred independent of phosphotyrosine binding and Fyn.

7 e region of IRS-2 that contains the putative phosphotyrosine binding and SAIN elements (188-591) is s

8 The phosphotyrosine binding and Shc and IRS-1 NPXY binding d

9 iate with the known phosphotyrosine-specific phosphotyrosine binding and src homology 2 protein domai

10 ay of interactions that likely includes both phosphotyrosine-binding and SH3-domain-containing protei

11 to mammalian X11/mint proteins, containing a phosphotyrosine-binding and two PDZ domains.

12 ture/function approach, we now show that the phosphotyrosine-binding, but not the Src homology 2, dom

13 It has been proposed that phosphotyrosine binding by the Lck SH2 domain may enhanc

14 il to CD45 by interactions other than direct phosphotyrosine binding by the SH2 domain.

15 Tyr(313)-phosphorylated hinge region and its phosphotyrosine-binding C2 domain that controls PKCdelta

16 its interaction with IL-2Rbeta in vitro, its phosphotyrosine binding capability was essential for the

17 alpha-carbon to optimize interactions in the phosphotyrosine-binding cavity of the Grb2-SH2 domain.

18 n encoded by this gene retains the conserved phosphotyrosine binding domain (PTB) in the N-terminal a

19 cC, which like ShcA contains an NH2-terminal phosphotyrosine binding domain (PTB), a central effector

20 The cell fate determinant Numb is a phosphotyrosine binding domain (PTB)-containing endocyti

21 ses mapped the ERalpha binding domain to the phosphotyrosine binding domain 2 (PTB2).

22 Full-length Dab1 or its phosphotyrosine binding domain alone increased surface l

23 Like ARH, xARH contains a highly conserved phosphotyrosine binding domain and a clathrin box.

24 his screening led to the identification of a phosphotyrosine binding domain and a pleckstrin homology

25 yrin repeats, two sterile alpha motifs and a phosphotyrosine binding domain and is ubiquitously expre

26 otein containing pleckstrin homology domain, phosphotyrosine binding domain and leucine zipper motif)

27 serine/threonine protein kinase Cdelta is a phosphotyrosine binding domain and present the crystal s

28 on of Su(H); both the C-terminal half of the phosphotyrosine binding domain and the C terminus of Num

29 Both the phosphotyrosine binding domain and the carboxyl-terminal

30 Thus, both the phosphotyrosine binding domain and the carboxyl-terminal

31 urthermore, Dok can homodimerize through its phosphotyrosine binding domain and Tyr(146) at the amino

32 The CED-6 protein contains a phosphotyrosine binding domain at its N terminus and a p

33 library approach, we have shown that the Dok phosphotyrosine binding domain binds phosphopeptides wit

34 uncation mutant consisting of the N-terminal phosphotyrosine binding domain blocks PP1-Axin interacti

35 Cbl-induced NFAT/AP1 activation requires the phosphotyrosine binding domain but not Crk(L)/p85 PI3K a

36 Because the Dab1 phosphotyrosine binding domain can interact simultaneous

37 B-1 encodes a signaling protein containing a phosphotyrosine binding domain homologous to that of dNu

38 In pull-down experiments, the xARH phosphotyrosine binding domain interacted with the LDL a

39 The phosphotyrosine binding domain of ARH interacted with th

40 GST-pulldown experiments indicate that the phosphotyrosine binding domain of ARH interacts with the

41 The phosphotyrosine binding domain of ARH plus either the cl

42 t, the G306E mutation, which inactivates the phosphotyrosine binding domain of Cbl, blocks NFAT/AP1 a

43 he NPXY domains of APP and apoEr2 and on the phosphotyrosine binding domain of Dab1 but did not depen

44 a direct interaction between the N-terminal phosphotyrosine binding domain of Dab2 and the MH2 domai

45 The carboxyl-terminal phosphotyrosine binding domain of FE65 interacts in vivo

46 The phosphotyrosine binding domain of GULP was necessary and

47 nsulin receptor substrate 1 (IRS-1), via the phosphotyrosine binding domain of IRS-1 and the NPXY mot

