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1 lysaccharide (LPS) or IL-1 protein to bind a tyrosine-phosphorylated protein.
2 62(dok), RasGAP, and an unidentified 145-kDa tyrosine-phosphorylated protein.
3 mmunoprecipitate with an unidentified 87 kDa tyrosine-phosphorylated protein.
4 and could be easily modified to evaluate any tyrosine-phosphorylated protein.
5 of a complex between c-Src and at least one tyrosine-phosphorylated protein.
6 converge, to similar cytoskeleton-dependent tyrosine phosphorylated proteins.
7 gressive motility, and alters the pattern of tyrosine phosphorylated proteins.
8 f PI-3K was associated with 100- and 180-kDa tyrosine phosphorylated proteins.
9 simultaneously via its SH2 domain with other tyrosine-phosphorylated proteins.
10 the ras related G protein rho A, as well as tyrosine-phosphorylated proteins.
11 reased Src kinase activity and PP2-sensitive tyrosine-phosphorylated proteins.
12 system was modified to identify partners of tyrosine-phosphorylated proteins.
13 point contacts containing enriched levels of tyrosine-phosphorylated proteins.
14 ted lipid rafts colocalized with the BCR and tyrosine-phosphorylated proteins.
15 mpetent to catalyze the dephosphorylation of tyrosine-phosphorylated proteins.
16 l contact components paxillin, vinculin, and tyrosine-phosphorylated proteins.
20 , we found that CRKL rapidly associates with tyrosine-phosphorylated proteins after cross-linking of
23 s talin and vinculin, have a central core of tyrosine phosphorylated proteins and are depleted of int
24 ombining mass spectrometry identification of tyrosine phosphorylated proteins and growth inhibition i
25 this site results in decreased affinity for tyrosine-phosphorylated proteins and decreased PI3K memb
26 man monocytes, M-CSF increased the levels of tyrosine-phosphorylated proteins and induced Akt activat
28 FR phosphorylation, decreased the numbers of tyrosine-phosphorylated proteins and levels of type I co
29 he stimulation of PI3-kinase associated with tyrosine-phosphorylated proteins and of p85/PI3-kinase a
30 recently that 14-3-3 associates with several tyrosine-phosphorylated proteins and phosphatidylinosito
32 ate may prove useful in the search for novel tyrosine-phosphorylated proteins and the identification
33 aralleled by morphological redistribution of tyrosine-phosphorylated proteins and the tyrosine kinase
34 y to bind to both substrates and appropriate tyrosine-phosphorylated proteins and therefore can compe
35 nding sites, an SH2 domain for binding other tyrosine phosphorylated proteins, and an enzymatic activ
37 qually applicable to serine-, threonine- and tyrosine-phosphorylated proteins, and is capable of sele
40 osphotyrosine and cortactin demonstrate that tyrosine-phosphorylated proteins, as well as cortactin,
42 ass spectrometric identification of a 155-kD tyrosine phosphorylated protein associated with src homo
43 ted with the Grb-2 adaptor and are the major tyrosine phosphorylated proteins associated with the Ras
44 demonstrated that SLP-76, a Grb2-associated tyrosine-phosphorylated protein, augments Interleukin-2
45 ory have shown that c-Cbl is the predominant tyrosine-phosphorylated protein bound to the p85 subunit
46 e binding (PTB) domain specifically binds to tyrosine-phosphorylated proteins, but differs in structu
47 Ganglioside G(M1), a lipid raft marker, and tyrosine-phosphorylated proteins, but not CD45 and trans
48 4-2 PCa cells showed a small set of discrete tyrosine-phosphorylated proteins, but these proteins wer
49 ir cell-surface antigen receptor overproduce tyrosine phosphorylated proteins; (c) lupus and lupus ne
50 lts in notable differences in the pattern of tyrosine phosphorylated proteins compared with that obta
51 ng tubular networks indicated differences in tyrosine phosphorylated proteins compared with the poorl
52 ably phosphorylated by Btk; however, a third tyrosine-phosphorylated protein coprecipitated with Brig
59 m of DEP-1 interacted with a small subset of tyrosine-phosphorylated proteins from lysates of the hum
60 nt study, we performed a global profiling of tyrosine-phosphorylated proteins from mutant Kit-driven
61 addition, DEP-1 coprecipitated with several tyrosine-phosphorylated proteins from pervanadate-treate
63 ecipitations of Dock also co-precipitate two tyrosine-phosphorylated proteins having molecular masses
65 ith a co-precipitating high molecular weight tyrosine-phosphorylated protein identified as desmoglein
66 CRKL has previously been shown to be a major tyrosine phosphorylated protein in neutrophils of patien
67 -regulated kinase (ERK)-1 and ERK-2 as major tyrosine phosphorylated proteins in IL-1 stimulated chon
68 o acids in cell culture (SILAC), to identify tyrosine phosphorylated proteins in isogenic human bronc
69 on of disease correlated with a reduction of tyrosine phosphorylated proteins in lymph node cells of
70 was shown to be the major CSF-1R-associated tyrosine-phosphorylated protein in CSF-1-treated BMM.
