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1 /F3 hematopoietic cells expressing exogenous PDGF beta receptor.
2 otein in the productive interaction with the PDGF beta receptor.
3 lex formation between the E5 protein and the PDGF beta receptor.
4 g activation and signaling mechanisms of the PDGF beta receptor.
5 FKBP fused to the insulin receptor or to the PDGF beta receptor.
6 m C127 fibroblasts, which express endogenous PDGF beta receptor.
7 ms a hydrogen bond with threonine 513 of the PDGF beta receptor.
8 otein transform cells without activating the PDGF beta receptor.
9 rtance of this position in activation of the PDGF beta receptor.
10 se C127 cells stably bound and activated the PDGF beta receptor.
11 actions with the transmembrane domain of the PDGF beta receptor.
12 brane domains that can bind and activate the PDGF beta receptor.
13 ed dimers and stably bound and activated the PDGF beta receptor.
14 ansmembrane sequence motifs can activate the PDGF beta receptor.
15 ow it to tolerate different mutations in the PDGF beta receptor.
16 for the complex between the E5 dimer and the PDGF beta receptor.
17 and to bind to and induce activation of the PDGF beta receptor.
18 cell transformation and interaction with the PDGF beta receptor.
19 nd their ability to bind to and activate the PDGF beta receptor.
20 orylation state of tyrosine 751 in the human PDGF-beta receptor.
21 human fibroblasts engineered to express the PDGF-beta receptor.
22 binding protein 2, son of sevenless, and the PDGF-beta receptor.
23 mily kinases, BCR-ABL, c-KIT, EPHA2, and the PDGF-beta receptor.
24 ne incorporation in PAE cells expressing the PDGF beta-receptors.
25 tivating the platelet-derived growth factor (PDGF) beta receptor.
26 1021 of the platelet-derived growth factor (PDGF) beta receptor.
27 quential stimulation of beta2-adrenergic and PDGF-beta receptors.
28 n of early endosomes containing internalised PDGF-beta receptors.
30 esults indicated that the E5 protein induced PDGF beta receptor activation by forming a stable comple
31 a) DNA binding, which suggests that the PDGF/PDGF-beta receptor/Akt pathway induces downstream HIF-1a
32 mbrane salt bridge between lysine 499 on the PDGF beta receptor and an acidic residue in the C termin
33 -Sis recognize distinct binding sites on the PDGF beta receptor and further clarify the nature of the
34 und that H2O2 induced phosphorylation of the PDGF beta receptor and increased ATM kinase activity, tw
35 tion and for productive interaction with the PDGF beta receptor and indicated that aspartic acid 33 w
36 The active chimera formed complexes with the PDGF beta receptor and induced receptor tyrosine phospho
37 ied transmembrane proteins that activate the PDGF beta receptor and revealed the importance of hydrop
39 ed important for its ability to activate the PDGF beta receptor and transform mouse fibroblasts: a pa
40 ugh the platelet-derived growth factor beta (PDGF beta) receptor and the ataxia telangiectasia mutate
41 ng the expression and activity of KCa3.1 and PDGF beta-receptors and inhibiting the rise in [Ca(2+)]i
42 the cellular platelet-derived growth factor (PDGF) beta receptor and induces constitutive tyrosine ph
43 omain of the platelet-derived growth factor (PDGF) beta receptor and induces ligand-independent recep
44 xpression of platelet-derived growth factor (PDGF)-beta receptor and potentiates chemotaxis to PDGF-B
45 xpression of platelet-derived growth factor (PDGF)-beta receptor and the proliferative response to pl
46 between the platelet-derived growth factor (PDGF)beta receptor and the sphingosine 1-phosphate recep
47 of the human platelet-derived growth factor (PDGF)beta receptor and the transmembrane and intracellul
49 reperfusion, and tyrosine phosphorylation of PDGF-beta receptor and PI3K was increased at 168 hours o
50 omplex containing both FAK and the activated PDGF-beta receptor and resulted in reduced tyrosine phos
51 d-stimulated tyrosine phosphorylation of the PDGF-beta receptor and the activation of mitogen-activat
52 , the native platelet-derived growth factor (PDGF)beta receptor, and c-KIT, but it does not inhibit S
