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1 varphi is a hydrophobic amino acid and pY is phosphotyrosine).
2 f that forms a direct salt bridge with bound phosphotyrosine.
3 cific for phosphoserine, phosphothreonine or phosphotyrosine.
4 mutant Y138F displayed reduced FGFR3-induced phosphotyrosine.
5 to bind phosphorylated substrates including phosphotyrosine.
6 ractions beyond the classical recognition of phosphotyrosine.
7 signaling interactions beyond recognition of phosphotyrosine.
8 s analyzed using specific antibodies against phosphotyrosine.
9 und peptides containing phosphothreonine and phosphotyrosine.
10 hifts in the spectroscopic identification of phosphotyrosines.
11 tual amino acid sequence and position of the phosphotyrosines.
12 "knocked-in" EpoR mutant lacking cytoplasmic phosphotyrosines.
13 ated with the unusual SH2 recognition of two phosphotyrosines.
16 mortem samples, there was an accumulation of phosphotyrosine 39 alpha-synuclein in brain tissues and
19 ne 416 (stimulatory site) and down-regulated phosphotyrosine 527 (inhibitory site) in retinal cells,
20 Transgenic osteoclasts showed a lower c-Src phosphotyrosine 527 level, greater c-Src kinase activity
22 lpha1-antitrypsin deficiency, and editing of phosphotyrosine 701 in STAT1, the activity switch of the
26 re, we investigated the possibility that the phosphotyrosine adaptor protein ShcA regulates nephrin t
27 bstitute tyrosine 104 with chemically stable phosphotyrosine analogue (p-Carboxymethyl-L-phenylalanin
28 alidation of the predicted sites using a pan-phosphotyrosine and a site-specific antibody, which we g
29 an increase in PI3K enzyme activity in anti-phosphotyrosine and anti-IGF-1R immunoprecipitates of RO
31 ed diversity in SH2 domain interactions with phosphotyrosine and classify the C-terminal SH2 domain o
32 to the synapse, suppressing accumulation of phosphotyrosine and myosin without affecting F-actin.
34 that cis-interactions between the C-terminal phosphotyrosines and SH2 domain within the protein tyros
35 iched in TCR, protein kinase C-theta, ZAP70, phosphotyrosine, and HS1), forming what we term a podo-s
36 binding partner, suggesting that Nck couples phosphotyrosine- and phosphoinositide-dependent signals.
37 gets and represents a key connection linking phosphotyrosine- and phosphoserine/threonine-mediated on
42 suggest a model in which dynamic changes in phosphotyrosine-based signaling confer plasticity to the
47 , we define a novel mechanism where the CCM2 phosphotyrosine binding (PTB) domain binds the ubiquitin
48 ion of KRIT1 and CCM2 and find that the CCM2 phosphotyrosine binding (PTB) domain displays a preferen
49 cellular experiments now show that the Mint1 phosphotyrosine binding (PTB) domain that binds to APP i
50 rtually every human Src homology 2 (SH2) and phosphotyrosine binding (PTB) domain, as well as microar
51 ough experimentation, we discovered a unique phosphotyrosine binding (PTB) domain, namely atypical ph
53 These proteins associate with TBC1D1 via its phosphotyrosine binding (PTB) domains and their interact
54 protein containing pleckstrin homology (PH), phosphotyrosine binding (PTB), and leucine zipper motifs
58 otein containing pleckstrin homology domain, phosphotyrosine binding domain and leucine zipper motif)
59 uncation mutant consisting of the N-terminal phosphotyrosine binding domain blocks PP1-Axin interacti
60 erface with MDM2, only one region within the phosphotyrosine binding domain of NUMB (amino acids 113-
62 eta phosphorylation site also located in the phosphotyrosine binding domain, threonine 206, had no ph
63 g of proteins that contain Src homology 2 or phosphotyrosine binding domains and whether mechanisms i