71 We initially identified a prominent 130-kDa tyrosine-phosphorylated protein in pervanadate-treated H
73 protein c-Cbl is one of the most prominently tyrosine-phosphorylated proteins in Bcr-Abl-expressing c
75 ling; however, current methods for analyzing tyrosine-phosphorylated proteins in crude protein extrac
76 tive Brk mutant (YF-Brk) and associates with tyrosine-phosphorylated proteins in deregulated signalin
77 identified by immunoaffinity purification of tyrosine-phosphorylated proteins in GIST cells before an
78 port that SHP-1 is associated with two major tyrosine-phosphorylated proteins in hematopoietic cells
79 e PTP, it preferentially targets a subset of tyrosine-phosphorylated proteins in host cells, includin
80 sk specifically associates with at least two tyrosine-phosphorylated proteins in normal human T cells
82 Shc PTB domain binds to 130 kDa and 145 kDa tyrosine-phosphorylated proteins in response to stimulat
84 n intriguing set of serine-, threonine-, and tyrosine-phosphorylated proteins in the Archaea that may
86 mmunoaffinity profiling strategy to identify tyrosine-phosphorylated proteins in the KG-1 cell line.
87 within minutes in the appearance of numerous tyrosine-phosphorylated proteins in the liver and kidney
88 te results in the rapid accumulation of many tyrosine-phosphorylated proteins in the liver and kidney
89 differences in the profiles of 75- and 80-kD tyrosine-phosphorylated proteins in the zyxin-null cells
90 6 was found to coimmunoprecipitate with five tyrosine phosphorylated proteins including p60fyn and p5
91 co-distribute in all cell cortex extensions, tyrosine-phosphorylated proteins including p190 appear t
92 stream of GP Ib, and associates with several tyrosine-phosphorylated proteins including the Fc recept
93 ulated cells, SLAP-2 associated with several tyrosine phosphorylated proteins, including the ubiquiti
94 pectrometry that identifies large numbers of tyrosine-phosphorylated proteins, including active kinas
95 ects that involve up-regulated expression of tyrosine-phosphorylated proteins, including beta-catenin
97 hat Btk formed stable complexes with several tyrosine-phosphorylated proteins, including PLCgamma2, o
98 fractions also contained discrete endogenous tyrosine-phosphorylated proteins, including prominent ba
99 ability of the Fyn SH2 domain to precipitate tyrosine-phosphorylated proteins, including the CD3zeta
100 TPIP1, or CD2-binding protein 1 (CD2BP1)], a tyrosine-phosphorylated protein involved in cytoskeletal
102 on of the actin cup and local recruitment of tyrosine phosphorylated proteins is markedly attenuated.