53 cells displayed increased phosphorylation of PDGF-beta receptor, and an enhanced mitogenic response,
54 let-derived growth factor (PDGF)-B chain and PDGF-beta receptor, and five intracellular signal protei
55 associated with elevated expression of PDGF, PDGF-beta receptor, and VEGFR2; this effect was greater
56 e ECM mediates this effect by preventing the PDGF beta receptor (betaPDGFR) from associating with the
58 ukemogenesis, we evaluated the role of mouse PDGF-beta-receptor binding sites for PI3-K (Y708, Y719)
59 ence of platelet-derived growth factor-beta (PDGF-beta) receptor blocks the association of the C-term
60 nist-induced tyrosine phosphorylation of the PDGF-beta receptor, but not the epidermal growth factor
61 lex with the platelet-derived growth factor (PDGF) beta receptor, causing receptor activation and cel
62 h PDGF-BB and in tissue reparative processes PDGF beta-receptors colocalize with the caveolae/lipid r
63 receptor-binding protein 2/son of sevenless/PDGF-beta receptor complex and activation of the pertuss
64 for the assembly of multiprotein, activated PDGF beta receptor complexes in response to the E5 prote
65 edimentation in sucrose gradients, activated PDGF beta receptor complexes were separated from monomer
66 eered to coexpress full-length and truncated PDGF beta receptors confirmed that the E5 protein induce
68 sm that involves up-regulation of PDGF-B and PDGF-beta receptor-dependent activation of the PI3K/Akt
69 and in colorectal adenocarcinoma, activated PDGF beta-receptors do not colocalize with caveolin-1.
70 * transmembrane domain in the context of the PDGF beta receptor facilitates receptor homodimerization
71 nd monomeric platelet-derived growth factor (PDGF) beta receptors fused to the FK506-binding protein
72 pparently undeleted HTLV-I provirus into the PDGF beta-receptor gene in an orientation enabling expre
73 ver, Stat3 was phosphorylated on tyrosine in PDGF beta receptor immunoprecipitates of PDGF-treated bu
74 esults confirm the central importance of the PDGF beta receptor in mediating E5 transformation and hi
77 ated only a small fraction of the endogenous PDGF beta receptor in transformed fibroblasts and sugges
85 tegral to p53 activation as either AG1433 (a PDGF beta receptor inhibitor) or caffeine (an ATM kinase
88 ng analyses with this antibody show that the PDGF-beta receptor is constitutively phosphorylated at t
89 f the various E5 mutant proteins to bind the PDGF beta receptor, lead to receptor tyrosine phosphoryl
90 bility and that HTLV-I-induced truncation of PDGF beta-receptor may correlate with HTLV-I-associated
91 nal proteins PLC gamma, SHC, MAPK, PI3K, and PDGF-beta receptor may play an important role in ischemi
92 human meningioma and suggest that activated PDGF-beta receptors might contribute to the pathology of
93 udies to molecularly characterize the 3.8 kb PDGF beta-receptor mRNA and show that it has resulted fr
95 ientation enabling expression of a truncated PDGF beta-receptor mRNA using the 3' HTLV-I long termina
96 the expression of PDGF-R alpha mRNA, but not PDGF-beta receptor mRNA, in asbestos-exposed rat lungs w
98 ese E5 mutants displayed lower activity with PDGF beta receptor mutants containing other transmembran
99 d a panel of platelet-derived growth factor (PDGF) beta receptor mutants (beta-PDGFR), which selectiv
102 tions did not form a stable complex with the PDGF beta receptor or transform cells, in agreement with
104 cted with a plasmid containing the truncated PDGF beta-receptor ORF plasmid generate colonies in soft
105 nd migration and prevented the expression of PDGF-beta receptor (PDGF-betar), alpha-smooth muscle act
106 HepG2 cells that express the kinase-inactive PDGF beta-receptor, PDGF-BB activates the PDGF alpha-rec
108 ate the mechanism for cross talk between the PDGF beta receptor (PDGFbetaR) and the EGFR, we stimulat
111 f platelet-derived growth factor (PDGF), the PDGF beta receptor (PDGFR) undergoes autophosphorylation
112 Platelet-derived growth factor (PDGF)-B and PDGF beta-receptor (PDGFR beta) deficiency in mice is em