48 The phosphotyrosine binding domain of JIP1 binds the cytopla

49 erface with MDM2, only one region within the phosphotyrosine binding domain of NUMB (amino acids 113-

50 Deletion analysis showed that the phosphotyrosine binding domain of Odin is not required f

51 We demonstrate that the phosphotyrosine binding domain of Shc is necessary and s

52 e in conferring high-affinity binding to the phosphotyrosine binding domain of shc or the src homolog

53 the negative regulatory function of the Cbl phosphotyrosine binding domain on protein-tyrosine kinas

54 Mutations in the phosphotyrosine binding domain protein ARH cause autosom

55 AB-6.2 bound to and colocalized with the PDZ/phosphotyrosine binding domain protein LIN-10.

56 der was shown to be caused by mutations in a phosphotyrosine binding domain protein, ARH, which is re

57 contains a pleckstrin homology domain and a phosphotyrosine binding domain that binds to phosphotyro

58 The GULP phosphotyrosine binding domain was able to specifically

59 fusions of cyan fluorescent protein (CFP), a phosphotyrosine binding domain, a consensus substrate fo

60 minal Pleckstrin homology domain, a putative phosphotyrosine binding domain, and a carboxyl-terminal

61 al pleckstrin homology domain, followed by a phosphotyrosine binding domain, followed by a group of l

62 rized inhibitor of Notch and also contains a phosphotyrosine binding domain, suggesting that Numb cou

63 eta phosphorylation site also located in the phosphotyrosine binding domain, threonine 206, had no ph

64 ulates the binding of Shc and possibly other phosphotyrosine binding domain- and SH2-containing prote

65 tensin like) is an Src homology 2 (SH2) and phosphotyrosine binding domain-containing focal adhesion

66 ain revealed that a recognition site for the phosphotyrosine binding domain-containing proteins is es

67 sponse to IL-4, the IL-4R activates a set of phosphotyrosine binding domain-containing proteins, incl

68 as docking sites for Src homology 2 (SH2) or phosphotyrosine binding domain-containing signaling mole

69 as found to bind directly to Shc through the phosphotyrosine binding domain.

70 otein has a pleckstrin homology domain and a phosphotyrosine binding domain.

71 ociate with the EGF receptor through the Shc phosphotyrosine binding domain.

72 tyrosine 1173, a site recognized by the Shc phosphotyrosine binding domain.

73 , as the principal contact sites for the Shc-phosphotyrosine binding domain.

74 n does not appear to have either an SH2 or a phosphotyrosine binding domain.

75 tion, we found that PP2A associates with the phosphotyrosine-binding domain (PTB domain) of Shc and t

76 variants that differ in the length of their phosphotyrosine-binding domain (PTB) and proline-rich re

77 Numb has a protein domain homologous to the phosphotyrosine-binding domain (PTB) in the adaptor prot

78 The crystal structure of the phosphotyrosine-binding domain (PTB) of the X11 protein

79 constitutively bound through its N-terminal phosphotyrosine-binding domain (PTB) to FGF receptors (F

80 Deletion of the phosphotyrosine-binding domain also inhibited synthesis.

81 tor-like protein that contains an N-terminal phosphotyrosine-binding domain and a C-terminal Src homo

82 if is predicted to bind directly to the Numb phosphotyrosine-binding domain and is critical for Numb

83 napsins I, II, and III through an N-terminal phosphotyrosine-binding domain interaction, which leads

84 the specificity of Src homology 2 (SH2) and phosphotyrosine-binding domain interactions are mediated

85 sed of the membrane targeting signal and the phosphotyrosine-binding domain of FRS2alpha fused to the

86 cterize such interaction networks within the phosphotyrosine-binding domain of insulin receptor subst

87 Similarly, the phosphotyrosine-binding domain of IRS-1 mediates a direc

88 This interaction occurred between the phosphotyrosine-binding domain of SH2D5 and an NxxF moti

89 ecomes tyrosine phosphorylated and binds the phosphotyrosine-binding domain of SHC in response to act

90 A juxtamembrane segment of FGFR-1 and the phosphotyrosine-binding domain of SNTs are both necessar

91 otein-interaction (PI) domain similar to the phosphotyrosine-binding domain of the Shc oncoprotein, i

