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1 on at S634 and S635 accounted for all doubly phosphorylated peptide.
2 dy developed using the CDKF;1 protein or the phosphorylated peptide.
3  The method also resulted in ECD of a doubly phosphorylated peptide.
4  Dbf4, in the presence and absence of a Cdc7 phosphorylated peptide.
5 nantly yielded E(258)SRLEDT(p)QK(266) as the phosphorylated peptide.
6 ted Thr187, but not between Skp2 and the non-phosphorylated peptide.
7 ? one order-of-magnitude weaker than the S19-phosphorylated peptide.
8  separate and quantify nonphosphorylated and phosphorylated peptide.
9 comitant increase in the (n x 80 Da)-shifted phosphorylated peptide.
10 was used to strengthen the identification of phosphorylated peptides.
11 resin but has shown the promise of enriching phosphorylated peptides.
12  were analyzed for the nonphosphorylated and phosphorylated peptides.
13 hereas TiO2 preferentially enriched multiply phosphorylated peptides.
14  oligohistidine-tagged proteins/peptides and phosphorylated peptides.
15 often precede mass spectrometric analyses of phosphorylated peptides.
16 e the positive surface selectively binds the phosphorylated peptides.
17 y profiles for both the unphosphorylated and phosphorylated peptides.
18 cation of seven synthetic enkephalin-related phosphorylated peptides.
19 sine profiling identified 193 differentially phosphorylated peptides.
20  SH2 mutant failed to interact with tyrosine-phosphorylated peptides.
21 r in order to test the specific retention of phosphorylated peptides.
22 ysis of phosphopeptides, especially multiply phosphorylated peptides.
23 ate inhibits binding of p85alpha to tyrosine-phosphorylated peptides.
24 tase fold that unexpectedly targets tyrosine-phosphorylated peptides.
25 he separation between phosphorylated and non-phosphorylated peptides.
26 ified peptides that correspond to previously phosphorylated peptides.
27 al affinity chromatography for enrichment of phosphorylated peptides.
28 e is the improved capability to characterize phosphorylated peptides.
29 osphorylated peptides and 55% or greater for phosphorylated peptides.
30  phosphorylation sites; iota PKC selectively phosphorylated peptide 1 (RTAS) within the death domain
31                An MS/MS spectrum of a triply phosphorylated peptide, 313-HTFSGVApSVEpSpSSGEAFHVGK-333
32 dopsin (330-348) were synthesized: the fully phosphorylated peptide (7P-peptide), the peptide with al
33 ve enrichment of almost all of 1214 multiply phosphorylated peptides (99.4%) in the Ga(3+)-IMAC, wher
34 eterminants of specificity of BRCA1-BRCT for phosphorylated peptides, a detailed kinetic and thermody
35 lidated in our bioinformatic pipeline by the phosphorylated peptide abundances that we observed, high
36 ral phosphorylation profiles of 222 tyrosine phosphorylated peptides across seven time points followi
37                                          The phosphorylated peptide also inhibited neurite outgrowth
38 of the known phosphorylation sites in >1,000 phosphorylated peptides analyzed.
39 PRQ has low PTPase activity against tyrosine-phosphorylated peptide and protein substrates but can de
40 ficantly outperformed UPLC-MS/MS in terms of phosphorylated peptide and total peptide IDs.
41                            Seven fluorescent phosphorylated peptides and 19 antibodies were evaluated
42 ncomitant disappearance of the major in vivo phosphorylated peptides and corresponding in vitro phosp
43 re the utility of UVPD for identification of phosphorylated peptides and find that UVPD fragmentation
44 ith and its application in the enrichment of phosphorylated peptides and lipids.
45 ty phosphatase that has activity toward both phosphorylated peptides and phospholipids.
46 ependence of the interaction between tyrosyl-phosphorylated peptides and SH2 domains.