113 actor (PDGF) and functions downstream of the PDGF-beta receptor (PDGFR) to mediate biological process
114 onstrate that, after ligand stimulation, the PDGF beta receptor (PDGFRbeta) becomes ubiquitinated in
115 show that Fer associates with the activated PDGF beta-receptor (PDGFRbeta) through multiple autophos
116 f both TGFbeta type I receptor (TbetaRI) and PDGF beta-receptor (PDGFRbeta), and it was prevented by
118 s where pericyte-like cells that express the PDGF-beta receptor (Pdgfrbeta) proliferate aberrantly an
119 f phosphatidylinositol 3-kinase (PI3K) or of PDGF-beta receptor phosphorylation abrogated both hypoxi
122 the subsequent up-regulation of a cohort of PDGF beta-receptors primarily confined to the non-lipid
123 owth factor- (PDGF)-BB activates a cohort of PDGF-beta receptors primarily confined to the lipid raft
124 These results indicate that the truncated PDGF beta-receptor protein acquires transforming capabil
125 ants to identify specific amino acids in the PDGF beta receptor required for productive interaction w
126 e that these mutants do in fact activate the PDGF beta receptor, resulting in cellular signaling and
127 utations that restored binding to the mutant PDGF beta receptor, resulting in receptor activation and
128 the cellular platelet-derived growth factor (PDGF) beta receptor, resulting in constitutive activatio
129 the cellular platelet-derived growth factor (PDGF) beta receptor, resulting in receptor activation an
130 the cellular platelet-derived growth factor (PDGF) beta receptor, resulting in sustained receptor sig
131 he intrinsic tyrosine kinase activity of the PDGF-beta receptor stimulates the formation of a membran
132 strated that platelet-derived growth factor (PDGF)-beta receptor stimulation, but not various other g
134 city of antisense oligonucleotides to reduce PDGF-beta receptor subunit (PDGFR-beta) expression and t
135 a receptor tyrosine phosphorylation, whereas PDGF beta receptor suppression with RNA interference imp
136 activated only a small fraction of the total PDGF beta receptor, that not all receptor molecules asso
137 apparently dimeric), tyrosine-phosphorylated PDGF beta receptor, the E5 protein, and associated cellu
138 the cellular platelet-derived growth factor (PDGF) beta receptor through transmembrane and juxtamembr
139 e endogenous platelet-derived growth factor (PDGF) beta receptor through transmembrane and juxtamembr
140 f the murine platelet-derived growth factor (PDGF) beta receptor to alanine-scanning mutagenesis.
142 llow it to tolerate the same mutation in the PDGF beta receptor transmembrane domain and that a mutat
143 of the library proteins bound and activated PDGF beta receptor transmembrane mutants that were not a
144 RKS: Although PKR is pre-associated with the PDGF beta-receptor, treatment with PDGF only modestly ac
145 mers of the E5 protein activate the cellular PDGF beta receptor tyrosine kinase by binding to its tra
146 protein bind the transmembrane region of the PDGF beta receptor tyrosine kinase, causing receptor dim
147 of ATM kinase had no effect on H2O2-induced PDGF beta receptor tyrosine phosphorylation, whereas PDG
149 ay and MAPK pathway activities and inhibited PDGF-beta receptor upregulation in raised glucose, and s
150 ize noncovalently, specifically activate the PDGF beta receptor via its transmembrane domain, and tra
151 in, in which the extracellular domain of the PDGF beta receptor was fused to the IgG(1) Fc domain, an
152 xpressed in HepG2 cells, the kinase-inactive PDGF beta-receptor was tyrosine phosphorylated in respon
153 transmembrane proteins for activators of the PDGF beta receptor, we isolated much smaller proteins, f
154 eta platelet-derived growth factor-receptor (PDGF beta-receptor), whereas HTLV-I-infected T-cell line
155 transmembrane domain of the wild type murine PDGF beta receptor with that of p185neu*, the oncogenic
156 y expressing platelet-derived growth factor (PDGF) beta receptors with mutations that eliminate activ
157 osphatidylinositol 3-kinase (PI 3-kinase) to PDGF-beta receptor with an IC50 of 0.445 +/- 0.047 micro
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