92 Mutations in the phosphotyrosine-binding domain protein ARH cause autosom

93 DL receptor is recognized redundantly by two phosphotyrosine-binding domain proteins, Dab2 and ARH; d

94 FGFR-1 is distinct from previously described phosphotyrosine-binding domain recognition motifs, lacki

95 nerated in which Tyr-1325 in a consensus Shc phosphotyrosine-binding domain recognition site was muta

96 The phosphotyrosine-binding domain specifically binds to pho

97 ARH contains an amino-terminal phosphotyrosine-binding domain that associates physicall

98 hosphotyrosine-dependent, thus identifying a phosphotyrosine-binding domain within the transforming r

99 ic partner molecule, an Src homology 2 (SH2) phosphotyrosine-binding domain, a DNA interaction domain

100 n containing a pleckstrin-homology domain, a phosphotyrosine-binding domain, and a leucine zipper mot

101 minal sequence that binds Munc18-1, a middle phosphotyrosine-binding domain, and two C-terminal PDZ d

102 The phosphotyrosine-binding domain, but not the pleckstrin d

103 structural features of c-Cbl, including the phosphotyrosine-binding domain, proline-rich domain, and

104 ant, inactive IRS-1 protein (deletion of the phosphotyrosine-binding domain, PTB) and does not requir

105 Whereas X11alpha interacts with APP via its phosphotyrosine-binding domain, recent reports indicate

106 the MuSK NPXY site leads to recruitment of a phosphotyrosine-binding domain-containing protein that f

107 partner ICAP1alpha, encodes a protein with a phosphotyrosine-binding domain.

108 ich further recruits p62dok via the latter's phosphotyrosine-binding domain.

109 omain linked to a PH domain and a C-terminal phosphotyrosine-binding domain.

110 ein receptor family members by recognizing a phosphotyrosine-binding domain.

111 However, CFTR does not possess a phosphotyrosine-binding domain.

112 proteins containing a Src homology 2 and/or phosphotyrosine-binding domain.

113 (pleckstrin homology) domain, a central PTB (phosphotyrosine binding) domain, and a C-terminal domain

114 racellular adapter protein containing a PTB (phosphotyrosine binding) domain, is tyrosyl-phosphorylat

115 alpha or X11beta (X11alpha/beta), whose PTB (phosphotyrosine-binding) domain binds to APP and a newly

116 Although HCPTPA possesses no identifiable phosphotyrosine binding domains (i.e. SH2 or phosphotyro

117 , such as Src homology (SH) 2 and 3 domains, phosphotyrosine binding domains (PTB), postsynaptic dens

118 h the amino-terminal pleckstrin homology and phosphotyrosine binding domains and the carboxyl-termina

119 g of proteins that contain Src homology 2 or phosphotyrosine binding domains and whether mechanisms i

120 furthermore both the pleckstrin homology and phosphotyrosine binding domains are highly homologous (a

121 The presence of pleckstrin homology and phosphotyrosine binding domains as well as multiple tyro

122 tandem of conserved pleckstrin homology and phosphotyrosine binding domains linked to a unique COOH-

123 14) interacts with the Src homology 2 and/or phosphotyrosine binding domains of Grb7, the only charac

124 to the consensus sequence recognized by the phosphotyrosine binding domains of insulin receptor subs

125 phosphotyrosine binding domains (i.e. SH2 or phosphotyrosine binding domains), it bound specifically

126 Shc contains two phosphotyrosine binding domains, an Src homology 2 (SH2)

127 proteins containing Src homology 2 (SH2) and phosphotyrosine binding domains.

128 c interaction involves both SHIP SH2 and Shc phosphotyrosine binding domains.

129 ction modules: one WW binding domain and two phosphotyrosine binding domains.

130 ilitated by modular Src homology 2 (SH2) and phosphotyrosine binding domains.

131 plified in studies with Src homology 2 (SH2) phosphotyrosine binding domains.

132 s for downstream effectors with SH2 or other phosphotyrosine binding domains.