64 e to investigate the effect of disruption of phosphotyrosine binding of the N-terminal SH2 domain of
65 eport the discovery of malonate bound in the phosphotyrosine binding pocket of the apo-Grb7-SH2 struc
67 to design inhibitors blocking its SH2 domain phosphotyrosine binding site that is responsible for bot
69 e assessed in Src homology 2 domain (SH2) or phosphotyrosine-binding (PTB) domain deletion mutants by
70 59249, p.Arg125Trp) in the N-terminal TBC1D1 phosphotyrosine-binding (PTB) domain has shown a replica
71 sent the detailed structural analysis of Shc phosphotyrosine-binding (PTB) domain in complex with the
72 step in this process involves interaction of phosphotyrosine-binding (PTB) domain in the N-terminal h
73 rystal structure at 1.37-A resolution of the phosphotyrosine-binding (PTB) domain of ARH in complex w
74 These characteristics are conserved in the phosphotyrosine-binding (PTB) domain of beta-amyloid pre
76 mprises a pleckstrin-homology (PH) domain, a phosphotyrosine-binding (PTB) domain, and C-terminal sit
77 ontaining a pleckstrin homology (PH) domain, phosphotyrosine-binding (PTB) domain, and leucine zipper
78 ontaining a pleckstrin-homology (PH) domain, phosphotyrosine-binding (PTB) domain, and leucine zipper
82 proteins containing Src homology 2 (SH2) and phosphotyrosine-binding (PTB) domains, which recognize p
85 ay of interactions that likely includes both phosphotyrosine-binding and SH3-domain-containing protei
86 Tyr(313)-phosphorylated hinge region and its phosphotyrosine-binding C2 domain that controls PKCdelta
87 Src SH2 domain strictly depends on an intact phosphotyrosine-binding competent SH2 domain and on tyro
88 variants that differ in the length of their phosphotyrosine-binding domain (PTB) and proline-rich re
89 tor-like protein that contains an N-terminal phosphotyrosine-binding domain and a C-terminal Src homo
90 if is predicted to bind directly to the Numb phosphotyrosine-binding domain and is critical for Numb
93 n containing a pleckstrin-homology domain, a phosphotyrosine-binding domain, and a leucine zipper mot
98 Unlike the monomeric nature of the SH2 and phosphotyrosine-binding domains, the architecture of the
102 hat, in the nematode Caenorhabditis elegans, phosphotyrosine-binding pseudo-phosphatases are key regu
103 mology 2 (SH2) and kinase domains and to the phosphotyrosine-binding site of the SH2 domain, respecti
104 KCtheta and specifically required a putative phosphotyrosine-binding site within its N-terminal C2 do
105 Through 7 phosphoinositide 3-kinase (PI3K) phosphotyrosine-binding sites, ErbB3 is able to recruit
106 ture/function approach, we now show that the phosphotyrosine-binding, but not the Src homology 2, dom
107 ich involves a transesterification to form a phosphotyrosine bond within the RepD active site, is clo
111 y 2 (SH2) domain-containing proteins and the phosphotyrosine-containing counterparts play significant
112 hose of the Src homology 2 (SH2) domain with phosphotyrosine-containing peptide motifs (pTyr), are ub
113 cking methods to identify phosphoserine- and phosphotyrosine-containing peptides as possible substrat
114 ng the nSH2-helical domain contact caused by phosphotyrosine-containing peptides binding to the enzym
115 hat the Vav2 SH2 domain binds selectively to phosphotyrosine-containing peptides corresponding to cor
116 ime-resolved luminescence of Tb(3+)-chelated phosphotyrosine-containing peptides, which facilitated e
118 ings demonstrate that FAK depletion switches phosphotyrosine-containing proteins from focal adhesions
119 se families, stimulate the ubiquitination of phosphotyrosine-containing proteins, including receptor
121 osine-binding (PTB) domains, which recognize phosphotyrosine-containing short linear motifs (SLiMs).