103 ectron microscopy studies revealed that this tyrosine-phosphorylated protein is localized to the cyto
104 n of PI-3K and its association with specific tyrosine-phosphorylated proteins may be important in ins
107 hows that CD72 ligation induces a variety of tyrosine-phosphorylated proteins, most of which were of
108 There was no difference in the pattern of tyrosine-phosphorylated proteins observed following stim
109 d in ganglioside G(M1) and cholesterol where tyrosine phosphorylated proteins occur at late anaphase
114 nd SH3 domain of CMS bound specifically to a tyrosine-phosphorylated protein of 120 kDa, which we ide
115 is associated through its PTB domain with a tyrosine-phosphorylated protein of 140 kD (p140) in vivo
117 in the co-immunoprecipitation of MUC1 with a tyrosine-phosphorylated protein of approximately 180 kDa
119 ts implicate Shc, Grb2, p140, and additional tyrosine-phosphorylated proteins of 61 and 200 kD in sig
120 In rabbit colonic muscularis mucosae cells, tyrosine-phosphorylated proteins of approximately 60 and
122 I to explore the functions of these abundant tyrosine-phosphorylated proteins of synaptic vesicles.
124 ar to that required to decrease the level of tyrosine phosphorylated proteins or of the protein tyros
126 NA cloning, and characterization of a 56-kDa tyrosine phosphorylated protein, p56(dok-2) (Dok-2), fro
131 h this increase is the appearance of several tyrosine phosphorylated proteins present only in differe
132 teins of both hck and fyn bound to a 150-kDa tyrosine-phosphorylated protein present in lysates of IL
134 [PtdIns(3,4,5)P3] and Src homology 2 domain [tyrosine-phosphorylated proteins, PtdIns(3,4,5)P3] of PL
136 suggest a model in which association with a tyrosine-phosphorylated protein restricts the repertoire
141 antibodies directed against known 60-70-kDa tyrosine-phosphorylated proteins suggest that pp68 may b
142 We have identified a high-molecular-mass tyrosine-phosphorylated protein that is rapidly phosphor
144 n the chronic phase contain a constitutively tyrosine-phosphorylated protein that migrates at 62 kDa
151 nduces a subsequent, specific recruitment of tyrosine phosphorylated proteins to APP, including Lyn a
152 lamellipodial extension, and localization of tyrosine phosphorylated proteins to the cell periphery.
153 y, SAP specifically interacted with a 75-kDa tyrosine-phosphorylated protein upon TCR stimulation.
154 tivation, Shc also associates with a 145-kDa tyrosine-phosphorylated protein upon triggering via anti
155 ssembly of signaling complexes by binding to tyrosine phosphorylated proteins using their SH2 domains
156 small GTPase Ras, Nck is presumed to bind to tyrosine-phosphorylated proteins using its SH2 domain an
157 na was prepared for Western blot analysis of tyrosine-phosphorylated proteins, vascular endothelial g
160 n the course of this purification, a 105-kDa tyrosine-phosphorylated protein was only detected in fra
163 nti-phosphotyrosine antibodies to enrich for tyrosine phosphorylated proteins, we have identified a n
164 atients (<4 months), various sizes of highly tyrosine phosphorylated proteins were observed as high b
165 haracterize flow-activated tyrosine kinases, tyrosine-phosphorylated proteins were immunoprecipitated
168 that some of the selected sequences encoded tyrosine phosphorylated proteins when expressed on phage
169 ion of the EGFR was confirmed by analysis of tyrosine phosphorylated proteins, which revealed a rapid
170 and Sos1 inducibly associate with a 180-kDa tyrosine-phosphorylated protein, which was determined to
171 TPH1-D811A mutant trapped primarily a 97-kDa tyrosine-phosphorylated protein, which was determined to
172 omes associated with an approximately 72-kDa tyrosine-phosphorylated protein, which we identify here
174 cked the assembly of F-actin, FAK, rho A and tyrosine-phosphorylated proteins while not affecting the
175 The SH2 domain of the Nck adaptor can bind tyrosine-phosphorylated proteins, while its SH3 domains
176 we report the identification of prominently tyrosine-phosphorylated proteins with a molecular mass o
178 tivation, and the association of a number of tyrosine-phosphorylated proteins with growth factor rece
180 the adaptor molecule CBL, and association of tyrosine-phosphorylated proteins with phosphatidylinosit
181 terially expressed Shd domain bound multiple tyrosine-phosphorylated proteins with relative molecular
182 accompanied by an increase in association of tyrosine-phosphorylated proteins with the adapter protei
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