133 ecule containing the pleckstrin homology and phosphotyrosine-binding domains associates with the insu

134 cal adhesions through the Src homology 2 and phosphotyrosine-binding domains but has lost its functio

135 ng sites in both the pleckstrin homology and phosphotyrosine-binding domains significantly reduced th

136 d sequence containing the Src homology 2 and phosphotyrosine-binding domains that are similar to the

137 s of IRS-1 (i.e. the pleckstrin homology and phosphotyrosine-binding domains), this fusion protein wa

138 ough the concurrent use of its two different phosphotyrosine-binding domains, could assemble multiple

139 APP adaptor proteins with phosphotyrosine-binding domains, including ShcA (SHC1),

140 APP adaptor proteins with phosphotyrosine-binding domains, including X11alpha (MIN

141 Unlike the monomeric nature of the SH2 and phosphotyrosine-binding domains, the architecture of the

142 tion (PI) domains (also known as the PTB, or phosphotyrosine binding, domains) of Shc and IRS-1 are r

143 ation of GRGDNP significantly decreased anti-phosphotyrosine binding during shear stress, suggesting

144 Thus a SOCS1 mutant defective in phosphotyrosine binding failed to bind to and induce ASK

145 ndent of tyrosine phosphorylation and of the phosphotyrosine binding function of Syk's tandem SH2 dom

146 Hakai acts through its phosphotyrosine-binding (HYB) domain, which bears a dime

147 To examine the role of phosphotyrosine binding in transformation by v-Src, we h

148 optimal phosphopeptide reveals a new mode of phosphotyrosine binding in which the phosphotyrosine moi

149 domain but the interaction is independent of phosphotyrosine binding, indicating a new molecular func

150 ssing constitutively activated Lck (F505) or phosphotyrosine-binding (K154F505 and C156F505) or kinas

151 Although phosphotyrosine-binding modules have been well-character

152 fecting the autophosphorylation site and the phosphotyrosine-binding motif (FLVRES) have been previou

153 pter protein that possesses an SH2 and a PTB phosphotyrosine-binding motif.

154 e to investigate the effect of disruption of phosphotyrosine binding of the N-terminal SH2 domain of

155 ode proteins with tandem pleckstrin homology-phosphotyrosine binding (PH-PTB) domains at their amino

156 homology (DH) domain that is similar to the phosphotyrosine binding/phosphotyrosine interaction (PTB

157 The structure of the phosphotyrosine binding pocket of Grb2 is similar to tha

158 eport the discovery of malonate bound in the phosphotyrosine binding pocket of the apo-Grb7-SH2 struc

159 inase activation loop bound in the canonical phosphotyrosine binding pocket of the SH2 domain and a s

160 Lck containing a mutation in the phosphotyrosine binding pocket of the SH2 domain was exp

161 reover, mutation of a key residue within the phosphotyrosine binding pocket of the Shc-PTB domain abr

162 analogues were designed on the basis of the phosphotyrosine binding pocket of the Src SH2 domain and

163 pen conformation for the BC loop and an open phosphotyrosine binding pocket, in contrast to earlier s

164 ly tentatively assigned to a cysteine in the phosphotyrosine binding pocket.

165 and mutations that interfere with the SH2D1A phosphotyrosine-binding pocket (e.g. C42W) abrogated SH2

166 hich the beta B5 arginine at the base of the phosphotyrosine-binding pocket has been replaced by a ly

167 tional changes upon binding to form a second phosphotyrosine-binding pocket in which pY346 is largely

168 ghly conserved FLVRES motif within it form a phosphotyrosine-binding pocket that is required for inte

169 ant contains a substitution that affects the phosphotyrosine-binding pocket, and this mutant is compr

170 ne-175, which makes critical contacts in the phosphotyrosine-binding pocket, was mutated to lysine or

171 or phosphotyrosine residue inserted into the phosphotyrosine-binding pocket.

172 e SH2 domain surface, far from the classical phosphotyrosine-binding pocket.

173 instead of the conserved arginine at the key phosphotyrosine-binding position, betaB5.

174 cture of the HYB domain is essential for the phosphotyrosine-binding property of Hakai.