47 ss spectrometry enables the determination of phosphorylated peptides (and thereby proteins) in scenar
48        Clostripain digestion resulted in two phosphorylated peptides, and cAMP decreased phosphorylat
49 Thr-containing peptides; a protein kinases C-phosphorylated peptide; and a phosphopeptide derived fro
50 orylated peptides and corresponding in vitro phosphorylated peptides; and (ii) comigration of the dig
51 of multiple enzyme digests; (iii) spectra of phosphorylated peptides; and (iv) spectra of peptides wi
52                            In a single step, phosphorylated peptides are covalently conjugated to a d
53                                              Phosphorylated peptides are easily recognized within the
54                              Moreover, IP(7) phosphorylated peptides are more acid-labile and more re
55                                        Thus, phosphorylated peptides are part of the repertoire of an
56  in affinities for binding singly and doubly phosphorylated peptides are reflected in the on rate, no
57                                       Singly phosphorylated peptides are retained weakly under these
58                          The resulting newly phosphorylated peptides are then isolated and identified
59 oactive peptides, only minor amounts of mono-phosphorylated peptides arising from alphas1- and beta-C
60 ne phosphatases (PTPs), employing a tyrosine-phosphorylated peptide as a substrate, has been develope
61 ass spectrometry (FAB MS/MS) analysis of the phosphorylated peptide as well as of its phosphate-conta
62  sites and resulted in the representation of phosphorylated peptides as doublets or triplets accordin
63   A novel procedure for micropurification of phosphorylated peptides, as a front end to mass spectrom
64 an be effectively fractionated from multiply phosphorylated peptides, as well as acidic peptides, via
65                             Using a panel of phosphorylated peptides based on Raf-1, we have defined
66                                 Studies with phosphorylated peptides based on the CTLA-4 intracellula
67     In the reciprocal experiments, synthetic phosphorylated peptides based on the immunoreceptor tyro
68 thousands of serine, threonine, and tyrosine phosphorylated peptides, being present in roughly equal
69 2 but is close to that for a singly tyrosine-phosphorylated peptide binding to a single SH2 domain.
70 e binary complex formed involves one MDM2 di-phosphorylated peptide bound to a dimer of 14-3-3sigma.
71 ich contain an NPxY motif, resembles that of phosphorylated peptides bound to the Shc and IRS-1 PTB d
72 e reasonably well with experimental data for phosphorylated peptide but less so for doubly charged ph
73 t serine 2, and to a lesser extent, serine 5 phosphorylated peptides, but has no affinity for unphosp
74 of hIL-4Ralpha, we demonstrate that tyrosine-phosphorylated peptides, but not their nonphosphorylated
75 n and subsequent site mapping of the heavily phosphorylated peptide by mass spectrometry.
76 face would be lost upon engagement of doubly phosphorylated peptides by the SH2 domains.
77                                  Analysis of phosphorylated peptides by two-dimensional gel electroph
78 tion site of histidine, arginine, and lysine phosphorylated peptides can be characterized by ETD.
79                                 Detection of phosphorylated peptides can be quite challenging during
80 cence emission on magnesium ion chelation by phosphorylated peptides carrying an artificial amino aci
81    The unmodified peptide, unlike the Ser378 phosphorylated peptide, changed conformation in the pres
82 on of several hundred low-abundance tyrosine phosphorylated peptides commonly dysregulated in cancer,
83                               Unlabeled dual phosphorylated peptide competed with the 125I-labeled pe
84      The assay design utilizes a fluorescent phosphorylated peptide complexed to a product-specific a
85 ments using affinity binding with a tyrosine-phosphorylated peptide containing an ITIM (ICAM-1 residu
86        We confirmed the presence of the Cdk2-phosphorylated peptide containing Ser(213) in PR from in
87 inase binds with high affinity to a tyrosine phosphorylated peptide containing the amino acids Glu, G
88 phosphatase activity against an in vitro PKA-phosphorylated peptide containing the Ser133 phosphoacce
89 ions for Tyr(446) and Tyr(496), and tyrosine-phosphorylated peptides containing Tyr(230) or Tyr(252/2
90                        In contrast, tyrosine-phosphorylated peptides containing Tyr374 or Tyr396 did
91 t the GST-Crk SH2 domain binds to a tyrosine-phosphorylated peptide corresponding to amino acids 770-
92 2-Bbeta (SH2-Bbeta (525-670)) and a tyrosine-phosphorylated peptide corresponding to the binding sequ
93  embryos resulted in the quantitation of 719 phosphorylated peptides corresponding to 449 phosphoryla
94                        We synthesised double phosphorylated peptides corresponding to regions within