122 rexpression in HEK293 cells increases global phosphotyrosine content, promotes anchorage-independent
123 ession levels, probe signal is linked to the phosphotyrosine-correlated activation state of the ERBB2
124 ing and dissociation of effectors containing phosphotyrosine-dependent binding modules such as Src ho
125 , it binds SHP-1 and SHP-2 phosphatases in a phosphotyrosine-dependent manner, facilitating their rec
126 cal importance, how vascular cells integrate phosphotyrosine-dependent signaling to elicit cytoskelet
128 structure and dynamics of complexes of three phosphotyrosine-derived peptides with the Src SH2 domain
129 ochemical analyses reveal that Apn2 resolves phosphotyrosine-DNA conjugates, terminal 2',3'-cyclic ph
130 rowth factor, there are only two established phosphotyrosine-docking sites (Tyr-490 and Tyr-785 on Tr
131 or tyrosine kinases generally act by forming phosphotyrosine-docking sites on their own endodomains t
132 (linker for activation of T cells)-Grb2-SOS phosphotyrosine-driven phase transition at the membrane.
134 we combine this approach with immunoaffinity phosphotyrosine enrichment, enabling the identification
136 e ShK-170 (ShK-L5), containing an N-terminal phosphotyrosine extension of the Stichodactyla helianthu
137 tamic acid (E) mutant Y138E, which can mimic phosphotyrosine, failed to induce transient DNA replicat
138 tamic acid (E) mutant Y131E, which may mimic phosphotyrosine, failed to stimulate transient DNA repli
139 l-cysteine-l-phenylalanine, or l-cysteine-l-phosphotyrosine formed on crystallographically textured
140 osine (160-fold), sulfotyrosine (3600-fold), phosphotyrosine (>8000-fold), and phosphoserine (>8000-f
143 Proteome analysis was based on 2D-DIGE, phosphotyrosine immunoprecipitations followed by 1D SDS-
144 ur finding that v-Src increased the level of phosphotyrosine in cellular proteins in RSV-transformed
148 sequences of approximately 100 aa that bind phosphotyrosines in signaling proteins and thereby media
149 tion of PLC-gamma1 by Itk requires a direct, phosphotyrosine-independent interaction between the Src
152 O6 is present on peripheral adaptor protein, phosphotyrosine interacting with PH domain and leucine z
153 and Tyr-1162 of ERBB4, as well as the intact phosphotyrosine-interacting SH2 domain of VAV3, are nece
156 concomitant decline of Ca(2+) dampens the C2-phosphotyrosine interaction so that PLCgamma2 activation
157 94Asn]) in the gene for the Adaptor Protein, Phosphotyrosine Interaction, PH domain, and leucine zipp
158 1 and APPL2 proteins (APPL (adaptor protein, phosphotyrosine interaction, pleckstrin homology (PH) do
159 e affinities and specificities of SH2 domain-phosphotyrosine interactions have been well characterize
161 egion 2600-2605 and incorporated unprotected phosphotyrosine into IkappaB-alpha using a modified gene
162 bosomes capable of incorporating unprotected phosphotyrosine into proteins from a phosphotyrosyl-tRNA
164 resulting in the activation of the specific phosphotyrosine kinases SRC, LYN, and SYK and the concom
166 B cell activation was indicated by high phosphotyrosine levels in caps and patches, expression o
167 bonate proportionally dictates total protein phosphotyrosine levels obtained after stimulation with e
168 otion is reinforced by their decreased total phosphotyrosine levels, mirroring a postactivated stage,
170 rise to both increased growth and decreased phosphotyrosine levels; cellular PTP activity can theref
172 required for the precise positioning of the phosphotyrosine linkage for nucleophilic attack by the 3
175 itors (TKIs), which has uncovered widespread phosphotyrosine-mediated regulation of drug transporters
176 provide insight into Eya's participation in phosphotyrosine-mediated signaling networks by demonstra