175 Memo thus represents a new class of phosphotyrosine-binding protein.

176 The phosphotyrosine-binding/protein interaction (PTB/PI) dom

177 hat, in the nematode Caenorhabditis elegans, phosphotyrosine-binding pseudo-phosphatases are key regu

178 Accordingly, phosphotyrosine binding (PTB) and postsynaptic density-9

179 The X11 proteins contain one phosphotyrosine binding (PTB) and two PSD-95.Dlg.ZO-1 (P

180 yrosine interaction domains, an NH2-terminal phosphotyrosine binding (PTB) domain and a COOH-terminal

181 ontains a pleckstrin homology (PH) domain, a phosphotyrosine binding (PTB) domain and a leucine zippe

182 The N terminus of IRS-1 contains a phosphotyrosine binding (PTB) domain and a pleckstrin ho

183 d precursor protein (APP) via its C-terminal phosphotyrosine binding (PTB) domain and affects APP pro

184 Pull-down assays using the Dok-6 phosphotyrosine binding (PTB) domain and GDNF-activated

185 otein containing pleckstrin homology domain, phosphotyrosine binding (PTB) domain and leucine zipper

186 med a close proximity between the amino Fe65 phosphotyrosine binding (PTB) domain and LRP cytoplasmic

187 , we define a novel mechanism where the CCM2 phosphotyrosine binding (PTB) domain binds the ubiquitin

188 The cytoplasmic tail of APP interacts with phosphotyrosine binding (PTB) domain containing proteins

189 ion of KRIT1 and CCM2 and find that the CCM2 phosphotyrosine binding (PTB) domain displays a preferen

190 ing virtually every Src homology 2 (SH2) and phosphotyrosine binding (PTB) domain encoded in the huma

191 the human homologue of JIP-1 that contains a phosphotyrosine binding (PTB) domain in addition to a JN

192 n the carboxyl terminus of the protein and a phosphotyrosine binding (PTB) domain in the amino termin

193 GF-mediated Shc phosphorylation, whereas the phosphotyrosine binding (PTB) domain is critical for the

194 CCM1/CCM2 association is dependent upon the phosphotyrosine binding (PTB) domain of CCM2.

195 d energetic analysis of one such domain, the phosphotyrosine binding (PTB) domain of Disabled-1 (Dab1

196 e (Nak), which interacts physically with the phosphotyrosine binding (PTB) domain of Numb.

197 The phosphotyrosine interaction (PI)/phosphotyrosine binding (PTB) domain of Shc binds specif

198 inositol phosphate kinase (PIPKIgamma), by a phosphotyrosine binding (PTB) domain of talin.

199 we determined the solution structure of the phosphotyrosine binding (PTB) domain of the insulin rece

200 The phosphotyrosine binding (PTB) domain of X11 binds to a p

201 NPXY motif is a known binding substrate for phosphotyrosine binding (PTB) domain proteins.

202 The SNT-1 phosphotyrosine binding (PTB) domain recognizes activate

203 We recently identified a phosphotyrosine binding (PTB) domain residing within the

204 The phosphotyrosine binding (PTB) domain specifically binds

205 region (Cbl-N; residues 1 to 357) harbors a phosphotyrosine binding (PTB) domain that binds to activ

206 cellular experiments now show that the Mint1 phosphotyrosine binding (PTB) domain that binds to APP i

207 Cbl associates via its phosphotyrosine binding (PTB) domain to the ZAP-70 pY292

208 e interaction (PI) domain (also known as the phosphotyrosine binding (PTB) domain) has been described

209 Shc comprises an N-terminal phosphotyrosine binding (PTB) domain, a C-terminal Src h

210 rminus, a pleckstrin homology (PH) domain, a phosphotyrosine binding (PTB) domain, and, spread over t

211 rtually every human Src homology 2 (SH2) and phosphotyrosine binding (PTB) domain, as well as microar

212 ARH contains a phosphotyrosine binding (PTB) domain, which in other pro

213 tegrins via a novel variant of the canonical phosphotyrosine binding (PTB) domain-NPxY ligand interac

214 in, the Src homology 2 (SH2) domain, and the phosphotyrosine binding (PTB) domain.

215 ated by a segment of CKA1 that constitutes a phosphotyrosine binding (PTB) domain.