95          We identified 1,936 unique tyrosine phosphorylated peptides, corresponding to 844 unique pho
96             This preferential binding of the phosphorylated peptides could be conveniently detected b
97            The identity of these doublets as phosphorylated peptides could be readily confirmed using
98 or substrate (IRS-1) complexed to a tyrosine-phosphorylated peptide derived from the interleukin 4 (I
99  and the ability to interact with a tyrosine-phosphorylated peptide derived from the interleukin-4 re
100 dem-SH2 domain of Syk (Syk-tSH2) to a dually phosphorylated peptide derived from the ITAM of the T ce
101                      We constructed a set of phosphorylated peptides derived from APN to probe for in
102 ther demonstrate that SHIP directly bound to phosphorylated peptides derived from FcgammaRIIa with a
103                           Synthetic tyrosine-phosphorylated peptides derived from five different regi
104 omain of the Syk kinase (Syk-tSH2) to doubly phosphorylated peptides derived from immune-receptor tyr
105                               Using tyrosine-phosphorylated peptides derived from Stat5A, we were abl
106 metry, we show now that unphosphorylated and phosphorylated peptides derived from the CaMKII-alpha re
107 ility to interact with both DNA and tyrosine-phosphorylated peptides derived from the IL-4 receptor a
108 ditionally, among hundreds of differentially phosphorylated peptides detected, an enrichment for phot
109 hosphorylation without having to measure the phosphorylated peptides directly or being affected by va
110                                          For phosphorylated peptides, ECD and CAD spectra give comple
111  In particular, for the analysis of labile N-phosphorylated peptides, ECD and ETD are emerging as a c
112                    Proteome-wide datasets of phosphorylated peptides, either measured in a condition
113                         Further, analysis of phosphorylated peptides enriched from the K562 human cel
114 ed on APEX2-driven biotinylation followed by phosphorylated peptides enrichment.
115 ed well with kindlin-2, whereas the Tyr(759)-phosphorylated peptide failed to bind kindlin-2 with mea
116 e, the product competes with the fluorescent phosphorylated peptide for the antibody.
117      We have screened various p53 C-terminal phosphorylated peptides for binding to two different iso
118 mple, CZE-MS/MS can identify over 500 unique phosphorylated peptides from a 200 ng sample, suggesting
119 m beta-casein were identified along with the phosphorylated peptides from alphas1-casein and alphas2-
120 AT-labeled peptides corresponding to known O-phosphorylated peptides from beta-casein were identified
121 and methods aimed at efficient enrichment of phosphorylated peptides from complex biological mixtures
122 ing and measuring the relative abundances of phosphorylated peptides from complex peptide mixtures re
123 -4-hydroxycinnamic acid for the detection of phosphorylated peptides from digests of beta-casein and
124                           Nearly 70 tyrosine-phosphorylated peptides from proteins in human T cells w
125 ry of protein phosphorylation, enrichment of phosphorylated peptides from proteolytic mixtures is oft
126                          With this approach, phosphorylated peptides from receptors digested with var
127 s of SOCS2-ElonginB-ElonginC in complex with phosphorylated peptides from substrates growth hormone r
128  small organic phosphates or, alternatively, phosphorylated peptides from the target proteins themsel
129  approach for the separation of hydrophilic, phosphorylated peptides from their unphosphorylated coun
130    Binding of the Shc PTB domain to tyrosine-phosphorylated peptides from TrkA, epidermal growth fact
131               Sld3 binds specifically to DDK-phosphorylated peptides from two MCM subunits (Mcm4, 6)
132 shown to be effective for differentiation of phosphorylated peptides from unphosphorylated ones; only
133                            In addition, some phosphorylated peptides generated by tryptic digest are
134                                          The phosphorylated peptide had no effect on phospholipid hyd
135                                              Phosphorylated peptides have smaller cross sections whic
136                                 The tyrosine phosphorylated peptide HGLDN-pY-R, its nonphosphorylated
137 ically compared UPLC-MS/MS and CZE-MS/MS for phosphorylated peptide identifications (IDs) using an en
138                                Comparison of phosphorylated peptides identified from Nb 2O 5 and TiO
139                       Among the 5,386 unique phosphorylated peptides identified in this study, we fou
140                               This number of phosphorylated peptide IDs is over 1 order of magnitude
141 order of magnitude higher than the number of phosphorylated peptide IDs previously reported by single
142 f CZE (2 mug vs 200 ng), UPLC generated more phosphorylated peptide IDs than CZE (3313 vs 1783).