179 ssibility of integrating the newly developed phosphotyrosine mimetic moiety into inhibitors designed
182 The interaction is independent of both a phosphotyrosine motif and a proline-rich sequence, the c
183 onserved architecture that recognizes linear phosphotyrosine motifs and is present in a wide range of
184 on DNA damage, the cytoskeleton, SH2-binding phosphotyrosine motifs and motif mimicry by pathogenic b
185 ich bears a dimeric fold that recognizes the phosphotyrosine motifs of E-cadherin, cortactin, DOK1, a
186 ntains a sterile-alpha motif (SAM) domain, 3 phosphotyrosine motifs, a proline-rich region, and a Src
190 rc homology (SH) 2 domain binds two specific phosphotyrosines on cortactin, a known Abl/Arg substrate
196 order to visualize synaptic accumulation of phosphotyrosine, paxillin, F-actin, and the major motor
201 method, targeted ECD allows analysis of both phosphotyrosine peptides and lower abundance phosphopept
202 e identification of 3168 unique nonredundant phosphotyrosine peptides in two LC-MS/MS runs from 8 mg
203 spectrometric data set of affinity-purified phosphotyrosine peptides obtained from normal and cancer
204 Proteomic analysis revealed several novel phosphotyrosine peptides, including Harvey rat sarcoma o
205 the opposite direction to that of canonical phosphotyrosine peptides, which may contribute to their
206 activity and suggested the involvement of a phosphotyrosine phosphatase 1b (PTP1b) in this process.
207 VEGFR2 by calpain via its substrate protein phosphotyrosine phosphatase 1B (PTP1B), and the relevanc
208 on of suppressor of cytokine signaling-3 and phosphotyrosine phosphatase 1B, two negative regulators
210 Tyr-1510 were phosphorylated on IQGAP1 when phosphotyrosine phosphatase activity was inhibited in ce
212 g in hematopoietic cells is regulated by the phosphotyrosine phosphatase SHP-1, which is not implied
213 phosphotyrosine signaling-tyrosine kinases, phosphotyrosine phosphatases, and Src Homology 2 (SH2) d
214 ing mechanism was ROS-mediated inhibition of phosphotyrosine phosphatases, which antagonize receptor
218 signaling pathways in HNSCC, we compared the phosphotyrosine profiles of a panel of HNSCC cell lines
219 highlights the application and potential of phosphotyrosine profiling for identifying clinically rel
220 ted under these conditions with quantitative phosphotyrosine profiling identified 193 differentially
222 ome similarity to that of low-molecular-mass phosphotyrosine protein phosphatase, although Ssu72 has
228 t nature of hydrogen bonding interactions in phosphotyrosine (pTyr) and sulfotyrosine (sTyr) residues
229 these effects, we analyzed the stability of phosphotyrosine (pTyr) sites in ovarian and colon tumors
234 specificity is highly biased toward a single phosphotyrosine (pY) motif among many potential pYXNX Gr
235 g sequence-specific antibodies (Abs) against phosphotyrosine (pY) motifs embedded in folded polypepti
236 to discover a BCR-ABL fusion in H929 cells: phosphotyrosine (pY) peptide IP, p85 regulatory subunit
237 th similar affinities to known Stat3-binding phosphotyrosine (pY) peptide motifs, including those of
238 veal hypothesized novel EPOR/JAK2 targets, a phosphotyrosine (PY) phosphoproteomics approach was appl
241 H2 ligand, a constrained mimic, in which the phosphotyrosine (pY) residue is preorganized in the boun
242 e binding of Src-homology 2 (SH2) domains to phosphotyrosine (pY) sites is critical for the autoinhib
243 for specific and absolute quantification of phosphotyrosine (pY) under the assistance of a protein t
244 reventing dephosphorylation of substrate Lck phosphotyrosine (pY)-505 versus preventing dephosphoryla