216 CKA1 binds an aPKC (PKC3) via a phosphotyrosine binding (PTB) domain.

217 or secondarily Tyr(1642), interacts with its phosphotyrosine binding (PTB) domain.

218 ogy (PH) domain, and the IH2(PTB) contains a phosphotyrosine binding (PTB) domain.

219 s of a Pleckstrin Homology (PH) domain and a Phosphotyrosine Binding (PTB) domain.

220 poprotein receptor through an amino-terminal phosphotyrosine binding (PTB) domain.

221 Pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains are structurally r

222 apped to the tensin Src homology 2 (SH2) and phosphotyrosine binding (PTB) domains at the C terminus

223 roteins contain pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains at their N termini

224 Proteins encoding phosphotyrosine binding (PTB) domains function as adapto

225 ls showed that the overexpression Shc SH2 or phosphotyrosine binding (PTB) domains of ShcA alone has

226 Phosphotyrosine binding (PTB) domains of the adaptor pro

227 eins through a domain that is related to the phosphotyrosine binding (PTB) domains of the Shc family

228 he NH2-terminal pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains, mediated phosphor

229 in receptors (TRKs) through their N-terminal phosphotyrosine binding (PTB) domains.

230 encompasses its pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains.

231 istinct from SH2 domains, referred to as the phosphotyrosine binding (PTB) or phosphotyrosine interac

232 ed Shc proteins with mutations in either the phosphotyrosine binding (PTB) or Src homology 2 domain t

233 protein containing pleckstrin homology (PH), phosphotyrosine binding (PTB), and leucine zipper motifs

234 GULP/CED-6 is a phosphotyrosine binding (PTB)-domain-containing adaptor

235 hic, NMR, and calorimetric analysis that the phosphotyrosine binding (PTB)-like domain of talin engag

236 g Src homology 2 (SH2; reviewed in [10]) and phosphotyrosine-binding (PTB) [11] domains.

237 c N-terminal sequences and common C-terminal phosphotyrosine-binding (PTB) and PDZ domains.

238 CED-6 is composed of a phosphotyrosine-binding (PTB) domain and a proline-rich

239 ase with the worm protein, hCED-6 contains a phosphotyrosine-binding (PTB) domain and potential Src-h

240 ARH has an N-terminal phosphotyrosine-binding (PTB) domain evolutionarily rela

241 59249, p.Arg125Trp) in the N-terminal TBC1D1 phosphotyrosine-binding (PTB) domain has shown a replica

242 sent the detailed structural analysis of Shc phosphotyrosine-binding (PTB) domain in complex with the

243 One serine residue located near the phosphotyrosine-binding (PTB) domain in IRS-1 (Ser(307)

244 step in this process involves interaction of phosphotyrosine-binding (PTB) domain in the N-terminal h

245 rystal structure at 1.37-A resolution of the phosphotyrosine-binding (PTB) domain of ARH in complex w

246 These characteristics are conserved in the phosphotyrosine-binding (PTB) domain of beta-amyloid pre

247 Here we show that the amino-terminal phosphotyrosine-binding (PTB) domain of Dab1 binds to th

248 proteins, we demonstrate that the N-terminal phosphotyrosine-binding (PTB) domain of Shc binds to a s

249 and association of a 150-kD protein with the phosphotyrosine-binding (PTB) domain of Shc.

250 he consensus sequence for recognition by the phosphotyrosine-binding (PTB) domain of the protooncogen

251 Here we show that the phosphotyrosine-binding (PTB) domain protein Ced-6, a we

252 97 that, when phosphorylated, interacts with phosphotyrosine-binding (PTB) domain proteins.