143 ting that CZE and UPLC are complementary for phosphorylated peptide IDs.
144 (10)(+*), which is reacted with deprotonated phosphorylated peptides in a 3-D ion trap mass spectrome
145 ography allows the selective dissociation of phosphorylated peptides in mixtures following chromatogr
146 Detection by MAC-MSMS of singly and multiply phosphorylated peptides in tryptic digests is demonstrat
147              Specifically, the abundances of phosphorylated peptides in tryptic digests of bovine bet
148 sed ion mobility has been used to filter for phosphorylated peptides in tryptic protein digests.
149  and more resistant to phosphatases than ATP phosphorylated peptides, indicating a different type of
150  phosphopeptides induced by ABA are multiply phosphorylated peptides, indicating their importance in
151 he 14-3-3? dimer and the S19- and S40-doubly phosphorylated peptide interact in multiple ways, with t
152 inases whose substrates are enriched amongst phosphorylated peptides, interactively illustrates kinas
153          binding epitope, whereas singly S40-phosphorylated peptide interacts with 14-3-3? one order-
154 ift time-m/z relationship for singly charged phosphorylated peptide ions is different from that for n
155                                         This phosphorylated peptide is a poor substrate for CDK9 comp
156  fluorescent moiety at the N-terminus of the phosphorylated peptide is a streptavidin europium crypta
157                                          The phosphorylated peptide is characterized by helix spannin
158                              The fluorescent phosphorylated peptide is then released from the antibod
159 DI TOF) mass spectrometry, the ionization of phosphorylated peptides is usually suppressed by nonphos
160 e domain effects dynamics of proline-rich or phosphorylated peptide ligand binding sites in distal c-
161 using the src homology 2 domain and tyrosine-phosphorylated peptide ligands as a model system.
162 cular evolution by phage display to identify phosphorylated peptide ligands that recognize the shallo
163 ains, the Dab1 PTB does not bind to tyrosine-phosphorylated peptide ligands.
164 ated native CHK from cellular extracts using phosphorylated peptides linked to Affi-Gel 15.
165                          Here we show that a phosphorylated peptide motif derived from human papillom
166 ubstrate of VE-PTP represented by a tyrosine-phosphorylated peptide of Tie-2 dissociates VE-PTP from
167 ions which enables their separation from non-phosphorylated peptides of the same m/z.
168            We quantified over 2700 different phosphorylated peptides of which 360 were significantly
169                           Direct analysis of phosphorylated peptides on IMAC beads does not adversely
170 in modules that specifically bind to tyrosyl phosphorylated peptides on signaling proteins.
171                               In this assay, phosphorylated peptide or protein produced by kinase rea
172 creased the fluorescence polarization of the phosphorylated peptide over its nonphosphorylated deriva
173 in 20s, and the increase in magnitude of the phosphorylated peptide peak was monitored to assess ERK
174                           The abundance of a phosphorylated peptide (phosphopeptide) is determined by
175         The immobilized complexes can adsorb phosphorylated peptides preferentially from protein dige
176  existence and origin of naturally processed phosphorylated peptides presented by MHC class I molecul
177                                          The phosphorylated peptide product is immunocomplexed with t
178 ty, as assayed with either small-molecule or phosphorylated-peptide PTP substrates.
179 e than 30%, with improved number of multiply phosphorylated peptides, quantification accuracy, and sh
180                                          The phosphorylated peptide regions of osteopontin were ident
181                      Of the seven identified phosphorylated peptide regions, three were localized on
182 plex with a 14-3-3sigma dimer and an MDM2 di-phosphorylated peptide resulting in the stabilization of
183 ttranslationally modified peptides: IRMPD of phosphorylated peptides results in few backbone (b- and
184 esistant phosphatase activity on a synthetic phosphorylated peptide, RRA(pT)VA, indicating that Pph1
185 ations of the repetitive and quasi-symmetric phosphorylated peptide sequence.