245 VHZ efficiently catalyzes the hydrolysis of phosphotyrosine (pY)-containing peptides but exhibits no
248 RTK(571-999) in incubations with recombinant phosphotyrosine-recognition sequences expressed as GST-f
249 hrough binding of the Nck1 SH2 domain to the phosphotyrosine residue at position 602 (Y602) of the Ep
250 consisting of an N-capped d-tetrapeptide, a phosphotyrosine residue, and a diester or a diamide grou
251 inds of D-tetrapeptide containing one or two phosphotyrosine residues and with the N-terminal capped
253 SH2 domain of STAT6 to block recruitment to phosphotyrosine residues on IL-4 or IL-13 receptors and
254 interaction between the STATc SH2 domain and phosphotyrosine residues on Pyk2 that are generated by a
256 dephosphorylation on the critical 1007-1008 phosphotyrosine residues, implying JAK2 inhibition and t
257 of neighboring negatively charged N-terminal phosphotyrosine residues, promoting swelling of caveolae
259 necessary for the formation of invadopodia, phosphotyrosine-rich structures which degrade the extrac
260 ns from 8 mg of HeLa peptides, each with 80% phosphotyrosine selectivity, at a peptide FDR of 0.2%.
262 estern blot phosphorylated Jak1, Jak3, and a phosphotyrosine signal attributed to the gamma(c)-chain,
263 ivision, NMY-2 is required for SRC-dependent phosphotyrosine signaling and acts in parallel with WNT-
264 in the modulation of point contact dynamics, phosphotyrosine signaling at filopodial tips, and lamell
265 e performed a quantitative comparison of the phosphotyrosine signaling network and resulting phenotyp
266 etic nephropathy, has been shown to activate phosphotyrosine signaling pathways in human podocytes.
269 Yet the three-part toolkit that regulates phosphotyrosine signaling-tyrosine kinases, phosphotyros
271 ll receptor signal transduction by enhancing phosphotyrosine signals and intracellular calcium fluxes
276 SP) and an SH2 domain that binds to multiple phosphotyrosine sites in the adhesion protein nephrin, l
277 studies identified noncatalytic tyrosine and phosphotyrosine sites that can be liganded by SuTEx frag
279 e purified phosphorylated protein bound to a phosphotyrosine specific antibody and permitted NF-kappa
280 mong the first to recognize the potential of phosphotyrosine-specific antibodies, Parsons and colleag
281 , substrates, and pathways through which the phosphotyrosine-specific ubiquitin ligases regulate dive
282 escence colocalization of Muc1/TLR5 and Muc1/phosphotyrosine staining patterns in mouse airway epithe
283 principally recognizes the phosphate of its phosphotyrosine substrate and further stabilizes the tyr
285 A peptide bound in the active site mimics a phosphotyrosine substrate, affords insight into substrat
286 ough some crystal contact surfaces involving phosphotyrosines suggested the possibility of tyrosine p
287 ability, ShK-192, contains a nonhydrolyzable phosphotyrosine surrogate, a methionine isostere, and a
290 N-Fmoc and O-Et protected phosphoserine and phosphotyrosine to prepare molecularly imprinted monolit
292 rts have established that GIV is involved in phosphotyrosine (Tyr(P))-based signaling in response to
293 differing only in their N-terminal residue, phosphotyrosine vs lysine, coassemble as stacks of antip
294 n the human genome that show specificity for phosphotyrosine, we identified six PTPs by quantitative
296 yl amino propionic acid (pCAP), an analog of phosphotyrosine, which can be incorporated into peptides
297 coumaryl amino propionic acid, an analog of phosphotyrosine, which can be incorporated into peptides
298 is binding of its tandem SH2 domains to dual phosphotyrosines within FcepsilonRIgamma-ITAMs (immunore
299 rosine phosphatase that targets two critical phosphotyrosines within GIV and antagonizes phospho-GIV-