253 Each contains a phosphotyrosine-binding (PTB) domain that is structurall

254 boxy terminal SH2 domain and a novel non-SH2 phosphotyrosine-binding (PTB) domain that specifically r

255 Binding of the talin phosphotyrosine-binding (PTB) domain to integrin beta su

256 Here we show that the phosphotyrosine-binding (PTB) domain within the N-termin

257 of the insulin receptor substrate-1 (IRS-1) phosphotyrosine-binding (PTB) domain, alone and complexe

258 yrosine-phosphorylated receptors through its phosphotyrosine-binding (PTB) domain, and a role for the

259 mprises a pleckstrin-homology (PH) domain, a phosphotyrosine-binding (PTB) domain, and C-terminal sit

260 rc homology 2 (SH2) domain and an N-terminal phosphotyrosine-binding (PTB) domain, and is itself phos

261 ontaining a pleckstrin homology (PH) domain, phosphotyrosine-binding (PTB) domain, and leucine zipper

262 ontaining a pleckstrin-homology (PH) domain, phosphotyrosine-binding (PTB) domain, and leucine zipper

263 Dab2, through its phosphotyrosine-binding (PTB) domain, inhibits platelet

264 sine-interaction domains present in Shc, the phosphotyrosine-binding (PTB) domain, rather than its SH

265 We show that the phosphotyrosine-binding (PTB) domain-containing protein

266 xY) in the beta integrin cytoplasmic tail to phosphotyrosine-binding (PTB) domain-containing proteins

267 ophic factor receptors predominantly via its phosphotyrosine-binding (PTB) domain.

268 el of talin F3 indicated that it resembles a phosphotyrosine-binding (PTB) domain.

269 DL-receptor family members via an N-terminal phosphotyrosine-binding (PTB) domain.

270 e intrinsic EGFR kinase, as well as the ShcD phosphotyrosine-binding (PTB) domain.

271 nt sequence similarity with any known SH2 or phosphotyrosine-binding (PTB) domain.

272 part of a canonical recognition sequence for phosphotyrosine-binding (PTB) domains, protein modules t

273 re cytoplasmic docking proteins that possess phosphotyrosine-binding (PTB) domains, through which the

274 ing modules such as Src homology 2 (SH2) and phosphotyrosine-binding (PTB) domains.

275 orylated and bind proteins containing SH2 or phosphotyrosine-binding (PTB) domains.

276 zed by proteins containing a domain known as phosphotyrosine-binding (PTB) or phosphotyrosine-interac

277 The phosphotyrosine binding region, but not the PDZ-binding

278 A single point mutation that abolishes phosphotyrosine binding renders the Grb2 SH2 domain inca

279 The phosphotyrosine-binding SH2 domain of SOCS1 was critical

280 tion of a recombinant protein containing the phosphotyrosine binding (SH2) domain from the adaptor pr

281 at mutation of amino acids important for SH2 phosphotyrosine binding significantly compromises the ab

282 ays different detail interactions within the phosphotyrosine binding site and in the recognition site

283 from the enzyme active site into the second phosphotyrosine binding site is described.

284 atalytically inactive, but the phosphatase's phosphotyrosine binding site is maintained.

285 salicylic acid-based ligands for the second phosphotyrosine binding site of PTP1B using a NMR-based

286 to design inhibitors blocking its SH2 domain phosphotyrosine binding site that is responsible for bot

287 a PLCgamma SH2 domain protein mutated at its phosphotyrosine binding site, or the SH2 domains of anot

288 s for both the catalytic site and the second phosphotyrosine binding site, we have identified a small

289 te and a portion of the noncatalytic, second phosphotyrosine binding site.

290 ) mutant revealed that it requires an intact phosphotyrosine-binding site in its COOH-terminal SH2 do

291 The C-terminal phosphotyrosine-binding site is very different from the

292 The phosphotyrosine-binding site of the SH2 domain in each m

293 mology 2 (SH2) and kinase domains and to the phosphotyrosine-binding site of the SH2 domain, respecti

294 This defines a novel phosphotyrosine-binding site on the talin F3 domain and

295 KCtheta and specifically required a putative phosphotyrosine-binding site within its N-terminal C2 do

296 caused local structural perturbations in the phosphotyrosine-binding site.

297 s between the two SH2 domains distant to the phosphotyrosine binding sites, Syk dissociates from the

298 Through 7 phosphoinositide 3-kinase (PI3K) phosphotyrosine-binding sites, ErbB3 is able to recruit

299 S and STAT5b for common GHR cytoplasmic tail phosphotyrosine-binding sites; and by a time-dependent i

300 We have investigated the role of the phosphotyrosine-binding Src homology-2 (SH2), domain of