186 in of the Src kinase to its consensus singly phosphorylated peptide (sequence pYEEI where pY indicate
187 r units, which recognize and bind to tyrosyl-phosphorylated peptide sequences on their target protein
188                            A screen with 360 phosphorylated peptides shows VHZ efficiently catalyzes
189 finity of N-terminal Mus101 with a synthetic phosphorylated peptide spanning the last 25 amino acids
190                                              Phosphorylated peptide substrates containing a quencher
191     Recombinant CDPKalpha, -beta, and -gamma phosphorylated peptide substrates containing the four-re
192                               Capture of the phosphorylated peptide substrates onto the SAM(2) membra
193 everely reduced the efficacy with which NEK6-phosphorylated peptide substrates, and moreover, mutatio
194  flight/mass spectrometry we identified five phosphorylated peptides that were present in both in viv
195            For both the unphosphorylated and phosphorylated peptides, the calculated FRET efficiencie
196  Moreover, for both the unphosphorylated and phosphorylated peptides, the statistical thermodynamic p
197 on to the above-mentioned mono- and multiply phosphorylated peptides, this fractionation ability was
198 r Western blots showed direct binding of the phosphorylated peptide to Nck-1 and SHIP-1.
199 rgy calculation of the binding of native and phosphorylated peptides to VHS domains suggests that thi
200 ment is based on the change of net charge of phosphorylated peptides under strong acidic conditions i
201 eties through a range of epitopes, including phosphorylated peptides used in diagnostics and therapeu
202 pared between nonphosphorylated and tyrosine phosphorylated peptides using electrospray tandem mass s
203 Western blotting of MKK2 protein and its T31 phosphorylated peptide verified the phosphoproteomic res
204 plays remarkable selectivity toward tyrosine-phosphorylated peptides versus serine/threonine phospho-
205                                          For phosphorylated peptides, very little loss of the labile
206                                          The phosphorylated peptide was also readily dephosphorylated
207  However, more selective isolation of singly phosphorylated peptides was observed with ZrO2 compared
208       High-resolution separation of multiply phosphorylated peptides was primarily achieved using elu
209 asis of conformational analysis of synthetic phosphorylated peptides, we show that aggregation of the
210                Using mutational analyses and phosphorylated peptides, we show that phosphorylation of
211        Next, by evaluating the CSD values of phosphorylated peptides, we were able to differentiate b
212                                       In the phosphorylated peptide weakened interaction occurs with
213    Proteins specifically precipitated by the phosphorylated peptide were identified by mass spectrome
214 , significant numbers of naturally processed phosphorylated peptides were detected in association wit
215                          The AQP0 C-terminal phosphorylated peptides were found to have 20-50-fold lo
216  HopQ1 is phosphorylated in tomato, and four phosphorylated peptides were identified by mass spectrom
217 acity via a dynamic pH junction method, 2313 phosphorylated peptides were identified with single-shot
218                                              Phosphorylated peptides were identified, one from alphaS
219                  The protonated molecules of phosphorylated peptides were sufficiently abundant that
220  to vaccination identified 53 differentially phosphorylated peptides when comparing low responders wi
221 o have potential as an additional screen for phosphorylated peptides, where up to 40% of observed pep
222 sine antibodies were used to purify tyrosine phosphorylated peptides, which were then identified by l
223 phorylation at S634 accounted for all singly phosphorylated peptide, while phosphorylation at S634 an
224 er-soluble deep cavitand hosts can recognize phosphorylated peptides with both site- and state-select
225              All PKC isozymes preferentially phosphorylated peptides with hydrophobic amino acids at
226 hotyrosine antibodies, tedious separation of phosphorylated peptides with phosphocellulose membranes,
227       A further comparison of these in vitro phosphorylated peptides with phosphopeptides derived fro
228 s, as a means to differentiate sulfated from phosphorylated peptides within the framework of a mass s

 
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