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

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